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Volumn 45, Issue 6, 2010, Pages 395-399

NAD+ and metabolic regulation of age-related proteoxicity: A possible role for methylglyoxal?

Author keywords

Aging; Altered proteins; Glycation; Glycerol; Glycolysis; Mitochondria; NADH; Oxaloacetate; Triose phosphates

Indexed keywords

GLUCOSE; GLYCEROL; METHYLGLYOXAL; NICOTINAMIDE ADENINE DINUCLEOTIDE; OXALOACETIC ACID; REACTIVE OXYGEN METABOLITE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE;

EID: 77952542221     PISSN: 05315565     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.exger.2010.03.006     Document Type: Note
Times cited : (9)

References (104)
  • 3
    • 77953251777 scopus 로고    scopus 로고
    • Protein modification and replicative senescence of WI-38 human embryonic fibroblasts. Aging Cell, in press. doi
    • Ahmed, E.K., Rogowska-Wrzesinska, A., Roepstorlt, P., Bulteau, A-M., Friguet, B. 2010. Protein modification and replicative senescence of WI-38 human embryonic fibroblasts. Aging Cell, in press. doi:. doi:10.1111/j.1474-9726.2010.00555.x.
    • (2010)
    • Ahmed, E.K.1    Rogowska-Wrzesinska, A.2    Roepstorlt, P.3    Bulteau, A.M.4    Friguet, B.5
  • 5
    • 38349130508 scopus 로고    scopus 로고
    • Dynamic regulation of PGC-1α localization and turnover implicates mitochondrial adaptation in caloric restriction and the stress response
    • Anderson R.M., Barger J.L., Edwards M.G., Braun K.H., O'Conner C.E., Prolla T.A., Weindruch R. Dynamic regulation of PGC-1α localization and turnover implicates mitochondrial adaptation in caloric restriction and the stress response. Aging Cell 2008, 7:101-111.
    • (2008) Aging Cell , vol.7 , pp. 101-111
    • Anderson, R.M.1    Barger, J.L.2    Edwards, M.G.3    Braun, K.H.4    O'Conner, C.E.5    Prolla, T.A.6    Weindruch, R.7
  • 6
    • 77952548478 scopus 로고    scopus 로고
    • Metabolic reprogramming, caloric restriction and aging. Trends Endocrinol. Metab., in press. doi
    • Anderson, R.M., Weindruch, R. 2010. Metabolic reprogramming, caloric restriction and aging. Trends Endocrinol. Metab., in press. doi:. doi:10.1016/j.bbapap.2009.09.030.
    • (2010)
    • Anderson, R.M.1    Weindruch, R.2
  • 8
    • 77953247010 scopus 로고    scopus 로고
    • Neuronal expression of a single-subunit yeast NADH-ubiquinone oxidoreducatse (Ndi1) extends Drosophila lifespan. Aging Cell, PMID: 20089120, in press
    • Bahadorani, S., Cho, J., Lo, Jr. T., Contreras, H., Lawal, H.O., Krantz, D.E., Bradley, T.J., Walker, D.W. 2010. Neuronal expression of a single-subunit yeast NADH-ubiquinone oxidoreducatse (Ndi1) extends Drosophila lifespan. Aging Cell, PMID: 20089120, in press.
    • (2010)
    • Bahadorani, S.1    Cho, J.2    Lo, Jr.T.3    Contreras, H.4    Lawal, H.O.5    Krantz, D.E.6    Bradley, T.J.7    Walker, D.W.8
  • 9
    • 34250647400 scopus 로고    scopus 로고
    • Mitochondrial oxygen consumption and reactive oxygen species production are independently modulated: implications for aging studies
    • Barja G. Mitochondrial oxygen consumption and reactive oxygen species production are independently modulated: implications for aging studies. Rejuven. Res. 2007, 10:215-224.
    • (2007) Rejuven. Res. , vol.10 , pp. 215-224
    • Barja, G.1
  • 10
    • 37849045126 scopus 로고    scopus 로고
    • Exercise and immobilization in aging animals: the involvement of oxidative stress and NF-κB activation
    • Bar-Shai M., Carmeli E., Ljubuncic P., Reznick A.Z. Exercise and immobilization in aging animals: the involvement of oxidative stress and NF-κB activation. Free Rad. Biol.Med. 2008, 44:202-214.
    • (2008) Free Rad. Biol.Med. , vol.44 , pp. 202-214
    • Bar-Shai, M.1    Carmeli, E.2    Ljubuncic, P.3    Reznick, A.Z.4
  • 11
    • 35948982621 scopus 로고    scopus 로고
    • The role of autophagy in aging its essential part in the anti-aging mechanism of caloric restriction
    • Bergamini E., Cavallini G., Donati A., Gori Z. The role of autophagy in aging its essential part in the anti-aging mechanism of caloric restriction. Ann. N.Y. Acad. Sci. 2007, 1114:69-78.
    • (2007) Ann. N.Y. Acad. Sci. , vol.1114 , pp. 69-78
    • Bergamini, E.1    Cavallini, G.2    Donati, A.3    Gori, Z.4
  • 12
    • 33947574775 scopus 로고    scopus 로고
    • Reduced TOR signalling extends chronological life span via increased respiration and upregulated mitochondrial gene expression
    • Bonawitz N.D., Chatenay-Lapointe M., Pan Y., Shadel G.S. Reduced TOR signalling extends chronological life span via increased respiration and upregulated mitochondrial gene expression. Cell Metab. 2007, 5:265-277.
    • (2007) Cell Metab. , vol.5 , pp. 265-277
    • Bonawitz, N.D.1    Chatenay-Lapointe, M.2    Pan, Y.3    Shadel, G.S.4
  • 13
    • 17144429302 scopus 로고    scopus 로고
    • Calorie restriction, sirt1 and metabolism: understanding longevity
    • Bordone L., Guarente L. Calorie restriction, sirt1 and metabolism: understanding longevity. Nature Revs. Mol. Cell Biol. 2005, 6:298-305.
    • (2005) Nature Revs. Mol. Cell Biol. , vol.6 , pp. 298-305
    • Bordone, L.1    Guarente, L.2
  • 14
    • 76749126321 scopus 로고    scopus 로고
    • Epigenetic oxidative redox shift (EORS) theory of aging unifies the free radical and insulin signalling theories
    • Brewer G.J. Epigenetic oxidative redox shift (EORS) theory of aging unifies the free radical and insulin signalling theories. Exp. Gerontol. 2009, 45:173-179.
    • (2009) Exp. Gerontol. , vol.45 , pp. 173-179
    • Brewer, G.J.1
  • 15
    • 50049091026 scopus 로고    scopus 로고
    • Repeated bouts of aerobic exercise lead to reductions in skeletal muscle free radical generation and nuclear factor κβ activation
    • Brooks S.V., Vasilaki A., Larkin L.M., McArdle A., Jackson M.J. Repeated bouts of aerobic exercise lead to reductions in skeletal muscle free radical generation and nuclear factor κβ activation. J. Physiol. 2008, 586:3979-3990.
    • (2008) J. Physiol. , vol.586 , pp. 3979-3990
    • Brooks, S.V.1    Vasilaki, A.2    Larkin, L.M.3    McArdle, A.4    Jackson, M.J.5
  • 16
    • 34447343125 scopus 로고    scopus 로고
    • Reduced oxidant stress and extended lifespan in mice exposed to a low glycotoxin diet. Association with increased AGER1 expression
    • Cai W., He J.C., Zhu L., Chen X., Wallenstein S., Striker G.E., Vlassara H. Reduced oxidant stress and extended lifespan in mice exposed to a low glycotoxin diet. Association with increased AGER1 expression. Am. J. Pathol. 2007, 170:1893-1902.
    • (2007) Am. J. Pathol. , vol.170 , pp. 1893-1902
    • Cai, W.1    He, J.C.2    Zhu, L.3    Chen, X.4    Wallenstein, S.5    Striker, G.E.6    Vlassara, H.7
  • 17
  • 19
    • 33751316738 scopus 로고    scopus 로고
    • Drosophila model of human inherited triosephosphate isomerase deficiency glycolytic enzymopathy
    • Celotto A.M., Frank A.C., Seigle J.L., Palladino M.J. Drosophila model of human inherited triosephosphate isomerase deficiency glycolytic enzymopathy. Genetics 2006, 174:1237-1246.
    • (2006) Genetics , vol.174 , pp. 1237-1246
    • Celotto, A.M.1    Frank, A.C.2    Seigle, J.L.3    Palladino, M.J.4
  • 21
    • 60249101187 scopus 로고    scopus 로고
    • Effects of aminoguanine on tissue oxidative stress induced by hindlimb unloading in rats
    • Chowdhury P., Soulsby M.E., Scott J.L. Effects of aminoguanine on tissue oxidative stress induced by hindlimb unloading in rats. Ann Clin. Lab. Sci. 2009, 39:64-70.
    • (2009) Ann Clin. Lab. Sci. , vol.39 , pp. 64-70
    • Chowdhury, P.1    Soulsby, M.E.2    Scott, J.L.3
  • 24
    • 70350069069 scopus 로고    scopus 로고
    • Live fast, die young: new lessons in mammalian longevity
    • Cox L.S. Live fast, die young: new lessons in mammalian longevity. Rejuven. Res. 2009, 12:1-6.
    • (2009) Rejuven. Res. , vol.12 , pp. 1-6
    • Cox, L.S.1
  • 25
    • 73949127970 scopus 로고    scopus 로고
    • Increased longevity through caloric restriction or rapamycin feeding in mammals: common mechanisms for common outcomes?
    • Cox L.S., Mattison J.A. Increased longevity through caloric restriction or rapamycin feeding in mammals: common mechanisms for common outcomes?. Aging Cell 2009, 8:607-613.
    • (2009) Aging Cell , vol.8 , pp. 607-613
    • Cox, L.S.1    Mattison, J.A.2
  • 26
    • 36749081539 scopus 로고    scopus 로고
    • MTOR controls mitochondrial oxidative function through a YY1-PGC-1α transcription complex
    • Cunningham J.T., Rodgers J.T., Arlow D.H., Vazquez F., Mootha V.K., Puigserver P. mTOR controls mitochondrial oxidative function through a YY1-PGC-1α transcription complex. Nature 2007, 450:736-740.
    • (2007) Nature , vol.450 , pp. 736-740
    • Cunningham, J.T.1    Rodgers, J.T.2    Arlow, D.H.3    Vazquez, F.4    Mootha, V.K.5    Puigserver, P.6
  • 27
    • 43449126527 scopus 로고    scopus 로고
    • Free radical generation by methylglyoxal in tissues
    • Desai K.M., Wu L. Free radical generation by methylglyoxal in tissues. Drug Metab. Drug Interact. 2008, 23:151-173.
    • (2008) Drug Metab. Drug Interact. , vol.23 , pp. 151-173
    • Desai, K.M.1    Wu, L.2
  • 28
    • 71949090833 scopus 로고    scopus 로고
    • Mitochondrial trafficking of APP and alpha-synuclein: relevance to mitochondrial dysfunction in Alzheimer's and Parkinson's diseases
    • Devi L., Anandatheerthavarada K. Mitochondrial trafficking of APP and alpha-synuclein: relevance to mitochondrial dysfunction in Alzheimer's and Parkinson's diseases. Biochim. Biophys. Acta 2009, 1802:11-19.
    • (2009) Biochim. Biophys. Acta , vol.1802 , pp. 11-19
    • Devi, L.1    Anandatheerthavarada, K.2
  • 30
    • 4444297565 scopus 로고    scopus 로고
    • Mitochondria: are they the seat of senescence?
    • Fridovich I. Mitochondria: are they the seat of senescence?. Aging Cell 2004, 3:13-16.
    • (2004) Aging Cell , vol.3 , pp. 13-16
    • Fridovich, I.1
  • 31
    • 33750052263 scopus 로고    scopus 로고
    • Wasted away, a drosophila mutation in triosephosphate isomerase, causes paralysis, neurodegeneration, and early death
    • Gnerer J.P., Kreber R.A., Ganetzky B. Wasted away, a drosophila mutation in triosephosphate isomerase, causes paralysis, neurodegeneration, and early death. Proc. Natl. Acad. Sci. USA 2006, 103:14987-14993.
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , pp. 14987-14993
    • Gnerer, J.P.1    Kreber, R.A.2    Ganetzky, B.3
  • 35
    • 73449114300 scopus 로고    scopus 로고
    • Nicotinamide adenine dinucleotide extends the lifespan of Caenorhabditis elegans mediated by sir-2 1 and daf-16
    • Hashimoto T., Horikawa M., Nomura T., Sakamoto K. Nicotinamide adenine dinucleotide extends the lifespan of Caenorhabditis elegans mediated by sir-2 1 and daf-16. Biogerontology 2010, 11:31-43.
    • (2010) Biogerontology , vol.11 , pp. 31-43
    • Hashimoto, T.1    Horikawa, M.2    Nomura, T.3    Sakamoto, K.4
  • 36
    • 67349249403 scopus 로고    scopus 로고
    • The bioenergetic and antioxidant status of neurons is controlled by continuous degradation of a key glycolytic enzyme by APC/C-Cdh1
    • Herrero-Mendez A., Almeida A., Fernandez E., Mastre C., Moncada S., Bolanos J.P. The bioenergetic and antioxidant status of neurons is controlled by continuous degradation of a key glycolytic enzyme by APC/C-Cdh1. Nature Cell Biol. 2009, 11:747-752.
    • (2009) Nature Cell Biol. , vol.11 , pp. 747-752
    • Herrero-Mendez, A.1    Almeida, A.2    Fernandez, E.3    Mastre, C.4    Moncada, S.5    Bolanos, J.P.6
  • 37
    • 33646793360 scopus 로고    scopus 로고
    • Accumulation of altered proteins and ageing: causes and effects
    • Hipkiss A.R. Accumulation of altered proteins and ageing: causes and effects. Exptl. Gerontol. 2006, 41:464-473.
    • (2006) Exptl. Gerontol. , vol.41 , pp. 464-473
    • Hipkiss, A.R.1
  • 38
    • 28344445558 scopus 로고    scopus 로고
    • Caloric restriction and ageing - is glycolysis the problem?
    • Hipkiss A.R. Caloric restriction and ageing - is glycolysis the problem?. Mech. Ageing Dev. 2006, 127:8-15.
    • (2006) Mech. Ageing Dev. , vol.127 , pp. 8-15
    • Hipkiss, A.R.1
  • 39
    • 38049056733 scopus 로고    scopus 로고
    • Energy metabolism, altered proteins, siruins and ageing: converging mechanisms?
    • Hipkiss A.R. Energy metabolism, altered proteins, siruins and ageing: converging mechanisms?. Biogerontology 2008, 9:49-55.
    • (2008) Biogerontology , vol.9 , pp. 49-55
    • Hipkiss, A.R.1
  • 40
    • 70349763406 scopus 로고    scopus 로고
    • + availability and proteotoxicity
    • + availability and proteotoxicity. Neuromol. Med. 2009, 11:97-100.
    • (2009) Neuromol. Med. , vol.11 , pp. 97-100
    • Hipkiss, A.R.1
  • 41
    • 63649121321 scopus 로고    scopus 로고
    • Regulation by exercise of skeletal muscle content of mitochondria and Glut4. J. Physiol. Pharmacol. 59 (Supp. 7)
    • Holloszy, J.O. 2008. Regulation by exercise of skeletal muscle content of mitochondria and Glut4. J. Physiol. Pharmacol. 59 (Supp. 7), 5-18.
    • (2008) , pp. 5-18
    • Holloszy, J.O.1
  • 42
    • 67651237067 scopus 로고    scopus 로고
    • Mechanisms of exercise-induced mitochondrial biogenesis in skeletal muscle
    • Hood D.A. Mechanisms of exercise-induced mitochondrial biogenesis in skeletal muscle. Appl. Physiol. Nutl.Metab. 2009, 34:465-472.
    • (2009) Appl. Physiol. Nutl.Metab. , vol.34 , pp. 465-472
    • Hood, D.A.1
  • 43
    • 63149089930 scopus 로고    scopus 로고
    • The NAD world: a new systematic regulatory network for metabolism and aging-sirt1, systemic NAD biosynthesis, and their importance
    • Imai S.-I. The NAD world: a new systematic regulatory network for metabolism and aging-sirt1, systemic NAD biosynthesis, and their importance. Cell Biochem. Biophys. 2009, 53:65-74.
    • (2009) Cell Biochem. Biophys. , vol.53 , pp. 65-74
    • Imai, S.-I.1
  • 44
    • 5444262718 scopus 로고    scopus 로고
    • Yeast replicative life span - the mitochondrial connection
    • Jazwinski S.M. Yeast replicative life span - the mitochondrial connection. FEMS Yeast Res. 2004, 5:119-125.
    • (2004) FEMS Yeast Res. , vol.5 , pp. 119-125
    • Jazwinski, S.M.1
  • 47
    • 70350365110 scopus 로고    scopus 로고
    • Glucose shortens the life span of C. elegans by downregulating DAF-16/FOXO activity and aquaporin gene expression
    • Lee S.-J., Murphy C.T., Kenyon C. Glucose shortens the life span of C. elegans by downregulating DAF-16/FOXO activity and aquaporin gene expression. Cell Metab. 2009, 10:379-391.
    • (2009) Cell Metab. , vol.10 , pp. 379-391
    • Lee, S.-J.1    Murphy, C.T.2    Kenyon, C.3
  • 48
    • 30044440497 scopus 로고    scopus 로고
    • Sirt1: a metabolic master switch that modulates lifespan
    • Leibiger I., Berggren P.-O. Sirt1: a metabolic master switch that modulates lifespan. Nature Med. 2006, 12:34-36.
    • (2006) Nature Med. , vol.12 , pp. 34-36
    • Leibiger, I.1    Berggren, P.-O.2
  • 49
    • 69949084211 scopus 로고    scopus 로고
    • Protein aggregation as a paradigm of aging
    • Lindner A.B., Demarez A. Protein aggregation as a paradigm of aging. Biochim. Biophys. Acta 2009, 1790:980-996.
    • (2009) Biochim. Biophys. Acta , vol.1790 , pp. 980-996
    • Lindner, A.B.1    Demarez, A.2
  • 50
    • 0347128279 scopus 로고    scopus 로고
    • Calorie restriction extends yeast life span by lowering the level of NADH
    • Lin S.-J., Ford E., Haigis M., Liszt G., Guarente L. Calorie restriction extends yeast life span by lowering the level of NADH. Genes Dev. 2004, 18:12-16.
    • (2004) Genes Dev. , vol.18 , pp. 12-16
    • Lin, S.-J.1    Ford, E.2    Haigis, M.3    Liszt, G.4    Guarente, L.5
  • 51
    • 0037376665 scopus 로고    scopus 로고
    • Nicotinamide adenine dinucleotide, a metabolic regulator of transcription, longevity and disease
    • Lin S.-J., Guarente L. Nicotinamide adenine dinucleotide, a metabolic regulator of transcription, longevity and disease. Curr. Opin. Cell Biol. 2003, 15:1-6.
    • (2003) Curr. Opin. Cell Biol. , vol.15 , pp. 1-6
    • Lin, S.-J.1    Guarente, L.2
  • 52
    • 57649217303 scopus 로고    scopus 로고
    • + depletion protects neurons against excitoxicity: bioenergetic effects of mild mitochondrial uncoupling and caloric restriction
    • + depletion protects neurons against excitoxicity: bioenergetic effects of mild mitochondrial uncoupling and caloric restriction. Ann. N.Y. Acad. Sci. 2008, 1147:275-282.
    • (2008) Ann. N.Y. Acad. Sci. , vol.1147 , pp. 275-282
    • Liu, D.1    Pitts, M.2    Mattson, M.P.3
  • 53
    • 33746228121 scopus 로고    scopus 로고
    • Sirtuins in aging and age-related disease
    • Longo V.D., Kennedy B.K. Sirtuins in aging and age-related disease. Cell 2006, 126:257-268.
    • (2006) Cell , vol.126 , pp. 257-268
    • Longo, V.D.1    Kennedy, B.K.2
  • 54
    • 77953288455 scopus 로고    scopus 로고
    • Regulation of yeast sirtuins by NAD+ metabolism and calorie restriction. Biochim.Biophys Acta, in press. doi
    • Lu, S-P., Lin, S-J. 2009. Regulation of yeast sirtuins by NAD+ metabolism and calorie restriction. Biochim.Biophys Acta, in press. doi:. doi:10.1016/j.bbapap.2009.09.030.
    • (2009)
    • Lu, S-P.1    Lin, S-J.2
  • 55
    • 33748540014 scopus 로고    scopus 로고
    • Caloric restriction and intermittent feeding: two potential diets for successful brain aging
    • Martin B., Mattson M.P., Maudsley S. Caloric restriction and intermittent feeding: two potential diets for successful brain aging. Ageing Res. Rev. 2006, 5:332-353.
    • (2006) Ageing Res. Rev. , vol.5 , pp. 332-353
    • Martin, B.1    Mattson, M.P.2    Maudsley, S.3
  • 56
    • 2642553131 scopus 로고    scopus 로고
    • Ageing: mice and mitochondria
    • Martin G.M., Loeb L.A. Ageing: mice and mitochondria. Nature 2004, 429:357-359.
    • (2004) Nature , vol.429 , pp. 357-359
    • Martin, G.M.1    Loeb, L.A.2
  • 57
    • 21244475897 scopus 로고    scopus 로고
    • Effect of every other day feeding diet on gene expression in normal and long-lived Ames dwarf mice
    • Masternak M.M., Al-Regaiey K.A., Bonkowski M.S., Panici J.A., Bartke A. Effect of every other day feeding diet on gene expression in normal and long-lived Ames dwarf mice. Exp. Gerontol. 2005, 40:491-497.
    • (2005) Exp. Gerontol. , vol.40 , pp. 491-497
    • Masternak, M.M.1    Al-Regaiey, K.A.2    Bonkowski, M.S.3    Panici, J.A.4    Bartke, A.5
  • 58
    • 14644390872 scopus 로고    scopus 로고
    • Beneficial effects of intermittent feeding and caloric restriction on the cardiovascular and cerebrovascular systems
    • Mattson M.P., Wan R. Beneficial effects of intermittent feeding and caloric restriction on the cardiovascular and cerebrovascular systems. J. Nutr. Biochem. 2005, 16:129-137.
    • (2005) J. Nutr. Biochem. , vol.16 , pp. 129-137
    • Mattson, M.P.1    Wan, R.2
  • 59
    • 34249704408 scopus 로고    scopus 로고
    • Participation of reactive oxygen species in muscle damage produced by hypokinesis
    • Miller E., Rutkowski M., Mrowicka M., Matuszewski T. Participation of reactive oxygen species in muscle damage produced by hypokinesis. Pol.Merkur. Lekarski. 2007, 22:314-317.
    • (2007) Pol.Merkur. Lekarski. , vol.22 , pp. 314-317
    • Miller, E.1    Rutkowski, M.2    Mrowicka, M.3    Matuszewski, T.4
  • 60
    • 56849084137 scopus 로고    scopus 로고
    • Mitochondrial turnover in liver is fast in vivo and is accelerated by dietary restriction: application of a simple dynamic model
    • Miwa S., Lawless C., von Zglinicki T. Mitochondrial turnover in liver is fast in vivo and is accelerated by dietary restriction: application of a simple dynamic model. Aging Cell 2008, 7:920-923.
    • (2008) Aging Cell , vol.7 , pp. 920-923
    • Miwa, S.1    Lawless, C.2    von Zglinicki, T.3
  • 61
    • 71649103265 scopus 로고    scopus 로고
    • Methylglyoxal augments intracellular oxidative stress in human aortic endothelial cells
    • Miyazawa N., Abe M., Souma T., Tanemoto M., Abe T., nakayama M., Ito S. Methylglyoxal augments intracellular oxidative stress in human aortic endothelial cells. Free Rad Res. 2009, 44:101-107.
    • (2009) Free Rad Res. , vol.44 , pp. 101-107
    • Miyazawa, N.1    Abe, M.2    Souma, T.3    Tanemoto, M.4    Abe, T.5    nakayama, M.6    Ito, S.7
  • 63
    • 44849094781 scopus 로고    scopus 로고
    • Proteotoxic stress and inducible chaperone networks in neurodegenerative disease and aging
    • Morimoto R.I. Proteotoxic stress and inducible chaperone networks in neurodegenerative disease and aging. Genes Dev. 2008, 22:1427-1428.
    • (2008) Genes Dev. , vol.22 , pp. 1427-1428
    • Morimoto, R.I.1
  • 66
    • 58149314211 scopus 로고    scopus 로고
    • Parkin is recruited selectively to impaired mitochondria and promote their autophagy
    • Norendra D., Tanaka A., Suen D.-F., Youle R.J. Parkin is recruited selectively to impaired mitochondria and promote their autophagy. J. Cell Biol. 2008, 183:795-803.
    • (2008) J. Cell Biol. , vol.183 , pp. 795-803
    • Norendra, D.1    Tanaka, A.2    Suen, D.-F.3    Youle, R.J.4
  • 67
    • 72149120003 scopus 로고    scopus 로고
    • Triosephosphate isomerase deficiency: new insights into an enigmatic disease
    • Orosz F., Olah J., Oveadl J. Triosephosphate isomerase deficiency: new insights into an enigmatic disease. Biochim. Biophys. Acta 2009, 1792:1168-1174.
    • (2009) Biochim. Biophys. Acta , vol.1792 , pp. 1168-1174
    • Orosz, F.1    Olah, J.2    Oveadl, J.3
  • 68
    • 0036487333 scopus 로고    scopus 로고
    • Rat hindlimb unloading: soleus and extensor digitorum longus histochemistry, mitochondrial DNA content and mitochondrial deletions
    • Pesce V., Cormio A., Fracasso F., Lezze A.M., Cantatore P., Gadaleta M.N. Rat hindlimb unloading: soleus and extensor digitorum longus histochemistry, mitochondrial DNA content and mitochondrial deletions. Biosci. Rep. 2002, 22:115-125.
    • (2002) Biosci. Rep. , vol.22 , pp. 115-125
    • Pesce, V.1    Cormio, A.2    Fracasso, F.3    Lezze, A.M.4    Cantatore, P.5    Gadaleta, M.N.6
  • 70
    • 70349422148 scopus 로고    scopus 로고
    • Role of mitochondrial dysfunction in the pathogenesis of Huntington's disease
    • Quintanilla R.A., Johnson G.V. Role of mitochondrial dysfunction in the pathogenesis of Huntington's disease. Brain Res. Bull. 2009, 80:242-247.
    • (2009) Brain Res. Bull. , vol.80 , pp. 242-247
    • Quintanilla, R.A.1    Johnson, G.V.2
  • 71
    • 53849092368 scopus 로고    scopus 로고
    • Dicarbonyls linked to damage to the powerhouse: glycation of mitochondrial proteins and oxidative stress
    • Rabbani N., Thornalley P.J. Dicarbonyls linked to damage to the powerhouse: glycation of mitochondrial proteins and oxidative stress. Biochem. Soc. Trans. 2008, 38:1045-1050.
    • (2008) Biochem. Soc. Trans. , vol.38 , pp. 1045-1050
    • Rabbani, N.1    Thornalley, P.J.2
  • 72
    • 42549117517 scopus 로고    scopus 로고
    • 2008b.The dicarbonyl proteome: proteins susceptible to dicarbonyl glycation at functional sites in health, aging and disease. Ann. NY. Acad. Sci. 1126
    • Rabbani, N., Thornalley, P.J. 2008b.The dicarbonyl proteome: proteins susceptible to dicarbonyl glycation at functional sites in health, aging and disease. Ann. NY. Acad. Sci. 1126, 124-127.
    • Rabbani, N.1    Thornalley, P.J.2
  • 73
    • 68149148549 scopus 로고    scopus 로고
    • Amyloid-beta leads to impaired cellular respiration, energy production and mitochondrial electron chain complex activities in human neuroblastoma cells
    • Rhein V., Baysang G., Rao S., Meir F., Bonert A., Muller-Spahn F., Eckert A. Amyloid-beta leads to impaired cellular respiration, energy production and mitochondrial electron chain complex activities in human neuroblastoma cells. Cell Mol. Neurobiol. 2009, 29:1063-1071.
    • (2009) Cell Mol. Neurobiol. , vol.29 , pp. 1063-1071
    • Rhein, V.1    Baysang, G.2    Rao, S.3    Meir, F.4    Bonert, A.5    Muller-Spahn, F.6    Eckert, A.7
  • 75
    • 67349273985 scopus 로고    scopus 로고
    • SIRT1: regulation of longevity via autophagy
    • Salminen A., Kaamiranta K. SIRT1: regulation of longevity via autophagy. Cell Signall. 2009, 21:1356-1360.
    • (2009) Cell Signall. , vol.21 , pp. 1356-1360
    • Salminen, A.1    Kaamiranta, K.2
  • 76
    • 76049118700 scopus 로고    scopus 로고
    • Impairment of mitochondrial respiratory chain activity in aortic endothelial cells induced by glycated low-density lipoprotein
    • Sangle G.V., Chowdhury S.K.R., Xie X., Stelmack G.L., Halayko G.L., Shen G.X. Impairment of mitochondrial respiratory chain activity in aortic endothelial cells induced by glycated low-density lipoprotein. Free Red. Biol. Med. 2010, 48:781-790.
    • (2010) Free Red. Biol. Med. , vol.48 , pp. 781-790
    • Sangle, G.V.1    Chowdhury, S.K.R.2    Xie, X.3    Stelmack, G.L.4    Halayko, G.L.5    Shen, G.X.6
  • 77
    • 0038199601 scopus 로고    scopus 로고
    • The role of mitochondrial oxidative stress in aging
    • Sastre J., Pallardo F.V., Vina J. The role of mitochondrial oxidative stress in aging. Free Rad. Biol. Med. 2003, 35:1-8.
    • (2003) Free Rad. Biol. Med. , vol.35 , pp. 1-8
    • Sastre, J.1    Pallardo, F.V.2    Vina, J.3
  • 79
    • 0034431493 scopus 로고    scopus 로고
    • Triosephosphate isomerase deficiency: historical perspectives and molecular aspects
    • Schneider A.S. Triosephosphate isomerase deficiency: historical perspectives and molecular aspects. Baillieres Best Pract.Res. Clin. Haematol. 2000, 13:119-140.
    • (2000) Baillieres Best Pract.Res. Clin. Haematol. , vol.13 , pp. 119-140
    • Schneider, A.S.1
  • 80
    • 33749662944 scopus 로고    scopus 로고
    • Protein modification in aging: an update
    • Schoneich C. Protein modification in aging: an update. Exp. Gerontol. 2006, 41:807-813.
    • (2006) Exp. Gerontol. , vol.41 , pp. 807-813
    • Schoneich, C.1
  • 81
    • 34748850786 scopus 로고    scopus 로고
    • Glucose restriction extends Caenorhabditis elegans lifespan by inducing mitochondrial respiration and increasing oxidative stress
    • Schulz T.J., Zarse K., Voigt A., Urban N., Birringer M., Ristow M. Glucose restriction extends Caenorhabditis elegans lifespan by inducing mitochondrial respiration and increasing oxidative stress. Cell Metab. 2007, 6:280-293.
    • (2007) Cell Metab. , vol.6 , pp. 280-293
    • Schulz, T.J.1    Zarse, K.2    Voigt, A.3    Urban, N.4    Birringer, M.5    Ristow, M.6
  • 82
    • 33644959683 scopus 로고    scopus 로고
    • Mitochondrial respiration and reactive oxygen species in mitochondrial aging mutants
    • Sedensky M.M., Morgan P.G. Mitochondrial respiration and reactive oxygen species in mitochondrial aging mutants. Expt. Gerontol. 2006, 41:237-245.
    • (2006) Expt. Gerontol. , vol.41 , pp. 237-245
    • Sedensky, M.M.1    Morgan, P.G.2
  • 83
    • 61849147844 scopus 로고    scopus 로고
    • Dicarbonyl-induced accelerated aging in vitro in human skin fibroblasts
    • Sejersen H., Rattan S.I. Dicarbonyl-induced accelerated aging in vitro in human skin fibroblasts. Biogerontology 2009, 10:203-211.
    • (2009) Biogerontology , vol.10 , pp. 203-211
    • Sejersen, H.1    Rattan, S.I.2
  • 84
    • 0032032578 scopus 로고    scopus 로고
    • Overexpression of glyoxalase-1 in bovine endothelial cells inhibits intracellular advanced glycation endproduct formation and prevents hyperglycemia-induced increases in macromolecular endocytosis
    • Shinohara M., Thornalley P.J., Giardino I., Beisswenger P., Thorp S.R., Onorato J., Brownlee M. Overexpression of glyoxalase-1 in bovine endothelial cells inhibits intracellular advanced glycation endproduct formation and prevents hyperglycemia-induced increases in macromolecular endocytosis. J. Clin. Invest. 1998, 101:1142-1147.
    • (1998) J. Clin. Invest. , vol.101 , pp. 1142-1147
    • Shinohara, M.1    Thornalley, P.J.2    Giardino, I.3    Beisswenger, P.4    Thorp, S.R.5    Onorato, J.6    Brownlee, M.7
  • 85
    • 17244378783 scopus 로고    scopus 로고
    • Possible involvement of glutamic and/or aspartic residue(s) and requirement of mitochondrial integrity for the protective effect of creatine against inhibition of cardiac mitochondrial respiration by methyglyoxal
    • SinhaRoy S., Banerjee S., Ray M., Ray S. Possible involvement of glutamic and/or aspartic residue(s) and requirement of mitochondrial integrity for the protective effect of creatine against inhibition of cardiac mitochondrial respiration by methyglyoxal. Mol. Cell Biochem. 2005, 271:167-176.
    • (2005) Mol. Cell Biochem. , vol.271 , pp. 167-176
    • SinhaRoy, S.1    Banerjee, S.2    Ray, M.3    Ray, S.4
  • 86
    • 33646793493 scopus 로고    scopus 로고
    • Oxidative damage to proteins
    • Kluwer Academic Publishers., The Netherlands, T. von Zglinicki (Ed.)
    • Sitte N. Oxidative damage to proteins. Aging at the Molecular Level 2003, 27-45. Kluwer Academic Publishers., The Netherlands. T. von Zglinicki (Ed.).
    • (2003) Aging at the Molecular Level , pp. 27-45
    • Sitte, N.1
  • 87
    • 40649129442 scopus 로고    scopus 로고
    • Non-enzymic posttranslational protein modification in aging
    • Soskic V., Groebe K., Schrattenholz A. Non-enzymic posttranslational protein modification in aging. Exp. Gerontol. 2007, 43:247-257.
    • (2007) Exp. Gerontol. , vol.43 , pp. 247-257
    • Soskic, V.1    Groebe, K.2    Schrattenholz, A.3
  • 89
    • 0035039021 scopus 로고    scopus 로고
    • Protein oxidation in aging and age-related diseases
    • Stadtman E.R. Protein oxidation in aging and age-related diseases. Ann. N.Y. Acd. Sci 2001, 928:22-38.
    • (2001) Ann. N.Y. Acd. Sci , vol.928 , pp. 22-38
    • Stadtman, E.R.1
  • 90
    • 68949158352 scopus 로고    scopus 로고
    • The neurodegenerative mitochondriopathies. J. Alzheimer's Dis., PMID 19542616, in press
    • Swerdlow, RH. 2009. The neurodegenerative mitochondriopathies. J. Alzheimer's Dis., PMID 19542616, in press.
    • (2009)
    • Swerdlow, R.H.1
  • 91
    • 0042707790 scopus 로고    scopus 로고
    • Mitochondrial recycling and aging of cardiac myocytes: the role of autophagocytosis
    • Terman A., Dalen H., Eaton J.W., Neuzil J., Brunk U.T. Mitochondrial recycling and aging of cardiac myocytes: the role of autophagocytosis. Exp. Gerontol. 2003, 38:863-876.
    • (2003) Exp. Gerontol. , vol.38 , pp. 863-876
    • Terman, A.1    Dalen, H.2    Eaton, J.W.3    Neuzil, J.4    Brunk, U.T.5
  • 92
    • 38349050179 scopus 로고    scopus 로고
    • Proteasome modulates mitochondrial function during cellular senescence
    • Torres C.A., Perez V.I. Proteasome modulates mitochondrial function during cellular senescence. Free Rad Biol Med. 2008, 44:403-414.
    • (2008) Free Rad Biol Med. , vol.44 , pp. 403-414
    • Torres, C.A.1    Perez, V.I.2
  • 94
    • 43449094351 scopus 로고    scopus 로고
    • Protein and nucleotide damage by glyoxal and methylglyoxal in physiological systems - role in aging and disease
    • Thornalley P.J. Protein and nucleotide damage by glyoxal and methylglyoxal in physiological systems - role in aging and disease. Drug Metabol. Drug Interact. 2008, 23:125-150.
    • (2008) Drug Metabol. Drug Interact. , vol.23 , pp. 125-150
    • Thornalley, P.J.1
  • 95
    • 77952552497 scopus 로고    scopus 로고
    • Glycotoxins, carbonyl stress and relevance to diabetes and its complications. Physiol. Res., PMID 19537931, in press
    • Turk, Z. 2009. Glycotoxins, carbonyl stress and relevance to diabetes and its complications. Physiol. Res., PMID 19537931, in press.
    • (2009)
    • Turk, Z.1
  • 96
    • 13844299858 scopus 로고    scopus 로고
    • Live fast-live long? A commentary on a recent paper by Speakman et al
    • Van Voorhies W.A. Live fast-live long? A commentary on a recent paper by Speakman et al. Aging Cell 2004, 3:527-530.
    • (2004) Aging Cell , vol.3 , pp. 527-530
    • Van Voorhies, W.A.1
  • 97
    • 71549144730 scopus 로고    scopus 로고
    • Identifying advanced glycation end products as a major source of oxidants in aging: implications for the management and/or prevention of reduced renal function in elderly persons
    • Vlassara H., Uribarri J., Ferrucci L., Cai W., Torreggiani M., Post Zheng F., Striker G.E. Identifying advanced glycation end products as a major source of oxidants in aging: implications for the management and/or prevention of reduced renal function in elderly persons. Semin. Nephrol. 2009, 29:594-603.
    • (2009) Semin. Nephrol. , vol.29 , pp. 594-603
    • Vlassara, H.1    Uribarri, J.2    Ferrucci, L.3    Cai, W.4    Torreggiani, M.5    Post Zheng, F.6    Striker, G.E.7
  • 98
    • 64249090462 scopus 로고    scopus 로고
    • Methylglyoxal-induced mitochondrial dysfunction in vascular smooth muscle cells
    • Wang H., Liu J., Wu L. Methylglyoxal-induced mitochondrial dysfunction in vascular smooth muscle cells. Biochem. Pharmacol. 2009, 77:1709-1715.
    • (2009) Biochem. Pharmacol. , vol.77 , pp. 1709-1715
    • Wang, H.1    Liu, J.2    Wu, L.3
  • 99
    • 64949161526 scopus 로고    scopus 로고
    • Respiratory function decline and DNA mutation in mitochondria, oxidative stress and altered gene expression during aging
    • Wei Y-H., Wu S-B., Ma Y-S., Lee H-C. Respiratory function decline and DNA mutation in mitochondria, oxidative stress and altered gene expression during aging. Chang. Gung. Med. J. 2009, 32:113-132.
    • (2009) Chang. Gung. Med. J. , vol.32 , pp. 113-132
    • Wei, Y.-H.1    Wu, S.-B.2    Ma, Y.-S.3    Lee, H.-C.4
  • 100
    • 60749101582 scopus 로고    scopus 로고
    • Stress-induced regulation of the heat shock factor 1 by the deacetylase SIRT1
    • Westerheide S.D., Anckar J., Stevens S.M., Sistomen L., Morimoto R.I. Stress-induced regulation of the heat shock factor 1 by the deacetylase SIRT1. Science 2009, 32:1063-1066.
    • (2009) Science , vol.32 , pp. 1063-1066
    • Westerheide, S.D.1    Anckar, J.2    Stevens, S.M.3    Sistomen, L.4    Morimoto, R.I.5
  • 101
    • 74049134984 scopus 로고    scopus 로고
    • Oxaloacetate supplementation increases lifespan in C. elegans through an AMPK/FOXO-dependent pathway.
    • Williams D.S., Cash A., Hamamdam L., Diemer T. Oxaloacetate supplementation increases lifespan in C. elegans through an AMPK/FOXO-dependent pathway. Aging cell 2009, 8:765-768.
    • (2009) Aging cell , vol.8 , pp. 765-768
    • Williams, D.S.1    Cash, A.2    Hamamdam, L.3    Diemer, T.4
  • 102
    • 33646785765 scopus 로고    scopus 로고
    • Uncoupling protein homologs may provide a link between mitochondria, metabolism and lifespan
    • Wolkow C.A., Iser W.B. Uncoupling protein homologs may provide a link between mitochondria, metabolism and lifespan. Ageing Res. Revs. 2006, 5:196-208.
    • (2006) Ageing Res. Revs. , vol.5 , pp. 196-208
    • Wolkow, C.A.1    Iser, W.B.2


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