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Volumn 6, Issue 12, 2005, Pages 971-976

Radical medicine: Treating ageing to cure disease

Author keywords

[No Author keywords available]

Indexed keywords

N METHYL DEXTRO ASPARTIC ACID RECEPTOR BLOCKING AGENT; REACTIVE OXYGEN METABOLITE;

EID: 28844473846     PISSN: 14710072     EISSN: 14710080     Source Type: Journal    
DOI: 10.1038/nrm1763     Document Type: Review
Times cited : (220)

References (74)
  • 1
    • 0027401203 scopus 로고
    • Mutations in Cu/Zn superoxide dismutase gene are associated with familial amyotrophic lateral sclerosis
    • Rosen, D. R. et al. Mutations in Cu/Zn superoxide dismutase gene are associated with familial amyotrophic lateral sclerosis. Nature 362, 59-62 (1993).
    • (1993) Nature , vol.362 , pp. 59-62
    • Rosen, D.R.1
  • 3
    • 3142514196 scopus 로고    scopus 로고
    • Oxidative stress in neurodegeneration: Cause or consequence?
    • Andersen, J. K. Oxidative stress in neurodegeneration: cause or consequence? Nature Med. 10, S18-S25 (2004).
    • (2004) Nature Med. , vol.10
    • Andersen, J.K.1
  • 4
    • 0242363670 scopus 로고    scopus 로고
    • Molecular pathways of neurodegeneration in Parkinson's disease
    • Dawson, T. M. & Dawson, V. L. Molecular pathways of neurodegeneration in Parkinson's disease. Science 302, 819-822 (2003).
    • (2003) Science , vol.302 , pp. 819-822
    • Dawson, T.M.1    Dawson, V.L.2
  • 5
    • 0037085288 scopus 로고    scopus 로고
    • Formation and removal of α-synuclein aggregates in cells exposed to mitochondrial inhibitors
    • Lee, H. J., Shin, S. Y., Choi, C., Lee, Y. H. & Lee, S. J. Formation and removal of α-synuclein aggregates in cells exposed to mitochondrial inhibitors. J. Biol. Chem. 277, 5411-5417 (2002).
    • (2002) J. Biol. Chem. , vol.277 , pp. 5411-5417
    • Lee, H.J.1    Shin, S.Y.2    Choi, C.3    Lee, Y.H.4    Lee, S.J.5
  • 6
    • 0033890821 scopus 로고    scopus 로고
    • α-Synuclein promotes mitochondrial deficit and oxidative stress
    • Hsu, L. J. et al. α-Synuclein promotes mitochondrial deficit and oxidative stress. Am. J. Pathol. 157, 401-410 (2000).
    • (2000) Am. J. Pathol. , vol.157 , pp. 401-410
    • Hsu, L.J.1
  • 7
    • 0037386532 scopus 로고    scopus 로고
    • Mitochondrial pathology and apoptotic muscle degeneration in Drosophila parkin mutants
    • Greene, J. C. et al. Mitochondrial pathology and apoptotic muscle degeneration in Drosophila parkin mutants. Proc. Natl Acad. Sci. USA 100, 4078-4083 (2003).
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 4078-4083
    • Greene, J.C.1
  • 8
    • 2442481789 scopus 로고    scopus 로고
    • Mitochondrial dysfunction and oxidative damage in parkin-deficient mice
    • Palacino, J. J. et al. Mitochondrial dysfunction and oxidative damage in parkin-deficient mice. J. Biol. Chem. 279, 18614-18622 (2004).
    • (2004) J. Biol. Chem. , vol.279 , pp. 18614-18622
    • Palacino, J.J.1
  • 9
    • 13944279784 scopus 로고    scopus 로고
    • Sensitivity to oxidative stress in DJ-1-deficient dopamine neurons: An ES-derived cell model of primary parkinsonism
    • Martinat, C. et al. Sensitivity to oxidative stress in DJ-1-deficient dopamine neurons: an ES-derived cell model of primary parkinsonism. PLoS Biol. 2, e327 (2004).
    • (2004) PLoS Biol. , vol.2
    • Martinat, C.1
  • 10
    • 20144389422 scopus 로고    scopus 로고
    • Hypersensitivity of DJ-1-deficient mice to 1-methyl-4-phenyl-1,2,3,6- tetrahydropyrindine (MPTP) and oxidative stress
    • Kim, R. H. et al. Hypersensitivity of DJ-1-deficient mice to 1-methyl-4-phenyl-1,2,3,6-tetrahydropyrindine (MPTP) and oxidative stress. Proc. Natl Acad. Sci. USA 102, 5215-5220 (2005).
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 5215-5220
    • Kim, R.H.1
  • 11
    • 2442668926 scopus 로고    scopus 로고
    • Hereditary early-onset Parkinson's disease caused by mutations in PINK1
    • Valente, E. M. et al. Hereditary early-onset Parkinson's disease caused by mutations in PINK1. Science 304, 1158-1160 (2004).
    • (2004) Science , vol.304 , pp. 1158-1160
    • Valente, E.M.1
  • 12
    • 0028233494 scopus 로고
    • Hydrogen peroxide mediates amyloid β protein toxicity
    • Behl, C., Davis, J. B., Lesley, R. & Schubert, D. Hydrogen peroxide mediates amyloid β protein toxicity. Cell 77, 817-827 (1994).
    • (1994) Cell , vol.77 , pp. 817-827
    • Behl, C.1    Davis, J.B.2    Lesley, R.3    Schubert, D.4
  • 13
    • 11144353586 scopus 로고    scopus 로고
    • ABAD directly links Aβ to mitochondrial toxicity in Alzheimer's disease
    • Lustbader, J. W. et al. ABAD directly links Aβ to mitochondrial toxicity in Alzheimer's disease. Science 304, 448-452 (2004).
    • (2004) Science , vol.304 , pp. 448-452
    • Lustbader, J.W.1
  • 14
    • 0037417238 scopus 로고    scopus 로고
    • Memantine in moderate-to-severe Alzheimer's disease
    • Reisberg, B. et al. Memantine in moderate-to-severe Alzheimer's disease. N. Engl. J. Med. 348, 1333-1341 (2003).
    • (2003) N. Engl. J. Med. , vol.348 , pp. 1333-1341
    • Reisberg, B.1
  • 15
    • 17844403545 scopus 로고    scopus 로고
    • Role of oxidative carbonylation in protein quality control and senescence
    • Nystrom, T. Role of oxidative carbonylation in protein quality control and senescence. EMBO J. 1311-1317 (2005).
    • (2005) EMBO J. , pp. 1311-1317
    • Nystrom, T.1
  • 16
    • 2342472071 scopus 로고    scopus 로고
    • The Drosophila carbonyl reductase sniffer prevents oxidative stress-induced neurodegeneration
    • Botella, J. A. et al. The Drosophila carbonyl reductase sniffer prevents oxidative stress-induced neurodegeneration. Curr. Biol. 14, 782-786 (2004).
    • (2004) Curr. Biol. , vol.14 , pp. 782-786
    • Botella, J.A.1
  • 17
    • 0030586350 scopus 로고    scopus 로고
    • Age-related decline of rat liver multicatalytic proteinase activity and protection from oxidative inactivation by heat-shock protein 90
    • Conconi, M., Szweda, L. I., Levine, R. L., Stadtman, E. R. & Friguet, B. Age-related decline of rat liver multicatalytic proteinase activity and protection from oxidative inactivation by heat-shock protein 90. Arch. Biochem. Biophys. 331, 232-240 (1996).
    • (1996) Arch. Biochem. Biophys. , vol.331 , pp. 232-240
    • Conconi, M.1    Szweda, L.I.2    Levine, R.L.3    Stadtman, E.R.4    Friguet, B.5
  • 18
    • 4344677922 scopus 로고    scopus 로고
    • Decreased proteolysis caused by protein aggregates, inclusion bodies, plaques, lipofuscin, ceroid, and 'aggresomes' during oxidative stress, aging, and disease
    • Grune, T., Jung, T., Merker, K. & Davies, K. J. Decreased proteolysis caused by protein aggregates, inclusion bodies, plaques, lipofuscin, ceroid, and 'aggresomes' during oxidative stress, aging, and disease. Int. J. Biochem. Cell Biol. 36, 2519-2530 (2004).
    • (2004) Int. J. Biochem. Cell Biol. , vol.36 , pp. 2519-2530
    • Grune, T.1    Jung, T.2    Merker, K.3    Davies, K.J.4
  • 19
    • 4344618623 scopus 로고    scopus 로고
    • Autophagy, proteasomes, lipofuscin, and oxidative stress in the aging brain
    • Keller, J. N. et al. Autophagy, proteasomes, lipofuscin, and oxidative stress in the aging brain. Int. J. Biochem. Cell Biol. 36, 2376-2391 (2004).
    • (2004) Int. J. Biochem. Cell Biol. , vol.36 , pp. 2376-2391
    • Keller, J.N.1
  • 20
    • 0036713692 scopus 로고    scopus 로고
    • Lon protease preferentially degrades oxidized mitochondrial aconitase by an ATP-stimulated mechanism
    • Bota, D. A. & Davies, K. J. Lon protease preferentially degrades oxidized mitochondrial aconitase by an ATP-stimulated mechanism. Nature Cell. Biol. 4, 674-680 (2002).
    • (2002) Nature Cell. Biol. , vol.4 , pp. 674-680
    • Bota, D.A.1    Davies, K.J.2
  • 21
    • 3042631024 scopus 로고    scopus 로고
    • Gene regulation and DNA damage in the ageing human brain
    • Lu, T. et al. Gene regulation and DNA damage in the ageing human brain. Nature 429, 883-891 (2004).
    • (2004) Nature , vol.429 , pp. 883-891
    • Lu, T.1
  • 23
    • 1542406446 scopus 로고    scopus 로고
    • NOX enzymes and the biology of reactive oxygen
    • Lambeth, J. D. NOX enzymes and the biology of reactive oxygen. Nature Rev. Immunol. 4, 181-189 (2004).
    • (2004) Nature Rev. Immunol. , vol.4 , pp. 181-189
    • Lambeth, J.D.1
  • 24
    • 0034696590 scopus 로고    scopus 로고
    • Vascular effects following homozygous disruption of p47(phox): An essential component of NADPH oxidase
    • Hsich, E. et al. Vascular effects following homozygous disruption of p47(phox): an essential component of NADPH oxidase. Circulation 101, 1234-1236 (2000).
    • (2000) Circulation , vol.101 , pp. 1234-1236
    • Hsich, E.1
  • 26
    • 0037199466 scopus 로고    scopus 로고
    • Mitochondrial integrity and function in atherogenesis
    • Ballinger, S. W. et al. Mitochondrial integrity and function in atherogenesis. Circulation 106, 544-549 (2002).
    • (2002) Circulation , vol.106 , pp. 544-549
    • Ballinger, S.W.1
  • 27
    • 13244262926 scopus 로고    scopus 로고
    • Oxidative stress in atherosclerosis-prone mouse is due to low antioxidant capacity of mitochondria
    • Oliveira, H. C. et al. Oxidative stress in atherosclerosis-prone mouse is due to low antioxidant capacity of mitochondria. FASEB J. 19, 278-280 (2005).
    • (2005) FASEB J. , vol.19 , pp. 278-280
    • Oliveira, H.C.1
  • 28
    • 8444228909 scopus 로고    scopus 로고
    • A cluster of metabolic defects caused by mutation in a mitochondrial tRNA
    • Wilson, F. H. et al. A cluster of metabolic defects caused by mutation in a mitochondrial tRNA. Science 306, 1190-1194 (2004).
    • (2004) Science , vol.306 , pp. 1190-1194
    • Wilson, F.H.1
  • 29
    • 0035856980 scopus 로고    scopus 로고
    • Biochemistry and molecular cell biology of diabetic complications
    • Brownlee, M. Biochemistry and molecular cell biology of diabetic complications. Nature 414, 813-820 (2001).
    • (2001) Nature , vol.414 , pp. 813-820
    • Brownlee, M.1
  • 30
    • 19944431011 scopus 로고    scopus 로고
    • Cardiovascular risk factors emerge after artificial selection for low aerobic capacity
    • Wisloff, U. et al. Cardiovascular risk factors emerge after artificial selection for low aerobic capacity. Science 307, 418-420 (2005).
    • (2005) Science , vol.307 , pp. 418-420
    • Wisloff, U.1
  • 31
    • 17244367828 scopus 로고    scopus 로고
    • Reactive oxygen species in tumor progression
    • Storz, P. Reactive oxygen species in tumor progression. Front Biosci. 10, 1881-1896 (2005).
    • (2005) Front Biosci. , vol.10 , pp. 1881-1896
    • Storz, P.1
  • 32
    • 0042568938 scopus 로고    scopus 로고
    • Essential role for the peroxiredoxin Prdx1 in erythrocyte antioxidant defence and tumour suppression
    • Neumann, C. A. et al. Essential role for the peroxiredoxin Prdx1 in erythrocyte antioxidant defence and tumour suppression. Nature 424, 561-565 (2003).
    • (2003) Nature , vol.424 , pp. 561-565
    • Neumann, C.A.1
  • 33
    • 12144288373 scopus 로고    scopus 로고
    • Life-long reduction in MnSOD activity results in increased DNA damage and higher incidence of cancer but does not accelerate aging
    • Van Remmen, H. et al. Life-long reduction in MnSOD activity results in increased DNA damage and higher incidence of cancer but does not accelerate aging. Physiol. Genomics 16, 29-37 (2003).
    • (2003) Physiol. Genomics , vol.16 , pp. 29-37
    • Van Remmen, H.1
  • 34
    • 0026021362 scopus 로고
    • Production of large amounts of hydrogen peroxide by human tumor cells
    • Szatrowski, T. P. & Nathan, C. F. Production of large amounts of hydrogen peroxide by human tumor cells. Cancer Res. 51, 794-798 (1991).
    • (1991) Cancer Res. , vol.51 , pp. 794-798
    • Szatrowski, T.P.1    Nathan, C.F.2
  • 35
    • 0037376674 scopus 로고    scopus 로고
    • Oxidant signals and oxidative stress
    • Finkel, T. Oxidant signals and oxidative stress. Curr. Opin. Cell Biol. 15, 247-254 (2003).
    • (2003) Curr. Opin. Cell Biol. , vol.15 , pp. 247-254
    • Finkel, T.1
  • 36
    • 0036285034 scopus 로고    scopus 로고
    • c-Myc can induce DNA damage, increase reactive oxygen species, and mitigate p53 function: A mechanism for oncogene-induced genetic instability
    • Vafa, O. et al. c-Myc can induce DNA damage, increase reactive oxygen species, and mitigate p53 function: a mechanism for oncogene-induced genetic instability. Mol. Cell 9, 1031-1044 (2002).
    • (2002) Mol. Cell , vol.9 , pp. 1031-1044
    • Vafa, O.1
  • 37
    • 2642527955 scopus 로고    scopus 로고
    • Activated oncogenes promote and cooperate with chromosomal instability for neoplastic transformation
    • Woo, R. A. & Poon, R. Y. Activated oncogenes promote and cooperate with chromosomal instability for neoplastic transformation. Genes Dev. 18, 1317-1330 (2004).
    • (2004) Genes Dev. , vol.18 , pp. 1317-1330
    • Woo, R.A.1    Poon, R.Y.2
  • 38
    • 0030944985 scopus 로고    scopus 로고
    • Oncogenic ras provokes premature cell senescence associated with accumulation of p53 and p16INK4a
    • Serrano, M., Lin, A. W., McCurrach, M. E., Beach, D. & Lowe, S. W. Oncogenic ras provokes premature cell senescence associated with accumulation of p53 and p16INK4a. Cell 88, 593-602 (1997).
    • (1997) Cell , vol.88 , pp. 593-602
    • Serrano, M.1    Lin, A.W.2    McCurrach, M.E.3    Beach, D.4    Lowe, S.W.5
  • 39
    • 0030980641 scopus 로고    scopus 로고
    • Mitogenic signaling mediated by oxidants in Ras-transformed fibroblasts
    • Irani, K. et al. Mitogenic signaling mediated by oxidants in Ras-transformed fibroblasts. Science 275, 1649-1652 (1997).
    • (1997) Science , vol.275 , pp. 1649-1652
    • Irani, K.1
  • 40
    • 0033583242 scopus 로고    scopus 로고
    • Ras proteins induce senescence by altering the intracellular levels of reactive oxygen species
    • Lee, A. C. et al. Ras proteins induce senescence by altering the intracellular levels of reactive oxygen species. J. Biol. Chem. 274, 7936-7940 (1999).
    • (1999) J. Biol. Chem. , vol.274 , pp. 7936-7940
    • Lee, A.C.1
  • 41
    • 11244347171 scopus 로고    scopus 로고
    • Glycolytic enzymes can modulate cellular life span
    • Kondoh, H. et al. Glycolytic enzymes can modulate cellular life span. Cancer Res. 65, 177-185 (2005).
    • (2005) Cancer Res. , vol.65 , pp. 177-185
    • Kondoh, H.1
  • 42
    • 10344229445 scopus 로고    scopus 로고
    • Regulation of cellular response to oncogenic and oxidative stress by seladin-1
    • Wu, C., Miloslavskaya, I., Demontis, S., Maestro, R. & Galaktionov, K. Regulation of cellular response to oncogenic and oxidative stress by seladin-1. Nature 432, 640-645 (2004).
    • (2004) Nature , vol.432 , pp. 640-645
    • Wu, C.1    Miloslavskaya, I.2    Demontis, S.3    Maestro, R.4    Galaktionov, K.5
  • 43
    • 0034307463 scopus 로고    scopus 로고
    • The human DIMINUTO/DWARF1 homolog seladin-1 confers resistance to Alzheimer's disease-associated neurodegeneration and oxidative stress
    • Greeve, I. et al. The human DIMINUTO/DWARF1 homolog seladin-1 confers resistance to Alzheimer's disease-associated neurodegeneration and oxidative stress. J. Neurosci. 20, 7345-7352 (2000).
    • (2000) J. Neurosci. , vol.20 , pp. 7345-7352
    • Greeve, I.1
  • 44
    • 4544346656 scopus 로고    scopus 로고
    • JunD reduces tumor angiogenesis by protecting cells from oxidative stress
    • Gerald, D. et al. JunD reduces tumor angiogenesis by protecting cells from oxidative stress. Cell 118, 781-794 (2004).
    • (2004) Cell , vol.118 , pp. 781-794
    • Gerald, D.1
  • 45
    • 0037154250 scopus 로고    scopus 로고
    • Reactive oxygen generated by Nox1 triggers the angiogenic switch
    • Arbiser, J. L. et al. Reactive oxygen generated by Nox1 triggers the angiogenic switch. Proc. Natl Acad. Sci. USA 99, 715-720 (2002).
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 715-720
    • Arbiser, J.L.1
  • 46
    • 4043161974 scopus 로고    scopus 로고
    • Mitochondrial redox control of matrix metalloproteinases
    • Nelson, K. K. & Melendez, J. A. Mitochondrial redox control of matrix metalloproteinases. Free Radic. Biol. Med. 37, 768-784 (2004).
    • (2004) Free Radic. Biol. Med. , vol.37 , pp. 768-784
    • Nelson, K.K.1    Melendez, J.A.2
  • 47
    • 13944278132 scopus 로고    scopus 로고
    • Mitochondria, oxidants, and aging
    • Balaban, R. S., Nemoto, S. & Finkel, T. Mitochondria, oxidants, and aging. Cell 120, 483-495 (2005).
    • (2005) Cell , vol.120 , pp. 483-495
    • Balaban, R.S.1    Nemoto, S.2    Finkel, T.3
  • 48
    • 0033214237 scopus 로고    scopus 로고
    • The SIR2/3/4 complex and SIR2 alone promote longevity in Saccharomyces cerevisiae by two different mechanisms
    • Kaeberlein, M., McVey, M. & Guarente, L. The SIR2/3/4 complex and SIR2 alone promote longevity in Saccharomyces cerevisiae by two different mechanisms. Genes Dev. 13, 2570-2580 (1999).
    • (1999) Genes Dev. , vol.13 , pp. 2570-2580
    • Kaeberlein, M.1    McVey, M.2    Guarente, L.3
  • 49
    • 0035826271 scopus 로고    scopus 로고
    • Increased dosage of a sir-2 gene extends lifespan in Caenorhabditis elegans
    • Tissenbaum, H. A. & Guarente, L. Increased dosage of a sir-2 gene extends lifespan in Caenorhabditis elegans. Nature 410, 227-230 (2001).
    • (2001) Nature , vol.410 , pp. 227-230
    • Tissenbaum, H.A.1    Guarente, L.2
  • 50
    • 0242585476 scopus 로고    scopus 로고
    • Asymmetric inheritance of oxidatively damaged proteins during cytokinesis
    • Aguilaniu, H., Gustafsson, L., Rigoulet, M. & Nystrom, T. Asymmetric inheritance of oxidatively damaged proteins during cytokinesis. Science 299, 1751-1753 (2003).
    • (2003) Science , vol.299 , pp. 1751-1753
    • Aguilaniu, H.1    Gustafsson, L.2    Rigoulet, M.3    Nystrom, T.4
  • 51
    • 17144424946 scopus 로고    scopus 로고
    • SIRT3, a mitochondrial sirtuin deacetylase, regulates mitochondrial function and thermogenesis in brown adipocytes
    • Shi, T., Wang, F., Stieren, E. & Tong, Q. SIRT3, a mitochondrial sirtuin deacetylase, regulates mitochondrial function and thermogenesis in brown adipocytes. J. Biol. Chem. 280, 13560-13567 (2005).
    • (2005) J. Biol. Chem. , vol.280 , pp. 13560-13567
    • Shi, T.1    Wang, F.2    Stieren, E.3    Tong, Q.4
  • 52
    • 18144411313 scopus 로고    scopus 로고
    • SIRT1 functionally interacts with the metabolic regulator and transcriptional coactivator PGC-1α
    • Nemoto, S., Fergusson, M. M. & Finkel, T. SIRT1 functionally interacts with the metabolic regulator and transcriptional coactivator PGC-1α. J. Biol. Chem. 280, 16456-16460 (2005).
    • (2005) J. Biol. Chem. , vol.280 , pp. 16456-16460
    • Nemoto, S.1    Fergusson, M.M.2    Finkel, T.3
  • 53
    • 4043165678 scopus 로고    scopus 로고
    • Increased nuclear NAD biosynthesis and SIRT1 activation prevent axonal degeneration
    • Araki, T., Sasaki, Y. & Milbrandt, J. Increased nuclear NAD biosynthesis and SIRT1 activation prevent axonal degeneration. Science 305, 1010-1013 (2004).
    • (2004) Science , vol.305 , pp. 1010-1013
    • Araki, T.1    Sasaki, Y.2    Milbrandt, J.3
  • 54
    • 16844375290 scopus 로고    scopus 로고
    • Resveratrol rescues mutant polyglutamine cytotoxicity in nematode and mammalian neurons
    • Parker, J. A. et al. Resveratrol rescues mutant polyglutamine cytotoxicity in nematode and mammalian neurons. Nature Genet. 37, 349-350 (2005).
    • (2005) Nature Genet. , vol.37 , pp. 349-350
    • Parker, J.A.1
  • 55
    • 0141719702 scopus 로고    scopus 로고
    • Small molecule activators of sirtuins extend Saccharomyces cerevisiae lifespan
    • Howitz, K. T. et al. Small molecule activators of sirtuins extend Saccharomyces cerevisiae lifespan. Nature 425, 191-196 (2003).
    • (2003) Nature , vol.425 , pp. 191-196
    • Howitz, K.T.1
  • 56
    • 0242695672 scopus 로고    scopus 로고
    • Resveratrol: From grapevines to mammalian biology
    • Pervaiz, S. Resveratrol: from grapevines to mammalian biology. FASEB J. 17, 1975-1985 (2003).
    • (2003) FASEB J. , vol.17 , pp. 1975-1985
    • Pervaiz, S.1
  • 57
    • 0033581704 scopus 로고    scopus 로고
    • The p66shc adaptor protein controls oxidative stress response and life span in mammals
    • Migliaccio, E. et al. The p66shc adaptor protein controls oxidative stress response and life span in mammals. Nature 402, 309-313 (1999).
    • (1999) Nature , vol.402 , pp. 309-313
    • Migliaccio, E.1
  • 58
    • 0037192473 scopus 로고    scopus 로고
    • Redox regulation of forkhead proteins through a p66shc-dependent signaling pathway
    • Nemoto, S. & Finkel, T. Redox regulation of forkhead proteins through a p66shc-dependent signaling pathway. Science 295, 2450-2452 (2002).
    • (2002) Science , vol.295 , pp. 2450-2452
    • Nemoto, S.1    Finkel, T.2
  • 59
    • 85047695800 scopus 로고    scopus 로고
    • A p53-p66Shc signalling pathway controls intracellular redox status, levels of oxidation-damaged DNA and oxidative stress-induced apoptosis
    • Trinei, M. et al. A p53-p66Shc signalling pathway controls intracellular redox status, levels of oxidation-damaged DNA and oxidative stress-induced apoptosis. Oncogene 21, 3872-3878 (2002).
    • (2002) Oncogene , vol.21 , pp. 3872-3878
    • Trinei, M.1
  • 60
    • 0037452461 scopus 로고    scopus 로고
    • Deletion of the p66Shc longevity gene reduces systemic and tissue oxidative stress, vascular cell apoptosis, and early atherogenesis in mice fed a high-fat diet
    • Napoli, C. et al. Deletion of the p66Shc longevity gene reduces systemic and tissue oxidative stress, vascular cell apoptosis, and early atherogenesis in mice fed a high-fat diet. Proc. Natl Acad. Sci. USA 100, 2112-2116 (2003).
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 2112-2116
    • Napoli, C.1
  • 61
    • 8144229685 scopus 로고    scopus 로고
    • Deletion of p66shc gene protects against age-related endothelial dysfunction
    • Francia, P. et al. Deletion of p66shc gene protects against age-related endothelial dysfunction. Circulation 110, 2889-2895 (2004).
    • (2004) Circulation , vol.110 , pp. 2889-2895
    • Francia, P.1
  • 62
    • 17144429302 scopus 로고    scopus 로고
    • Calorie restriction, SIRT1 and metabolism: Understanding longevity
    • Bordone, L. & Guarente, L. Calorie restriction, SIRT1 and metabolism: understanding longevity. Nature Rev. Mol. Cell Biol. 6, 298-305 (2005).
    • (2005) Nature Rev. Mol. Cell Biol. , vol.6 , pp. 298-305
    • Bordone, L.1    Guarente, L.2
  • 63
    • 0002458132 scopus 로고
    • The effects of retarded growth upon the length of life span and upon the ultimate body size
    • McCay C. M., Crowell, M. F. & Maynard, L. A. The effects of retarded growth upon the length of life span and upon the ultimate body size. J. Nutr. 10, 63-79 (1935).
    • (1935) J. Nutr. , vol.10 , pp. 63-79
    • McCay, C.M.1    Crowell, M.F.2    Maynard, L.A.3
  • 64
    • 84882160556 scopus 로고
    • The influence of diet on transplanted and spontaneous mouse tumors
    • Rous, P. The influence of diet on transplanted and spontaneous mouse tumors. J. Exp. Med. 20, 433-451 (1914).
    • (1914) J. Exp. Med. , vol.20 , pp. 433-451
    • Rous, P.1
  • 65
    • 1542377615 scopus 로고    scopus 로고
    • Caloric restriction and incidence of breast cancer
    • Michels, K. B. & Ekbom, A. Caloric restriction and incidence of breast cancer. JAMA 291, 1226-1230 (2004).
    • (2004) JAMA , vol.291 , pp. 1226-1230
    • Michels, K.B.1    Ekbom, A.2
  • 66
    • 2342647592 scopus 로고    scopus 로고
    • Long-term calorie restriction is highly effective in reducing the risk for atherosclerosis in humans
    • Fontana, L., Meyer, T. E., Klein, S. & Holloszy, J. O. Long-term calorie restriction is highly effective in reducing the risk for atherosclerosis in humans. Proc. Natl Acad. Sci. USA 101, 6659-6663 (2004).
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 6659-6663
    • Fontana, L.1    Meyer, T.E.2    Klein, S.3    Holloszy, J.O.4
  • 67
    • 21144434217 scopus 로고    scopus 로고
    • Extension of murine life span by overexpression of catalase targeted to mitochondria
    • Schriner, S. E. et al. Extension of murine life span by overexpression of catalase targeted to mitochondria. Science 308, 1909-1911 (2005).
    • (2005) Science , vol.308 , pp. 1909-1911
    • Schriner, S.E.1
  • 68
    • 14844327760 scopus 로고    scopus 로고
    • Reactive oxygen species promote TNFα-induced death and sustained JNK activation by inhibiting MAP kinase phosphatases
    • Kamata, H. et al. Reactive oxygen species promote TNFα-induced death and sustained JNK activation by inhibiting MAP kinase phosphatases. Cell 120, 649-661 (2005).
    • (2005) Cell , vol.120 , pp. 649-661
    • Kamata, H.1
  • 69
    • 0037434561 scopus 로고    scopus 로고
    • Circulating endothelial progenitor cells, vascular function, and cardiovascular risk
    • Hill, J. M. et al. Circulating endothelial progenitor cells, vascular function, and cardiovascular risk. N. Engl. J. Med. 348, 593-600 (2003).
    • (2003) N. Engl. J. Med. , vol.348 , pp. 593-600
    • Hill, J.M.1
  • 70
    • 8644232705 scopus 로고    scopus 로고
    • Stress defense in murine embryonic stem cells is superior to that of various differentiated murine cells
    • Saretzki, G., Armstrong, L., Leake, A., Lako, M. & von Zglinicki, T. Stress defense in murine embryonic stem cells is superior to that of various differentiated murine cells. Stem Cells 22, 962-971 (2004).
    • (2004) Stem Cells , vol.22 , pp. 962-971
    • Saretzki, G.1    Armstrong, L.2    Leake, A.3    Lako, M.4    Von Zglinicki, T.5
  • 71
    • 0034774583 scopus 로고    scopus 로고
    • Oxygen-mediated regulation of skeletal muscle satellite cell proliferation and adipogenesis in culture
    • Csete, M. et al. Oxygen-mediated regulation of skeletal muscle satellite cell proliferation and adipogenesis in culture. J. Cell. Physiol. 189, 189-196 (2001).
    • (2001) J. Cell. Physiol. , vol.189 , pp. 189-196
    • Csete, M.1
  • 72
    • 8644273225 scopus 로고    scopus 로고
    • Cell-density-dependent regulation of neural precursor cell function
    • Limoli, C. L. et al. Cell-density-dependent regulation of neural precursor cell function. Proc. Natl Acad. Sci. USA 101, 16052-16057 (2004).
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 16052-16057
    • Limoli, C.L.1
  • 73
    • 4043184065 scopus 로고    scopus 로고
    • Progenitor cell trafficking is regulated by hypoxic gradients through HIF-1 induction of SDF-1
    • Ceradini, D. J. et al. Progenitor cell trafficking is regulated by hypoxic gradients through HIF-1 induction of SDF-1. Nature Med. 10, 858-864 (2004).
    • (2004) Nature Med. , vol.10 , pp. 858-864
    • Ceradini, D.J.1
  • 74
    • 7244250309 scopus 로고    scopus 로고
    • Regulation of oxidative stress by ATM is required for self-renewal of haematopoietic stem cells
    • Ito, K. et al. Regulation of oxidative stress by ATM is required for self-renewal of haematopoietic stem cells. Nature 431, 997-1002 (2004).
    • (2004) Nature , vol.431 , pp. 997-1002
    • Ito, K.1


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