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1. Poulalhon N, Dalle S, Thomas L: [Dermoscopic diagnosis of dysplastic nevus]. Ann Dermatol Venereol; 2010 Mar;137(3):244-6
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  • [Title] [Dermoscopic diagnosis of dysplastic nevus].
  • [Transliterated title] Diagnostic dermoscopique des naevus dysplasiques.
  • [MeSH-major] Dermoscopy. Dysplastic Nevus Syndrome / diagnosis

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  • (PMID = 20227573.001).
  • [ISSN] 0151-9638
  • [Journal-full-title] Annales de dermatologie et de vénéréologie
  • [ISO-abbreviation] Ann Dermatol Venereol
  • [Language] fre
  • [Publication-type] Journal Article
  • [Publication-country] France
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2. Yamaguti GG, Lourenço GJ, Costa FF, Lima CS: High risk of 'de novo' acute myeloid leukaemia in individuals with cytochrome P450 A1 (CYP1A1) and NAD(P)H:quinone oxidoreductase 1 (NQO1) gene defects. Eur J Haematol; 2009 Sep;83(3):270-2
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  • [Title] High risk of 'de novo' acute myeloid leukaemia in individuals with cytochrome P450 A1 (CYP1A1) and NAD(P)H:quinone oxidoreductase 1 (NQO1) gene defects.
  • [MeSH-major] Cytochrome P-450 CYP1A1 / genetics. Leukemia, Myeloid, Acute / diagnosis. Leukemia, Myeloid, Acute / genetics. NAD(P)H Dehydrogenase (Quinone) / genetics

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  • (PMID = 19456854.001).
  • [ISSN] 1600-0609
  • [Journal-full-title] European journal of haematology
  • [ISO-abbreviation] Eur. J. Haematol.
  • [Language] eng
  • [Publication-type] Letter
  • [Publication-country] England
  • [Chemical-registry-number] EC 1.14.14.1 / Cytochrome P-450 CYP1A1; EC 1.6.5.2 / NAD(P)H Dehydrogenase (Quinone); EC 1.6.5.2 / NQO1 protein, human
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3. Vorob'eva VV, Mazina NK, Shabanov PD: [Mechanism of the cardioprotective effect of nifedipine in rabbits under vibration exposure conditions]. Eksp Klin Farmakol; 2010 Jun;73(6):5-9
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  • Nifedipine (7.5 mg/kg per os) activated the NAD-dependent site of respiratory chain and prevented hyperactivation of the succinate-dependent breath.

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  • (PMID = 20726343.001).
  • [ISSN] 0869-2092
  • [Journal-full-title] Eksperimental'naia i klinicheskaia farmakologiia
  • [ISO-abbreviation] Eksp Klin Farmakol
  • [Language] rus
  • [Publication-type] English Abstract; Journal Article
  • [Publication-country] Russia (Federation)
  • [Chemical-registry-number] 0 / Calcium Channel Blockers; 0 / Cardiotonic Agents; I9ZF7L6G2L / Nifedipine
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4. Minami M, Kamimura T, Isaka M, Tatsuno I, Ohta M, Hasegawa T: Clindamycin-induced CovS-mediated regulation of the production of virulent exoproteins streptolysin O, NAD glycohydrolase, and streptokinase in Streptococcus pyogenes. Antimicrob Agents Chemother; 2010 Jan;54(1):98-102
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  • [Title] Clindamycin-induced CovS-mediated regulation of the production of virulent exoproteins streptolysin O, NAD glycohydrolase, and streptokinase in Streptococcus pyogenes.
  • We aimed to evaluate the effect of CLI on the in vitro production of three major virulent exoproteins, namely, streptolysin O (Slo), NAD glycohydrolase (Nga), and streptokinase (Ska), by CLI-resistant S. pyogenes strains.
  • [MeSH-major] Anti-Bacterial Agents / pharmacology. Clindamycin / pharmacology. Genes, Bacterial / genetics. Intracellular Signaling Peptides and Proteins / genetics. NAD+ Nucleosidase / biosynthesis. NAD+ Nucleosidase / genetics. Streptococcus pyogenes / drug effects. Streptococcus pyogenes / genetics. Streptokinase / biosynthesis. Streptokinase / genetics. Streptolysins / biosynthesis. Streptolysins / genetics

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  • (PMID = 19805566.001).
  • [ISSN] 1098-6596
  • [Journal-full-title] Antimicrobial agents and chemotherapy
  • [ISO-abbreviation] Antimicrob. Agents Chemother.
  • [Language] eng
  • [Publication-type] Journal Article; Research Support, Non-U.S. Gov't
  • [Publication-country] United States
  • [Chemical-registry-number] 0 / Anti-Bacterial Agents; 0 / Bacterial Proteins; 0 / CovS protein, Streptococcus pyogenes; 0 / Intracellular Signaling Peptides and Proteins; 0 / Lincosamides; 0 / RNA, Bacterial; 0 / Streptolysins; 0 / streptolysin O; 3U02EL437C / Clindamycin; EC 3.2.2.5 / NAD+ Nucleosidase; EC 3.4.- / Streptokinase
  • [Other-IDs] NLM/ PMC2798487
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5. Scatolini M, Grand MM, Grosso E, Venesio T, Pisacane A, Balsamo A, Sirovich R, Risio M, Chiorino G: Altered molecular pathways in melanocytic lesions. Int J Cancer; 2010 Apr 15;126(8):1869-81
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  • To identify gene expression changes in melanocytic lesions, biopsies from 18 common nevi (CMN), 11 dysplastic nevi (DN), 8 radial and 15 vertical growth phase melanomas (RGPM, VGPM), and 5 melanoma metastases (MTS) were analyzed using whole genome microarrays.
  • DN exhibited rather heterogeneous molecular profiles, with some proliferation genes expressed at higher levels than in CMN, altered regulation of transcription compared to RGPM and a subset of processes, such as mismatch repair, equally expressed as in VGPM.
  • This holds true for dysplastic nevi in particular.
  • [MeSH-major] Melanoma / genetics. Nevus / genetics. Oligonucleotide Array Sequence Analysis. Skin Neoplasms / genetics


6. Sharkey MA, Engel PC: Modular coenzyme specificity: a domain-swopped chimera of glutamate dehydrogenase. Proteins; 2009 Nov 1;77(2):268-78
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  • Domain-swopped chimeras of the glutamate dehydrogenases from Clostridium symbiosum (CsGDH) (NAD(+)-specific) and Escherichia coli (EcGDH) (NADP(+)-specific) have been produced, with the aim of testing the localization of determinants of coenzyme specificity.
  • An active chimera consisting of the substrate-binding domain (Domain I) of CsGDH and the coenzyme-binding domain (Domain II) of EcGDH has been purified to homogeneity, and a thorough kinetic analysis has been carried out.
  • Results indicate that selectivity for the phosphorylated coenzyme does indeed reside solely in Domain II; the chimera utilizes NAD(+) at 0.8% of the rate observed with NADP(+), similar to the 0.5% ratio for EcGDH.
  • [MeSH-minor] Kinetics. NAD / metabolism. NADP / metabolism. Protein Structure, Tertiary / genetics. Structure-Activity Relationship. Substrate Specificity

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  • (PMID = 19425107.001).
  • [ISSN] 1097-0134
  • [Journal-full-title] Proteins
  • [ISO-abbreviation] Proteins
  • [Language] eng
  • [Publication-type] Journal Article; Research Support, Non-U.S. Gov't
  • [Publication-country] United States
  • [Chemical-registry-number] 0 / Coenzymes; 0 / Recombinant Fusion Proteins; 0U46U6E8UK / NAD; 53-59-8 / NADP; EC 1.4.1.2 / Glutamate Dehydrogenase
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7. Sutra T, Morena M, Bargnoux AS, Caporiccio B, Canaud B, Cristol JP: Superoxide production: a procalcifying cell signalling event in osteoblastic differentiation of vascular smooth muscle cells exposed to calcification media. Free Radic Res; 2008 Sep;42(9):789-97
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  • This study aimed at investigating the role of NAD(P)H oxidase in vascular calcification processes.
  • NAD(P)H oxidase sub-unit (p22(phox)), Cbfa-1, ERK phosphorylation and bone alkaline phosphatase (ALP) expressions were measured by Western blotting.
  • Results from this model strongly suggest a major implication of vascular NAD(P)H oxidase in vascular calcification supported by VSMCs osteoblastic differentiation.

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  • (PMID = 19051077.001).
  • [ISSN] 1029-2470
  • [Journal-full-title] Free radical research
  • [ISO-abbreviation] Free Radic. Res.
  • [Language] eng
  • [Publication-type] Journal Article; Research Support, Non-U.S. Gov't
  • [Publication-country] England
  • [Chemical-registry-number] 0 / Glycerophosphates; 11062-77-4 / Superoxides; BBX060AN9V / Hydrogen Peroxide; EC 3.1.3.1 / Alkaline Phosphatase; WWH06G87W6 / beta-glycerophosphoric acid
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8. Sottero B, Gamba P, Gargiulo S, Leonarduzzi G, Poli G: Cholesterol oxidation products and disease: an emerging topic of interest in medicinal chemistry. Curr Med Chem; 2009;16(6):685-705
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  • Oxysterols of pathophysiologic relevance generally possess a strong pro-oxidant effect, chiefly since they activate NAD(P)H oxidases.
  • Selective metabolic inhibitors of NAD(P)H oxidase and the MAPK pathway might quench or even prevent the cytotoxic effects of pathological accumulation of cholesterol oxides in cells and tissues.
  • The marked reduction of plasma oxysterols reported for statin-based therapy is interesting: it has been associated with a lower incidence and prevalence of Alzheimer's disease (AD) and vascular dementia.


9. Suzuki E, Okuda H, Nishida K, Fujimoto S, Nagasawa K: Protective effect of nicotinamide against poly(ADP-ribose) polymerase-1-mediated astrocyte death depends on its transporter-mediated uptake. Life Sci; 2010 Apr 24;86(17-18):676-82
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  • [Title] Protective effect of nicotinamide against poly(ADP-ribose) polymerase-1-mediated astrocyte death depends on its transporter-mediated uptake.
  • AIM: Poly(ADP-ribose) polymerase-1 (PARP-1) is a DNA repair enzyme, and its excessive activation, following ischemia, trauma, etc., depletes cellular nicotinamide adenine dinucleotide (NAD(+)) as a substrate and eventually leads to brain cell death.
  • Nicotinamide, an NAD(+) precursor and a PARP-1 inhibitor, is known to prevent PARP-1-triggered cell death, but there is no available information on the mechanisms involved in its transport.
  • Here we clarified the transport characteristics of nicotinamide in primary cultured mouse astrocytes.
  • MAIN METHODS: Uptake characteristics of [(14)C]nicotinamide were assessed by a conventional method with primary cultured mouse astrocytes.
  • KEY FINDINGS: PARP-1 activation was induced by treatment of astrocytes with N-methyl-N'-nitro-N-nitrosoguanidine (MNNG), an alkylating agent.
  • MNNG-triggered astrocyte death and PAR accumulation were completely inhibited by treatment with nicotinamide as with DPQ (3,4-dihydro-5-(4-(1-piperidinyl)butoxy)-1(2H)-isoquinolinone), a second generation PARP inhibitor.
  • The uptake of [(14)C]nicotinamide was time-, temperature-, concentration- and pH-dependent, and was inhibited and stimulated by co- and pre-treatment with N-methylnicotinamide, a representative substrate of an organic cation transport system, respectively.
  • Co-treatment of astrocytes with nicotinamide and N-methylnicotinamide resulted in a decrease in PAR accumulation and absolute prevention of cell death.
  • SIGNIFICANCE: These findings suggest that nicotinamide has a protective effect against PARP-1-induced astrocyte death and that its transporter-mediated uptake, which is extracellular pH-sensitive and common to N-methylnicotinamide, is critical for prevention of PARP-1-triggered cell death.

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  • (PMID = 20188745.001).
  • [ISSN] 1879-0631
  • [Journal-full-title] Life sciences
  • [ISO-abbreviation] Life Sci.
  • [Language] eng
  • [Publication-type] Journal Article; Research Support, Non-U.S. Gov't
  • [Publication-country] Netherlands
  • [Chemical-registry-number] 12001-76-2 / Vitamin B Complex; 25X51I8RD4 / Niacinamide; EC 2.4.2.30 / Parp1 protein, mouse; EC 2.4.2.30 / Poly(ADP-ribose) Polymerases; X3I82S5L8I / N-methylnicotinamide
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10. Kovacs K, Toth A, Deres P, Kalai T, Hideg K, Gallyas F Jr, Sumegi B: Critical role of PI3-kinase/Akt activation in the PARP inhibitor induced heart function recovery during ischemia-reperfusion. Biochem Pharmacol; 2006 Feb 14;71(4):441-52
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  • Poly(ADP-ribose) polymerase (PARP) inhibitors protect hearts from ischemia-reperfusion (IR)-induced damages by limiting nicotinamide adenine dinucleotide (NAD+) and ATP depletion, and by other, not yet elucidated mechanisms.
  • To clarify this possibility, we studied the effect of a well-characterized (4-hydroxyquinazoline) and a novel (carboxaminobenzimidazol-derivative) PARP inhibitor on the activation of phosphatidylinositol-3-kinase (PI3-kinase)/Akt pathway in Langendorff-perfused hearts.
  • All these data suggest that contrary to the original view, which considered preservation of NAD+ and consequently ATP pools as the exclusive underlying mechanism for the cytoprotective effect of PARP inhibitors, the activation of PI3-kinase/Akt pathway and related processes are at least equally important in the cardioprotective effects of PARP inhibitors during ischemia-reperfusion.

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  • (PMID = 16337154.001).
  • [ISSN] 0006-2952
  • [Journal-full-title] Biochemical pharmacology
  • [ISO-abbreviation] Biochem. Pharmacol.
  • [Language] eng
  • [Publication-type] Journal Article; Research Support, Non-U.S. Gov't
  • [Publication-country] England
  • [Chemical-registry-number] 0 / Androstadienes; 0 / Benzimidazoles; 0 / Chromones; 0 / Enzyme Inhibitors; 0 / HO 3089; 0 / Morpholines; 0 / Poly(ADP-ribose) Polymerase Inhibitors; 0 / Quinazolines; 0 / Quinazolinones; 0 / Thiobarbituric Acid Reactive Substances; 154447-36-6 / 2-(4-morpholinyl)-8-phenyl-4H-1-benzopyran-4-one; 491-36-1 / 4-hydroxyquinazoline; EC 2.7.1.- / Phosphatidylinositol 3-Kinases; EC 2.7.11.1 / Akt1 protein, rat; EC 2.7.11.1 / Proto-Oncogene Proteins c-akt; EC 2.7.11.1 / glycogen synthase kinase 3 beta; EC 2.7.11.26 / Glycogen Synthase Kinase 3; XVA4O219QW / wortmannin
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11. Xie L, Chang L, Guan Y, Wang X: C-reactive protein augments interleukin-8 secretion in human peripheral blood monocytes. J Cardiovasc Pharmacol; 2005 Nov;46(5):690-6
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  • C-reactive protein could augment the production of reactive oxygen species (ROS) as measured by chemiluminescence and inhibitors of NAD(P)H oxidase (DPI and PAO) and ROS scavengers (superoxide dismutase, catalase, and 1% dimethyl sulphoxide) abolished C-reactive protein-induced IL-8 secretion.
  • Thus, our data indicate that C-reactive protein at pathologic levels increases IL-8 secretion and mRNA via enhancing ROS derived mainly from NAD(P)H oxidase and the subsequent activation of ERK1/2, p38 MAPK, and NF-kappaB.


12. Nakahata Y, Kaluzova M, Grimaldi B, Sahar S, Hirayama J, Chen D, Guarente LP, Sassone-Corsi P: The NAD+-dependent deacetylase SIRT1 modulates CLOCK-mediated chromatin remodeling and circadian control. Cell; 2008 Jul 25;134(2):329-40
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  • [Title] The NAD+-dependent deacetylase SIRT1 modulates CLOCK-mediated chromatin remodeling and circadian control.
  • We show that the HDAC activity of the NAD(+)-dependent SIRT1 enzyme is regulated in a circadian manner, correlating with rhythmic acetylation of BMAL1 and H3 Lys9/Lys14 at circadian promoters.

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  • (PMID = 18662547.001).
  • [ISSN] 1097-4172
  • [Journal-full-title] Cell
  • [ISO-abbreviation] Cell
  • [Language] ENG
  • [Grant] United States / NIA NIH HHS / AG / AG011119-18; United States / NIA NIH HHS / AG / R37 AG011119-18; United States / NIGMS NIH HHS / GM / R01-GM081634-01; United States / NIA NIH HHS / AG / R37 AG011119; United States / NIGMS NIH HHS / GM / R01 GM081634
  • [Publication-type] Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't
  • [Publication-country] United States
  • [Chemical-registry-number] 0 / ARNTL Transcription Factors; 0 / Arntl protein, mouse; 0 / Basic Helix-Loop-Helix Transcription Factors; 0 / DNA-Binding Proteins; 0 / Dbp protein, mouse; 0 / Histones; 0 / Trans-Activators; 0 / Transcription Factors; 0U46U6E8UK / NAD; EC 2.3.1.48 / CLOCK Proteins; EC 2.3.1.48 / Clock protein, mouse; EC 3.5.1.- / Sirt1 protein, mouse; EC 3.5.1.- / Sirtuin 1; EC 3.5.1.- / Sirtuins; K3Z4F929H6 / Lysine
  • [Other-IDs] NLM/ NIHMS106176; NLM/ PMC3526943
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13. Dehn DL, Siegel D, Zafar KS, Reigan P, Swann E, Moody CJ, Ross D: 5-Methoxy-1,2-dimethyl-3-[(4-nitrophenoxy)methyl]indole-4,7-dione, a mechanism-based inhibitor of NAD(P)H:quinone oxidoreductase 1, exhibits activity against human pancreatic cancer in vitro and in vivo. Mol Cancer Ther; 2006 Jul;5(7):1702-9
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  • [Title] 5-Methoxy-1,2-dimethyl-3-[(4-nitrophenoxy)methyl]indole-4,7-dione, a mechanism-based inhibitor of NAD(P)H:quinone oxidoreductase 1, exhibits activity against human pancreatic cancer in vitro and in vivo.
  • The enzyme NAD(P)H:quinone oxidoreductase 1 (NQO1) has been found to be up-regulated in pancreatic cancer as well as many other solid tumors.
  • [MeSH-major] Antineoplastic Agents / pharmacology. Enzyme Inhibitors / pharmacology. Indolequinones / pharmacology. NAD(P)H Dehydrogenase (Quinone) / antagonists & inhibitors. Pancreatic Neoplasms / enzymology


14. Grahnert A, Richter S, Siegert F, Berndt A, Hauschildt S: The orthologue of the "acatalytic" mammalian ART4 in chicken is an arginine-specific mono-ADP-ribosyltransferase. BMC Mol Biol; 2008;9:86
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  • BACKGROUND: Human ART4, carrier of the GPI-(glycosyl-phosphatidylinositol) anchored Dombrock blood group antigens, is an apparently inactive member of the mammalian mono-ADP-ribosyltransferase (ART) family named after the enzymatic transfer of a single ADP-ribose moiety from NAD+ to arginine residues of extracellular target proteins.
  • Upon ectopic expression in C-33A cells, recombinant chicken ART4 localized at the cell surface as a GPI-anchored, highly glycosylated protein, which displayed arginine-specific ART activity (apparent Km of the recombinant protein for etheno-NAD+ 1.0 +/- 0.18 microM).

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  • (PMID = 18854029.001).
  • [ISSN] 1471-2199
  • [Journal-full-title] BMC molecular biology
  • [ISO-abbreviation] BMC Mol. Biol.
  • [Language] eng
  • [Publication-type] Journal Article; Research Support, Non-U.S. Gov't
  • [Publication-country] England
  • [Chemical-registry-number] 0 / Glycoproteins; 0 / Glycosylphosphatidylinositols; 94ZLA3W45F / Arginine; EC 2.4.2.- / ADP Ribose Transferases
  • [Other-IDs] NLM/ PMC2576468
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15. Wallius E, Tohka J, Hirvonen J, Hietala J, Ruotsalainen U: Evaluation of the automatic three-dimensional delineation of caudate and putamen for PET receptor occupancy studies. Nucl Med Commun; 2008 Jan;29(1):53-65
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  • OBJECTIVE: PET receptor occupancy studies with a baseline study and an intervention study are increasingly used as an aid in dose-finding procedures for central nervous system drug development.
  • With the test-retest dataset, the reproducibility (normalized absolute differences (NAD)) and reliability (intraclass correlation coefficient (ICC)) of binding potential values were assessed with the proposed methods designed specifically for receptor occupancy and compared with the manual segmentation.
  • The corresponding values for the manual two-dimensional segmentation were 3.45 to 6.65% and 0.82 to 0.96 (NAD differences non-significant).

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  • (PMID = 18049098.001).
  • [ISSN] 0143-3636
  • [Journal-full-title] Nuclear medicine communications
  • [ISO-abbreviation] Nucl Med Commun
  • [Language] eng
  • [Publication-type] Comparative Study; Evaluation Studies; Journal Article; Research Support, Non-U.S. Gov't
  • [Publication-country] England
  • [Chemical-registry-number] 0 / Receptors, Dopamine D2; 0 / Receptors, Neurokinin-1
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16. Aktas DF, Cook PF: Role of residues in the adenosine binding site of NAD of the Ascaris suum malic enzyme. Biochim Biophys Acta; 2008 Dec;1784(12):2059-64
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  • [Title] Role of residues in the adenosine binding site of NAD of the Ascaris suum malic enzyme.
  • Ascaris suum mitochondrial malic enzyme catalyzes the divalent metal ion dependent conversion of l-malate to pyruvate and CO(2), with concomitant reduction of NAD(P) to NAD(P)H.
  • In this study, some of the residues that form the adenosine binding site of NAD were mutated to determine their role in binding of the cofactor and/or catalysis.
  • D361, which is completely conserved among species, is located in the dinucleotide-binding Rossmann fold and makes a salt bridge with R370, which is also highly conserved.
  • D361 was mutated to E, A and N.
  • R370 was mutated to K and A.
  • D361E and A mutant enzymes were inactive, likely a result of the increase in the volume in the case of the D361E mutant enzyme that caused clashes with the surrounding residues, and loss of the ionic interaction between D361 and R370, for D361A.
  • Overall, results suggest that the salt bridge between D361 and R370 is important for maintaining the productive conformation of the NAD binding site.
  • Mutation of residues involved leads to nonproductive binding of NAD.
  • The interaction stabilizes one of the Rossmann fold loops that NAD binds.
  • Mutation of H377 to lysine, which is conserved in NADP-specific malic enzymes and proposed to be a cofactor specificity determinant, did not cause a shift in cofactor specificity of the Ascaris malic enzyme from NAD to NADP.
  • [MeSH-major] Ascaris suum / enzymology. Coenzymes / chemistry. Helminth Proteins / chemistry. Malate Dehydrogenase / chemistry. NAD / chemistry. NADP / chemistry

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  • (PMID = 18725329.001).
  • [ISSN] 0006-3002
  • [Journal-full-title] Biochimica et biophysica acta
  • [ISO-abbreviation] Biochim. Biophys. Acta
  • [Language] eng
  • [Publication-type] Journal Article; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, Non-P.H.S.
  • [Publication-country] Netherlands
  • [Chemical-registry-number] 0 / Coenzymes; 0 / Helminth Proteins; 0U46U6E8UK / NAD; 53-59-8 / NADP; EC 1.1.1.37 / Malate Dehydrogenase
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17. Longo C, Segura S, Cesinaro AM, Bassoli S, Seidenari S, Pellacani G: An atypical Meyerson's naevus: a dermoscopic, confocal microscopic and immunohistochemical description of one case. J Eur Acad Dermatol Venereol; 2007 Mar;21(3):414-6
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  • [Title] An atypical Meyerson's naevus: a dermoscopic, confocal microscopic and immunohistochemical description of one case.
  • [MeSH-major] Nevus, Pigmented / pathology. Skin Neoplasms / pathology
  • [MeSH-minor] Adult. Dermoscopy. Diagnosis, Differential. Female. Humans. Immunohistochemistry. Microscopy, Confocal

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  • (PMID = 17309482.001).
  • [ISSN] 0926-9959
  • [Journal-full-title] Journal of the European Academy of Dermatology and Venereology : JEADV
  • [ISO-abbreviation] J Eur Acad Dermatol Venereol
  • [Language] eng
  • [Publication-type] Case Reports; Letter
  • [Publication-country] Netherlands
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18. Bello Z, Stitt B, Grubmeyer C: Interactions at the 2 and 5 positions of 5-phosphoribosyl pyrophosphate are essential in Salmonella typhimurium quinolinate phosphoribosyltransferase. Biochemistry; 2010 Feb 23;49(7):1377-87
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  • Quinolinate phosphoribosyltransferase (QAPRTase, EC 2.4.2.19) catalyzes an unusual phosphoribosyl transfer that is linked to a decarboxylation reaction to form the NAD precursor nicotinate mononucleotide, carbon dioxide, and pyrophosphate from quinolinic acid (QA) and 5-phosphoribosyl 1-pyrophosphate (PRPP).

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  • (PMID = 20047307.001).
  • [ISSN] 1520-4995
  • [Journal-full-title] Biochemistry
  • [ISO-abbreviation] Biochemistry
  • [Language] ENG
  • [Grant] United States / NIGMS NIH HHS / GM / GM048623-11; United States / NIGMS NIH HHS / GM / R01 GM048623; United States / NIGMS NIH HHS / GM / GM48623; United States / NIGMS NIH HHS / GM / R01 GM048623-11
  • [Publication-type] Comparative Study; Journal Article; Research Support, N.I.H., Extramural
  • [Publication-country] United States
  • [Chemical-registry-number] 0 / Bacterial Proteins; 30KYC7MIAI / Aspartic Acid; 3KX376GY7L / Glutamic Acid; 7540-64-9 / Phosphoribosyl Pyrophosphate; EC 2.4.2.- / Pentosyltransferases; EC 2.4.2.19 / nicotinate-nucleotide diphosphorylase (carboxylating); K3Z4F929H6 / Lysine
  • [Other-IDs] NLM/ NIHMS195528; NLM/ PMC2891058
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19. Sabri M, Dunford AJ, McLean KJ, Neeli R, Scrutton NS, Leys D, Munro AW: Characterization of coenzyme binding and selectivity determinants in Mycobacterium tuberculosis flavoprotein reductase A: analysis of Arg(199) and Arg(200) mutants at the NADP(H) 2'-phosphate binding site. Biochem J; 2009 Jan 01;417(1):103-12
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  • Mycobacterium tuberculosis FprA (flavoprotein reductase A) is an NAD(P)H- and FAD-binding reductase that is structurally/evolutionarily related to adrenodoxin reductase.
  • [MeSH-minor] Binding Sites / genetics. Flavin-Adenine Dinucleotide / metabolism. Kinetics. Mutagenesis, Site-Directed. Mutation. Protein Binding. Protein Structure, Secondary. Structure-Activity Relationship

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  • (PMID = 18767989.001).
  • [ISSN] 1470-8728
  • [Journal-full-title] The Biochemical journal
  • [ISO-abbreviation] Biochem. J.
  • [Language] eng
  • [Grant] United Kingdom / Biotechnology and Biological Sciences Research Council / / BB/D01963X/1; United Kingdom / Biotechnology and Biological Sciences Research Council / / BBS/B/06288/2
  • [Publication-type] Journal Article
  • [Publication-country] England
  • [Chemical-registry-number] 0 / Coenzymes; 146-14-5 / Flavin-Adenine Dinucleotide; 53-59-8 / NADP; 94ZLA3W45F / Arginine; EC 1.18.1.- / FprA protein, M tuberculosis; EC 1.6.- / NADH, NADPH Oxidoreductases
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20. Starodub OT, Demitrack ES, Baumgartner HK, Montrose MH: Disruption of the Cox-1 gene slows repair of microscopic lesions in the mouse gastric epithelium. Am J Physiol Cell Physiol; 2008 Jan;294(1):C223-32
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  • Two-photon damage was initiated by scanning approximately 200 microm(2) of gastric surface cells with high laser intensity, causing rapid bleaching of NAD(P)H fluorescence in optically targeted cells.

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  • (PMID = 17959725.001).
  • [ISSN] 0363-6143
  • [Journal-full-title] American journal of physiology. Cell physiology
  • [ISO-abbreviation] Am. J. Physiol., Cell Physiol.
  • [Language] ENG
  • [Grant] United States / NIDDK NIH HHS / DK / R01 DK054940; United States / NIDDK NIH HHS / DK / R01-DK-54940
  • [Publication-type] Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't
  • [Publication-country] United States
  • [Chemical-registry-number] 0 / Membrane Proteins; 53-59-8 / NADP; EC 1.14.99.1 / Cyclooxygenase 1; EC 1.14.99.1 / Ptgs1 protein, mouse; M790V82VAC / 16,16-Dimethylprostaglandin E2
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21. King JD, Harmer NJ, Preston A, Palmer CM, Rejzek M, Field RA, Blundell TL, Maskell DJ: Predicting protein function from structure--the roles of short-chain dehydrogenase/reductase enzymes in Bordetella O-antigen biosynthesis. J Mol Biol; 2007 Nov 30;374(3):749-63
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  • These proteins exhibit typical SDR architecture and coordinate NAD.

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  • (PMID = 17950751.001).
  • [ISSN] 1089-8638
  • [Journal-full-title] Journal of molecular biology
  • [ISO-abbreviation] J. Mol. Biol.
  • [Language] eng
  • [Databank-accession-numbers] PDB/ 2PZJ/ 2PZK/ 2PZL/ 2PZM/ 2Q1S/ 2Q1T/ 2Q1U/ 2Q1W
  • [Grant] United Kingdom / Biotechnology and Biological Sciences Research Council / / BBS/E/J/000C0618; United Kingdom / Wellcome Trust / / 054588; United Kingdom / Wellcome Trust / / 064597; United Kingdom / Wellcome Trust / / 065482
  • [Publication-type] Journal Article; Research Support, Non-U.S. Gov't
  • [Publication-country] England
  • [Chemical-registry-number] 0 / O Antigens; EC 1.- / Oxidoreductases
  • [Other-IDs] NLM/ PMC2279256
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22. Korashy HM, El-Kadi AO: The role of aryl hydrocarbon receptor and the reactive oxygen species in the modulation of glutathione transferase by heavy metals in murine hepatoma cell lines. Chem Biol Interact; 2006 Sep 25;162(3):237-48
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  • Recently, we showed that heavy metals particularly Hg2+, Pb2+, and Cu2+ modulate the expression of phase II detoxifying enzymes such as NAD(P)H:quinone oxidoreductase 1 and Gsta1 in a concentration- and time-dependent manner.
  • Co-administration of heavy metals with AhR ligands differentially modulated Gst activity, in that co-exposure to Hg2+ plus AhR ligands could be beneficial in protecting against cytotoxicity as demonstrated by the increase in Gst activity with a proportional decrease in ROS production.

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  • (PMID = 16914127.001).
  • [ISSN] 0009-2797
  • [Journal-full-title] Chemico-biological interactions
  • [ISO-abbreviation] Chem. Biol. Interact.
  • [Language] eng
  • [Publication-type] Journal Article; Research Support, Non-U.S. Gov't
  • [Publication-country] Ireland
  • [Chemical-registry-number] 0 / Ligands; 0 / Reactive Oxygen Species; 0 / Receptors, Aryl Hydrocarbon; 2P299V784P / Lead; 789U1901C5 / Copper; EC 2.5.1.18 / Glutathione Transferase; FXS1BY2PGL / Mercury
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23. Ueno O, Yoshimura Y, Sentoku N: Variation in the activity of some enzymes of photorespiratory metabolism in C4 grasses. Ann Bot; 2005 Oct;96(5):863-9
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  • Both the NAD-malic enzyme and phosphoenolpyruvate carboxykinase grasses had high granal index in the BS chloroplasts.

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  • (PMID = 16100226.001).
  • [ISSN] 0305-7364
  • [Journal-full-title] Annals of botany
  • [ISO-abbreviation] Ann. Bot.
  • [Language] eng
  • [Publication-type] Journal Article; Research Support, Non-U.S. Gov't
  • [Publication-country] England
  • [Chemical-registry-number] 0 / Plant Proteins; 142M471B3J / Carbon Dioxide; EC 1.1.- / Alcohol Oxidoreductases; EC 1.1.1.81 / Hydroxypyruvate Reductase; EC 1.1.3.15 / glycollate oxidase; EC 1.11.1.6 / Catalase; S88TT14065 / Oxygen
  • [Other-IDs] NLM/ PMC4247052
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24. Goetz MP, Toft D, Reid J, Ames M, Stensgard B, Safgren S, Adjei AA, Sloan J, Atherton P, Vasile V, Salazaar S, Adjei A, Croghan G, Erlichman C: Phase I trial of 17-allylamino-17-demethoxygeldanamycin in patients with advanced cancer. J Clin Oncol; 2005 Feb 20;23(6):1078-87
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  • We also characterized the pharmacokinetics of 17-AAG, its effect on chaperone and client proteins, and whether cytochrome P450 (CYP) 3A5 and NAD(P)H:quinone oxidoreductase 1 (NQO1) polymorphisms affected 17-AAG disposition or toxicity.
  • [MeSH-minor] Adult. Aged. Antineoplastic Agents / administration & dosage. Antineoplastic Agents / adverse effects. Benzoquinones. Biomarkers / analysis. Cytochrome P-450 CYP3A. Cytochrome P-450 Enzyme System / genetics. Drug Administration Schedule. Female. HSP90 Heat-Shock Proteins / metabolism. Humans. Lactams, Macrocyclic. Male. Maximum Tolerated Dose. Middle Aged. NAD(P)H Dehydrogenase (Quinone) / genetics. Polymorphism, Genetic

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  • (PMID = 15718306.001).
  • [ISSN] 0732-183X
  • [Journal-full-title] Journal of clinical oncology : official journal of the American Society of Clinical Oncology
  • [ISO-abbreviation] J. Clin. Oncol.
  • [Language] eng
  • [Grant] United States / NCI NIH HHS / CA / CA15083; United States / NCI NIH HHS / CA / CA69912; United States / NCI NIH HHS / CA / CA90390; United States / NCRR NIH HHS / RR / M01-RR00585
  • [Publication-type] Clinical Trial; Clinical Trial, Phase I; Journal Article; Research Support, U.S. Gov't, P.H.S.
  • [Publication-country] United States
  • [Chemical-registry-number] 0 / Antineoplastic Agents; 0 / Benzoquinones; 0 / Biomarkers; 0 / HSP90 Heat-Shock Proteins; 0 / Lactams, Macrocyclic; 1W306TDA6S / Rifabutin; 4GY0AVT3L4 / tanespimycin; 9035-51-2 / Cytochrome P-450 Enzyme System; EC 1.14.14.1 / CYP3A protein, human; EC 1.14.14.1 / CYP3A5 protein, human; EC 1.14.14.1 / Cytochrome P-450 CYP3A; EC 1.6.5.2 / NAD(P)H Dehydrogenase (Quinone); EC 1.6.5.2 / NQO1 protein, human
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25. Teixeira AP, Portugal CA, Carinhas N, Dias JM, Crespo JP, Alves PM, Carrondo MJ, Oliveira R: In situ 2D fluorometry and chemometric monitoring of mammalian cell cultures. Biotechnol Bioeng; 2009 Mar 1;102(4):1098-106
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  • It was observed that the intensity of fluorescence signals in the excitation/emission wavelength range of amino acids, vitamins and NAD(P)H changed along culture time, although the dynamics of single fluorophors could not be correlated with the dynamics of the target state variables.

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  • (PMID = 18853411.001).
  • [ISSN] 1097-0290
  • [Journal-full-title] Biotechnology and bioengineering
  • [ISO-abbreviation] Biotechnol. Bioeng.
  • [Language] eng
  • [Publication-type] Evaluation Studies; Journal Article; Research Support, Non-U.S. Gov't
  • [Publication-country] United States
  • [Chemical-registry-number] 0 / Immunoglobulin G; 0 / Interleukin-2; 0 / Recombinant Fusion Proteins
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26. Hu CA, Khalil S, Zhaorigetu S, Liu Z, Tyler M, Wan G, Valle D: Human Delta1-pyrroline-5-carboxylate synthase: function and regulation. Amino Acids; 2008 Nov;35(4):665-72
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  • Mammalian Delta(1)-pyrroline-5-carboxylate synthase (P5CS) is a bifunctional ATP- and NAD(P)H-dependent mitochondrial enzyme that catalyzes the coupled phosphorylation and reduction-conversion of L: -glutamate to P5C, a pivotal step in the biosynthesis of L: -proline, L: -ornithine and L: -arginine.

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  • (PMID = 18401542.001).
  • [ISSN] 1438-2199
  • [Journal-full-title] Amino acids
  • [ISO-abbreviation] Amino Acids
  • [Language] ENG
  • [Grant] United States / NCI NIH HHS / CA / CA106644-03; United States / NCI NIH HHS / CA / R01 CA106644; United States / NCI NIH HHS / CA / R01 CA106644-04; United States / NCI NIH HHS / CA / CA106644-04; United States / NCI NIH HHS / CA / R01 CA106644-03; United States / NCI NIH HHS / CA / 5R01 CA106644; United States / NCRR NIH HHS / RR / RR016480-086585; United States / Howard Hughes Medical Institute / / ; United States / NCRR NIH HHS / RR / 2 P20 RR016480-04; United States / NCRR NIH HHS / RR / P20 RR016480-086585; United States / NCRR NIH HHS / RR / P20 RR016480
  • [Publication-type] Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, Non-P.H.S.
  • [Publication-country] Austria
  • [Chemical-registry-number] 3KX376GY7L / Glutamic Acid; 4TI98Z838E / Estradiol; 7S5I7G3JQL / Dexamethasone; 9DLQ4CIU6V / Proline; EC 2.6.1.13 / Ornithine-Oxo-Acid Transaminase; WI4X0X7BPJ / Hydrocortisone
  • [Other-IDs] NLM/ NIHMS95580; NLM/ PMC2707934
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27. Smith BC, Denu JM: Acetyl-lysine analog peptides as mechanistic probes of protein deacetylases. J Biol Chem; 2007 Dec 21;282(51):37256-65
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  • Class III histone deacetylases (Sir2 or sirtuins) catalyze the NAD+-dependent conversion of acetyl-lysine residues to nicotinamide, 2'-O-acetyl-ADP-ribose (OAADPr), and deacetylated lysine.
  • For the sirtuin Hst2, acetyl-lysine analog peptide binding correlated with the hydrophobic substituent parameter pi with a slope of -0.35 from a plot of log Kd versus pi.
  • The rate of catalysis with the acetyl-lysine analog peptides varied over five orders of magnitude with the class III deacetylase Hst2, revealing a linear free energy relationship with a slope of -1.57 when plotted versus the Taft constant, sigma*.
  • HDAC8, a class I deacetylase, displayed the opposite trend with a slope of +0.79.

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  • (PMID = 17951578.001).
  • [ISSN] 0021-9258
  • [Journal-full-title] The Journal of biological chemistry
  • [ISO-abbreviation] J. Biol. Chem.
  • [Language] eng
  • [Grant] United States / NIGMS NIH HHS / GM / 5 T32 GM08349; United States / NIGMS NIH HHS / GM / GM065386
  • [Publication-type] Journal Article; Research Support, N.I.H., Extramural
  • [Publication-country] United States
  • [Chemical-registry-number] 0 / 2-O-acetyl-ADP-ribose; 0 / Molecular Probes; 0 / O-Acetyl-ADP-Ribose; 0 / Peptides; 25X51I8RD4 / Niacinamide; EC 3.5.1.- / Sirtuins; EC 3.5.1.98 / Histone Deacetylases; K3Z4F929H6 / Lysine
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28. Ota H, Akishita M, Eto M, Iijima K, Kaneki M, Ouchi Y: Sirt1 modulates premature senescence-like phenotype in human endothelial cells. J Mol Cell Cardiol; 2007 Nov;43(5):571-9
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  • Mammalian Sirt1 NAD(+)-dependent protein deacetylase, the closest homolog of Sir2, regulates cell cycle, cellular senescence, apoptosis and metabolism, by functional interactions with a number of biological molecules such as p53.

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  • (PMID = 17916362.001).
  • [ISSN] 0022-2828
  • [Journal-full-title] Journal of molecular and cellular cardiology
  • [ISO-abbreviation] J. Mol. Cell. Cardiol.
  • [Language] eng
  • [Publication-type] Journal Article; Research Support, Non-U.S. Gov't
  • [Publication-country] England
  • [Chemical-registry-number] 0 / RNA, Small Interfering; 0 / Recombinant Proteins; EC 1.14.13.39 / Nitric Oxide Synthase; EC 3.2.1.23 / beta-Galactosidase; EC 3.5.1.- / SIRT1 protein, human; EC 3.5.1.- / Sirtuin 1; EC 3.5.1.- / Sirtuins
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29. Nitenberg A: [Hypertension, endothelial dysfunction and cardiovascular risk]. Arch Mal Coeur Vaiss; 2006 Oct;99(10):915-21
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  • It is related to activation of membranous NAD(P)H oxidases initiated by the stimulation of activating mecanosensors of protein C kinase.

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  • (PMID = 17100143.001).
  • [ISSN] 0003-9683
  • [Journal-full-title] Archives des maladies du coeur et des vaisseaux
  • [ISO-abbreviation] Arch Mal Coeur Vaiss
  • [Language] fre
  • [Publication-type] English Abstract; Journal Article; Review
  • [Publication-country] France
  • [Number-of-references] 27
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30. Mercade M, Cocaign-Bousquet M, Loubière P: Glyceraldehyde-3-phosphate dehydrogenase regulation in Lactococcus lactis ssp. cremoris MG1363 or relA mutant at low pH. J Appl Microbiol; 2006 Jun;100(6):1364-72
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  • In L. lactis MG1363, the GAPDH was strongly inhibited in vitro by decreased pH values, but this inhibition was totally compensated in vivo by the lower NADH/NAD+ ratio and more efficiently by the important increase in the intracellular amount of GAPDH.
  • CONCLUSIONS: Despite a better resistance to acid stress, the increased survival in L. lactis relA mutant at low pH was not related with an improved pH homeostasis but was associated with a diminished capacity to maintain a high flux through glycolysis.

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  • (PMID = 16696685.001).
  • [ISSN] 1364-5072
  • [Journal-full-title] Journal of applied microbiology
  • [ISO-abbreviation] J. Appl. Microbiol.
  • [Language] eng
  • [Publication-type] Journal Article
  • [Publication-country] England
  • [Chemical-registry-number] 0 / Culture Media; 8558G7RUTR / Pyruvic Acid; EC 1.2.1.- / Glyceraldehyde-3-Phosphate Dehydrogenases; EC 6.- / Ligases; EC 6.- / guanosine 3',5'-polyphosphate synthetases; IY9XDZ35W2 / Glucose
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31. Zhu H, Itoh K, Yamamoto M, Zweier JL, Li Y: Role of Nrf2 signaling in regulation of antioxidants and phase 2 enzymes in cardiac fibroblasts: protection against reactive oxygen and nitrogen species-induced cell injury. FEBS Lett; 2005 Jun 6;579(14):3029-36
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  • These include catalase, reduced glutathione (GSH), glutathione reductase (GR), GSH S-transferase (GST), and NAD(P)H:quinone oxidoreductase-1 (NQO1).
  • [MeSH-minor] Animals. Catalase / metabolism. Cells, Cultured. Enzyme Induction. Fibroblasts / enzymology. Fibroblasts / metabolism. Glutathione / metabolism. Glutathione Peroxidase / metabolism. Glutathione Reductase / metabolism. Heart / drug effects. Mice. Mice, Knockout. NAD(P)H Dehydrogenase (Quinone) / genetics. NAD(P)H Dehydrogenase (Quinone) / metabolism. NF-E2-Related Factor 2. RNA, Messenger / genetics. RNA, Messenger / metabolism. Superoxide Dismutase / metabolism. Thiones / pharmacology. Thiophenes / pharmacology. Xanthine / pharmacology

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  • (PMID = 15896789.001).
  • [ISSN] 0014-5793
  • [Journal-full-title] FEBS letters
  • [ISO-abbreviation] FEBS Lett.
  • [Language] eng
  • [Grant] United States / NCI NIH HHS / CA / CA91895; United States / NHLBI NIH HHS / HL / HL38324; United States / NHLBI NIH HHS / HL / HL63744; United States / NHLBI NIH HHS / HL / HL65608; United States / NHLBI NIH HHS / HL / HL71190
  • [Publication-type] Journal Article; Research Support, N.I.H., Extramural; Research Support, U.S. Gov't, P.H.S.
  • [Publication-country] Netherlands
  • [Chemical-registry-number] 0 / Antioxidants; 0 / DNA-Binding Proteins; 0 / NF-E2-Related Factor 2; 0 / Nfe2l2 protein, mouse; 0 / RNA, Messenger; 0 / Reactive Nitrogen Species; 0 / Reactive Oxygen Species; 0 / Thiones; 0 / Thiophenes; 0 / Trans-Activators; 1AVZ07U9S7 / Xanthine; 534-25-8 / 1,2-dithiol-3-thione; EC 1.11.1.6 / Catalase; EC 1.11.1.9 / Glutathione Peroxidase; EC 1.15.1.1 / Superoxide Dismutase; EC 1.6.5.2 / NAD(P)H Dehydrogenase (Quinone); EC 1.6.5.2 / NQO1 protein, human; EC 1.8.1.7 / Glutathione Reductase; GAN16C9B8O / Glutathione
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32. Safonova OA, Popova TN, Artyukhov VG, Matasova LV: Function of cytoplasmic NAD-dependent malate dehydrogenase from rat myocardium under conditions of ischemia. Bull Exp Biol Med; 2005 Jul;140(1):25-8
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  • [Title] Function of cytoplasmic NAD-dependent malate dehydrogenase from rat myocardium under conditions of ischemia.
  • NAD-dependent malate dehydrogenase activity decreased by 2.7 times in the myocardium of rats with experimental ischemia.
  • Cytoplasmic NAD-dependent malate dehydrogenase from intact and ischemic rat heart was purified by 91.4 and 95.5 times.

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  • (PMID = 16254612.001).
  • [ISSN] 0007-4888
  • [Journal-full-title] Bulletin of experimental biology and medicine
  • [ISO-abbreviation] Bull. Exp. Biol. Med.
  • [Language] eng
  • [Publication-type] Comparative Study; Journal Article; Research Support, Non-U.S. Gov't
  • [Publication-country] United States
  • [Chemical-registry-number] 789U1901C5 / Copper; BBX060AN9V / Hydrogen Peroxide; E1UOL152H7 / Iron; EC 1.1.1.37 / Malate Dehydrogenase; GAN16C9B8O / Glutathione; SY7Q814VUP / Calcium
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33. Yamada K, Hara N, Shibata T, Osago H, Tsuchiya M: The simultaneous measurement of nicotinamide adenine dinucleotide and related compounds by liquid chromatography/electrospray ionization tandem mass spectrometry. Anal Biochem; 2006 May 15;352(2):282-5
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  • [Title] The simultaneous measurement of nicotinamide adenine dinucleotide and related compounds by liquid chromatography/electrospray ionization tandem mass spectrometry.
  • We have developed a liquid chromatographic-tandem mass spectrometric method that is sensitive and specific and that simultaneously measures cellular NAD(+) and related compounds.
  • Using this method, NAD(+), NAAD, NMN, NAMN, NAM, NA, ADPR, and 5'AMP were first separated over a reverse-phase high-performance liquid chromatography resin in a mobile ammonium formate-methanol linear gradient.
  • We found a good linear response for each NAD(+)-related compound.
  • The limits of quantification for NAD(+) and related compounds range from 0.1 to 1 pmol.
  • The extraction efficiency of NAD(+) and related compounds from mouse erythrocytes is between 84 and 114%.
  • Using our method, we measured, in a single analysis, the amounts of NMN, NAMN, NAD(+), and 5'AMP present in mouse erythrocytes.
  • These results indicate that our method sensitively, specifically, and simultaneously measures cellular NAD(+) and related compounds.
  • [MeSH-major] NAD / analysis. Spectrometry, Mass, Electrospray Ionization / methods
  • [MeSH-minor] Adenosine Diphosphate Ribose / analysis. Adenosine Monophosphate / analysis. Animals. Chromatography, Liquid / methods. Erythrocytes / chemistry. HL-60 Cells. Humans. Mice. Mice, Inbred BALB C. Niacin / analysis. Niacinamide / analysis. Nicotinamide Mononucleotide / analogs & derivatives. Nicotinamide Mononucleotide / analysis. Sensitivity and Specificity

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  • (PMID = 16574057.001).
  • [ISSN] 0003-2697
  • [Journal-full-title] Analytical biochemistry
  • [ISO-abbreviation] Anal. Biochem.
  • [Language] eng
  • [Publication-type] Journal Article
  • [Publication-country] United States
  • [Chemical-registry-number] 0U46U6E8UK / NAD; 108646-17-9 / nicotinamide arabinoside adenine dinucleotide; 1094-61-7 / Nicotinamide Mononucleotide; 20762-30-5 / Adenosine Diphosphate Ribose; 25X51I8RD4 / Niacinamide; 2679MF687A / Niacin; 321-02-8 / nicotinate mononucleotide; 415SHH325A / Adenosine Monophosphate
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34. Ross-Inta C, Omanska-Klusek A, Wong S, Barrow C, Garcia-Arocena D, Iwahashi C, Berry-Kravis E, Hagerman RJ, Hagerman PJ, Giulivi C: Evidence of mitochondrial dysfunction in fragile X-associated tremor/ataxia syndrome. Biochem J; 2010 Aug 1;429(3):545-52
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  • FXTAS (fragile X-associated tremor/ataxia syndrome) is a late-onset neurodegenerative disorder that affects individuals who are carriers of premutation expansions (55-200 CGG repeats) in the 5' untranslated region of the FMR1 (fragile X mental retardation 1) gene.
  • The role of MD (mitochondrial dysfunction) in FXTAS was evaluated in fibroblasts and brain samples from premutation carriers with and without FXTAS symptoms, with a range of CGG repeats.
  • This study resulted in several important conclusions: (i) decreased NAD- and FAD-linked oxygen uptake rates and uncoupling between electron transport and synthesis of ATP were observed in fibroblasts from premutation carriers;.
  • Detection of MD is of critical importance to the management of FXTAS, since it opens up additional treatment options for this disorder.

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  • (PMID = 20513237.001).
  • [ISSN] 1470-8728
  • [Journal-full-title] The Biochemical journal
  • [ISO-abbreviation] Biochem. J.
  • [Language] ENG
  • [Grant] United States / NIA NIH HHS / AG / AG032115; United States / NIDCR NIH HHS / DE / UL1 DE019583; United States / NIA NIH HHS / AG / R01 AG024488; United States / NIDCR NIH HHS / DE / UL1 DE19583; United States / NIA NIH HHS / AG / RL1 AG032119; United States / NIA NIH HHS / AG / AG024488; United States / NIA NIH HHS / AG / RL1 AG032115; United States / NICHD NIH HHS / HD / R01 HD036071; United States / NIEHS NIH HHS / ES / R01 ES012691
  • [Publication-type] Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't
  • [Publication-country] England
  • [Chemical-registry-number] 0 / FMR1 protein, human; 139135-51-6 / Fragile X Mental Retardation Protein; 8L70Q75FXE / Adenosine Triphosphate
  • [Other-IDs] NLM/ NIHMS440729; NLM/ PMC4011071
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35. Liu JC, Chen CH, Chen JJ, Cheng TH: Urotensin II induces rat cardiomyocyte hypertrophy via the transient oxidization of Src homology 2-containing tyrosine phosphatase and transactivation of epidermal growth factor receptor. Mol Pharmacol; 2009 Dec;76(6):1186-95
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  • Apocynin, an NAD(P)H oxidase inhibitor, and N-acetyl cysteine (NAC), an ROS scavenger, both inhibited EGFR transactivation induced by U-II.

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  • (PMID = 19755521.001).
  • [ISSN] 1521-0111
  • [Journal-full-title] Molecular pharmacology
  • [ISO-abbreviation] Mol. Pharmacol.
  • [Language] eng
  • [Publication-type] Journal Article; Research Support, Non-U.S. Gov't
  • [Publication-country] United States
  • [Chemical-registry-number] 0 / Reactive Oxygen Species; 0 / Shc Signaling Adaptor Proteins; 0 / Urotensins; 9047-55-6 / urotensin II; EC 2.7.10.1 / Receptor, Epidermal Growth Factor; EC 3.1.3.48 / Protein Tyrosine Phosphatases
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36. You M, Cao Q, Liang X, Ajmo JM, Ness GC: Mammalian sirtuin 1 is involved in the protective action of dietary saturated fat against alcoholic fatty liver in mice. J Nutr; 2008 Mar;138(3):497-501
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  • Sirtuins 1 (SIRT1), a NAD+-dependent class III histone deacetylase, was upregulated by ethanol administration in mice fed the HSF diet (P < 0.05).

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  • (PMID = 18287356.001).
  • [ISSN] 1541-6100
  • [Journal-full-title] The Journal of nutrition
  • [ISO-abbreviation] J. Nutr.
  • [Language] ENG
  • [Grant] United States / NIAAA NIH HHS / AA / R01 AA015951; United States / NIAAA NIH HHS / AA / AA013623; United States / NIAAA NIH HHS / AA / AA015951
  • [Publication-type] Journal Article; Research Support, N.I.H., Extramural
  • [Publication-country] United States
  • [Chemical-registry-number] 0 / Dietary Fats; 0 / Fatty Acids; 0 / Fatty Acids, Unsaturated; 0 / Histones; 0 / RNA, Messenger; 0 / Srebf1 protein, mouse; 0 / Sterol Regulatory Element Binding Protein 1; 3K9958V90M / Ethanol; EC 1.14.19.1 / Scd1 protein, mouse; EC 1.14.19.1 / Stearoyl-CoA Desaturase; EC 3.5.1.- / Sirt1 protein, mouse; EC 3.5.1.- / Sirtuin 1; EC 3.5.1.- / Sirtuins
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37. Dunlap T, Chandrasena RE, Wang Z, Sinha V, Wang Z, Thatcher GR: Quinone formation as a chemoprevention strategy for hybrid drugs: balancing cytotoxicity and cytoprotection. Chem Res Toxicol; 2007 Dec;20(12):1903-12
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  • Drugs bioactivated to quinones have the potential to activate antioxidant/electrophile responsive element (ARE) transcription of genes for cytoprotective phase 2 enzymes such as NAD(P)H-dependent quinone oxidoreductase (NQO1) but can also cause cellular damage.
  • [MeSH-minor] Animals. Catalysis. Cell Line, Tumor. Cell Survival / drug effects. Chemoprevention. Cytoprotection. Esterases / metabolism. Glutathione / metabolism. Luciferases / genetics. Metabolic Detoxication, Phase II. Mice. Models, Biological. NAD(P)H Dehydrogenase (Quinone). NADPH Dehydrogenase / biosynthesis. NADPH Dehydrogenase / genetics. Response Elements / genetics. Swine

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  • (PMID = 17975886.001).
  • [ISSN] 0893-228X
  • [Journal-full-title] Chemical research in toxicology
  • [ISO-abbreviation] Chem. Res. Toxicol.
  • [Language] eng
  • [Grant] United States / NCI NIH HHS / CA / CA102590
  • [Publication-type] Journal Article; Research Support, N.I.H., Extramural
  • [Publication-country] United States
  • [Chemical-registry-number] 0 / Anti-Inflammatory Agents, Non-Steroidal; 0 / Benzoquinones; 0 / NCX 4040; 0 / Nitro Compounds; 175033-36-0 / nitroaspirin; 3T006GV98U / benzoquinone; EC 1.13.12.- / Luciferases; EC 1.6.5.2 / NAD(P)H Dehydrogenase (Quinone); EC 1.6.5.2 / Nqo1 protein, mouse; EC 1.6.99.1 / NADPH Dehydrogenase; EC 3.1.- / Esterases; GAN16C9B8O / Glutathione; R16CO5Y76E / Aspirin
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38. Di Costanzo L, Gomez GA, Christianson DW: Crystal structure of lactaldehyde dehydrogenase from Escherichia coli and inferences regarding substrate and cofactor specificity. J Mol Biol; 2007 Feb 16;366(2):481-93
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  • Lactaldehyde dehydrogenase from Escherichia coli (aldA gene product, P25553) is an NAD(+)-dependent enzyme implicated in the metabolism of l-fucose and l-rhamnose.
  • The structure of the ternary complex reveals that the nicotinamide ring of the cofactor is disordered between two conformations: one with the ring positioned in the active site in the so-called hydrolysis conformation, and another with the ring extended out of the active site into the solvent region, designated the out conformation.

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  • (PMID = 17173928.001).
  • [ISSN] 0022-2836
  • [Journal-full-title] Journal of molecular biology
  • [ISO-abbreviation] J. Mol. Biol.
  • [Language] ENG
  • [Databank-accession-numbers] PDB/ 2HG2/ 2ILU/ 2IMP
  • [Grant] United States / NIGMS NIH HHS / GM / R01 GM056838; United States / NIGMS NIH HHS / GM / GM56838
  • [Publication-type] Journal Article; Research Support, N.I.H., Extramural
  • [Publication-country] England
  • [Chemical-registry-number] 0 / Coenzymes; 33X04XA5AT / Lactic Acid; 53-59-8 / NADP; EC 1.2.- / Aldehyde Oxidoreductases; EC 1.2.1.22 / lactaldehyde dehydrogenase
  • [Other-IDs] NLM/ NIHMS17636; NLM/ PMC1866264
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39. Kovács KL, Kovács AT, Maróti G, Mészáros LS, Balogh J, Latinovics D, Fülöp A, Dávid R, Dorogházi E, Rákhely G: The hydrogenases of Thiocapsa roseopersicina. Biochem Soc Trans; 2005 Feb;33(Pt 1):61-3
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  • A third hydrogenase activity was located in the soluble fraction and was analogous to the NAD-reducing hydrogenases of cyanobacteria.
  • Although the genes encoding a typical H(2) sensor (hupUV) and a two-component regulator (hupR and hupT) are present in T. roseopersicina, the system is cryptic in the wild-type BBS strain.

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  • (PMID = 15667265.001).
  • [ISSN] 0300-5127
  • [Journal-full-title] Biochemical Society transactions
  • [ISO-abbreviation] Biochem. Soc. Trans.
  • [Language] eng
  • [Publication-type] Journal Article; Research Support, Non-U.S. Gov't
  • [Publication-country] England
  • [Chemical-registry-number] EC 1.12.7.2 / Hydrogenase
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40. Ju LK, Chen F, Xia Q: Monitoring microaerobic denitrification of Pseudomonas aeruginosa by online NAD(P)H fluorescence. J Ind Microbiol Biotechnol; 2005 Dec;32(11-12):622-8
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  • [Title] Monitoring microaerobic denitrification of Pseudomonas aeruginosa by online NAD(P)H fluorescence.
  • Being extremely sensitive to the change in cellular electron-accepting mechanisms, NAD(P)H fluorescence provides a useful ways for online monitoring of microaerobic metabolism.
  • (1) online monitoring of anaerobic nitrate respiration by NAD(P)H fluorescence, (2) effects of denitrification on P. aeruginosa phenotypes, (3) microaerobic denitrification of P. aeruginosa in continuous culture, and (4) correlation between NAD(P)H fluorescence and denitrification-to-respiration ratio.
  • Online NAD(P)H fluorescence is shown to sensitively detect the changes of cellular metabolism.
  • The applicability of online NAD(P)H fluorescence in monitoring and quantitatively describing the sensitive microaerobic state of microorganisms is clearly demonstrated.

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  • (PMID = 16228188.001).
  • [ISSN] 1367-5435
  • [Journal-full-title] Journal of industrial microbiology & biotechnology
  • [ISO-abbreviation] J. Ind. Microbiol. Biotechnol.
  • [Language] eng
  • [Publication-type] Journal Article; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, Non-P.H.S.; Review
  • [Publication-country] Germany
  • [Chemical-registry-number] 0 / Culture Media; 0 / Nitrates; 53-59-8 / NADP
  • [Number-of-references] 38
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41. Bayraktutan U: Coronary microvascular endothelial cell growth regulates expression of the gene encoding p22-phox. Free Radic Biol Med; 2005 Nov 15;39(10):1342-52
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  • The mRNA expression of p22-phox, a membrane-bound component of NAD(P)H oxidase, is elevated in proliferating compared to quiescent rat coronary microvascular endothelial cells (CMEC).
  • This study shows greater levels of p22-phox mRNA/protein expression, NAD(P)H oxidase activity, and superoxide anion (O(2)(-)) production in proliferating versus fully confluent and growth-arrested 50% confluent CMEC.
  • Suppression of O(2)(-) availability by a cell-permeable superoxide dismutase mimetic or inhibition of NAD(P)H oxidase activity via its specific inhibitors (apocynin, diphenyleneiodinium, phenylarsine oxide, and 4-(2-aminoethyl)bezenesulfonyl fluoride) or antisense p22-phox cDNA attenuated cell growth independent of changes in intracellular antioxidant glutathione levels.

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  • (PMID = 16257643.001).
  • [ISSN] 0891-5849
  • [Journal-full-title] Free radical biology & medicine
  • [ISO-abbreviation] Free Radic. Biol. Med.
  • [Language] eng
  • [Publication-type] Journal Article
  • [Publication-country] United States
  • [Chemical-registry-number] 0 / Acetophenones; 0 / Arsenicals; 0 / Enzyme Inhibitors; 0 / Membrane Transport Proteins; 0 / Oligonucleotides, Antisense; 0 / Onium Compounds; 0 / Phosphoproteins; 0 / Proteins; 0 / RNA, Messenger; 0 / Sulfones; 0HUR2WY345 / oxophenylarsine; 1CC1JFE158 / Dactinomycin; 31C4KY9ESH / Nitric Oxide; 34284-75-8 / 4-(2-aminoethyl)benzenesulfonylfluoride; 53-59-8 / NADP; 6HJ411TU98 / diphenyleneiodonium; 98600C0908 / Cycloheximide; B6J7B9UDTR / acetovanillone; EC 1.6.3.1 / CYBA protein, human; EC 1.6.3.1 / NADPH Oxidase; GAN16C9B8O / Glutathione; S88TT14065 / Oxygen; VC2W18DGKR / Thymidine
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42. French SW: The pathogenesis and significance of the urinary alcohol cycle in rats fed ethanol intragastrically. Alcohol Clin Exp Res; 2005 Nov;29(11 Suppl):158S-161S
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  • What happens instead of the cycle is that the blood alcohol level rises to a lethal level when ethanol is given continuously at a dose of 11 g/kg/day by stomach tube.
  • The third element essential to the cycle is the generation of NAD to support the oxidation of alcohol by alcohol dehydrogenase.
  • Thus NADH increases and NAD decreases at the peak of the cycle.
  • Without the fluxuation of NAD, ADH activity cannot fluctuate during the cycle and the cycle is prevented.
  • The significance of the BALC in the understanding of alcohol liver disease pathogenesis is that there's a marked difference in the gene expression and liver toxicity when the peaks and troughs of the cycle are compared.
  • The NADH/NAD ratio is markedly increased and ATP levels are markedly decreased at the BAL peaks.
  • [MeSH-minor] Animals. Anoxia. Catecholamines / metabolism. Gene Expression. Hypothalamo-Hypophyseal System / metabolism. Liver / drug effects. Liver / pathology. NAD / metabolism. Periodicity. Rats. Thyroid Gland / metabolism

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  • (PMID = 16344601.001).
  • [ISSN] 0145-6008
  • [Journal-full-title] Alcoholism, clinical and experimental research
  • [ISO-abbreviation] Alcohol. Clin. Exp. Res.
  • [Language] eng
  • [Publication-type] Journal Article; Review
  • [Publication-country] United States
  • [Chemical-registry-number] 0 / Catecholamines; 0U46U6E8UK / NAD; 3K9958V90M / Ethanol
  • [Number-of-references] 19
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43. Shan C, Li F, Yuan F, Yang G, Niu L, Zhang Q: Size-controlled synthesis of monodispersed gold nanoparticles stabilized by polyelectrolyte-functionalized ionic liquid. Nanotechnology; 2008 Jul 16;19(28):285601
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  • The resulting AuNPs' size, with a narrow distribution, can be tuned by the concentration of HAuCl(4).
  • In addition, the PFIL-AuNPs exhibited obvious electrocatalytical activity toward β-nicotinamide adenine dinucleotide (NADH for short, a cofactor in enzymatic reactions of NAD(+)/NADH(-)-dependent dehydrogenases) oxidation, suggesting a potential application for bioelectroanalysis.

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  • (PMID = 21828732.001).
  • [ISSN] 0957-4484
  • [Journal-full-title] Nanotechnology
  • [ISO-abbreviation] Nanotechnology
  • [Language] eng
  • [Publication-type] Journal Article
  • [Publication-country] England
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44. Zee RS, Yoo CB, Pimentel DR, Perlman DH, Burgoyne JR, Hou X, McComb ME, Costello CE, Cohen RA, Bachschmid MM: Redox regulation of sirtuin-1 by S-glutathiolation. Antioxid Redox Signal; 2010 Oct 1;13(7):1023-32
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  • Sirtuin-1 (SIRT1) is an NAD(+)-dependent protein deacetylase that is sensitive to oxidative signals.

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  • (PMID = 20392170.001).
  • [ISSN] 1557-7716
  • [Journal-full-title] Antioxidants & redox signaling
  • [ISO-abbreviation] Antioxid. Redox Signal.
  • [Language] ENG
  • [Grant] United States / NHLBI NIH HHS / HV / N01-HV-28178; United States / NCRR NIH HHS / RR / S10-RR20946; United States / PHS HHS / / S10-R15942; United States / NHLBI NIH HHS / HL / P01 HL068758; United States / NCRR NIH HHS / RR / P41-RR10888; United States / NHLBI NIH HHS / HL / HL007969-06A1; United States / NHLBI NIH HHS / HL / R37 HL104017
  • [Publication-type] Journal Article; Research Support, N.I.H., Extramural
  • [Publication-country] United States
  • [Chemical-registry-number] 0 / Disulfides; 0 / Nitroso Compounds; 0 / Proteins; 0 / Stilbenes; 57564-91-7 / S-Nitrosoglutathione; EC 3.5.1.- / Sirtuin 1; GAN16C9B8O / Glutathione; K848JZ4886 / Cysteine; Q369O8926L / resveratrol
  • [Other-IDs] NLM/ PMC2959181
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45. Koller J: [Pigment nevi in children]. Hautarzt; 2010 May;61(5):443-51; quiz 452
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  • [Title] [Pigment nevi in children].
  • Almost all fair-skinned children demonstrate one or more pigment nevi at the integument.
  • While most pigmented nevi are per se harmless, congenital and atypical (dysplastic) nevi are considered as precursors of melanoma and risk indicators.
  • Although one normal nevus in isolation generally presents no risk, children and adults with multiple pigment nevi are at increased risk of developing a melanoma in the course of their life.
  • Since the onset of pigment nevi is undisputedly triggered by ultraviolet light, appropriate prevention and protection is crucial.
  • The differential diagnosis between nevus cell nevi and melanoma is particularly challenging, especially in the case of atypical nevi.
  • [MeSH-major] Dysplastic Nevus Syndrome / diagnosis. Melanoma / diagnosis. Neoplasms, Radiation-Induced / diagnosis. Nevus, Pigmented / diagnosis. Skin Neoplasms / diagnosis. Ultraviolet Rays / adverse effects
  • [MeSH-minor] Adolescent. Child. Dermatologic Surgical Procedures. Diagnosis, Differential. Humans. Skin / pathology. Wound Healing / physiology

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  • (PMID = 20437126.001).
  • [ISSN] 1432-1173
  • [Journal-full-title] Der Hautarzt; Zeitschrift für Dermatologie, Venerologie, und verwandte Gebiete
  • [ISO-abbreviation] Hautarzt
  • [Language] ger
  • [Publication-type] English Abstract; Journal Article
  • [Publication-country] Germany
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46. Heltweg B, Gatbonton T, Schuler AD, Posakony J, Li H, Goehle S, Kollipara R, Depinho RA, Gu Y, Simon JA, Bedalov A: Antitumor activity of a small-molecule inhibitor of human silent information regulator 2 enzymes. Cancer Res; 2006 Apr 15;66(8):4368-77
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  • SIRT1 and other NAD-dependent deacetylases have been implicated in control of cellular responses to stress and in tumorigenesis through deacetylation of important regulatory proteins, including p53 and the BCL6 oncoprotein.
  • Hereby, we describe the identification of a compound we named cambinol that inhibits NAD-dependent deacetylase activity of human SIRT1 and SIRT2.
  • Inhibitors of NAD-dependent deacetylases may constitute novel anticancer agents.

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  • (PMID = 16618762.001).
  • [ISSN] 0008-5472
  • [Journal-full-title] Cancer research
  • [ISO-abbreviation] Cancer Res.
  • [Language] eng
  • [Grant] United States / NCI NIH HHS / CA / CA78746; United States / NIDDK NIH HHS / DK / DK56465; United States / NHLBI NIH HHS / HL / HL04211
  • [Publication-type] Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't
  • [Publication-country] United States
  • [Chemical-registry-number] 0 / Antineoplastic Agents; 0 / BCL6 protein, human; 0 / DNA-Binding Proteins; 0 / Enzyme Inhibitors; 0 / Histone Deacetylase Inhibitors; 0 / Naphthalenes; 0 / Pyrimidinones; 0 / TP53 protein, human; 0 / Tubulin; 0 / Tumor Suppressor Protein p53; 0 / cambinol; EC 3.5.1.- / SIRT1 protein, human; EC 3.5.1.- / SIRT2 protein, human; EC 3.5.1.- / Sirtuin 1; EC 3.5.1.- / Sirtuin 2; EC 3.5.1.- / Sirtuins
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47. Planelles D, Nagore E, Moret A, Botella-Estrada R, Vila E, Guillén C, Montoro JA: HLA class II polymorphisms in Spanish melanoma patients: homozygosity for HLA-DQA1 locus can be a potential melanoma risk factor. Br J Dermatol; 2006 Feb;154(2):261-6
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  • This DQA1 homozygosity-specific association was particularly dependent on some features in melanoma patients such as light hair colour, skin type I or II, early age at diagnosis, absence of atypical naevi, or abscence of atypical naevus syndrome phenotype (aetiological fractions about 10-20%).
  • [MeSH-major] HLA-DQ Antigens / genetics. Melanoma / genetics. Polymorphism, Genetic. Skin Neoplasms / genetics
  • [MeSH-minor] Adult. Gene Frequency. Genes, MHC Class II. Genetic Predisposition to Disease. HLA-DQ alpha-Chains. Hair Color. Homozygote. Humans. Polymerase Chain Reaction / methods. Risk Factors. Skin Pigmentation. Spain

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  • (PMID = 16433795.001).
  • [ISSN] 0007-0963
  • [Journal-full-title] The British journal of dermatology
  • [ISO-abbreviation] Br. J. Dermatol.
  • [Language] eng
  • [Publication-type] Journal Article; Research Support, Non-U.S. Gov't
  • [Publication-country] England
  • [Chemical-registry-number] 0 / HLA-DQ Antigens; 0 / HLA-DQ alpha-Chains; 0 / HLA-DQA1 antigen
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48. Cruzado MC, Risler NR, Miatello RM, Yao G, Schiffrin EL, Touyz RM: Vascular smooth muscle cell NAD(P)H oxidase activity during the development of hypertension: Effect of angiotensin II and role of insulinlike growth factor-1 receptor transactivation. Am J Hypertens; 2005 Jan;18(1):81-7
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  • [Title] Vascular smooth muscle cell NAD(P)H oxidase activity during the development of hypertension: Effect of angiotensin II and role of insulinlike growth factor-1 receptor transactivation.
  • The ROS production and NAD(P)H oxidase activation were determined by fluorescence and chemiluminescence, respectively.
  • Basal NAD(P)H oxidase activity was higher in VSMCs from 9-week-old SHR versus 4-week-old rats (P < .05).
  • Pretreatment of 9- and 16-week-old SHR cells with AG1024 reduced Ang II-mediated NAD(P)H oxidase activation (P < .05).
  • CONCLUSIONS: Basal and Ang II-induced NAD(P)H-driven ROS generation are enhanced in VSMCs from SHR during development of hypertension, but not in cells from prehypertensive rats.

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  • (PMID = 15691621.001).
  • [ISSN] 0895-7061
  • [Journal-full-title] American journal of hypertension
  • [ISO-abbreviation] Am. J. Hypertens.
  • [Language] eng
  • [Publication-type] Comparative Study; Journal Article; Research Support, Non-U.S. Gov't
  • [Publication-country] United States
  • [Chemical-registry-number] 0 / Reactive Oxygen Species; 0 / Vasoconstrictor Agents; 11128-99-7 / Angiotensin II; EC 1.6.3.1 / NADPH Oxidase; EC 2.7.10.1 / Receptor, IGF Type 1; EC 2.7.11.24 / Mitogen-Activated Protein Kinases
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49. Dumas JF, Argaud L, Cottet-Rousselle C, Vial G, Gonzalez C, Detaille D, Leverve X, Fontaine E: Effect of transient and permanent permeability transition pore opening on NAD(P)H localization in intact cells. J Biol Chem; 2009 May 29;284(22):15117-25
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  • [Title] Effect of transient and permanent permeability transition pore opening on NAD(P)H localization in intact cells.
  • To study the effect of mitochondrial permeability transition pore (PTP) opening on NAD(P)H localization, intact cells were exposed to the Ca(2+) ionophore A23187.
  • PTP opening, mitochondrial membrane potential, mitochondrial volume, and NAD(P)H localization were assessed by time-lapse laser confocal microscopy using the calcein-cobalt technique, tetramethylrhodamine methyl ester, MitoTracker, and NAD(P)H autofluorescence, respectively.
  • Concomitant with PTP opening, NAD(P)H fluorescence increased outside mitochondria.
  • NAD(P)H autofluorescence remained elevated after PTP opening, particularly after membrane potential had been collapsed by an uncoupler.
  • Extraction of nucleotide for NAD(P)H quantification confirmed that PTP opening led to an increase in NAD(P)H content.
  • [MeSH-minor] Biological Transport / drug effects. Cell Line. Cell Respiration / drug effects. Cell Separation. Fluorescence. Hepatocytes / drug effects. Hepatocytes / metabolism. Humans. Imaging, Three-Dimensional. Membrane Potential, Mitochondrial / drug effects. Mitochondria / drug effects. Mitochondria / metabolism. NAD / pharmacology. Organelle Size / drug effects. Oxidation-Reduction / drug effects

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  • (PMID = 19346250.001).
  • [ISSN] 0021-9258
  • [Journal-full-title] The Journal of biological chemistry
  • [ISO-abbreviation] J. Biol. Chem.
  • [Language] eng
  • [Publication-type] Journal Article; Research Support, Non-U.S. Gov't
  • [Publication-country] United States
  • [Chemical-registry-number] 0 / Mitochondrial Membrane Transport Proteins; 0 / mitochondrial permeability transition pore; 0U46U6E8UK / NAD; 53-59-8 / NADP
  • [Other-IDs] NLM/ PMC2685693
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50. Liang L, Zhang J, Lin Z: Altering coenzyme specificity of Pichia stipitis xylose reductase by the semi-rational approach CASTing. Microb Cell Fact; 2007;6:36
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  • BACKGROUND: The NAD(P)H-dependent Pichia stipitis xylose reductase (PsXR) is one of the key enzymes for xylose fermentation, and has been cloned into the commonly used ethanol-producing yeast Saccharomyces cerevisiae.
  • RESULTS: Based on a homology model of PsXR, six residues were predicted to interact with the adenine ribose of NAD(P)H in PsXR and altered using a semi-rational mutagenesis approach (CASTing).
  • Three rounds of saturation mutagenesis were carried to randomize these residues, and a microplate-based assay was applied in the screening.
  • CONCLUSION: A seemingly simplistic and yet very effective mutagenesis approach, CASTing, was applied successfully to alter the NAD(P)H preference for Pichia stipitis xylose reductase, an important enzyme for xylose-fermenting yeast.
  • The observed change in the NAD(P)H preference for this enzyme seems to have resulted from the altered active site that is more unfavorable for NADPH than NADH in terms of both Km and kcat.

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  • (PMID = 18028553.001).
  • [ISSN] 1475-2859
  • [Journal-full-title] Microbial cell factories
  • [ISO-abbreviation] Microb. Cell Fact.
  • [Language] eng
  • [Publication-type] Journal Article
  • [Publication-country] England
  • [Other-IDs] NLM/ PMC2213684
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51. Flores H, Ellington AD: A modified consensus approach to mutagenesis inverts the cofactor specificity of Bacillus stearothermophilus lactate dehydrogenase. Protein Eng Des Sel; 2005 Aug;18(8):369-77
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  • Lactate dehydrogenase from Bacillus stearothermophilus is specific for NAD+.
  • There have been several attempts to alter the cofactor specificity of this enzyme, but these have yielded enzymes with relatively low activities that still largely prefer NAD+.
  • Mut31 was also better at utilizing NAD+ than the wild-type enzyme and was weakly active with NADP+ and NMN+.
  • When two previously identified amino acid substitutions were introduced into the Mut31 background, the resultant quintuply substituted enzyme not only utilized NADP+ far better than the wild-type enzyme, it actually inverted its preference for NAD+ and NADP+.
  • [MeSH-minor] Amino Acid Substitution. Consensus Sequence. Directed Molecular Evolution. Fructosediphosphates / metabolism. Gene Library. Kinetics. Models, Molecular. Mutagenesis, Site-Directed. NAD / metabolism. NADP / metabolism. Phylogeny. Substrate Specificity

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  • (PMID = 16012175.001).
  • [ISSN] 1741-0126
  • [Journal-full-title] Protein engineering, design & selection : PEDS
  • [ISO-abbreviation] Protein Eng. Des. Sel.
  • [Language] eng
  • [Publication-type] Journal Article; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, Non-P.H.S.
  • [Publication-country] England
  • [Chemical-registry-number] 0 / Fructosediphosphates; 0U46U6E8UK / NAD; 53-59-8 / NADP; EC 1.1.1.27 / L-Lactate Dehydrogenase
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52. Włoch K: [Role of the physician in recognition of casuses and circumstances of alcohol abuse by patients in general rural dispensaries. Functioning model of health care of alcohol abuse patients and optimal model (Part II)]. Wiad Lek; 2005;58(9-10):508-12
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  • [Transliterated title] Rola lekarza w rozpoznawaniu przyczyn i okoliczności naduzywania alkoholu przez pacjentów poradni ogólnych wiejskich ośrodków zdrowia. Cześć II. Funkcjonujacy i optymalny model opieki nad osobami naduzywajacymi alkoholu.
  • [MeSH-major] Alcoholism / diagnosis. Primary Health Care / organization & administration. Rural Health / statistics & numerical data. Rural Health Services / organization & administration

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  • (PMID = 16529060.001).
  • [ISSN] 0043-5147
  • [Journal-full-title] Wiadomości lekarskie (Warsaw, Poland : 1960)
  • [ISO-abbreviation] Wiad. Lek.
  • [Language] pol
  • [Publication-type] English Abstract; Journal Article
  • [Publication-country] Poland
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53. Cwiek D: [The impact of education in birthing schools on the course of pregnancy, labor, puerperium, and neonatal care]. Ann Acad Med Stetin; 2006;52(1):79-90
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  • [Transliterated title] Ocena wpływu edukacji w szkołach rodzenia na przebieg ciazy, porodu i połogu oraz opieke nad noworodkiem.
  • It is also the time of an intense quest for answers to annoying questions and a motivating factor to search for information on the physiology of pregnancy, as well as on labor, puerperium and child care.


54. Kim HJ, Vaziri ND: Contribution of impaired Nrf2-Keap1 pathway to oxidative stress and inflammation in chronic renal failure. Am J Physiol Renal Physiol; 2010 Mar;298(3):F662-71
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  • In confirmation of earlier studies, rats with chronic renal failure exhibited increased lipid peroxidation, glutathione depletion, NF-kappaB activation, mononuclear cell infiltration, and upregulation of monocyte chemoattractant protein-1, NAD(P)H oxidase, cyclooxygenase-2, and 12-lipoxygenase in the remnant kidney pointing to oxidative stress and inflammation.
  • Despite severe oxidative stress and inflammation, remnant kidney tissue Nrf2 activity (nuclear translocation) was mildly reduced at 6 wk and markedly reduced at 12 wk, whereas the Nrf2 repressor Keap1 was upregulated and the products of Nrf2 target genes [catalase, superoxide dismutase, glutathione peroxidase, heme oxygenase-1, NAD(P)H quinone oxidoreductase, and glutamate-cysteine ligase] were reduced or unchanged at 6 wk and significantly diminished at 12 wk.

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  • (PMID = 20007347.001).
  • [ISSN] 1522-1466
  • [Journal-full-title] American journal of physiology. Renal physiology
  • [ISO-abbreviation] Am. J. Physiol. Renal Physiol.
  • [Language] eng
  • [Publication-type] Journal Article
  • [Publication-country] United States
  • [Chemical-registry-number] 0 / Antioxidants; 0 / Enzymes; 0 / Inflammation Mediators; 0 / Intracellular Signaling Peptides and Proteins; 0 / KEAP1 protein, rat; 0 / NF-E2-Related Factor 2; 0 / Nfe2l2 protein, rat; 0 / Proteins; 0 / Reactive Oxygen Species; GAN16C9B8O / Glutathione
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55. Yao EH, Fukuda N, Matsumoto T, Katakawa M, Yamamoto C, Han Y, Ueno T, Kobayashi N, Matsumoto K: Effects of the antioxidative beta-blocker celiprolol on endothelial progenitor cells in hypertensive rats. Am J Hypertens; 2008 Sep;21(9):1062-8
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  • The expression of nicotinamine adenine dinucleotide phosphate (NAD(P)H) oxidase component mRNAs in the renal cortex, aorta, and heart were evaluated by real-time PCR.
  • Celiprolol inhibited oxidation in EPCs from SHRs, and decreased the expression of NAD(P)H oxidase component mRNAs in the renal cortex, aorta, and heart.

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  • (PMID = 18636069.001).
  • [ISSN] 0895-7061
  • [Journal-full-title] American journal of hypertension
  • [ISO-abbreviation] Am. J. Hypertens.
  • [Language] eng
  • [Publication-type] Journal Article; Research Support, Non-U.S. Gov't
  • [Publication-country] United States
  • [Chemical-registry-number] 0 / Adrenergic beta-Antagonists; 0 / Antioxidants; 0 / RNA, Messenger; DRB57K47QC / Celiprolol; EC 1.6.3.1 / NADPH Oxidase
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56. Lin Y, Alguindigue SS, Volkman J, Nicholas KM, West AH, Cook PF: Complete kinetic mechanism of homoisocitrate dehydrogenase from Saccharomyces cerevisiae. Biochemistry; 2007 Jan 23;46(3):890-8
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  • Curvature is observed in the double-reciprocal plots for product inhibition by NADH and the dead-end inhibition by 3-acetylpyridine adenine dinucleotide phosphate when MgHIc is the varied substrate.
  • At low concentrations of MgHIc, the inhibition by both nucleotides is competitive, but as the MgHIc concentration increases, the inhibition changes to uncompetitive, consistent with a steady state random mechanism with preferred binding of MgHIc before NAD.
  • Isocitrate is a slow substrate with a rate (V/E(t)) 216-fold slower than that measured with HIc.
  • The kinetic mechanism in the direction of oxidative decarboxylation of isocitrate, on the basis of initial velocity studies in the absence and presence of dead-end inhibitors, suggests random addition of NAD and isocitrate with Mg2+ binding before isocitrate in rapid equilibrium, and the mechanism approximates rapid equilibrium random.

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  • (PMID = 17223711.001).
  • [ISSN] 0006-2960
  • [Journal-full-title] Biochemistry
  • [ISO-abbreviation] Biochemistry
  • [Language] ENG
  • [Grant] United States / NIGMS NIH HHS / GM / R01 GM071417; United States / NIGMS NIH HHS / GM / R01 GM071417-04; United States / NIGMS NIH HHS / GM / GM 071417
  • [Publication-type] Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't
  • [Publication-country] United States
  • [Chemical-registry-number] 0 / Isocitrates; 0 / Tricarboxylic Acids; 0 / homoisocitric acid; 320-77-4 / isocitric acid; EC 1.1.- / Alcohol Oxidoreductases; EC 1.1.1.87 / homoisocitrate dehydrogenase; I38ZP9992A / Magnesium
  • [Other-IDs] NLM/ NIHMS61809; NLM/ PMC2527762
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57. Zhang HN, Wang ZQ, Cui GJ, Lin TB: [Difference in seedlings ammonium assimilation of wheat cultivars with different drought resistance under osmotic stress]. Ying Yong Sheng Tai Xue Bao; 2009 Oct;20(10):2406-10
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  • The plant biomass had an obvious decrease under osmotic stress, with a larger decrement for Zhoumai-18 than Luohan-6.
  • The NADH-dependent glutamate dehydrogenase (NADH-GDH) increased with increasing osmotic stress, with a marked increment under low osmotic stress for Zhoumai-18, and under high osmotic stress for Luohan-6.
  • The NAD(+)-dependent glutamate dehydrogenase (NAD(+)-GDH) and NADP-dependent isocitrate dehydrogenase (NADP-ICDH) activities also increased with increasing osmotic stress, with a greater increment of NAD(+)-GDH activity for Zhoumai-18, and of NADP-ICDH activity for Luohan-6.

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  • (PMID = 20077697.001).
  • [ISSN] 1001-9332
  • [Journal-full-title] Ying yong sheng tai xue bao = The journal of applied ecology
  • [ISO-abbreviation] Ying Yong Sheng Tai Xue Bao
  • [Language] CHI
  • [Publication-type] English Abstract; Journal Article; Research Support, Non-U.S. Gov't
  • [Publication-country] China
  • [Chemical-registry-number] 0 / Quaternary Ammonium Compounds
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58. Higashi N, Tanimoto K, Nishioka M, Ishikawa K, Taya M: Investigating a catalytic mechanism of hyperthermophilic L-threonine dehydrogenase from Pyrococcus horikoshii. J Biochem; 2008 Jul;144(1):77-85
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  • It was found that the E152D mutant showed 3-fold higher turnover rate and reduced affinities toward L-threonine and NAD(+), compared to wild-type PhTDH.
  • The results obtained from pH dependency of kinetic parameters suggested that Glu152 to Asp substitution causes the enhancement of deprotonation of His47 or ionization of zinc-bound water and threonine in the enzyme-NAD(+) complex.
  • Furthermore, it was predicted that the access of threonine substrate to the enzyme-NAD(+) complex induces a large conformational change in the active domain of PhTDH.

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  • (PMID = 18390572.001).
  • [ISSN] 0021-924X
  • [Journal-full-title] Journal of biochemistry
  • [ISO-abbreviation] J. Biochem.
  • [Language] eng
  • [Publication-type] Journal Article; Research Support, Non-U.S. Gov't
  • [Publication-country] Japan
  • [Chemical-registry-number] 0 / Archaeal Proteins; EC 1.1.- / Alcohol Oxidoreductases; EC 1.1.1.103 / L-threonine 3-dehydrogenase; J41CSQ7QDS / Zinc
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59. Singh A, Karimpour-Fard A, Gill RT: Increased mutation frequency in redox-impaired Escherichia coli due to RelA- and RpoS-mediated repression of DNA repair. Appl Environ Microbiol; 2010 Aug;76(16):5463-70
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  • We hypothesized that the increased mutation frequency was due to an increased NADH/NAD(+) ratio in this strain.
  • Using several redox-impaired strains of E. coli and different redox conditions, we confirmed a significant correlation (P < 0.01) between intracellular-NADH/NAD(+) ratio and mutation frequency.

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  • (PMID = 20581184.001).
  • [ISSN] 1098-5336
  • [Journal-full-title] Applied and environmental microbiology
  • [ISO-abbreviation] Appl. Environ. Microbiol.
  • [Language] ENG
  • [Databank-accession-numbers] GEO/ GSE21995
  • [Grant] United States / NLM NIH HHS / LM / T15 LM009451; United States / NLM NIH HHS / LM / 5T15LM009451-03
  • [Publication-type] Journal Article; Research Support, N.I.H., Extramural; Research Support, U.S. Gov't, Non-P.H.S.
  • [Publication-country] United States
  • [Chemical-registry-number] 0 / Bacterial Proteins; 0 / Sigma Factor; 0 / sigma factor KatF protein, Bacteria; 0U46U6E8UK / NAD; EC 1.1.1.27 / L-Lactate Dehydrogenase; EC 2.3.1.- / Acetyltransferases; EC 2.3.1.54 / formate C-acetyltransferase; EC 6.- / Ligases; EC 6.- / guanosine 3',5'-polyphosphate synthetases
  • [Other-IDs] NLM/ PMC2918982
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60. Talbiersky P, Bastkowski F, Klärner FG, Schrader T: Molecular clip and tweezer introduce new mechanisms of enzyme inhibition. J Am Chem Soc; 2008 Jul 30;130(30):9824-8
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  • IC50 values and kinetic investigations point to two different new mechanisms of interference with the NAD(+)-dependent oxidoreductase: While the clip seems to pull the cofactor out of its cleft, the tweezer docks onto lysine residues around the active site.
  • However, while cofactor depletion by clip 1 was in part restored by subsequent NAD(+) addition, the tweezer (2) inhibition requires the competitive action of lysine derivatives.
  • [MeSH-minor] Circular Dichroism. Kinetics. Lysine / chemistry. Molecular Conformation. NAD / chemistry. NAD / metabolism

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  • (PMID = 18605724.001).
  • [ISSN] 1520-5126
  • [Journal-full-title] Journal of the American Chemical Society
  • [ISO-abbreviation] J. Am. Chem. Soc.
  • [Language] eng
  • [Publication-type] Journal Article; Research Support, Non-U.S. Gov't
  • [Publication-country] United States
  • [Chemical-registry-number] 0 / Enzyme Inhibitors; 0 / Organophosphates; 0 / Polycyclic Hydrocarbons, Aromatic; 0U46U6E8UK / NAD; EC 1.1.1.1 / Alcohol Dehydrogenase; K3Z4F929H6 / Lysine
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61. Watanabe S, Abu Saleh A, Pack SP, Annaluru N, Kodaki T, Makino K: Ethanol production from xylose by recombinant Saccharomyces cerevisiae expressing protein-engineered NADH-preferring xylose reductase from Pichia stipitis. Microbiology; 2007 Sep;153(Pt 9):3044-54
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  • A recombinant Saccharomyces cerevisiae strain transformed with xylose reductase (XR) and xylitol dehydrogenase (XDH) genes from Pichia stipitis (PsXR and PsXDH, respectively) has the ability to convert xylose to ethanol together with the unfavourable excretion of xylitol, which may be due to intercellular redox imbalance caused by the different coenzyme specificity between NADPH-preferring XR and NAD(+)-dependent XDH.
  • Measurement of intracellular coenzyme concentrations suggested that maintenance of the of NADPH/NADP(+) and NADH/NAD(+) ratios is important for efficient ethanol fermentation from xylose by recombinant S. cerevisiae.
  • [MeSH-minor] Fermentation. Industrial Microbiology / methods. NAD / metabolism. Protein Engineering. Transformation, Genetic

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  • (PMID = 17768247.001).
  • [ISSN] 1350-0872
  • [Journal-full-title] Microbiology (Reading, England)
  • [ISO-abbreviation] Microbiology (Reading, Engl.)
  • [Language] eng
  • [Publication-type] Evaluation Studies; Journal Article; Research Support, Non-U.S. Gov't
  • [Publication-country] England
  • [Chemical-registry-number] 0U46U6E8UK / NAD; 3K9958V90M / Ethanol; A1TA934AKO / Xylose; EC 1.1.1.21 / Aldehyde Reductase
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62. Chatterjee S, Mallick S, Dutta TK: Pathways in the degradation of hydrolyzed alcohols of butyl benzyl phthalate in metabolically diverse Gordonia sp. strain MTCC 4818. J Mol Microbiol Biotechnol; 2005;9(2):110-20
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  • Numbers of dehydrogenases, both NAD+-dependent and NAD+-independent, were found to be involved in the degradation of benzyl alcohol and 1-butanol, where several dehydrogenases exhibited relaxed substrate specificity.

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  • [Copyright] Copyright 2005 S. Karger AG, Basel
  • (PMID = 16319500.001).
  • [ISSN] 1464-1801
  • [Journal-full-title] Journal of molecular microbiology and biotechnology
  • [ISO-abbreviation] J. Mol. Microbiol. Biotechnol.
  • [Language] eng
  • [Publication-type] Journal Article; Research Support, Non-U.S. Gov't
  • [Publication-country] Switzerland
  • [Chemical-registry-number] 0 / Phthalic Acids; YPC4PJX59M / butylbenzyl phthalate
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63. Munné-Bosch S, Shikanai T, Asada K: Enhanced ferredoxin-dependent cyclic electron flow around photosystem I and alpha-tocopherol quinone accumulation in water-stressed ndhB-inactivated tobacco mutants. Planta; 2005 Oct;222(3):502-11
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  • Xanthi) mutants, which are impaired in NAD(P)H dehydrogenase-dependent cyclic electron flow around PSI.
  • Thus, a deficiency in NAD(P)H dehydrogenase-dependent cyclic electron flow around PSI does not lead to oxidative damage because the mutant compensates for this deficiency by activating alternative dissipating routes of excess photon energy, such as up-regulation of ferredoxin-dependent cyclic electron flow around PSI and increased accumulation of alpha-tocopherol quinone.

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  • [Publication-type] Journal Article; Research Support, Non-U.S. Gov't
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64. Matic S, Geisler DA, Møller IM, Widell S, Rasmusson AG: Alamethicin permeabilizes the plasma membrane and mitochondria but not the tonoplast in tobacco (Nicotiana tabacum L. cv Bright Yellow) suspension cells. Biochem J; 2005 Aug 1;389(Pt 3):695-704
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  • ) Bright Yellow-2 cells were treated with AlaM, the cells became permeable for low-molecular-mass molecules as shown by induced leakage of NAD(P)+.
  • Inhibitor-sensitive oxidation of the respiratory substrates succinate, malate and NADH was observed after the addition of the appropriate coenzymes (ATP, NAD+).

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  • [ISSN] 1470-8728
  • [Journal-full-title] The Biochemical journal
  • [ISO-abbreviation] Biochem. J.
  • [Language] eng
  • [Publication-type] Journal Article; Research Support, Non-U.S. Gov't
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65. Kucińska M, Murias M: [Sirtuins--way to longevity or just a fad?]. Pol Merkur Lekarski; 2010 Feb;28(164):158-61
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  • Sir2 proteins known as sirtuins belong to the family of NAD(+)-dependent deacetylases.

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  • (PMID = 20369747.001).
  • [ISSN] 1426-9686
  • [Journal-full-title] Polski merkuriusz lekarski : organ Polskiego Towarzystwa Lekarskiego
  • [ISO-abbreviation] Pol. Merkur. Lekarski
  • [Language] pol
  • [Publication-type] English Abstract; Journal Article; Review
  • [Publication-country] Poland
  • [Chemical-registry-number] EC 3.5.1.- / SIRT2 protein, human; EC 3.5.1.- / Sirtuin 2; EC 3.5.1.- / Sirtuins
  • [Number-of-references] 23
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66. Patterson RL, van Rossum DB, Kaplin AI, Barrow RK, Snyder SH: Inositol 1,4,5-trisphosphate receptor/GAPDH complex augments Ca2+ release via locally derived NADH. Proc Natl Acad Sci U S A; 2005 Feb 1;102(5):1357-9
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  • Addition of native GAPDH and NAD+ to WT IP3R stimulates calcium release, whereas no stimulation occurs with C992S/995S IP3R that cannot bind GAPDH.

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  • [ISSN] 0027-8424
  • [Journal-full-title] Proceedings of the National Academy of Sciences of the United States of America
  • [ISO-abbreviation] Proc. Natl. Acad. Sci. U.S.A.
  • [Language] ENG
  • [Grant] United States / NIMH NIH HHS / MH / MH68830; United States / NIMH NIH HHS / MH / R37 MH018501; United States / NIMH NIH HHS / MH / R01 MH018501; United States / NIMH NIH HHS / MH / P50 MH068830; United States / NIMH NIH HHS / MH / MH-18501; United States / NIH HHS / NH / NH65090
  • [Publication-type] Journal Article; Research Support, U.S. Gov't, P.H.S.
  • [Publication-country] United States
  • [Chemical-registry-number] 0 / Calcium Channels; 0 / ITPR1 protein, human; 0 / Inositol 1,4,5-Trisphosphate Receptors; 0 / Peptide Fragments; 0 / Receptors, Cytoplasmic and Nuclear; 0 / Recombinant Proteins; 0U46U6E8UK / NAD; EC 1.2.1.12 / Glyceraldehyde-3-Phosphate Dehydrogenase (Phosphorylating); SY7Q814VUP / Calcium
  • [Other-IDs] NLM/ PMC547892
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67. Inoue T, Hiratsuka M, Osaki M, Oshimura M: The molecular biology of mammalian SIRT proteins: SIRT2 in cell cycle regulation. Cell Cycle; 2007 May 2;6(9):1011-8
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  • Sir2, an NAD+-dependent protein deacetylase, extends the lifespan in diverse species from yeast to flies.

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  • (PMID = 17457050.001).
  • [ISSN] 1551-4005
  • [Journal-full-title] Cell cycle (Georgetown, Tex.)
  • [ISO-abbreviation] Cell Cycle
  • [Language] eng
  • [Publication-type] Journal Article; Research Support, Non-U.S. Gov't; Review
  • [Publication-country] United States
  • [Chemical-registry-number] 0 / Histones; 0 / Silent Information Regulator Proteins, Saccharomyces cerevisiae; 0 / Tubulin; EC 3.5.1.- / SIR2 protein, S cerevisiae; EC 3.5.1.- / Sirtuin 2; EC 3.5.1.- / Sirtuins; EC 3.5.1.98 / Histone Deacetylases
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68. Yang Z, Kahn BB, Shi H, Xue BZ: Macrophage alpha1 AMP-activated protein kinase (alpha1AMPK) antagonizes fatty acid-induced inflammation through SIRT1. J Biol Chem; 2010 Jun 18;285(25):19051-9
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  • Activating AMPK signaling in macrophages by 5-aminoimidazole-4-carboxamide-1-beta4-ribofuranoside or constitutively active alpha1AMPK (CA-alpha1) significantly inhibits; although inhibiting alpha1AMPK by short hairpin RNA knock-down or dominant-negative alpha1AMPK (DN-alpha1) increases LPS- and FFA-induced tumor necrosis factor alpha expression.
  • Activation of AMPK by CA-alpha1 increases the SIRT1 activator NAD(+) content and SIRT1 expression in macrophages.

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  • (PMID = 20421294.001).
  • [ISSN] 1083-351X
  • [Journal-full-title] The Journal of biological chemistry
  • [ISO-abbreviation] J. Biol. Chem.
  • [Language] ENG
  • [Grant] United States / NIDDK NIH HHS / DK / R01 DK084172; United States / NIDDK NIH HHS / DK / R37 DK043051; United States / NIDDK NIH HHS / DK / P01DK56116; United States / NIDDK NIH HHS / DK / P01 DK056116; United States / NIDDK NIH HHS / DK / R01DK084172
  • [Publication-type] Journal Article; Research Support, N.I.H., Extramural
  • [Publication-country] United States
  • [Chemical-registry-number] 0 / Fatty Acids; 0 / NF-kappa B; EC 2.7.11.1 / AMP-Activated Protein Kinases; EC 2.7.11.1 / AMPK alpha1 subunit, mouse; EC 2.7.11.1 / PRKAA1 protein, human; EC 3.5.1.- / SIRT1 protein, human; EC 3.5.1.- / Sirt1 protein, mouse; EC 3.5.1.- / Sirtuin 1; IY9XDZ35W2 / Glucose
  • [Other-IDs] NLM/ PMC2885183
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69. Li J, Ding T, Zheng LL, Li L, Song LR: [Physiological character and the ratio of the sinking Microcystis in Lake Dianchi]. Huan Jing Ke Xue; 2010 Mar;31(3):667-72
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  • 05), but did significantly on the electron transfer rate and nicotinamide adenine dinucleotide (phosphate), reduced disodium salt [ NAD (P) H] dependent oxidoreductase and dehydrogenase activities (p < 0.01).
  • During the time from October 2007 to May 2008, the sinking ratio reached climax about 40% in winter, and a negative correlation between the sinking ratio and chlorophyll a concentration was observed (p < 0.05).

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  • (PMID = 20358824.001).
  • [ISSN] 0250-3301
  • [Journal-full-title] Huan jing ke xue= Huanjing kexue
  • [ISO-abbreviation] Huan Jing Ke Xue
  • [Language] CHI
  • [Publication-type] English Abstract; Journal Article; Research Support, Non-U.S. Gov't
  • [Publication-country] China
  • [Chemical-registry-number] 0 / Water Pollutants, Chemical; 1406-65-1 / Chlorophyll; YF5Q9EJC8Y / chlorophyll a
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70. Singh U, Jialal I: Oxidative stress and atherosclerosis. Pathophysiology; 2006 Aug;13(3):129-42
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  • A main source of ROS in vascular cells is the reduced nicotinamide adenine dinucleotide/nicotinamide adenine dinucleotide phosphate (NAD(P)H) oxidase system.

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  • (PMID = 16757157.001).
  • [ISSN] 0928-4680
  • [Journal-full-title] Pathophysiology : the official journal of the International Society for Pathophysiology
  • [ISO-abbreviation] Pathophysiology
  • [Language] ENG
  • [Publication-type] Journal Article
  • [Publication-country] Netherlands
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71. Buchwald UK, Lees A, Steinitz M, Pirofski LA: A peptide mimotope of type 8 pneumococcal capsular polysaccharide induces a protective immune response in mice. Infect Immun; 2005 Jan;73(1):325-33
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  • Increasing antibiotic resistance and a rising patient population at risk for infection due to impaired immunity underscore the importance of vaccination against pneumococci.
  • We used a human monoclonal immunoglobulin A (IgA) antibody (NAD) to type 8 Streptococcus pneumoniae capsular polysaccharide (type 8 PS) to screen a phage display library, and the phage PUB1 displaying the peptide FHLPYNHNWFAL was selected after three rounds of biopanning.

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  • (PMID = 15618169.001).
  • [ISSN] 0019-9567
  • [Journal-full-title] Infection and immunity
  • [ISO-abbreviation] Infect. Immun.
  • [Language] ENG
  • [Grant] United States / NIAID NIH HHS / AI / R01 AI035370; United States / NIAID NIH HHS / AI / R01 AI 35370; United States / NIAID NIH HHS / AI / R01 AI 44374; United States / NIAID NIH HHS / AI / R01 AI 45459
  • [Publication-type] Journal Article; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, P.H.S.
  • [Publication-country] United States
  • [Chemical-registry-number] 0 / Antibodies, Bacterial; 0 / CPG-oligonucleotide; 0 / Oligodeoxyribonucleotides; 0 / Pneumococcal Vaccines; 0 / Polysaccharides, Bacterial; 0 / Tetanus Toxoid; 0 / Vaccines, Conjugate; 0 / pneumococcal polysaccharide, type 8; 0U46U6E8UK / NAD
  • [Other-IDs] NLM/ PMC538987
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72. Belmonte Serrano MÁ: [Is the DAS28 Score the Most Adequate Method to Estimate Activity in Rheumatoid Arthritis? Clinimetric Considerations and Simulations Scenarios]. Reumatol Clin; 2008 Sep;4(5):183-90
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  • [Transliterated title] ¿Es la puntuación DAS28 el método más adecuado para estimar la actividad de la artritis reumatoide? Consideracionens clinimétricas y escenarios de simulación.
  • RESULTS: Tender joint count (NAD) and erithrosedimentation rate (ESR) have a weight of 35- 40% each on the total DAS28 score, while swollen join count (SJC) and global health assessed by the patient (GH) only contribute with 15% each.

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  • [Copyright] Copyright © 2008 Elsevier España S.L Barcelona. Published by Elsevier Espana. All rights reserved.
  • (PMID = 21794528.001).
  • [ISSN] 1699-258X
  • [Journal-full-title] Reumatología clinica
  • [ISO-abbreviation] Reumatol Clin
  • [Language] spa
  • [Publication-type] English Abstract; Journal Article
  • [Publication-country] Spain
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73. Jasso-Chávez R, Pacheco-Rosales A, Lira-Silva E, Gallardo-Pérez JC, García N, Moreno-Sánchez R: Toxic effects of Cr(VI) and Cr(III) on energy metabolism of heterotrophic Euglena gracilis. Aquat Toxicol; 2010 Nov 15;100(4):329-38
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  • The cell growth IC₅₀ value was 12 and >250μM for Cr(VI) and Cr(III), respectively; in these cells chromium was accumulated and a fraction compartmentalized into mitochondria, and synthesis of cysteine and glutathione was induced.
  • In turn, cellular and mitochondrial respiration, respiratory Complexes I, III and IV, glycolysis and cytosolic NAD(+)-alcohol and -lactate dehydrogenases from cells cultured with Cr(VI) were significantly lower than control, whereas AOX and external NADH dehydrogenase activities were unaltered or increased, respectively.

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  • [Copyright] Copyright © 2010 Elsevier B.V. All rights reserved.
  • (PMID = 20851473.001).
  • [ISSN] 1879-1514
  • [Journal-full-title] Aquatic toxicology (Amsterdam, Netherlands)
  • [ISO-abbreviation] Aquat. Toxicol.
  • [Language] eng
  • [Publication-type] Journal Article; Research Support, Non-U.S. Gov't
  • [Publication-country] Netherlands
  • [Chemical-registry-number] 0 / Environmental Pollutants; 0 / Glucans; 0R0008Q3JB / Chromium; 18540-29-9 / chromium hexavalent ion; 4Y8F71G49Q / Malondialdehyde; 51052-65-4 / paramylon; 7440-44-0 / Carbon
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74. Martin FL, Patel II, Sozeri O, Singh PB, Ragavan N, Nicholson CM, Frei E, Meinl W, Glatt H, Phillips DH, Arlt VM: Constitutive expression of bioactivating enzymes in normal human prostate suggests a capability to activate pro-carcinogens to DNA-damaging metabolites. Prostate; 2010 Oct 01;70(14):1586-99
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  • An analysis of gene and protein expression of candidate metabolizing enzymes, including cytochrome P450 (CYP)1A1, CYP1A2, CYP1B1, N-acetyltransferase 1 (NAT1), sulfotransferase (SULT)1A1, SULT1A3, NAD(P)H:quinone oxidoreductase (NQO1), prostaglandin H synthase 1 (cyclooxygenase 1; COX1), and CYP oxidoreductase (POR) was carried out.

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  • [Copyright] (c) 2010 Wiley-Liss, Inc.
  • (PMID = 20687231.001).
  • [ISSN] 1097-0045
  • [Journal-full-title] The Prostate
  • [ISO-abbreviation] Prostate
  • [Language] eng
  • [Grant] United Kingdom / Medical Research Council / / G0802851; United Kingdom / Cancer Research UK / /
  • [Publication-type] Journal Article; Research Support, Non-U.S. Gov't
  • [Publication-country] United States
  • [Chemical-registry-number] 0 / Carcinogens; 0 / DNA Adducts; 0 / Sex Hormone-Binding Globulin; 3XMK78S47O / Testosterone; 4TI98Z838E / Estradiol; EC 1.14.14.1 / Aryl Hydrocarbon Hydroxylases; EC 1.14.14.1 / CYP1B1 protein, human; EC 1.14.14.1 / Cytochrome P-450 CYP1A1; EC 1.14.14.1 / Cytochrome P-450 CYP1A2; EC 1.14.14.1 / Cytochrome P-450 CYP1B1; EC 2.3.1.1 / Amino-Acid N-Acetyltransferase
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75. Stiborová M, Martínek V, Svobodová M, Sístková J, Dvorák Z, Ulrichová J, Simánek V, Frei E, Schmeiser HH, Phillips DH, Arlt VM: Mechanisms of the different DNA adduct forming potentials of the urban air pollutants 2-nitrobenzanthrone and carcinogenic 3-nitrobenzanthrone. Chem Res Toxicol; 2010 Jul 19;23(7):1192-201
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  • We compared the efficiencies of human enzymatic systems [hepatic microsomes and cytosols, NAD(P)H:quinone oxidoreductase 1 (NQO1), xanthine oxidase, NADPH:cytochrome P450 reductase, N,O-acetyltransferases, and sulfotransferases] and human primary hepatocytes to activate 2-NBA and its isomer 3-NBA to species forming DNA adducts.
  • [MeSH-minor] Binding Sites. Catalytic Domain. Cells, Cultured. Computer Simulation. Hepatocytes / metabolism. Humans. Isomerism. Liver / enzymology. NAD(P)H Dehydrogenase (Quinone) / chemistry

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  • (PMID = 20545351.001).
  • [ISSN] 1520-5010
  • [Journal-full-title] Chemical research in toxicology
  • [ISO-abbreviation] Chem. Res. Toxicol.
  • [Language] eng
  • [Publication-type] Journal Article; Research Support, Non-U.S. Gov't
  • [Publication-country] United States
  • [Chemical-registry-number] 0 / 3-nitrobenzanthrone; 0 / Air Pollutants; 0 / Benz(a)Anthracenes; 0 / Carcinogens; 0 / DNA Adducts; EC 1.6.5.2 / NAD(P)H Dehydrogenase (Quinone); EC 1.6.5.2 / NQO1 protein, human
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76. Beiser DG, Wang H, Li J, Wang X, Yordanova V, Das A, Mirzapoiazova T, Garcia JG, Stern SA, Vanden Hoek TL: Plasma and myocardial visfatin expression changes are associated with therapeutic hypothermia protection during murine hemorrhagic shock/resuscitation. Resuscitation; 2010 Jun;81(6):742-8
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  • Visfatin is a recently described protein that functions both as a proinflammatory plasma cytokine and an intracellular enzyme within the nicotinamide adenine dinucleotide (NAD(+)) salvage pathway.
  • METHODS: Mice were bled and maintained at a mean arterial pressure (MAP) of 35 mmHg.

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  • [Copyright] Copyright 2010 Elsevier Ireland Ltd. All rights reserved.
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  • (PMID = 20347206.001).
  • [ISSN] 1873-1570
  • [Journal-full-title] Resuscitation
  • [ISO-abbreviation] Resuscitation
  • [Language] ENG
  • [Grant] United States / NHLBI NIH HHS / HL / HL091184-01A1; United States / NHLBI NIH HHS / HL / HL091184-02; United States / NHLBI NIH HHS / HL / K08 HL091184; United States / NHLBI NIH HHS / HL / K08 HL091184-02; United States / NHLBI NIH HHS / HL / K08HL091184; United States / NHLBI NIH HHS / HL / K08 HL091184-01A1; United States / NHLBI NIH HHS / HL / K08 HL091184-03; United States / NHLBI NIH HHS / HL / HL091184-03
  • [Publication-type] Comparative Study; Journal Article; Research Support, N.I.H., Extramural; Research Support, U.S. Gov't, Non-P.H.S.
  • [Publication-country] Ireland
  • [Chemical-registry-number] 0 / Chemokines; 0 / Interleukin-6; 0 / Myoglobin; 0 / Tumor Necrosis Factor-alpha; 147037-79-4 / keratinocyte-derived chemokines; EC 2.4.2.12 / Nicotinamide Phosphoribosyltransferase
  • [Other-IDs] NLM/ NIHMS193386; NLM/ PMC2963096
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77. Sharma M, Zhou Z, Miura H, Papapetropoulos A, McCarthy ET, Sharma R, Savin VJ, Lianos EA: ADMA injures the glomerular filtration barrier: role of nitric oxide and superoxide. Am J Physiol Renal Physiol; 2009 Jun;296(6):F1386-95
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  • A similar increase in P(alb) was caused by l-NMMA but at a concentration two orders of magnitude higher than that of ADMA.
  • The SOD mimetic tempol or the NAD(P)H oxidase inhibitor apocynin also prevented the ADMA-induced increase in P(alb).

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  • (PMID = 19297451.001).
  • [ISSN] 1931-857X
  • [Journal-full-title] American journal of physiology. Renal physiology
  • [ISO-abbreviation] Am. J. Physiol. Renal Physiol.
  • [Language] ENG
  • [Grant] United States / NHLBI NIH HHS / HL / R01 HL080173-02; United States / NHLBI NIH HHS / HL / R01 HL080173-01A2; United States / NHLBI NIH HHS / HL / R01-HL-080173; United States / NHLBI NIH HHS / HL / HL080173-02; United States / NHLBI NIH HHS / HL / R01 HL080173; United States / PHS HHS / / R01-061588; United States / NHLBI NIH HHS / HL / HL080173-01A2
  • [Publication-type] Journal Article; Research Support, N.I.H., Extramural
  • [Publication-country] United States
  • [Chemical-registry-number] 0 / Albumins; 0 / Anthracenes; 0 / Free Radical Scavengers; 0 / Receptors, Cytoplasmic and Nuclear; 11062-77-4 / Superoxides; 27JT06E6GR / omega-N-Methylarginine; 30315-93-6 / N,N-dimethylarginine; 31C4KY9ESH / Nitric Oxide; 94ZLA3W45F / Arginine; EC 1.14.13.39 / Nitric Oxide Synthase; EC 1.6.3.1 / NADPH Oxidase; EC 4.6.1.2 / Guanylate Cyclase; EC 4.6.1.2 / soluble guanylyl cyclase; T75W9911L6 / Propane
  • [Other-IDs] NLM/ PMC2692444
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78. Lloyd D: Respiratory oscillations in yeasts. Adv Exp Med Biol; 2008;641:118-40
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  • Most detailed understanding comes from the latter system, where continuous, noninvasive real-time monitoring (of 02 uptake, CO2 production, and NAD(P)H redox state) is combined with frequent discrete time samples (for other redox components, including H2S, GSH and cytochromes, metabolites, and mRNA levels).
  • A redox switch lies at the heart of this ultradian clock and a plethora of outputs is optimized to a time-base that is genetically-determined and differs in different organisms.

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  • (PMID = 18783176.001).
  • [ISSN] 0065-2598
  • [Journal-full-title] Advances in experimental medicine and biology
  • [ISO-abbreviation] Adv. Exp. Med. Biol.
  • [Language] eng
  • [Publication-type] Journal Article; Review
  • [Publication-country] United States
  • [Chemical-registry-number] 0 / Reactive Oxygen Species
  • [Number-of-references] 130
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79. Fermani S, Sparla F, Falini G, Martelli PL, Casadio R, Pupillo P, Ripamonti A, Trost P: Molecular mechanism of thioredoxin regulation in photosynthetic A2B2-glyceraldehyde-3-phosphate dehydrogenase. Proc Natl Acad Sci U S A; 2007 Jun 26;104(26):11109-14
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  • Chloroplast glyceraldehyde-3-phosphate dehydrogenase (GAPDH) is a light-regulated, NAD(P)H-dependent enzyme involved in plant photosynthetic carbon reduction.
  • Unlike lower photosynthetic organisms, which only contain A(4)-GAPDH, the major GAPDH isoform of land plants is made up of A and B subunits, the latter containing a C-terminal extension (CTE) with fundamental regulatory functions.
  • The tridimensional structure of A(2)B(2)-GAPDH from spinach chloroplasts, crystallized in the oxidized state, shows that each disulfide-containing CTE is docked into a deep cleft between a pair of A and B subunits.

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  • (PMID = 17573533.001).
  • [ISSN] 1091-6490
  • [Journal-full-title] Proceedings of the National Academy of Sciences of the United States of America
  • [ISO-abbreviation] Proc. Natl. Acad. Sci. U.S.A.
  • [Language] eng
  • [Databank-accession-numbers] PDB/ 2PKQ/ 2PKR
  • [Publication-type] Journal Article; Research Support, Non-U.S. Gov't
  • [Publication-country] United States
  • [Chemical-registry-number] 0 / Protein Subunits; 52500-60-4 / Thioredoxins; EC 1.2.1.13 / Glyceraldehyde-3-Phosphate Dehydrogenase (NADP+)(Phosphorylating)
  • [Other-IDs] NLM/ PMC1904167
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80. Yan LJ, Yang SH, Shu H, Prokai L, Forster MJ: Histochemical staining and quantification of dihydrolipoamide dehydrogenase diaphorase activity using blue native PAGE. Electrophoresis; 2007 Apr;28(7):1036-45
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  • Mammalian mitochondrial dihydrolipoamide dehydrogenase (DLDH, EC 1.8.1.4) catalyzes NAD(+)-dependent oxidation of dihydrolipoamide in vivo and can also act as a diaphorase catalyzing in vitro nicotinamide adenine dinucleotide (reduced form) (NADH)-dependent reduction of electron-accepting molecules such as ubiquinone and nitroblue tetrazolium (NBT).
  • [MeSH-minor] Animals. Chromatography, Liquid. Electrophoresis, Polyacrylamide Gel. Enzyme Activation. Ethylmaleimide / metabolism. NAD / metabolism. Nitroblue Tetrazolium / chemistry. Oxidation-Reduction. Rats. Rats, Sprague-Dawley. Spectrometry, Mass, Electrospray Ionization. Staining and Labeling. Tandem Mass Spectrometry. Thioctic Acid / analogs & derivatives. Thioctic Acid / metabolism

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  • (PMID = 17315258.001).
  • [ISSN] 0173-0835
  • [Journal-full-title] Electrophoresis
  • [ISO-abbreviation] Electrophoresis
  • [Language] eng
  • [Grant] United States / NIA NIH HHS / AG / AG022550; United States / NIA NIH HHS / AG / AG025384
  • [Publication-type] Journal Article; Research Support, N.I.H., Extramural
  • [Publication-country] Germany
  • [Chemical-registry-number] 0 / Mitochondrial Proteins; 0U46U6E8UK / NAD; 298-83-9 / Nitroblue Tetrazolium; 3884-47-7 / dihydrolipoamide; 73Y7P0K73Y / Thioctic Acid; EC 1.8.1.4 / Dihydrolipoamide Dehydrogenase; O3C74ACM9V / Ethylmaleimide
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81. Boerboom AM, Vermeulen M, van der Woude H, Bremer BI, Lee-Hilz YY, Kampman E, van Bladeren PJ, Rietjens IM, Aarts JM: Newly constructed stable reporter cell lines for mechanistic studies on electrophile-responsive element-mediated gene expression reveal a role for flavonoid planarity. Biochem Pharmacol; 2006 Jul 14;72(2):217-26
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  • Two stably transfected luciferase reporter cell lines were developed, EpRE(hNQO1)-LUX and EpRE(mGST-Ya)-LUX, based on EpRE sequences from the human NAD(P)H:quinone oxidoreductase (hNQO1) and the mouse glutathione-S-transferase Ya (mGST-Ya) gene, containing one and two tandem EpRE core sequences, respectively.
  • Five different flavonoids with a planar molecular structure were found to induce various levels of luciferase activity, whereas taxifolin, a non-planar flavonoid, did not induce luciferase activity.

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  • (PMID = 16756964.001).
  • [ISSN] 0006-2952
  • [Journal-full-title] Biochemical pharmacology
  • [ISO-abbreviation] Biochem. Pharmacol.
  • [Language] eng
  • [Publication-type] Journal Article; Research Support, Non-U.S. Gov't
  • [Publication-country] England
  • [Chemical-registry-number] 0 / DNA Primers; 0 / Flavonoids; EC 1.13.12.- / Luciferases
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82. Pech V, Sikka SC, Sindhu RK, Vaziri ND, Majid DS: Oxidant stress and blood pressure responses to angiotensin II administration in rats fed varying salt diets. Am J Hypertens; 2006 May;19(5):534-40
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  • To examine the hypothesis that NAD(P)H oxidase (Nox)-derived superoxide generation is involved in the development of angiotensin II (ANG II)-induced hypertension, we evaluated the responses to ANG II infusion (65 ng/min; osmotic mini-pump) for 2 weeks in rats treated with or without apocynin (APO) (inhibitor of Nox subunits assembly) in drinking water (12 mmol/L).
  • [MeSH-major] Angiotensin II / administration & dosage. Blood Pressure / drug effects. Diet, Sodium-Restricted. Oxidative Stress / drug effects. Vasoconstrictor Agents / administration & dosage

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  • (PMID = 16647629.001).
  • [ISSN] 0895-7061
  • [Journal-full-title] American journal of hypertension
  • [ISO-abbreviation] Am. J. Hypertens.
  • [Language] eng
  • [Grant] United States / NHLBI NIH HHS / HL / HL-66432
  • [Publication-type] Comparative Study; Journal Article; Research Support, N.I.H., Extramural
  • [Publication-country] United States
  • [Chemical-registry-number] 0 / Acetophenones; 0 / Enzyme Inhibitors; 0 / Thiobarbituric Acid Reactive Substances; 0 / Vasoconstrictor Agents; 11128-99-7 / Angiotensin II; 27415-26-5 / 8-epi-prostaglandin F2alpha; B6J7B9UDTR / acetovanillone; B7IN85G1HY / Dinoprost
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83. Da Ros R, Assaloni R, Ceriello A: Molecular targets of diabetic vascular complications and potential new drugs. Curr Drug Targets; 2005 Jun;6(4):503-9
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  • This process, depleting NAD+, slowing glycolsis, ATP formation and electron transport, results in acute endothelial dysfunction in diabetic blood vessels and contributes to the development of diabetic complications.

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  • (PMID = 16026269.001).
  • [ISSN] 1389-4501
  • [Journal-full-title] Current drug targets
  • [ISO-abbreviation] Curr Drug Targets
  • [Language] eng
  • [Publication-type] Journal Article; Review
  • [Publication-country] Netherlands
  • [Chemical-registry-number] 0 / Angiotensin II Type 1 Receptor Blockers; 0 / Angiotensin-Converting Enzyme Inhibitors; 0 / Antioxidants; 0 / Hydroxymethylglutaryl-CoA Reductase Inhibitors
  • [Number-of-references] 125
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84. Li ZJ, Cai L, Wu Q, Chen GQ: Overexpression of NAD kinase in recombinant Escherichia coli harboring the phbCAB operon improves poly(3-hydroxybutyrate) production. Appl Microbiol Biotechnol; 2009 Jul;83(5):939-47
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  • [Title] Overexpression of NAD kinase in recombinant Escherichia coli harboring the phbCAB operon improves poly(3-hydroxybutyrate) production.
  • NAD kinase was overexpressed to enhance the accumulation of poly(3-hydroxybutyrate) (PHB) in recombinant Escherichia coli harboring PHB synthesis pathway via an accelerated supply of NADPH, which is one of the most crucial factors influencing PHB production.
  • A high copy number expression plasmid pE76 led to a stronger NAD kinase activity than that brought about by the low copy number plasmid pELRY.
  • Overexpressing NAD kinase in recombinant E. coli was found not to have a negative effect on cell growth in the absence of PHB synthesis.
  • Shake flask experiments demonstrated that excess NAD kinase in E. coli harboring the PHB synthesis operon could increase the accumulation of PHB to 16-35 wt.
  • Although the two NAD kinase overexpression recombinants exhibited large disparity on NAD kinase activity, their influence on cell growth and PHB accumulation was not proportional.
  • Under the same growth conditions without process optimization, the NAD kinase-overexpressing recombinant produced 14 g/L PHB compared with 7 g/L produced by the control in a 28-h fermentor study.
  • In addition, substrate to PHB yield Y (PHB/glucose) showed an increase from 0.08 g PHB/g glucose for the control to 0.15 g PHB/g glucose for the NAD kinase-overexpressing strain, a 76% increase for the Y (PHB/glucose).
  • These results clearly showed that the overexpression of NAD kinase could be used to enhance the PHB synthesis.

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  • (PMID = 19357844.001).
  • [ISSN] 1432-0614
  • [Journal-full-title] Applied microbiology and biotechnology
  • [ISO-abbreviation] Appl. Microbiol. Biotechnol.
  • [Language] eng
  • [Publication-type] Journal Article; Research Support, Non-U.S. Gov't
  • [Publication-country] Germany
  • [Chemical-registry-number] 0 / Bacterial Proteins; 0 / Escherichia coli Proteins; 0 / Hydroxybutyrates; 0 / Polyesters; 26063-00-3 / poly-beta-hydroxybutyrate; 53-59-8 / NADP; EC 2.7.- / Phosphotransferases; EC 2.7.1.- / NadK protein, E coli
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85. Dong X, Mumper RJ: The metabolism of fatty alcohols in lipid nanoparticles by alcohol dehydrogenase. Drug Dev Ind Pharm; 2006 Sep;32(8):973-80
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  • The purpose of these studies was to determine whether horse liver alcohol dehydrogenase (HLADH), a NAD-dependent enzyme, could metabolize the fatty alcohols within the NPs and thus serve as a mechanism to degrade these NPs in the body.
  • NPs were incubated with the enzyme and NAD+ at 37 degrees C for up to 48 h, and the concentrations of fatty alcohols were quantitatively determined over time by gas chromatography (GC).
  • It was concluded that horse liver alcohol dehydrogenase/NAD+ was able to metabolize the fatty alcohols within the NPs, suggesting that NPs made of fatty alcohols may be metabolized in the body via endogenous alcohol dehydrogenase enzyme systems.
  • [MeSH-minor] Animals. Chromatography, Gas. Fluorescence. Horses. Liver / enzymology. NAD / metabolism. Polyethylene Glycols / pharmacology

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  • (PMID = 16954110.001).
  • [ISSN] 0363-9045
  • [Journal-full-title] Drug development and industrial pharmacy
  • [ISO-abbreviation] Drug Dev Ind Pharm
  • [Language] eng
  • [Publication-type] Journal Article
  • [Publication-country] United States
  • [Chemical-registry-number] 0 / Fatty Alcohols; 0U46U6E8UK / NAD; 2KR89I4H1Y / stearyl alcohol; 30IQX730WE / Polyethylene Glycols; 9005-00-9 / octadecyl polyoxyethylene ether; 936JST6JCN / cetyl alcohol; EC 1.1.1.1 / Alcohol Dehydrogenase
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86. Lin H, Wong RP, Martinka M, Li G: Loss of SNF5 expression correlates with poor patient survival in melanoma. Clin Cancer Res; 2009 Oct 15;15(20):6404-11
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  • EXPERIMENTAL DESIGN: Using tissue microarray and immunohistochemistry, we evaluated SNF5 staining in 51 dysplastic nevi, 88 primary melanomas, and 48 metastatic melanomas.
  • RESULTS: SNF5 expression was reduced in metastatic melanoma compared with dysplastic nevi (P = 0.005), in advanced primary melanoma (Clark's level V) compared with low risk Clark's level II melanoma (P = 0.019), and in melanoma at sun-exposed sites compared with sun-protected sites (P = 0.044).
  • Furthermore, we showed a strong correlation between negative SNF5 expression and a worse 5-year survival in melanoma patients (P = 0.016).
  • [MeSH-major] Chromosomal Proteins, Non-Histone / metabolism. DNA-Binding Proteins / metabolism. Skin Neoplasms / metabolism. Transcription Factors / metabolism

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  • (PMID = 19808872.001).
  • [ISSN] 1078-0432
  • [Journal-full-title] Clinical cancer research : an official journal of the American Association for Cancer Research
  • [ISO-abbreviation] Clin. Cancer Res.
  • [Language] eng
  • [Publication-type] Journal Article; Research Support, Non-U.S. Gov't
  • [Publication-country] United States
  • [Chemical-registry-number] 0 / Biomarkers, Tumor; 0 / Chromosomal Proteins, Non-Histone; 0 / DNA-Binding Proteins; 0 / SMARCB1 protein, human; 0 / Transcription Factors
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87. Tomanek L, Zuzow MJ: The proteomic response of the mussel congeners Mytilus galloprovincialis and M. trossulus to acute heat stress: implications for thermal tolerance limits and metabolic costs of thermal stress. J Exp Biol; 2010 Oct 15;213(Pt 20):3559-74
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  • [Title] The proteomic response of the mussel congeners Mytilus galloprovincialis and M. trossulus to acute heat stress: implications for thermal tolerance limits and metabolic costs of thermal stress.
  • Using two-dimensional gel electrophoresis and tandem mass spectrometry we identified 47 and 61 distinct proteins that changed abundance in M. galloprovincialis and M. trossulus, respectively.
  • Levels of NAD-dependent deacetylase (sirtuin 5), which are correlated with lifespan, were lower in M. trossulus in response to heat stress.

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  • (PMID = 20889836.001).
  • [ISSN] 1477-9145
  • [Journal-full-title] The Journal of experimental biology
  • [ISO-abbreviation] J. Exp. Biol.
  • [Language] eng
  • [Publication-type] Journal Article; Research Support, U.S. Gov't, Non-P.H.S.
  • [Publication-country] England
  • [Chemical-registry-number] 0 / Proteome
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88. Chambellon E, Rijnen L, Lorquet F, Gitton C, van Hylckama Vlieg JE, Wouters JA, Yvon M: The D-2-hydroxyacid dehydrogenase incorrectly annotated PanE is the sole reduction system for branched-chain 2-keto acids in Lactococcus lactis. J Bacteriol; 2009 Feb;191(3):873-81
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  • Its probable physiological role is to regenerate the NAD(+) necessary to catabolize branched-chain amino acids, leading to the production of ATP and aroma compounds.

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  • (PMID = 19047348.001).
  • [ISSN] 1098-5530
  • [Journal-full-title] Journal of bacteriology
  • [ISO-abbreviation] J. Bacteriol.
  • [Language] eng
  • [Publication-type] Journal Article; Research Support, Non-U.S. Gov't
  • [Publication-country] United States
  • [Chemical-registry-number] 0 / Bacterial Proteins; 0 / Keto Acids; 0 / Recombinant Proteins; EC 1.- / Oxidoreductases; EC 1.1.1.27 / L-Lactate Dehydrogenase; GMW67QNF9C / Leucine
  • [Other-IDs] NLM/ PMC2632062
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89. Carrigan JB, Engel PC: Probing the determinants of coenzyme specificity in Peptostreptococcus asaccharolyticus glutamate dehydrogenase by site-directed mutagenesis. FEBS J; 2007 Oct;274(19):5167-74
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  • Sequence alignments across the wider family of NAD(P)-dependent dehydrogenases might suggest that this preference is mainly due to a negatively charged glutamate at position 243 (E243) in the adenine ribose-binding pocket.
  • By contrast, replacement with a more positively charged lysine or arginine, as found in NADPH-dependent members of other dehydrogenase families, allows a more than 1000-fold shift toward NADPH, resulting in enzymes equally efficient with NADH or NADPH.

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  • (PMID = 17850332.001).
  • [ISSN] 1742-464X
  • [Journal-full-title] The FEBS journal
  • [ISO-abbreviation] FEBS J.
  • [Language] eng
  • [Publication-type] Journal Article; Research Support, Non-U.S. Gov't
  • [Publication-country] England
  • [Chemical-registry-number] 0 / Molecular Probes; 53-59-8 / NADP; EC 1.4.1.2 / Glutamate Dehydrogenase
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90. Rose P, Whiteman M, Moore PK, Zhu YZ: Bioactive S-alk(en)yl cysteine sulfoxide metabolites in the genus Allium: the chemistry of potential therapeutic agents. Nat Prod Rep; 2005 Jun;22(3):351-68
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  • Recent reports have shown onion and garlic extracts, along with several principal sulfur constituents, can induce phase II detoxification enzymes like glutathione-S-transferases (EC 2.5.1.18) and quinone reductase (QR) NAD(P)H: (quinine acceptor) oxidoreductase (EC 1.6.99.2) in mammalian tissues, as well as also influencing cell cycle arrest and apoptosis in numerous in vitro cancer cell models.


91. Mazurczak T: [Importance of studies about the etiopathogenesis of childhood diseases for clinical practice. Introduction]. Med Wieku Rozwoj; 2009 Apr-Jun;13(2):79-80
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  • [Transliterated title] Znaczenie badań nad etiopatogeneza chorób dziedzicznych u człowieka dla praktyki klinicznej. Wprowadzenie.

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  • (PMID = 19852103.001).
  • [Journal-full-title] Medycyna wieku rozwojowego
  • [ISO-abbreviation] Med Wieku Rozwoj
  • [Language] pol
  • [Publication-type] Introductory Journal Article
  • [Publication-country] Poland
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92. Zhang ZH, Yu Y, Wei SG, Felder RB: Centrally administered lipopolysaccharide elicits sympathetic excitation via NAD(P)H oxidase-dependent mitogen-activated protein kinase signaling. J Hypertens; 2010 Apr;28(4):806-16
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  • [Title] Centrally administered lipopolysaccharide elicits sympathetic excitation via NAD(P)H oxidase-dependent mitogen-activated protein kinase signaling.
  • LPS increased (P < 0.05) hypothalamic mRNA for NAD(P)H oxidase subunits p47 and gp91, NAD(P)H oxidase-dependent superoxide generation, hypothalamic mRNA for tumor necrosis factor-alpha, cyclooxygenase-2 and cerebrospinal fluid levels of tumor necrosis factor-alpha and prostaglandin E2.
  • Tempol, apocynin [NAD(P)H oxidase inhibitor], SB203580 and NS398 (cyclooxygenase-2 inhibitor) all reduced cerebrospinal fluid prostaglandin E2 and the sympathoexcitatory response to LPS.
  • CONCLUSION: These findings suggest that central inflammation in pathophysiological conditions activates the sympathetic nervous system via NAD(P)H oxidase and p38 mitogen-activated protein kinase-dependent synthesis of prostaglandin E2.

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  • (PMID = 20027123.001).
  • [ISSN] 1473-5598
  • [Journal-full-title] Journal of hypertension
  • [ISO-abbreviation] J. Hypertens.
  • [Language] ENG
  • [Grant] United States / NHLBI NIH HHS / HL / R01 HL073986; United States / NHLBI NIH HHS / HL / R01 HL073986-04; United States / NHLBI NIH HHS / HL / R01 HL073986-05A2; United States / NHLBI NIH HHS / HL / HL073986-04; United States / NHLBI NIH HHS / HL / R01HL073986; United States / NHLBI NIH HHS / HL / HL073986-05A2
  • [Publication-type] Journal Article; Research Support, N.I.H., Extramural; Research Support, U.S. Gov't, Non-P.H.S.
  • [Publication-country] England
  • [Chemical-registry-number] 0 / Acetophenones; 0 / Cyclic N-Oxides; 0 / Inflammation Mediators; 0 / Lipopolysaccharides; 0 / Receptor, Angiotensin, Type 1; 0 / Spin Labels; 0 / Tumor Necrosis Factor-alpha; 11062-77-4 / Superoxides; B6J7B9UDTR / acetovanillone; EC 1.14.99.1 / Cyclooxygenase 2; EC 1.6.3.1 / NADPH Oxidase; EC 2.7.11.24 / Mitogen-Activated Protein Kinases; U78ZX2F65X / tempol
  • [Other-IDs] NLM/ NIHMS221836; NLM/ PMC2929929
  • [Keywords] NOTNLM ; inflammation / lipopolysaccharide / oxidative stress / paraventricular nucleus of hypothalamus / prostaglandins
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93. Rosenstock TR, Bertoncini CR, Teles AV, Hirata H, Fernandes MJ, Smaili SS: Glutamate-induced alterations in Ca2+ signaling are modulated by mitochondrial Ca2+ handling capacity in brain slices of R6/1 transgenic mice. Eur J Neurosci; 2010 Jul;32(1):60-70
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  • Huntington's disease is a neurodegenerative disorder caused by an expansion of CAGs repeats and characterized by alterations in mitochondrial functions.
  • The aim of this study was to investigate the possible alterations in Ca(2+) handling capacity and the relationship with mitochondrial dysfunction evaluated by NAD(P)H fluorescence, reactive oxygen species levels, mitochondrial membrane potential (DeltaPsi(m)) measurements and respiration in whole brain slices from R6/1 mice of different ages, evaluated in situ by real-time real-space microscopy.
  • In addition, Glu also lead to a decrease in NAD(P)H fluorescence, a loss in DeltaPsi(m) and a further increase in respiration, which may have evoked a decrease in mitochondrial Ca(2+) Ca(2+)(m) uptake capacity.
  • Taken together, these results show that alterations in Ca(2+) homeostasis in transgenic mice are associated with a decrease in Ca(2+)(m) uptake mechanism with a diminished Ca(2+) handling ability that ultimately causes dysfunctions and worsening of the neurodegenerative and the disease processes.

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  • (PMID = 20608968.001).
  • [ISSN] 1460-9568
  • [Journal-full-title] The European journal of neuroscience
  • [ISO-abbreviation] Eur. J. Neurosci.
  • [Language] eng
  • [Publication-type] Journal Article; Research Support, Non-U.S. Gov't
  • [Publication-country] France
  • [Chemical-registry-number] 0 / Enzyme Inhibitors; 0 / Reactive Oxygen Species; 0 / Uncoupling Agents; 370-86-5 / Carbonyl Cyanide p-Trifluoromethoxyphenylhydrazone; 3KX376GY7L / Glutamic Acid; 53-59-8 / NADP; 67526-95-8 / Thapsigargin; SY7Q814VUP / Calcium
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94. Chang YH, Huang TJ, Chuang LY, Hwang CC: Role of S114 in the NADH-induced conformational change and catalysis of 3alpha-hydroxysteroid dehydrogenase/carbonyl reductase from Comamonas testosteroni. Biochim Biophys Acta; 2009 Oct;1794(10):1459-66
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  • 3alpha-Hydroxysteroid dehydrogenase/carbonyl reductase reversibly catalyzes the oxidation of androsterone with NAD(+) to form androstanedione and NADH.
  • The binding of NADH into a hydrophobic pocket in the active site of wild-type and S114A mutant enzymes restricts its motion and shields the fluorescence quenching from solvent, with an increase in the fluorescence intensity and a blue shift at the maximum wavelength.
  • Substitution of alanine for S114 eliminates the hydrogen bonding interaction with P185, causing a conformational change in a nonproductive binding of NADH and a significant loss of activity.
  • [MeSH-minor] Amino Acid Substitution. Catalytic Domain / genetics. Circular Dichroism. Conserved Sequence. Fluorescence Polarization. Hydrophobic and Hydrophilic Interactions. Kinetics. Models, Molecular. Mutagenesis, Site-Directed. NAD / metabolism. Protein Conformation. Protein Structure, Secondary. Recombinant Proteins / chemistry. Recombinant Proteins / genetics. Recombinant Proteins / metabolism. Spectrometry, Fluorescence

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  • (PMID = 19520191.001).
  • [ISSN] 0006-3002
  • [Journal-full-title] Biochimica et biophysica acta
  • [ISO-abbreviation] Biochim. Biophys. Acta
  • [Language] eng
  • [Publication-type] Journal Article; Research Support, Non-U.S. Gov't
  • [Publication-country] Netherlands
  • [Chemical-registry-number] 0 / Recombinant Proteins; 0U46U6E8UK / NAD; EC 1.1.- / 3alpha-hydroxysteroid dehydrogenase-carbonyl reductase; EC 1.1.- / Hydroxysteroid Dehydrogenases
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95. Attene-Ramos MS, Kitiphongspattana K, Ishii-Schrade K, Gaskins HR: Temporal changes of multiple redox couples from proliferation to growth arrest in IEC-6 intestinal epithelial cells. Am J Physiol Cell Physiol; 2005 Nov;289(5):C1220-8
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  • From the first day of culture until 1 day before confluence, an increase in GSH concentrations and a significant reduction in the redox potential of the GSSG/2GSH couple were observed.
  • These changes were accompanied by a decrease in relative reactive oxygen species (ROS) and nitric oxide (NO) concentrations and oxidation of the redox potential of the NADP(+)/reduced NADP and NAD(+)/NADH couples.
  • Postconfluent cells exhibited a significant decrease in GSH concentrations and a significant oxidation of the GSSG/2GSH couple.
  • When cell proliferation decreased, relative ROS concentrations increased (P < 0.01), whereas NO concentrations remained unchanged, and the NAD(+)/NADH couple became more reduced.
  • [MeSH-minor] Adenosine Diphosphate / physiology. Adenosine Triphosphate / physiology. Animals. Cell Cycle / physiology. Cell Line. Glutathione / physiology. Glutathione Disulfide / physiology. NADP / physiology. Nitric Oxide / physiology. Oxidation-Reduction. Reactive Oxygen Species / metabolism. Signal Transduction. Time Factors

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  • (PMID = 15958525.001).
  • [ISSN] 0363-6143
  • [Journal-full-title] American journal of physiology. Cell physiology
  • [ISO-abbreviation] Am. J. Physiol., Cell Physiol.
  • [Language] eng
  • [Grant] United States / NIDDK NIH HHS / DK / 5T32-DK-59802; United States / NIDDK NIH HHS / DK / R01-DK-061568
  • [Publication-type] Journal Article; Research Support, N.I.H., Extramural; Research Support, U.S. Gov't, P.H.S.
  • [Publication-country] United States
  • [Chemical-registry-number] 0 / Reactive Oxygen Species; 31C4KY9ESH / Nitric Oxide; 53-59-8 / NADP; 61D2G4IYVH / Adenosine Diphosphate; 8L70Q75FXE / Adenosine Triphosphate; GAN16C9B8O / Glutathione; ULW86O013H / Glutathione Disulfide
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96. Sheline CT, Cai AL, Zhu J, Shi C: Serum or target deprivation-induced neuronal death causes oxidative neuronal accumulation of Zn2+ and loss of NAD+. Eur J Neurosci; 2010 Sep;32(6):894-904
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  • [Title] Serum or target deprivation-induced neuronal death causes oxidative neuronal accumulation of Zn2+ and loss of NAD+.
  • We have previously shown that neurotoxicity of extracellular Zn(2+) required entry, increased [Zn(2+) ](i) , and reduction of NAD(+) and ATP levels causing inhibition of glycolysis and cellular metabolism.
  • Exogenous NAD(+) and sirtuin inhibition attenuated Zn(2+) neurotoxicity.
  • (2) NAD(+) loss is involved - restoration of NAD(+) using exogenous NAD(+) , pyruvate or nicotinamide attenuated these injuries, and potentiation of NAD(+) loss potentiated injury;.
  • (3) neurons from genetically modified mouse strains which reduce intracellular Zn(2+) content (MT-III knockout), reduce NAD(+) catabolism (PARP-1 knockout) or increase expression of an NAD(+) synthetic enzyme (Wld(s) ) each had attenuated SD and oxidant neurotoxicities;.
  • (5) visual cortex ablation (VCA) induces Zn(2+) staining and death only in ipsilateral LGNd neurons, and a 1 mg/kg Zn(2+) diet attenuated injury; and finally (6) NAD(+) synthesis and levels are involved given that LGNd neuronal death after VCA was dramatically reduced in Wld(s) animals, and by intraperitoneal pyruvate or nicotinamide.

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  • [Copyright] © 2010 The Authors. European Journal of Neuroscience © 2010 Federation of European Neuroscience Societies and Blackwell Publishing Ltd.
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  • (PMID = 20722716.001).
  • [ISSN] 1460-9568
  • [Journal-full-title] The European journal of neuroscience
  • [ISO-abbreviation] Eur. J. Neurosci.
  • [Language] ENG
  • [Grant] United States / NIDDK NIH HHS / DK / R01 DK073446-06; United States / NIDDK NIH HHS / DK / DK073446-01A1; United States / NIDDK NIH HHS / DK / R01 DK073446-03; United States / NIDDK NIH HHS / DK / R01 DK073446-02; United States / NIDDK NIH HHS / DK / DK073446-05; United States / NIDDK NIH HHS / DK / R01 DK073446; United States / NIDDK NIH HHS / DK / R01 DK073446-01A1; United States / NIDDK NIH HHS / DK / DK073446-02; United States / NINDS NIH HHS / NS / R01 NS030337-13; United States / NIDDK NIH HHS / DK / DK073446-05S2; United States / NIDDK NIH HHS / DK / R01 DK073446-04; United States / NINDS NIH HHS / NS / NS030337-13; United States / NIDDK NIH HHS / DK / R01 DK073446-05S2; United States / NIDDK NIH HHS / DK / DK073446-04; United States / NIDDK NIH HHS / DK / R01 DK073446-05; United States / NIDDK NIH HHS / DK / DK073446-03; United States / NINDS NIH HHS / NS / NS 030337; United States / NIDDK NIH HHS / DK / DK073446-06; United States / NIDDK NIH HHS / DK / DK 073446; United States / NINDS NIH HHS / NS / R01 NS030337
  • [Publication-type] Comparative Study; Journal Article; Research Support, N.I.H., Extramural
  • [Publication-country] France
  • [Chemical-registry-number] 0 / Cations, Divalent; 0 / Serum Albumin; 0U46U6E8UK / NAD; EC 3.5.1.- / Sirt1 protein, mouse; EC 3.5.1.- / Sirtuin 1; J41CSQ7QDS / Zinc
  • [Other-IDs] NLM/ NIHMS219455; NLM/ PMC2946389
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97. Tang YJ, Shui W, Myers S, Feng X, Bertozzi C, Keasling JD: Central metabolism in Mycobacterium smegmatis during the transition from O2-rich to O2-poor conditions as studied by isotopomer-assisted metabolite analysis. Biotechnol Lett; 2009 Aug;31(8):1233-40
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  • [Source] The source of this record is MEDLINE®, a database of the U.S. National Library of Medicine.
  • (1) isocitrate lyase activity increased, which further induced glyoxylate pathway and glycine dehydrogenase for replenishing NAD(+);.
  • [MeSH-minor] Acetyl Coenzyme A / metabolism. Aerobiosis. Anaerobiosis. Citric Acid Cycle. Glycine Dehydrogenase / metabolism. Isocitrate Lyase / metabolism. NAD / metabolism. Pentose Phosphate Pathway. Stress, Physiological

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  • (PMID = 19357814.001).
  • [ISSN] 1573-6776
  • [Journal-full-title] Biotechnology letters
  • [ISO-abbreviation] Biotechnol. Lett.
  • [Language] eng
  • [Publication-type] Journal Article; Research Support, Non-U.S. Gov't
  • [Publication-country] Netherlands
  • [Chemical-registry-number] 0U46U6E8UK / NAD; 72-89-9 / Acetyl Coenzyme A; EC 1.4.1.10 / Glycine Dehydrogenase; EC 4.1.3.1 / Isocitrate Lyase
  • [Other-IDs] NLM/ PMC2709878
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98. Lau C, Niere M, Ziegler M: The NMN/NaMN adenylyltransferase (NMNAT) protein family. Front Biosci (Landmark Ed); 2009;14:410-31