메뉴 건너뛰기




Volumn 33, Issue 12, 2014, Pages 1304-1320

Regulation of G6PD acetylation by SIRT2 and KAT9 modulates NADPH homeostasis and cell survival during oxidative stress

Author keywords

acetylation; G6PD; nicotinamide adenine dinucleotide phosphate; reactive oxygen species; SIRT2

Indexed keywords

ELP 3 PROTEIN; GLUCOSE 6 PHOSPHATE DEHYDROGENASE; KAT 9 PROTEIN; LYSINE; PROTEIN; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE; SIRTUIN 2; UNCLASSIFIED DRUG;

EID: 84903317314     PISSN: 02614189     EISSN: 14602075     Source Type: Journal    
DOI: 10.1002/embj.201387224     Document Type: Article
Times cited : (253)

References (82)
  • 2
    • 0034654509 scopus 로고    scopus 로고
    • Human glucose-6-phosphate dehydrogenase: The crystal structure reveals a structural NADP(+) molecule and provides insights into enzyme deficiency
    • Au SW, Gover S, Lam VM, Adams MJ, (2000) Human glucose-6-phosphate dehydrogenase: the crystal structure reveals a structural NADP(+) molecule and provides insights into enzyme deficiency. Structure 8: 293-303
    • (2000) Structure , vol.8 , pp. 293-303
    • Au, S.W.1    Gover, S.2    Lam, V.M.3    Adams, M.J.4
  • 3
    • 15244355745 scopus 로고    scopus 로고
    • Mechanism of sirtuin inhibition by nicotinamide: Altering the NAD(+) cosubstrate specificity of a Sir2 enzyme
    • Avalos JL, Bever KM, Wolberger C, (2005) Mechanism of sirtuin inhibition by nicotinamide: altering the NAD(+) cosubstrate specificity of a Sir2 enzyme. Mol Cell 17: 855-868
    • (2005) Mol Cell , vol.17 , pp. 855-868
    • Avalos, J.L.1    Bever, K.M.2    Wolberger, C.3
  • 4
    • 0017155142 scopus 로고
    • Genetic variants of human erythrocyte glucose-6-phosphate dehydrogenase. Kinetic and thermodynamic parameters of variants A, B, and A- in relation to quaternary structure
    • Babalola AO, Beetlestone JG, Luzzatto L, (1976) Genetic variants of human erythrocyte glucose-6-phosphate dehydrogenase. Kinetic and thermodynamic parameters of variants A, B, and A- in relation to quaternary structure. J Biol Chem 251: 2993-3002
    • (1976) J Biol Chem , vol.251 , pp. 2993-3002
    • Babalola, A.O.1    Beetlestone, J.G.2    Luzzatto, L.3
  • 5
    • 0344344573 scopus 로고
    • Glucose-6-phosphate dehydrogenase deficiency and the incidence of cancer
    • Beaconsfield P, Rainsbury R, Kalton G, (1965) Glucose-6-phosphate dehydrogenase deficiency and the incidence of cancer. Oncology 19: 11-19
    • (1965) Oncology , vol.19 , pp. 11-19
    • Beaconsfield, P.1    Rainsbury, R.2    Kalton, G.3
  • 7
    • 0037160097 scopus 로고    scopus 로고
    • Inhibition of silencing and accelerated aging by nicotinamide, a putative negative regulator of yeast sir2 and human SIRT1
    • Bitterman KJ, Anderson RM, Cohen HY, Latorre-Esteves M, Sinclair DA, (2002) Inhibition of silencing and accelerated aging by nicotinamide, a putative negative regulator of yeast sir2 and human SIRT1. J Biol Chem 277: 45099-45107
    • (2002) J Biol Chem , vol.277 , pp. 45099-45107
    • Bitterman, K.J.1    Anderson, R.M.2    Cohen, H.Y.3    Latorre-Esteves, M.4    Sinclair, D.A.5
  • 8
    • 25444467580 scopus 로고    scopus 로고
    • Large-scale 13C-flux analysis reveals mechanistic principles of metabolic network robustness to null mutations in yeast
    • Blank LM, Kuepfer L, Sauer U, (2005) Large-scale 13C-flux analysis reveals mechanistic principles of metabolic network robustness to null mutations in yeast. Genome Biol 6: R49
    • (2005) Genome Biol , vol.6
    • Blank, L.M.1    Kuepfer, L.2    Sauer, U.3
  • 9
    • 37549026846 scopus 로고    scopus 로고
    • Glucose-6-phosphate dehydrogenase deficiency
    • Cappellini MD, Fiorelli G, (2008) Glucose-6-phosphate dehydrogenase deficiency. Lancet 371: 64-74
    • (2008) Lancet , vol.371 , pp. 64-74
    • Cappellini, M.D.1    Fiorelli, G.2
  • 10
    • 79957944140 scopus 로고    scopus 로고
    • Advances in characterization of human sirtuin isoforms: Chemistries, targets and therapeutic applications
    • Cen Y, Youn DY, Sauve AA, (2011) Advances in characterization of human sirtuin isoforms: chemistries, targets and therapeutic applications. Curr Med Chem 18: 1919-1935
    • (2011) Curr Med Chem , vol.18 , pp. 1919-1935
    • Cen, Y.1    Youn, D.Y.2    Sauve, A.A.3
  • 13
    • 0031982856 scopus 로고    scopus 로고
    • Mortality in a cohort of men expressing the glucose-6-phosphate dehydrogenase deficiency
    • Cocco P, Todde P, Fornera S, Manca MB, Manca P, Sias AR, (1998) Mortality in a cohort of men expressing the glucose-6-phosphate dehydrogenase deficiency. Blood 91: 706-709
    • (1998) Blood , vol.91 , pp. 706-709
    • Cocco, P.1    Todde, P.2    Fornera, S.3    Manca, M.B.4    Manca, P.5    Sias, A.R.6
  • 14
    • 0014487356 scopus 로고
    • Human glucose-6-phosphate dehydrogenase: Purification of the erythrocyte enzyme and the influence of ions on its activity
    • Cohen P, Rosemeyer MA, (1969) Human glucose-6-phosphate dehydrogenase: purification of the erythrocyte enzyme and the influence of ions on its activity. Eur J Biochem 8: 1-7
    • (1969) Eur J Biochem , vol.8 , pp. 1-7
    • Cohen, P.1    Rosemeyer, M.A.2
  • 15
    • 0029421199 scopus 로고
    • Upregulation of glucose-6-phosphate dehydrogenase in response to hepatocellular oxidative stress: Studies with diquat
    • Cramer CT, Cooke S, Ginsberg LC, Kletzien RF, Stapleton SR, Ulrich RG, (1995) Upregulation of glucose-6-phosphate dehydrogenase in response to hepatocellular oxidative stress: studies with diquat. J Biochem Toxicol 10: 293-298
    • (1995) J Biochem Toxicol , vol.10 , pp. 293-298
    • Cramer, C.T.1    Cooke, S.2    Ginsberg, L.C.3    Kletzien, R.F.4    Stapleton, S.R.5    Ulrich, R.G.6
  • 17
    • 65549113750 scopus 로고    scopus 로고
    • CBP/p300-mediated acetylation of histone H3 on lysine 56
    • Das C, Lucia MS, Hansen KC, Tyler JK, (2009) CBP/p300-mediated acetylation of histone H3 on lysine 56. Nature 459: 113-117
    • (2009) Nature , vol.459 , pp. 113-117
    • Das, C.1    Lucia, M.S.2    Hansen, K.C.3    Tyler, J.K.4
  • 19
    • 2542455473 scopus 로고    scopus 로고
    • Imaging dynamic redox changes in mammalian cells with green fluorescent protein indicators
    • Dooley CT, Dore TM, Hanson GT, Jackson WC, Remington SJ, Tsien RY, (2004) Imaging dynamic redox changes in mammalian cells with green fluorescent protein indicators. J Biol Chem 279: 22284-22293
    • (2004) J Biol Chem , vol.279 , pp. 22284-22293
    • Dooley, C.T.1    Dore, T.M.2    Hanson, G.T.3    Jackson, W.C.4    Remington, S.J.5    Tsien, R.Y.6
  • 21
    • 84886686038 scopus 로고    scopus 로고
    • Activation of the protein deacetylase SIRT6 by long-chain fatty acids and widespread deacylation by mammalian sirtuins
    • Feldman JL, Baeza J, Denu JM, (2013) Activation of the protein deacetylase SIRT6 by long-chain fatty acids and widespread deacylation by mammalian sirtuins. J Biol Chem 288: 31350-31356
    • (2013) J Biol Chem , vol.288 , pp. 31350-31356
    • Feldman, J.L.1    Baeza, J.2    Denu, J.M.3
  • 22
    • 0037444772 scopus 로고    scopus 로고
    • Failure to increase glucose consumption through the pentose-phosphate pathway results in the death of glucose-6-phosphate dehydrogenase gene-deleted mouse embryonic stem cells subjected to oxidative stress
    • Filosa S, Fico A, Paglialunga F, Balestrieri M, Crooke A, Verde P, Abrescia P, Bautista JM, Martini G, (2003) Failure to increase glucose consumption through the pentose-phosphate pathway results in the death of glucose-6-phosphate dehydrogenase gene-deleted mouse embryonic stem cells subjected to oxidative stress. Biochem J 370: 935-943
    • (2003) Biochem J , vol.370 , pp. 935-943
    • Filosa, S.1    Fico, A.2    Paglialunga, F.3    Balestrieri, M.4    Crooke, A.5    Verde, P.6    Abrescia, P.7    Bautista, J.M.8    Martini, G.9
  • 23
    • 0035793107 scopus 로고    scopus 로고
    • Potent histone deacetylase inhibitors built from trichostatin A and cyclic tetrapeptide antibiotics including trapoxin
    • Furumai R, Komatsu Y, Nishino N, Khochbin S, Yoshida M, Horinouchi S, (2001) Potent histone deacetylase inhibitors built from trichostatin A and cyclic tetrapeptide antibiotics including trapoxin. Proc Natl Acad Sci USA 98: 87-92
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 87-92
    • Furumai, R.1    Komatsu, Y.2    Nishino, N.3    Khochbin, S.4    Yoshida, M.5    Horinouchi, S.6
  • 24
    • 0028386519 scopus 로고
    • Purification, characterization, and cDNA sequence of glucose-6-phosphate dehydrogenase from potato (Solanum tuberosum L.)
    • Graeve K, von Schaewen A, Scheibe R, (1994) Purification, characterization, and cDNA sequence of glucose-6-phosphate dehydrogenase from potato (Solanum tuberosum L.). Plant J 5: 353-361
    • (1994) Plant J , vol.5 , pp. 353-361
    • Graeve, K.1    Von Schaewen, A.2    Scheibe, R.3
  • 26
    • 79958206937 scopus 로고    scopus 로고
    • Franklin H Epstein Lecture: Sirtuins, aging, and medicine
    • Guarente L, (2011) Franklin H Epstein Lecture: sirtuins, aging, and medicine. N Engl J Med 364: 2235-2244
    • (2011) N Engl J Med , vol.364 , pp. 2235-2244
    • Guarente, L.1
  • 27
    • 57749170458 scopus 로고    scopus 로고
    • The many roles of histone deacetylases in development and physiology: Implications for disease and therapy
    • Haberland M, Montgomery RL, Olson EN, (2009) The many roles of histone deacetylases in development and physiology: implications for disease and therapy. Nat Rev Genet 10: 32-42
    • (2009) Nat Rev Genet , vol.10 , pp. 32-42
    • Haberland, M.1    Montgomery, R.L.2    Olson, E.N.3
  • 28
    • 0141675950 scopus 로고    scopus 로고
    • Differential regulation of glucose-6-phosphate dehydrogenase isoenzyme activities in potato
    • Hauschild R, von Schaewen A, (2003) Differential regulation of glucose-6-phosphate dehydrogenase isoenzyme activities in potato. Plant Physiol 133: 47-62
    • (2003) Plant Physiol , vol.133 , pp. 47-62
    • Hauschild, R.1    Von Schaewen, A.2
  • 29
    • 82955233648 scopus 로고    scopus 로고
    • Old enzymes, new tricks: Sirtuins are NAD(+)-dependent de-acylases
    • Hirschey MD, (2011) Old enzymes, new tricks: sirtuins are NAD(+)-dependent de-acylases. Cell Metab 14: 718-719
    • (2011) Cell Metab , vol.14 , pp. 718-719
    • Hirschey, M.D.1
  • 30
    • 0034677535 scopus 로고    scopus 로고
    • Transcriptional silencing and longevity protein Sir2 is an NAD-dependent histone deacetylase
    • Imai S, Armstrong CM, Kaeberlein M, Guarente L, (2000) Transcriptional silencing and longevity protein Sir2 is an NAD-dependent histone deacetylase. Nature 403: 795-800
    • (2000) Nature , vol.403 , pp. 795-800
    • Imai, S.1    Armstrong, C.M.2    Kaeberlein, M.3    Guarente, L.4
  • 31
    • 79952280229 scopus 로고    scopus 로고
    • P53 regulates biosynthesis through direct inactivation of glucose-6-phosphate dehydrogenase
    • Jiang P, Du W, Wang X, Mancuso A, Gao X, Wu M, Yang X, (2011a) p53 regulates biosynthesis through direct inactivation of glucose-6-phosphate dehydrogenase. Nat Cell Biol 13: 310-316
    • (2011) Nat Cell Biol , vol.13 , pp. 310-316
    • Jiang, P.1    Du, W.2    Wang, X.3    Mancuso, A.4    Gao, X.5    Wu, M.6    Yang, X.7
  • 32
    • 79959906869 scopus 로고    scopus 로고
    • Acetylation regulates gluconeogenesis by promoting PEPCK1 degradation via recruiting the UBR5 ubiquitin ligase
    • Jiang W, Wang S, Xiao M, Lin Y, Zhou L, Lei Q, Xiong Y, Guan KL, Zhao S, (2011b) Acetylation regulates gluconeogenesis by promoting PEPCK1 degradation via recruiting the UBR5 ubiquitin ligase. Mol Cell 43: 33-44
    • (2011) Mol Cell , vol.43 , pp. 33-44
    • Jiang, W.1    Wang, S.2    Xiao, M.3    Lin, Y.4    Zhou, L.5    Lei, Q.6    Xiong, Y.7    Guan, K.L.8    Zhao, S.9
  • 33
    • 0029829625 scopus 로고    scopus 로고
    • Mutants that show increased sensitivity to hydrogen peroxide reveal an important role for the pentose phosphate pathway in protection of yeast against oxidative stress
    • Juhnke H, Krems B, Kotter P, Entian KD, (1996) Mutants that show increased sensitivity to hydrogen peroxide reveal an important role for the pentose phosphate pathway in protection of yeast against oxidative stress. Mol Gen Genet 252: 456-464
    • (1996) Mol Gen Genet , vol.252 , pp. 456-464
    • Juhnke, H.1    Krems, B.2    Kotter, P.3    Entian, K.D.4
  • 35
    • 34547616314 scopus 로고    scopus 로고
    • Regulation of singlet oxygen-induced apoptosis by cytosolic NADP+-dependent isocitrate dehydrogenase
    • Kim SY, Lee SM, Tak JK, Choi KS, Kwon TK, Park JW, (2007) Regulation of singlet oxygen-induced apoptosis by cytosolic NADP+-dependent isocitrate dehydrogenase. Mol Cell Biochem 302: 27-34
    • (2007) Mol Cell Biochem , vol.302 , pp. 27-34
    • Kim, S.Y.1    Lee, S.M.2    Tak, J.K.3    Choi, K.S.4    Kwon, T.K.5    Park, J.W.6
  • 36
    • 0028176627 scopus 로고
    • Glucose-6-phosphate dehydrogenase: A "housekeeping" enzyme subject to tissue-specific regulation by hormones, nutrients, and oxidant stress
    • Kletzien RF, Harris PK, Foellmi LA, (1994) Glucose-6-phosphate dehydrogenase: a "housekeeping" enzyme subject to tissue-specific regulation by hormones, nutrients, and oxidant stress. FASEB J 8: 174-181
    • (1994) FASEB J , vol.8 , pp. 174-181
    • Kletzien, R.F.1    Harris, P.K.2    Foellmi, L.A.3
  • 38
    • 33846243745 scopus 로고    scopus 로고
    • An integrated view of oxidative stress in aging: Basic mechanisms, functional effects, and pathological considerations
    • Kregel KC, Zhang HJ, (2007) An integrated view of oxidative stress in aging: basic mechanisms, functional effects, and pathological considerations. Am J Physiol Regul Integr Comp Physiol 292: R18-R36
    • (2007) Am J Physiol Regul Integr Comp Physiol , vol.292
    • Kregel, K.C.1    Zhang, H.J.2
  • 42
    • 0014034838 scopus 로고
    • Associations between red cell glucose-6-phosphate dehydrogenase variants and vascular diseases
    • Long WK, Wilson SW, Frenkel EP, (1967) Associations between red cell glucose-6-phosphate dehydrogenase variants and vascular diseases. Am J Hum Genet 19: 35-53
    • (1967) Am J Hum Genet , vol.19 , pp. 35-53
    • Long, W.K.1    Wilson, S.W.2    Frenkel, E.P.3
  • 45
    • 47249160785 scopus 로고    scopus 로고
    • Glutathione peroxidase family - An evolutionary overview
    • Margis R, Dunand C, Teixeira FK, Margis-Pinheiro M, (2008) Glutathione peroxidase family-an evolutionary overview. FEBS J 275: 3959-3970
    • (2008) FEBS J , vol.275 , pp. 3959-3970
    • Margis, R.1    Dunand, C.2    Teixeira, F.K.3    Margis-Pinheiro, M.4
  • 46
    • 34547702206 scopus 로고    scopus 로고
    • G6PD deficiency: The genotype-phenotype association
    • Mason PJ, Bautista JM, Gilsanz F, (2007) G6PD deficiency: the genotype-phenotype association. Blood Rev 21: 267-283
    • (2007) Blood Rev , vol.21 , pp. 267-283
    • Mason, P.J.1    Bautista, J.M.2    Gilsanz, F.3
  • 48
    • 0025093599 scopus 로고
    • Genetic analysis of histone H4: Essential role of lysines subject to reversible acetylation
    • Megee PC, Morgan BA, Mittman BA, Smith MM, (1990) Genetic analysis of histone H4: essential role of lysines subject to reversible acetylation. Science 247: 841-845
    • (1990) Science , vol.247 , pp. 841-845
    • Megee, P.C.1    Morgan, B.A.2    Mittman, B.A.3    Smith, M.M.4
  • 50
    • 34249083199 scopus 로고    scopus 로고
    • Sirtuins in mammals: Insights into their biological function
    • Michan S, Sinclair D, (2007) Sirtuins in mammals: insights into their biological function. Biochem J 404: 1-13
    • (2007) Biochem J , vol.404 , pp. 1-13
    • Michan, S.1    Sinclair, D.2
  • 51
    • 26244436281 scopus 로고    scopus 로고
    • Evolutionarily conserved and nonconserved cellular localizations and functions of human SIRT proteins
    • Michishita E, Park JY, Burneskis JM, Barrett JC, Horikawa I, (2005) Evolutionarily conserved and nonconserved cellular localizations and functions of human SIRT proteins. Mol Biol Cell 16: 4623-4635
    • (2005) Mol Biol Cell , vol.16 , pp. 4623-4635
    • Michishita, E.1    Park, J.Y.2    Burneskis, J.M.3    Barrett, J.C.4    Horikawa, I.5
  • 52
    • 35648956629 scopus 로고    scopus 로고
    • Gene-nutrient interactions in G6PD-deficient subjects-implications for cardiovascular disease susceptibility
    • Muntoni S, (2008) Gene-nutrient interactions in G6PD-deficient subjects-implications for cardiovascular disease susceptibility. J Nutrigenet Nutrigenomics 1: 49-54
    • (2008) J Nutrigenet Nutrigenomics , vol.1 , pp. 49-54
    • Muntoni, S.1
  • 53
    • 40949099577 scopus 로고    scopus 로고
    • Genetically encoding N(epsilon)-acetyllysine in recombinant proteins
    • Neumann H, Peak-Chew SY, Chin JW, (2008) Genetically encoding N(epsilon)-acetyllysine in recombinant proteins. Nat Chem Biol 4: 232-234
    • (2008) Nat Chem Biol , vol.4 , pp. 232-234
    • Neumann, H.1    Peak-Chew, S.Y.2    Chin, J.W.3
  • 55
    • 0025863734 scopus 로고
    • Glucose-6-phosphate dehydrogenase deficiency and diabetes mellitus
    • Niazi GA, (1991) Glucose-6-phosphate dehydrogenase deficiency and diabetes mellitus. Int J Hematol 54: 295-298
    • (1991) Int J Hematol , vol.54 , pp. 295-298
    • Niazi, G.A.1
  • 56
    • 0037291214 scopus 로고    scopus 로고
    • The human Sir2 ortholog, SIRT2, is an NAD+-dependent tubulin deacetylase
    • North BJ, Marshall BL, Borra MT, Denu JM, Verdin E, (2003) The human Sir2 ortholog, SIRT2, is an NAD+-dependent tubulin deacetylase. Mol Cell 11: 437-444
    • (2003) Mol Cell , vol.11 , pp. 437-444
    • North, B.J.1    Marshall, B.L.2    Borra, M.T.3    Denu, J.M.4    Verdin, E.5
  • 57
    • 0034054138 scopus 로고    scopus 로고
    • Human mutations in glucose 6-phosphate dehydrogenase reflect evolutionary history
    • Notaro R, Afolayan A, Luzzatto L, (2000) Human mutations in glucose 6-phosphate dehydrogenase reflect evolutionary history. FASEB J 14: 485-494
    • (2000) FASEB J , vol.14 , pp. 485-494
    • Notaro, R.1    Afolayan, A.2    Luzzatto, L.3
  • 59
    • 0028834278 scopus 로고
    • Targeted disruption of the housekeeping gene encoding glucose 6-phosphate dehydrogenase (G6PD): G6PD is dispensable for pentose synthesis but essential for defense against oxidative stress
    • Pandolfi PP, Sonati F, Rivi R, Mason P, Grosveld F, Luzzatto L, (1995) Targeted disruption of the housekeeping gene encoding glucose 6-phosphate dehydrogenase (G6PD): G6PD is dispensable for pentose synthesis but essential for defense against oxidative stress. EMBO J 14: 5209-5215
    • (1995) EMBO J , vol.14 , pp. 5209-5215
    • Pandolfi, P.P.1    Sonati, F.2    Rivi, R.3    Mason, P.4    Grosveld, F.5    Luzzatto, L.6
  • 60
    • 84867167138 scopus 로고    scopus 로고
    • Glucose-6-phosphate dehydrogenase and NADPH redox regulates cardiac myocyte L-type calcium channel activity and myocardial contractile function
    • Rawat DK, Hecker P, Watanabe M, Chettimada S, Levy RJ, Okada T, Edwards JG, Gupte SA, (2012) Glucose-6-phosphate dehydrogenase and NADPH redox regulates cardiac myocyte L-type calcium channel activity and myocardial contractile function. PLoS ONE 7: e45365
    • (2012) PLoS ONE , vol.7
    • Rawat, D.K.1    Hecker, P.2    Watanabe, M.3    Chettimada, S.4    Levy, R.J.5    Okada, T.6    Edwards, J.G.7    Gupte, S.A.8
  • 61
    • 0021986438 scopus 로고
    • Association of glucose-6-phosphate dehydrogenase deficiency with diabetes mellitus
    • Saeed TK, Hamamy HA, Alwan AA, (1985) Association of glucose-6-phosphate dehydrogenase deficiency with diabetes mellitus. Diabet Med 2: 110-112
    • (1985) Diabet Med , vol.2 , pp. 110-112
    • Saeed, T.K.1    Hamamy, H.A.2    Alwan, A.A.3
  • 62
    • 0034940164 scopus 로고    scopus 로고
    • Dietary regulation of expression of glucose-6-phosphate dehydrogenase
    • Salati LM, Amir-Ahmady B, (2001) Dietary regulation of expression of glucose-6-phosphate dehydrogenase. Annu Rev Nutr 21: 121-140
    • (2001) Annu Rev Nutr , vol.21 , pp. 121-140
    • Salati, L.M.1    Amir-Ahmady, B.2
  • 63
    • 80054771657 scopus 로고    scopus 로고
    • The role of mammalian sirtuins in the regulation of metabolism, aging, and longevity
    • Satoh A, Stein L, Imai S, (2011) The role of mammalian sirtuins in the regulation of metabolism, aging, and longevity. Handb Exp Pharmacol 206: 125-162
    • (2011) Handb Exp Pharmacol , vol.206 , pp. 125-162
    • Satoh, A.1    Stein, L.2    Imai, S.3
  • 64
    • 38649123072 scopus 로고    scopus 로고
    • Conserved metabolic regulatory functions of sirtuins
    • Schwer B, Verdin E, (2008) Conserved metabolic regulatory functions of sirtuins. Cell Metab 7: 104-112
    • (2008) Cell Metab , vol.7 , pp. 104-112
    • Schwer, B.1    Verdin, E.2
  • 65
    • 0029828902 scopus 로고    scopus 로고
    • The yeast copper/zinc superoxide dismutase and the pentose phosphate pathway play overlapping roles in oxidative stress protection
    • Slekar KH, Kosman DJ, Culotta VC, (1996) The yeast copper/zinc superoxide dismutase and the pentose phosphate pathway play overlapping roles in oxidative stress protection. J Biol Chem 271: 28831-28836
    • (1996) J Biol Chem , vol.271 , pp. 28831-28836
    • Slekar, K.H.1    Kosman, D.J.2    Culotta, V.C.3
  • 66
    • 53649086367 scopus 로고    scopus 로고
    • Mechanisms and molecular probes of sirtuins
    • Smith BC, Hallows WC, Denu JM, (2008) Mechanisms and molecular probes of sirtuins. Chem Biol 15: 1002-1013
    • (2008) Chem Biol , vol.15 , pp. 1002-1013
    • Smith, B.C.1    Hallows, W.C.2    Denu, J.M.3
  • 68
    • 0001498164 scopus 로고
    • The regulation of glycolysis and the pentose phosphate pathway
    • Stumpf P.K. Conn E.E. (eds), 2, pp. New York: Academic Press
    • Turner JF, Turner DH, (1980) The regulation of glycolysis and the pentose phosphate pathway. In: Biochemistry of Plants, Stumpf PK, Conn EE, (eds), Vol. 2, pp 279-316. New York: Academic Press
    • (1980) Biochemistry of Plants , pp. 279-316
    • Turner, J.F.1    Turner, D.H.2
  • 69
    • 0030957038 scopus 로고    scopus 로고
    • Enhanced expression of glucose-6-phosphate dehydrogenase in human cells sustaining oxidative stress
    • Ursini MV, Parrella A, Rosa G, Salzano S, Martini G, (1997) Enhanced expression of glucose-6-phosphate dehydrogenase in human cells sustaining oxidative stress. Biochem J 323 (Pt 3): 801-806
    • (1997) Biochem J , vol.323 , Issue.PART 3 , pp. 801-806
    • Ursini, M.V.1    Parrella, A.2    Rosa, G.3    Salzano, S.4    Martini, G.5
  • 71
    • 0027259193 scopus 로고
    • Variants of glucose-6-phosphate dehydrogenase are due to missense mutations spread throughout the coding region of the gene
    • Vulliamy T, Beutler E, Luzzatto L, (1993) Variants of glucose-6-phosphate dehydrogenase are due to missense mutations spread throughout the coding region of the gene. Hum Mutat 2: 159-167
    • (1993) Hum Mutat , vol.2 , pp. 159-167
    • Vulliamy, T.1    Beutler, E.2    Luzzatto, L.3
  • 72
    • 0742299380 scopus 로고    scopus 로고
    • Glucose-6-phosphate dehydrogenase deficiency and related disorders
    • Handin R.I. et al (eds), pp. Philadelphia, PA: Lippincott Williams and Wilkins
    • Vulliamy TJ, Luzzatto L, (2003) Glucose-6-phosphate dehydrogenase deficiency and related disorders. In: Blood: Principles and Practice of Hematology, Handin RI, et al (eds), pp 1921-1950. Philadelphia, PA: Lippincott Williams and Wilkins
    • (2003) Blood: Principles and Practice of Hematology , pp. 1921-1950
    • Vulliamy, T.J.1    Luzzatto, L.2
  • 73
    • 34447626095 scopus 로고    scopus 로고
    • SIRT2 deacetylates FOXO3a in response to oxidative stress and caloric restriction
    • Wang F, Nguyen M, Qin FX, Tong Q, (2007) SIRT2 deacetylates FOXO3a in response to oxidative stress and caloric restriction. Aging Cell 6: 505-514
    • (2007) Aging Cell , vol.6 , pp. 505-514
    • Wang, F.1    Nguyen, M.2    Qin, F.X.3    Tong, Q.4
  • 74
    • 33747880180 scopus 로고    scopus 로고
    • Functional properties of two mutants of human glucose 6-phosphate dehydrogenase, R393G and R393H, corresponding to the clinical variants G6PD Wisconsin and Nashville
    • Wang XT, Lam VM, Engel PC, (2006) Functional properties of two mutants of human glucose 6-phosphate dehydrogenase, R393G and R393H, corresponding to the clinical variants G6PD Wisconsin and Nashville. Biochim Biophys Acta 1762: 767-774
    • (2006) Biochim Biophys Acta , vol.1762 , pp. 767-774
    • Wang, X.T.1    Lam, V.M.2    Engel, P.C.3
  • 75
    • 67651111819 scopus 로고    scopus 로고
    • Clinical mutants of human glucose 6-phosphate dehydrogenase: Impairment of NADP(+) binding affects both folding and stability
    • Wang XT, Engel PC, (2009) Clinical mutants of human glucose 6-phosphate dehydrogenase: impairment of NADP(+) binding affects both folding and stability. Biochim Biophys Acta 1792: 804-809
    • (2009) Biochim Biophys Acta , vol.1792 , pp. 804-809
    • Wang, X.T.1    Engel, P.C.2
  • 76
    • 26844519964 scopus 로고    scopus 로고
    • Diabetes causes inhibition of glucose-6-phosphate dehydrogenase via activation of PKA, which contributes to oxidative stress in rat kidney cortex
    • Xu Y, Osborne BW, Stanton RC, (2005) Diabetes causes inhibition of glucose-6-phosphate dehydrogenase via activation of PKA, which contributes to oxidative stress in rat kidney cortex. Am J Physiol Renal Physiol 289: F1040-F1047
    • (2005) Am J Physiol Renal Physiol , vol.289
    • Xu, Y.1    Osborne, B.W.2    Stanton, R.C.3
  • 77
    • 76149131708 scopus 로고    scopus 로고
    • Glucose-6-phosphate dehydrogenase-deficient mice have increased renal oxidative stress and increased albuminuria
    • Xu Y, Zhang Z, Hu J, Stillman IE, Leopold JA, Handy DE, Loscalzo J, Stanton RC, (2010) Glucose-6-phosphate dehydrogenase-deficient mice have increased renal oxidative stress and increased albuminuria. FASEB J 24: 609-616
    • (2010) FASEB J , vol.24 , pp. 609-616
    • Xu, Y.1    Zhang, Z.2    Hu, J.3    Stillman, I.E.4    Leopold, J.A.5    Handy, D.E.6    Loscalzo, J.7    Stanton, R.C.8
  • 78
    • 0034704167 scopus 로고    scopus 로고
    • High glucose inhibits glucose-6-phosphate dehydrogenase via cAMP in aortic endothelial cells
    • Zhang Z, Apse K, Pang J, Stanton RC, (2000) High glucose inhibits glucose-6-phosphate dehydrogenase via cAMP in aortic endothelial cells. J Biol Chem 275: 40042-40047
    • (2000) J Biol Chem , vol.275 , pp. 40042-40047
    • Zhang, Z.1    Apse, K.2    Pang, J.3    Stanton, R.C.4
  • 80
    • 1542298916 scopus 로고    scopus 로고
    • Structure and substrate binding properties of cobB, a Sir2 homolog protein deacetylase from Escherichia coli
    • Zhao K, Chai X, Marmorstein R, (2004) Structure and substrate binding properties of cobB, a Sir2 homolog protein deacetylase from Escherichia coli. J Mol Biol 337: 731-741
    • (2004) J Mol Biol , vol.337 , pp. 731-741
    • Zhao, K.1    Chai, X.2    Marmorstein, R.3
  • 82
    • 81155155536 scopus 로고    scopus 로고
    • The QKI-PLP pathway controls SIRT2 abundance in CNS myelin
    • Zhu H, Zhao L, Wang E, Dimova N, Liu G, Feng Y, Cambi F, (2012) The QKI-PLP pathway controls SIRT2 abundance in CNS myelin. Glia 60: 69-82
    • (2012) Glia , vol.60 , pp. 69-82
    • Zhu, H.1    Zhao, L.2    Wang, E.3    Dimova, N.4    Liu, G.5    Feng, Y.6    Cambi, F.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.