메뉴 건너뛰기




Volumn 190, Issue 5, 2010, Pages 719-729

Protein homeostasis and aging in neurodegeneration

Author keywords

[No Author keywords available]

Indexed keywords

HEAT SHOCK TRANSCRIPTION FACTOR 1; PROTEOME; SIRTUIN; SOMATOMEDIN C;

EID: 77956362155     PISSN: 00219525     EISSN: 00219525     Source Type: Journal    
DOI: 10.1083/jcb.201005144     Document Type: Review
Times cited : (296)

References (144)
  • 1
    • 0028227962 scopus 로고
    • Role of abnormally phosphorylated tau in the breakdown of microtubules in Alzheimer disease
    • doi:10.1073/pnas.91.12.5562
    • Alonso, A.C., T. Zaidi, I. Grundke-Iqbal, and K. Iqbal. 1994. Role of abnormally phosphorylated tau in the breakdown of microtubules in Alzheimer disease. Proc. Natl. Acad. Sci. USA. 91:5562-5566. doi:10.1073/pnas.91.12.5562
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 5562-5566
    • Alonso, A.C.1    Zaidi, T.2    Grundke-Iqbal, I.3    Iqbal, K.4
  • 2
    • 0029999787 scopus 로고    scopus 로고
    • Alzheimer's disease hyperphosphorylated tau sequesters normal tau into tangles of filaments and disassembles microtubules
    • doi:10.1038/nm0796-783
    • Alonso, A.C., I. Grundke-Iqbal, and K. Iqbal. 1996. Alzheimer's disease hyperphosphorylated tau sequesters normal tau into tangles of filaments and disassembles microtubules. Nat. Med. 2:783-787. doi:10.1038/nm0796-783
    • (1996) Nat. Med. , vol.2 , pp. 783-787
    • Alonso, A.C.1    Grundke-Iqbal, I.2    Iqbal, K.3
  • 3
    • 34250860632 scopus 로고    scopus 로고
    • Comparative analysis of the effects of resveratrol in two apoptotic models: Inhibition of complex I and potassium deprivation in cerebellar neurons
    • doi:10.1016/j.neuroscience.2007.04.029
    • Alvira, D., M. Yeste-Velasco, J. Folch, E. Verdaguer, A.M. Canudas, M. Pallàs, and A. Camins. 2007. Comparative analysis of the effects of resveratrol in two apoptotic models: inhibition of complex I and potassium deprivation in cerebellar neurons. Neuroscience. 147:746-756. doi:10.1016/j.neuroscience.2007.04.029
    • (2007) Neuroscience , vol.147 , pp. 746-756
    • Alvira, D.1    Yeste-Velasco, M.2    Folch, J.3    Verdaguer, E.4    Canudas, A.M.5    Pallàs, M.6    Camins, A.7
  • 4
    • 0028856460 scopus 로고
    • An English translation of Alzheimer's 1907 paper, "Uber eine eigenartige Erkankung der Hirnrinde"
    • doi:10.1002/ca.980080612
    • Alzheimer, A., R.A. Stelzmann, H.N. Schnitzlein, and F.R. Murtagh. 1995. An English translation of Alzheimer's 1907 paper, "Uber eine eigenartige Erkankung der Hirnrinde". Clin. Anat. 8:429-431. doi:10.1002/ca.980080612
    • (1995) Clin. Anat. , vol.8 , pp. 429-431
    • Alzheimer, A.1    Stelzmann, R.A.2    Schnitzlein, H.N.3    Murtagh, F.R.4
  • 5
    • 7244236320 scopus 로고    scopus 로고
    • Inclusion body formation reduces levels of mutant huntingtin and the risk of neuronal death
    • doi:10.1038/nature02998
    • Arrasate, M., S. Mitra, E.S. Schweitzer, M.R. Segal, and S. Finkbeiner. 2004. Inclusion body formation reduces levels of mutant huntingtin and the risk of neuronal death. Nature. 431:805-810. doi:10.1038/nature02998
    • (2004) Nature , vol.431 , pp. 805-810
    • Arrasate, M.1    Mitra, S.2    Schweitzer, E.S.3    Segal, M.R.4    Finkbeiner, S.5
  • 6
    • 0026740795 scopus 로고
    • Neurofibrillary tangles but not senile plaques parallel duration and severity of Alzheimer's disease
    • Arriagada, P.V., J.H. Growdon, E.T. Hedley-Whyte, and B.T. Hyman. 1992. Neurofibrillary tangles but not senile plaques parallel duration and severity of Alzheimer's disease. Neurology. 42:631-639.
    • (1992) Neurology , vol.42 , pp. 631-639
    • Arriagada, P.V.1    Growdon, J.H.2    Hedley-Whyte, E.T.3    Hyman, B.T.4
  • 7
    • 74049145768 scopus 로고    scopus 로고
    • The growth hormone receptor gene-disrupted mouse fails to respond to an intermittent fasting diet
    • doi:10.1111/j.1474-9726.2009.00520.x
    • Arum, O., M.S. Bonkowski, J.S. Rocha, and A. Bartke. 2009. The growth hormone receptor gene-disrupted mouse fails to respond to an intermittent fasting diet. Aging Cell. 8:756-760. doi:10.1111/j.1474-9726.2009.00520.x
    • (2009) Aging Cell , vol.8 , pp. 756-760
    • Arum, O.1    Bonkowski, M.S.2    Rocha, J.S.3    Bartke, A.4
  • 8
    • 39349083915 scopus 로고    scopus 로고
    • Adapting proteostasis for disease intervention
    • doi:10.1126/science.1141448
    • Balch, W.E., R.I. Morimoto, A. Dillin, and J.W. Kelly. 2008. Adapting proteostasis for disease intervention. Science. 319:916-919. doi:10.1126/science.1141448
    • (2008) Science , vol.319 , pp. 916-919
    • Balch, W.E.1    Morimoto, R.I.2    Dillin, A.3    Kelly, J.W.4
  • 9
    • 34848927457 scopus 로고    scopus 로고
    • Effects of resveratrol on lifespan in Drosophila melanogaster and Caenorhabditis elegans
    • doi:10.1016/j.mad.2007.07.007
    • Bass, T.M., D. Weinkove, K. Houthoofd, D. Gems, and L. Partridge. 2007. Effects of resveratrol on lifespan in Drosophila melanogaster and Caenorhabditis elegans. Mech. Ageing Dev. 128:546-552. doi:10.1016/j.mad.2007.07.007
    • (2007) Mech. Ageing Dev. , vol.128 , pp. 546-552
    • Bass, T.M.1    Weinkove, D.2    Houthoofd, K.3    Gems, D.4    Partridge, L.5
  • 12
    • 70349266064 scopus 로고    scopus 로고
    • Collapse of proteostasis represents an early molecular event in Caenorhabditis elegans aging
    • doi:10.1073/pnas.0902882106
    • Ben-Zvi, A., E.A. Miller, and R.I. Morimoto. 2009. Collapse of proteostasis represents an early molecular event in Caenorhabditis elegans aging. Proc. Natl. Acad. Sci. USA. 106:14914-14919. doi:10.1073/pnas.0902882106
    • (2009) Proc. Natl. Acad. Sci. USA , vol.106 , pp. 14914-14919
    • Ben-Zvi, A.1    Miller, E.A.2    Morimoto, R.I.3
  • 13
    • 1542268242 scopus 로고    scopus 로고
    • Neurofibrillary tangles mediate the association of amyloid load with clinical Alzheimer disease and level of cognitive function
    • doi:10.1001/archneur.61.3.378
    • Bennett, D.A., J.A. Schneider, R.S. Wilson, J.L. Bienias, and S.E. Arnold. 2004. Neurofibrillary tangles mediate the association of amyloid load with clinical Alzheimer disease and level of cognitive function. Arch. Neurol. 61:378-384. doi:10.1001/archneur.61.3.378
    • (2004) Arch. Neurol. , vol.61 , pp. 378-384
    • Bennett, D.A.1    Schneider, J.A.2    Wilson, R.S.3    Bienias, J.L.4    Arnold, S.E.5
  • 14
    • 33744976074 scopus 로고    scopus 로고
    • C. elegans SIR-2.1 interacts with 14-3-3 proteins to activate DAF-16 and extend life span
    • doi:10.1016/j.cell.2006.04.036
    • Berdichevsky, A., M. Viswanathan, H.R. Horvitz, and L. Guarente. 2006. C. elegans SIR-2.1 interacts with 14-3-3 proteins to activate DAF-16 and extend life span. Cell. 125:1165-1177. doi:10.1016/j.cell.2006.04.036
    • (2006) Cell , vol.125 , pp. 1165-1177
    • Berdichevsky, A.1    Viswanathan, M.2    Horvitz, H.R.3    Guarente, L.4
  • 16
    • 34147125835 scopus 로고    scopus 로고
    • Accumulation of pathological tau species and memory loss in a conditional model of tauopathy
    • doi:10.1523/JNEUROSCI.0587-07.2007
    • Berger, Z., H. Roder, A. Hanna, A. Carlson, V. Rangachari, M. Yue, Z. Wszolek, K. Ashe, J. Knight, D. Dickson, et al. 2007. Accumulation of pathological tau species and memory loss in a conditional model of tauopathy. J. Neurosci. 27:3650-3662. doi:10.1523/JNEUROSCI.0587-07.2007
    • (2007) J. Neurosci. , vol.27 , pp. 3650-3662
    • Berger, Z.1    Roder, H.2    Hanna, A.3    Carlson, A.4    Rangachari, V.5    Yue, M.6    Wszolek, Z.7    Ashe, K.8    Knight, J.9    Dickson, D.10
  • 18
    • 0022365608 scopus 로고
    • The distribution of tau in the mammalian central nervous system
    • doi:10.1083/jcb.101.4.1371
    • Binder, L.I., A. Frankfurter, and L.I. Rebhun. 1985. The distribution of tau in the mammalian central nervous system. J. Cell Biol. 101:1371-1378. doi:10.1083/jcb.101.4.1371
    • (1985) J. Cell Biol. , vol.101 , pp. 1371-1378
    • Binder, L.I.1    Frankfurter, A.2    Rebhun, L.I.3
  • 19
    • 35348972430 scopus 로고    scopus 로고
    • Genetic links between diet and lifespan: Shared mechanisms from yeast to humans
    • doi:10.1038/nrg2188
    • Bishop, N.A., and L. Guarente. 2007. Genetic links between diet and lifespan: shared mechanisms from yeast to humans. Nat. Rev. Genet. 8:835-844. doi:10.1038/nrg2188
    • (2007) Nat. Rev. Genet. , vol.8 , pp. 835-844
    • Bishop, N.A.1    Guarente, L.2
  • 20
    • 0037942739 scopus 로고    scopus 로고
    • Extended longevity in mice lacking the insulin receptor in adipose tissue
    • doi:10.1126/science.1078223
    • Blüher, M., B.B. Kahn, and C.R. Kahn. 2003. Extended longevity in mice lacking the insulin receptor in adipose tissue. Science. 299:572-574. doi:10.1126/science.1078223
    • (2003) Science , vol.299 , pp. 572-574
    • Blüher, M.1    Kahn, B.B.2    Kahn, C.R.3
  • 22
    • 3142596164 scopus 로고    scopus 로고
    • Molecular pathways to neurodegeneration
    • doi:10.1038/nm1067
    • Bossy-Wetzel, E., R. Schwarzenbacher, and S.A. Lipton. 2004. Molecular pathways to neurodegeneration. Nat. Med. 10:S2-S9. doi:10.1038/nm1067
    • (2004) Nat. Med. , vol.10
    • Bossy-Wetzel, E.1    Schwarzenbacher, R.2    Lipton, S.A.3
  • 23
    • 0030881836 scopus 로고    scopus 로고
    • Phosphorylation of the translational repressor PHAS-I by the mammalian target of rapamycin
    • doi:10.1126/science.277.5322.99
    • Brunn, G.J., C.C. Hudson, A. Sekulić, J.M. Williams, H. Hosoi, P.J. Houghton, J.C. Lawrence Jr., and R.T. Abraham. 1997. Phosphorylation of the translational repressor PHAS-I by the mammalian target of rapamycin. Science. 277:99-101. doi:10.1126/science.277.5322.99
    • (1997) Science , vol.277 , pp. 99-101
    • Brunn, G.J.1    Hudson, C.C.2    Sekulić, A.3    Williams, J.M.4    Hosoi, H.5    Houghton, P.J.6    Lawrence Jr., J.C.7    Abraham, R.T.8
  • 25
    • 0030841343 scopus 로고    scopus 로고
    • Conformational disease
    • doi:10.1016/S0140-6736(97)02073-4
    • Carrell, R.W., and D.A. Lomas. 1997. Conformational disease. Lancet. 350:134-138. doi:10.1016/S0140-6736(97)02073-4
    • (1997) Lancet , vol.350 , pp. 134-138
    • Carrell, R.W.1    Lomas, D.A.2
  • 26
    • 0037551741 scopus 로고    scopus 로고
    • Protofibrils, pores, fibrils, and neurodegeneration: Separating the responsible protein aggregates from the innocent bystanders
    • doi:10.1146/annurev.neuro.26.010302.081142
    • Caughey, B., and P.T. Lansbury. 2003. Protofibrils, pores, fibrils, and neurodegeneration: separating the responsible protein aggregates from the innocent bystanders. Annu. Rev. Neurosci. 26:267-298. doi:10.1146/annurev.neuro. 26.010302.081142
    • (2003) Annu. Rev. Neurosci. , vol.26 , pp. 267-298
    • Caughey, B.1    Lansbury, P.T.2
  • 28
    • 67149107430 scopus 로고    scopus 로고
    • HIF-1 modulates dietary restriction-mediated lifespan extension via IRE-1 in Caenorhabditis elegans
    • doi:10.1371/journal.pgen.1000486
    • Chen, D., E.L. Thomas, and P. Kapahi. 2009. HIF-1 modulates dietary restriction-mediated lifespan extension via IRE-1 in Caenorhabditis elegans. PLoS Genet. 5:e1000486. doi:10.1371/journal.pgen.1000486
    • (2009) PLoS Genet. , vol.5
    • Chen, D.1    Thomas, E.L.2    Kapahi, P.3
  • 30
    • 0032895651 scopus 로고    scopus 로고
    • Transgenic mice with Alzheimer presenilin 1 mutations show accelerated neurodegeneration without amyloid plaque formation
    • doi:10.1038/8438
    • Chui, D.H., H. Tanahashi, K. Ozawa, S. Ikeda, F. Checler, O. Ueda, H. Suzuki, W. Araki, H. Inoue, K. Shirotani, et al. 1999. Transgenic mice with Alzheimer presenilin 1 mutations show accelerated neurodegeneration without amyloid plaque formation. Nat. Med. 5:560-564. doi:10.1038/8438
    • (1999) Nat. Med. , vol.5 , pp. 560-564
    • Chui, D.H.1    Tanahashi, H.2    Ozawa, K.3    Ikeda, S.4    Checler, F.5    Ueda, O.6    Suzuki, H.7    Araki, W.8    Inoue, H.9    Shirotani, K.10
  • 31
    • 33748792821 scopus 로고    scopus 로고
    • Opposing activities protect against age-onset proteotoxicity
    • doi:10.1126/science.1124646
    • Cohen, E., J. Bieschke, R.M. Perciavalle, J.W. Kelly, and A. Dillin. 2006. Opposing activities protect against age-onset proteotoxicity. Science. 313:1604-1610. doi:10.1126/science.1124646
    • (2006) Science , vol.313 , pp. 1604-1610
    • Cohen, E.1    Bieschke, J.2    Perciavalle, R.M.3    Kelly, J.W.4    Dillin, A.5
  • 35
    • 0141741347 scopus 로고    scopus 로고
    • Parkinson's disease: Mechanisms and models
    • doi:10.1016/S0896-6273(03)00568-3
    • Dauer, W., and S. Przedborski. 2003. Parkinson's disease: mechanisms and models. Neuron. 39:889-909. doi:10.1016/S0896-6273(03)00568-3
    • (2003) Neuron , vol.39 , pp. 889-909
    • Dauer, W.1    Przedborski, S.2
  • 36
    • 0030752709 scopus 로고    scopus 로고
    • Aggregation of huntingtin in neuronal intranuclear inclusions and dystrophic neurites in brain
    • doi:10.1126/science.277.5334.1990
    • DiFiglia, M., E. Sapp, K.O. Chase, S.W. Davies, G.P. Bates, J.P. Vonsattel, and N. Aronin. 1997. Aggregation of huntingtin in neuronal intranuclear inclusions and dystrophic neurites in brain. Science. 277:1990-1993. doi:10.1126/science.277.5334.1990
    • (1997) Science , vol.277 , pp. 1990-1993
    • DiFiglia, M.1    Sapp, E.2    Chase, K.O.3    Davies, S.W.4    Bates, G.P.5    Vonsattel, J.P.6    Aronin, N.7
  • 38
    • 67649306771 scopus 로고    scopus 로고
    • Molecular chaperones antagonize proteotoxicity by differentially modulating protein aggregation pathways
    • doi:10.4161/pri.3.2.8587
    • Douglas, P.M., D.W. Summers, and D.M. Cyr. 2009. Molecular chaperones antagonize proteotoxicity by differentially modulating protein aggregation pathways. Prion. 3:51-58. doi:10.4161/pri.3.2.8587
    • (2009) Prion , vol.3 , pp. 51-58
    • Douglas, P.M.1    Summers, D.W.2    Cyr, D.M.3
  • 39
    • 0027058857 scopus 로고
    • Modulation of the dynamic instability of tubulin assembly by the microtubule-associated protein tau
    • Drechsel, D.N., A.A. Hyman, M.H. Cobb, and M.W. Kirschner. 1992. Modulation of the dynamic instability of tubulin assembly by the microtubule-associated protein tau. Mol. Biol. Cell. 3:1141-1154.
    • (1992) Mol. Biol. Cell , vol.3 , pp. 1141-1154
    • Drechsel, D.N.1    Hyman, A.A.2    Cobb, M.H.3    Kirschner, M.W.4
  • 40
    • 0033566286 scopus 로고    scopus 로고
    • Dietary restriction and 2-deoxyglucose administration improve behavioral outcome and reduce degeneration of dopaminergic neurons in models of Parkinson's disease
    • doi:10.1002/(SICI)1097-4547(19990715)57:2〈195::AID-JNR5〉3.0. CO;2-P
    • Duan, W., and M.P. Mattson. 1999. Dietary restriction and 2-deoxyglucose administration improve behavioral outcome and reduce degeneration of dopaminergic neurons in models of Parkinson's disease. J. Neurosci. Res. 57:195-206. doi:10.1002/(SICI)1097-4547(19990715)57:2〈195::AID-JNR5〉3. 0.CO;2-P
    • (1999) J. Neurosci. Res. , vol.57 , pp. 195-206
    • Duan, W.1    Mattson, M.P.2
  • 41
    • 0025295039 scopus 로고
    • Cleavage of amyloid beta peptide during constitutive processing of its precursor
    • doi:10.1126/science.2111583
    • Esch, F.S., P.S. Keim, E.C. Beattie, R.W. Blacher, A.R. Culwell, T. Oltersdorf, D. McClure, and P.J. Ward. 1990. Cleavage of amyloid beta peptide during constitutive processing of its precursor. Science. 248:1122-1124. doi:10.1126/science.2111583
    • (1990) Science , vol.248 , pp. 1122-1124
    • Esch, F.S.1    Keim, P.S.2    Beattie, E.C.3    Blacher, R.W.4    Culwell, A.R.5    Oltersdorf, T.6    McClure, D.7    Ward, P.J.8
  • 42
    • 79952455618 scopus 로고    scopus 로고
    • TOR signaling never gets old: Aging, longevity and TORC1 activity
    • 10.1016/j.arr.2010.04.001
    • Evans, D.S., P. Kapahi, W.C. Hsueh, and L. Kockel. 2010. TOR signaling never gets old: Aging, longevity and TORC1 activity. Ageing Res. Rev. 10.1016/j.arr.2010.04.001.
    • (2010) Ageing Res. Rev.
    • Evans, D.S.1    Kapahi, P.2    Hsueh, W.C.3    Kockel, L.4
  • 43
    • 0034662929 scopus 로고    scopus 로고
    • BACE2, a beta -secretase homolog, cleaves at the beta site and within the amyloid-beta region of the amyloid-beta precursor protein
    • doi:10.1073/pnas.160115697
    • Farzan, M., C.E. Schnitzler, N. Vasilieva, D. Leung, and H. Choe. 2000. BACE2, a beta -secretase homolog, cleaves at the beta site and within the amyloid-beta region of the amyloid-beta precursor protein. Proc. Natl. Acad. Sci. USA. 97:9712-9717. doi:10.1073/pnas.160115697
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 9712-9717
    • Farzan, M.1    Schnitzler, C.E.2    Vasilieva, N.3    Leung, D.4    Choe, H.5
  • 44
    • 0034704752 scopus 로고    scopus 로고
    • Drosophila model of Parkinson's disease
    • doi:10.1038/35006074
    • Feany, M.B., and W.W. Bender. 2000. A Drosophila model of Parkinson's disease. Nature. 404:394-398. doi:10.1038/35006074
    • (2000) Nature , vol.404 , pp. 394-398
    • Feany, M.B.1    Bender, W.W.2
  • 45
    • 36248971777 scopus 로고    scopus 로고
    • Mechanisms of amyloid plaque pathogenesis
    • doi:10.1007/s00401-007-0284-8
    • Fiala, J.C. 2007. Mechanisms of amyloid plaque pathogenesis. Acta Neuropathol. 114:551-571. doi:10.1007/s00401-007-0284-8
    • (2007) Acta Neuropathol. , vol.114 , pp. 551-571
    • Fiala, J.C.1
  • 46
    • 0031033373 scopus 로고    scopus 로고
    • Aging, metabolism, and Alzheimer disease: Review and hypotheses
    • doi:10.1006/exnr.1996.6339
    • Finch, C.E., and D.M. Cohen. 1997. Aging, metabolism, and Alzheimer disease: review and hypotheses. Exp. Neurol. 143:82-102. doi:10.1006/exnr.1996. 6339
    • (1997) Exp. Neurol. , vol.143 , pp. 82-102
    • Finch, C.E.1    Cohen, D.M.2
  • 48
    • 70349672704 scopus 로고    scopus 로고
    • Neuronal IGF-1 resistance reduces Abeta accumulation and protects against premature death in a model of Alzheimer's disease
    • doi:10.1096/fj.09-132043
    • Freude, S., M.M. Hettich, C. Schumann, O. Stöhr, L. Koch, C. Köhler, M. Udelhoven, U. Leeser, M. Müller, N. Kubota, et al. 2009. Neuronal IGF-1 resistance reduces Abeta accumulation and protects against premature death in a model of Alzheimer's disease. FASEB J. 23:3315-3324. doi:10.1096/fj.09-132043
    • (2009) FASEB J. , vol.23 , pp. 3315-3324
    • Freude, S.1    Hettich, M.M.2    Schumann, C.3    Stöhr, O.4    Koch, L.5    Köhler, C.6    Udelhoven, M.7    Leeser, U.8    Müller, M.9    Kubota, N.10
  • 49
    • 33644850056 scopus 로고    scopus 로고
    • Progressive disruption of cellular protein folding in models of polyglutamine diseases
    • doi:10.1126/science.1124514
    • Gidalevitz, T., A. Ben-Zvi, K.H. Ho, H.R. Brignull, and R.I. Morimoto. 2006. Progressive disruption of cellular protein folding in models of polyglutamine diseases. Science. 311:1471-1474. doi:10.1126/science.1124514
    • (2006) Science , vol.311 , pp. 1471-1474
    • Gidalevitz, T.1    Ben-Zvi, A.2    Ho, K.H.3    Brignull, H.R.4    Morimoto, R.I.5
  • 50
    • 0021256895 scopus 로고
    • Alzheimer's disease: Initial report of the purification and characterization of a novel cerebrovascular amyloid protein
    • doi:10.1016/S0006-291X(84)80190-4
    • Glenner, G.G., and C.W. Wong. 1984. Alzheimer's disease: initial report of the purification and characterization of a novel cerebrovascular amyloid protein. Biochem. Biophys. Res. Commun. 120:885-890. doi:10.1016/S0006-291X(84) 80190-4
    • (1984) Biochem. Biophys. Res. Commun. , vol.120 , pp. 885-890
    • Glenner, G.G.1    Wong, C.W.2
  • 51
    • 18544390506 scopus 로고    scopus 로고
    • Post-translational modifications of tau protein in Alzheimer's disease
    • doi:10.1007/s00702-004-0221-0
    • Gong, C.X., F. Liu, I. Grundke-Iqbal, and K. Iqbal. 2005. Post-translational modifications of tau protein in Alzheimer's disease. J. Neural Transm. 112:813-838. doi:10.1007/s00702-004-0221-0
    • (2005) J. Neural Transm. , vol.112 , pp. 813-838
    • Gong, C.X.1    Liu, F.2    Grundke-Iqbal, I.3    Iqbal, K.4
  • 52
    • 34848850156 scopus 로고    scopus 로고
    • An AMPK-FOXO pathway mediates longevity induced by a novel method of dietary restriction in C. elegans
    • doi:10.1016/j.cub.2007.08.047
    • Greer, E.L., D. Dowlatshahi, M.R. Banko, J. Villen, K. Hoang, D. Blanchard, S.P. Gygi, and A. Brunet. 2007. An AMPK-FOXO pathway mediates longevity induced by a novel method of dietary restriction in C. elegans. Curr. Biol. 17:1646-1656. doi:10.1016/j.cub.2007.08.047
    • (2007) Curr. Biol. , vol.17 , pp. 1646-1656
    • Greer, E.L.1    Dowlatshahi, D.2    Banko, M.R.3    Villen, J.4    Hoang, K.5    Blanchard, D.6    Gygi, S.P.7    Brunet, A.8
  • 53
    • 33847662852 scopus 로고    scopus 로고
    • Soluble protein oligomers in neurodegeneration: Lessons from the Alzheimer's amyloid beta-peptide
    • doi:10.1038/nrm2101
    • Haass, C., and D.J. Selkoe. 2007. Soluble protein oligomers in neurodegeneration: lessons from the Alzheimer's amyloid beta-peptide. Nat. Rev. Mol. Cell Biol. 8:101-112. doi:10.1038/nrm2101
    • (2007) Nat. Rev. Mol. Cell Biol. , vol.8 , pp. 101-112
    • Haass, C.1    Selkoe, D.J.2
  • 54
    • 33751113602 scopus 로고    scopus 로고
    • Mammalian sirtuins - Emerging roles in physiology, aging, and calorie restriction
    • doi:10.1101/gad.1467506
    • Haigis, M.C., and L.P. Guarente. 2006. Mammalian sirtuins - emerging roles in physiology, aging, and calorie restriction. Genes Dev. 20:2913-2921. doi:10.1101/gad.1467506
    • (2006) Genes Dev. , vol.20 , pp. 2913-2921
    • Haigis, M.C.1    Guarente, L.P.2
  • 55
    • 33846423520 scopus 로고    scopus 로고
    • Lifespan extension by conditions that inhibit translation in Caenorhabditis elegans
    • doi:10.1111/j.1474-9726.2006.00267.x
    • Hansen, M., S. Taubert, D. Crawford, N. Libina, S.J. Lee, and C. Kenyon. 2007. Lifespan extension by conditions that inhibit translation in Caenorhabditis elegans. Aging Cell. 6:95-110. doi:10.1111/j.1474-9726.2006. 00267.x
    • (2007) Aging Cell , vol.6 , pp. 95-110
    • Hansen, M.1    Taubert, S.2    Crawford, D.3    Libina, N.4    Lee, S.J.5    Kenyon, C.6
  • 57
    • 29444434751 scopus 로고    scopus 로고
    • Amyloid double trouble
    • doi:10.1038/ng0106-11
    • Hardy, J. 2006. Amyloid double trouble. Nat. Genet. 38:11-12. doi:10.1038/ng0106-11
    • (2006) Nat. Genet. , vol.38 , pp. 11-12
    • Hardy, J.1
  • 59
    • 0035857377 scopus 로고    scopus 로고
    • Incidence of dementia and Alzheimer disease in 2 communities: Yoruba residing in Ibadan, Nigeria, and African Americans residing in Indianapolis, Indiana
    • doi:10.1001/jama.285.6.739
    • Hendrie, H.C., A. Ogunniyi, K.S. Hall, O. Baiyewu, F.W. Unverzagt, O. Gureje, S. Gao, R.M. Evans, A.O. Ogunseyinde, A.O. Adeyinka, et al. 2001. Incidence of dementia and Alzheimer disease in 2 communities: Yoruba residing in Ibadan, Nigeria, and African Americans residing in Indianapolis, Indiana. JAMA. 285:739-747. doi:10.1001/jama.285.6.739
    • (2001) JAMA , vol.285 , pp. 739-747
    • Hendrie, H.C.1    Ogunniyi, A.2    Hall, K.S.3    Baiyewu, O.4    Unverzagt, F.W.5    Gureje, O.6    Gao, S.7    Evans, R.M.8    Ogunseyinde, A.O.9    Adeyinka, A.O.10
  • 60
    • 0347664057 scopus 로고    scopus 로고
    • IGF-1 receptor regulates life-span and resistance to oxidative stress in mice
    • doi:10.1038/nature01298
    • Holzenberger, M., J. Dupont, B. Ducos, P. Leneuve, A. Géloën, P.C. Even, P. Cervera, and Y. Le Bouc. 2003. IGF-1 receptor regulates life-span and resistance to oxidative stress in mice. Nature. 421:182-187. doi:10.1038/nature01298
    • (2003) Nature , vol.421 , pp. 182-187
    • Holzenberger, M.1    Dupont, J.2    Ducos, B.3    Leneuve, P.4    Géloën, A.5    Even, P.C.6    Cervera, P.7    Le Bouc, Y.8
  • 61
    • 59649120539 scopus 로고    scopus 로고
    • Signalling through RHEB-1 mediates intermittent fasting-induced longevity in C. elegans
    • doi:10.1038/nature07583
    • Honjoh, S., T. Yamamoto, M. Uno, and E. Nishida. 2009. Signalling through RHEB-1 mediates intermittent fasting-induced longevity in C. elegans. Nature. 457:726-730. doi:10.1038/nature07583
    • (2009) Nature , vol.457 , pp. 726-730
    • Honjoh, S.1    Yamamoto, T.2    Uno, M.3    Nishida, E.4
  • 63
    • 0038701745 scopus 로고    scopus 로고
    • Regulation of aging and age-related disease by DAF-16 and heat-shock factor
    • doi:10.1126/science.1083701
    • Hsu, A.L., C.T. Murphy, and C. Kenyon. 2003. Regulation of aging and age-related disease by DAF-16 and heat-shock factor. Science. 300:1142-1145. doi:10.1126/science.1083701
    • (2003) Science , vol.300 , pp. 1142-1145
    • Hsu, A.L.1    Murphy, C.T.2    Kenyon, C.3
  • 64
    • 0033214237 scopus 로고    scopus 로고
    • The SIR2/3/4 complex and SIR2 alone promote longevity in Saccharomyces cerevisiae by two different mechanisms
    • doi:10.1101/gad.13.19.2570
    • Kaeberlein, M., M. McVey, and L. Guarente. 1999. The SIR2/3/4 complex and SIR2 alone promote longevity in Saccharomyces cerevisiae by two different mechanisms. Genes Dev. 13:2570-2580. doi:10.1101/gad.13.19.2570
    • (1999) Genes Dev. , vol.13 , pp. 2570-2580
    • Kaeberlein, M.1    McVey, M.2    Guarente, L.3
  • 65
    • 19344374925 scopus 로고    scopus 로고
    • Sir2-independent life span extension by calorie restriction in yeast
    • doi:10.1371/journal.pbio.0020296
    • Kaeberlein, M., K.T. Kirkland, S. Fields, and B.K. Kennedy. 2004. Sir2-independent life span extension by calorie restriction in yeast. PLoS Biol. 2:E296. doi:10.1371/journal.pbio.0020296
    • (2004) PLoS Biol. , vol.2
    • Kaeberlein, M.1    Kirkland, K.T.2    Fields, S.3    Kennedy, B.K.4
  • 66
  • 68
    • 3042648746 scopus 로고    scopus 로고
    • Regulation of lifespan in Drosophila by modulation of genes in the TOR signaling pathway
    • doi:10.1016/j.cub.2004.03.059
    • Kapahi, P., B.M. Zid, T. Harper, D. Koslover, V. Sapin, and S. Benzer. 2004. Regulation of lifespan in Drosophila by modulation of genes in the TOR signaling pathway. Curr. Biol. 14:885-890. doi:10.1016/j.cub.2004.03.059
    • (2004) Curr. Biol. , vol.14 , pp. 885-890
    • Kapahi, P.1    Zid, B.M.2    Harper, T.3    Koslover, D.4    Sapin, V.5    Benzer, S.6
  • 69
    • 0242668337 scopus 로고    scopus 로고
    • Common structure of soluble amyloid oligomers implies common mechanism of pathogenesis
    • doi:10.1126/science.1079469
    • Kayed, R., E. Head, J.L. Thompson, T.M. McIntire, S.C. Milton, C.W. Cotman, and C.G. Glabe. 2003. Common structure of soluble amyloid oligomers implies common mechanism of pathogenesis. Science. 300:486-489. doi:10.1126/science.1079469
    • (2003) Science , vol.300 , pp. 486-489
    • Kayed, R.1    Head, E.2    Thompson, J.L.3    McIntire, T.M.4    Milton, S.C.5    Cotman, C.W.6    Glabe, C.G.7
  • 70
    • 12844287619 scopus 로고    scopus 로고
    • An unusual soluble beta-turn-rich conformation of prion is involved in fibril formation and toxic to neuronal cells
    • doi:10.1016/j.bbrc.2004.12.172
    • Kazlauskaite, J., A. Young, C.E. Gardner, J.V. Macpherson, C. Vénien-Bryan, and T.J. Pinheiro. 2005. An unusual soluble beta-turn-rich conformation of prion is involved in fibril formation and toxic to neuronal cells. Biochem. Biophys. Res. Commun. 328:292-305. doi:10.1016/j.bbrc.2004.12. 172
    • (2005) Biochem. Biophys. Res. Commun. , vol.328 , pp. 292-305
    • Kazlauskaite, J.1    Young, A.2    Gardner, C.E.3    Macpherson, J.V.4    Vénien-Bryan, C.5    Pinheiro, T.J.6
  • 71
    • 77950200010 scopus 로고    scopus 로고
    • The genetics of ageing
    • doi:10.1038/nature08980
    • Kenyon, C.J. 2010. The genetics of ageing. Nature. 464:504-512. doi:10.1038/nature08980
    • (2010) Nature , vol.464 , pp. 504-512
    • Kenyon, C.J.1
  • 72
    • 0027771804 scopus 로고
    • C. elegans mutant that lives twice as long as wild type
    • doi:10.1038/366461a0
    • Kenyon, C., J. Chang, E. Gensch, A. Rudner, and R. Tabtiang. 1993. A C. elegans mutant that lives twice as long as wild type. Nature. 366:461-464. doi:10.1038/366461a0
    • (1993) Nature , vol.366 , pp. 461-464
    • Kenyon, C.1    Chang, J.2    Gensch, E.3    Rudner, A.4    Tabtiang, R.5
  • 73
    • 37049048544 scopus 로고
    • Paired helical filaments in electron microscopy of Alzheimer's disease
    • doi:10.1038/197192b0
    • Kidd, M. 1963. Paired helical filaments in electron microscopy of Alzheimer's disease. Nature. 197:192-193. doi:10.1038/197192b0
    • (1963) Nature , vol.197 , pp. 192-193
    • Kidd, M.1
  • 76
    • 0032590053 scopus 로고    scopus 로고
    • Huntington aggregates may not predict neuronal death in Huntington's disease
    • doi:10.1002/1531-8249(199912)46:6〈842::AID-ANA6〉3.0.CO;2-O
    • Kuemmerle, S., C.A. Gutekunst, A.M. Klein, X.J. Li, S.H. Li, M.F. Beal, S.M. Hersch, and R.J. Ferrante. 1999. Huntington aggregates may not predict neuronal death in Huntington's disease. Ann. Neurol. 46:842-849. doi:10.1002/1531-8249(199912)46:6〈842::AID-ANA6〉3.0.CO;2-O
    • (1999) Ann. Neurol. , vol.46 , pp. 842-849
    • Kuemmerle, S.1    Gutekunst, C.A.2    Klein, A.M.3    Li, X.J.4    Li, S.H.5    Beal, M.F.6    Hersch, S.M.7    Ferrante, R.J.8
  • 77
    • 0034091707 scopus 로고    scopus 로고
    • Behavioral disturbances without amyloid deposits in mice overexpressing human amyloid precursor protein with Flemish (A692G) or Dutch (E693Q) mutation
    • doi:10.1006/nbdi.1999.0272
    • Kumar-Singh, S., I. Dewachter, D. Moechars, U. Lübke, C. De Jonghe, C. Ceuterick, F. Checler, A. Naidu, B. Cordell, P. Cras, et al. 2000. Behavioral disturbances without amyloid deposits in mice overexpressing human amyloid precursor protein with Flemish (A692G) or Dutch (E693Q) mutation. Neurobiol. Dis. 7:9-22. doi:10.1006/nbdi.1999.0272
    • (2000) Neurobiol. Dis. , vol.7 , pp. 9-22
    • Kumar-Singh, S.1    Dewachter, I.2    Moechars, D.3    Lübke, U.4    De Jonghe, C.5    Ceuterick, C.6    Checler, F.7    Naidu, A.8    Cordell, B.9    Cras, P.10
  • 79
    • 0034703217 scopus 로고    scopus 로고
    • Requirement of NAD and SIR2 for life-span extension by calorie restriction in Saccharomyces cerevisiae
    • doi:10.1126/science.289.5487.2126
    • Lin, S.J., P.A. Defossez, and L. Guarente. 2000. Requirement of NAD and SIR2 for life-span extension by calorie restriction in Saccharomyces cerevisiae. Science. 289:2126-2128. doi:10.1126/science.289.5487.2126
    • (2000) Science , vol.289 , pp. 2126-2128
    • Lin, S.J.1    Defossez, P.A.2    Guarente, L.3
  • 80
    • 3242739968 scopus 로고    scopus 로고
    • O-GlcNAcylation regulates phosphorylation of tau: A mechanism involved in Alzheimer's disease
    • doi:10.1073/pnas.0400348101
    • Liu, F., K. Iqbal, I. Grundke-Iqbal, G.W. Hart, and C.X. Gong. 2004. O-GlcNAcylation regulates phosphorylation of tau: a mechanism involved in Alzheimer's disease. Proc. Natl. Acad. Sci. USA. 101:10804-10809. doi:10.1073/pnas.0400348101
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 10804-10809
    • Liu, F.1    Iqbal, K.2    Grundke-Iqbal, I.3    Hart, G.W.4    Gong, C.X.5
  • 81
    • 0036679197 scopus 로고    scopus 로고
    • Alpha-Synucleinopathy and selective dopaminergic neuron loss in a rat lentiviral-based model of Parkinson's disease
    • doi:10.1073/pnas.152339799
    • Lo Bianco, C., J.L. Ridet, B.L. Schneider, N. Deglon, and P. Aebischer. 2002. alpha-Synucleinopathy and selective dopaminergic neuron loss in a rat lentiviral-based model of Parkinson's disease. Proc. Natl. Acad. Sci. USA. 99:10813-10818. doi:10.1073/pnas.152339799
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 10813-10818
    • Lo Bianco, C.1    Ridet, J.L.2    Schneider, B.L.3    Deglon, N.4    Aebischer, P.5
  • 82
    • 0036797552 scopus 로고    scopus 로고
    • Impaired dopamine storage resulting from alpha-synuclein mutations may contribute to the pathogenesis of Parkinson's disease
    • doi:10.1093/hmg/11.20.2395
    • Lotharius, J., and P. Brundin. 2002. Impaired dopamine storage resulting from alpha-synuclein mutations may contribute to the pathogenesis of Parkinson's disease. Hum. Mol. Genet. 11:2395-2407. doi:10.1093/hmg/11.20.2395
    • (2002) Hum. Mol. Genet. , vol.11 , pp. 2395-2407
    • Lotharius, J.1    Brundin, P.2
  • 83
    • 0036334166 scopus 로고    scopus 로고
    • Caloric intake and the risk of Alzheimer disease
    • doi:10.1001/archneur.59.8.1258
    • Luchsinger, J.A., M.X. Tang, S. Shea, and R. Mayeux. 2002. Caloric intake and the risk of Alzheimer disease. Arch. Neurol. 59:1258-1263. doi:10.1001/archneur.59.8.1258
    • (2002) Arch. Neurol. , vol.59 , pp. 1258-1263
    • Luchsinger, J.A.1    Tang, M.X.2    Shea, S.3    Mayeux, R.4
  • 84
    • 67349217986 scopus 로고    scopus 로고
    • Molecular mechanisms of mTOR-mediated translational control
    • doi:10.1038/nrm2672
    • Ma, X.M., and J. Blenis. 2009. Molecular mechanisms of mTOR-mediated translational control. Nat. Rev. Mol. Cell Biol. 10:307-318. doi:10.1038/nrm2672
    • (2009) Nat. Rev. Mol. Cell Biol. , vol.10 , pp. 307-318
    • Ma, X.M.1    Blenis, J.2
  • 85
    • 84887212584 scopus 로고    scopus 로고
    • Optimizing dietary restriction for genetic epistasis analysis and gene discovery in C. elegans
    • doi:10.1371/journal.pone.0004535
    • Mair, W., S.H. Panowski, R.J. Shaw, and A. Dillin. 2009. Optimizing dietary restriction for genetic epistasis analysis and gene discovery in C. elegans. PLoS One. 4:e4535. doi:10.1371/journal.pone.0004535
    • (2009) PLoS One , vol.4
    • Mair, W.1    Panowski, S.H.2    Shaw, R.J.3    Dillin, A.4
  • 86
    • 27844497059 scopus 로고    scopus 로고
    • Resveratrol promotes clearance of Alzheimer's disease amyloid-beta peptides
    • doi:10.1074/jbc.M508246200
    • Marambaud, P., H. Zhao, and P. Davies. 2005. Resveratrol promotes clearance of Alzheimer's disease amyloid-beta peptides. J. Biol. Chem. 280:37377-37382. doi:10.1074/jbc.M508246200
    • (2005) J. Biol. Chem. , vol.280 , pp. 37377-37382
    • Marambaud, P.1    Zhao, H.2    Davies, P.3
  • 89
    • 20744435383 scopus 로고    scopus 로고
    • Molecular pathophysiology of Parkinson's disease
    • doi:10.1146/annurev.neuro.28.061604.135718
    • Moore, D.J., A.B. West, V.L. Dawson, and T.M. Dawson. 2005. Molecular pathophysiology of Parkinson's disease. Annu. Rev. Neurosci. 28:57-87. doi:10.1146/annurev.neuro.28.061604.135718
    • (2005) Annu. Rev. Neurosci. , vol.28 , pp. 57-87
    • Moore, D.J.1    West, A.B.2    Dawson, V.L.3    Dawson, T.M.4
  • 90
    • 44849094781 scopus 로고    scopus 로고
    • Proteotoxic stress and inducible chaperone networks in neurodegenerative disease and aging
    • doi: 10.1101/gad.1657108
    • Morimoto, R.I. 2008. Proteotoxic stress and inducible chaperone networks in neurodegenerative disease and aging. Genes Dev. 22:1427-1438. doi: 10.1101/gad.1657108
    • (2008) Genes Dev. , vol.22 , pp. 1427-1438
    • Morimoto, R.I.1
  • 91
    • 0742323000 scopus 로고    scopus 로고
    • Regulation of longevity in Caenorhabditis elegans by heat shock factor and molecular chaperones
    • doi:10.1091/mbc.E03-07-0532
    • Morley, J.F., and R.I. Morimoto. 2004. Regulation of longevity in Caenorhabditis elegans by heat shock factor and molecular chaperones. Mol. Biol. Cell. 15:657-664. doi:10.1091/mbc.E03-07-0532
    • (2004) Mol. Biol. Cell , vol.15 , pp. 657-664
    • Morley, J.F.1    Morimoto, R.I.2
  • 92
    • 0036678146 scopus 로고    scopus 로고
    • The threshold for polyglutamine-expansion protein aggregation and cellular toxicity is dynamic and influenced by aging in Caenorhabditis elegans
    • doi:10.1073/pnas.152161099
    • Morley, J.F., H.R. Brignull, J.J. Weyers, and R.I. Morimoto. 2002. The threshold for polyglutamine-expansion protein aggregation and cellular toxicity is dynamic and influenced by aging in Caenorhabditis elegans. Proc. Natl. Acad. Sci. USA. 99:10417-10422. doi:10.1073/pnas.152161099
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 10417-10422
    • Morley, J.F.1    Brignull, H.R.2    Weyers, J.J.3    Morimoto, R.I.4
  • 93
    • 0024448365 scopus 로고
    • Dietary restriction suppresses age-related changes in dendritic spines
    • doi:10.1016/0197-4580(89)90042-0
    • Moroi-Fetters, S.E., R.F. Mervis, E.D. London, and D.K. Ingram. 1989. Dietary restriction suppresses age-related changes in dendritic spines. Neurobiol. Aging. 10:317-322. doi:10.1016/0197-4580(89)90042-0
    • (1989) Neurobiol. Aging , vol.10 , pp. 317-322
    • Moroi-Fetters, S.E.1    Mervis, R.F.2    London, E.D.3    Ingram, D.K.4
  • 94
    • 2442534084 scopus 로고    scopus 로고
    • Differential cytotoxicity of human wild type and mutant alpha-synuclein in human neuroblastoma SH-SY5Y cells in the presence of dopamine
    • doi:10.1021/bi036114f
    • Moussa, C.E., C. Wersinger, Y. Tomita, and A. Sidhu. 2004. Differential cytotoxicity of human wild type and mutant alpha-synuclein in human neuroblastoma SH-SY5Y cells in the presence of dopamine. Biochemistry. 43:5539-5550. doi:10.1021/bi036114f
    • (2004) Biochemistry , vol.43 , pp. 5539-5550
    • Moussa, C.E.1    Wersinger, C.2    Tomita, Y.3    Sidhu, A.4
  • 95
    • 11144243412 scopus 로고    scopus 로고
    • Modulation of neurodegeneration by molecular chaperones
    • doi:10.1038/nrn1587
    • Muchowski, P.J., and J.L. Wacker. 2005. Modulation of neurodegeneration by molecular chaperones. Nat. Rev. Neurosci. 6:11-22. doi:10.1038/nrn1587
    • (2005) Nat. Rev. Neurosci. , vol.6 , pp. 11-22
    • Muchowski, P.J.1    Wacker, J.L.2
  • 97
    • 0032512636 scopus 로고    scopus 로고
    • Tor, a phosphatidylinositol kinase homologue, controls autophagy in yeast
    • doi:10.1074/jbc.273.7.3963
    • Noda, T., and Y. Ohsumi. 1998. Tor, a phosphatidylinositol kinase homologue, controls autophagy in yeast. J. Biol. Chem. 273:3963-3966. doi:10.1074/jbc.273.7.3963
    • (1998) J. Biol. Chem. , vol.273 , pp. 3963-3966
    • Noda, T.1    Ohsumi, Y.2
  • 98
    • 2342652188 scopus 로고    scopus 로고
    • Genome-wide RNA interference screen identifies previously undescribed regulators of polyglutamine aggregation
    • doi:10.1073/pnas.0307697101
    • Nollen, E.A., S.M. Garcia, G. van Haaften, S. Kim, A. Chavez, R.I. Morimoto, and R.H. Plasterk. 2004. Genome-wide RNA interference screen identifies previously undescribed regulators of polyglutamine aggregation. Proc. Natl. Acad. Sci. USA. 101:6403-6408. doi:10.1073/pnas.0307697101
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 6403-6408
    • Nollen, E.A.1    Garcia, S.M.2    Van Haaften, G.3    Kim, S.4    Chavez, A.5    Morimoto, R.I.6    Plasterk, R.H.7
  • 101
    • 53249114029 scopus 로고    scopus 로고
    • Inhibition of specific HDACs and sirtuins suppresses pathogenesis in a Drosophila model of Huntington's disease
    • doi:10.1093/hmg/ddn273
    • Pallos, J., L. Bodai, T. Lukacsovich, J.M. Purcell, J.S. Steffan, L.M. Thompson, and J.L. Marsh. 2008. Inhibition of specific HDACs and sirtuins suppresses pathogenesis in a Drosophila model of Huntington's disease. Hum. Mol. Genet. 17:3767-3775. doi:10.1093/hmg/ddn273
    • (2008) Hum. Mol. Genet. , vol.17 , pp. 3767-3775
    • Pallos, J.1    Bodai, L.2    Lukacsovich, T.3    Purcell, J.M.4    Steffan, J.S.5    Thompson, L.M.6    Marsh, J.L.7
  • 102
    • 34249888736 scopus 로고    scopus 로고
    • PHA-4/Foxa mediates diet-restriction-induced longevity of C. elegans
    • doi:10.1038/nature05837
    • Panowski, S.H., S. Wolff, H. Aguilaniu, J. Durieux, and A. Dillin. 2007. PHA-4/Foxa mediates diet-restriction-induced longevity of C. elegans. Nature. 447:550-555. doi:10.1038/nature05837
    • (2007) Nature , vol.447 , pp. 550-555
    • Panowski, S.H.1    Wolff, S.2    Aguilaniu, H.3    Durieux, J.4    Dillin, A.5
  • 103
    • 0025072207 scopus 로고
    • Dietary restriction slows the abnormally rapid loss of spiral ganglion neurons in C57BL/6 mice
    • doi:10.1016/0378-5955(90)90067-Y
    • Park, J.C., K.C. Cook, and E.A. Verde. 1990. Dietary restriction slows the abnormally rapid loss of spiral ganglion neurons in C57BL/6 mice. Hear. Res. 48:275-279. doi:10.1016/0378-5955(90)90067-Y
    • (1990) Hear. Res. , vol.48 , pp. 275-279
    • Park, J.C.1    Cook, K.C.2    Verde, E.A.3
  • 104
    • 16844375290 scopus 로고    scopus 로고
    • Resveratrol rescues mutant polyglutamine cytotoxicity in nematode and mammalian neurons
    • doi:10.1038/ng1534
    • Parker, J.A., M. Arango, S. Abderrahmane, E. Lambert, C. Tourette, H. Catoire, and C. Néri. 2005. Resveratrol rescues mutant polyglutamine cytotoxicity in nematode and mammalian neurons. Nat. Genet. 37:349-350. doi:10.1038/ng1534
    • (2005) Nat. Genet. , vol.37 , pp. 349-350
    • Parker, J.A.1    Arango, M.2    Abderrahmane, S.3    Lambert, E.4    Tourette, C.5    Catoire, H.6    Néri, C.7
  • 105
    • 48349144852 scopus 로고    scopus 로고
    • Resveratrol delays age-related deterioration and mimics transcriptional aspects of dietary restriction without extending life span
    • doi:10.1016/j.cmet.2008.06.011
    • Pearson, K.J., J.A. Baur, K.N. Lewis, L. Peshkin, N.L. Price, N. Labinskyy, W.R. Swindell, D. Kamara, R.K. Minor, E. Perez, et al. 2008. Resveratrol delays age-related deterioration and mimics transcriptional aspects of dietary restriction without extending life span. Cell Metab. 8:157-168. doi:10.1016/j.cmet.2008.06.011
    • (2008) Cell Metab. , vol.8 , pp. 157-168
    • Pearson, K.J.1    Baur, J.A.2    Lewis, K.N.3    Peshkin, L.4    Price, N.L.5    Labinskyy, N.6    Swindell, W.R.7    Kamara, D.8    Minor, R.K.9    Perez, E.10
  • 106
    • 42149165496 scopus 로고    scopus 로고
    • A closer look at alpha-secretase
    • doi:10.2174/156720508783954668
    • Postina, R. 2008. A closer look at alpha-secretase. Curr. Alzheimer Res. 5:179-186. doi:10.2174/156720508783954668
    • (2008) Curr. Alzheimer Res. , vol.5 , pp. 179-186
    • Postina, R.1
  • 107
    • 0032506187 scopus 로고    scopus 로고
    • Prions
    • doi:10.1073/pnas.95.23.13363
    • Prusiner, S.B. 1998. Prions. Proc. Natl. Acad. Sci. USA. 95:13363-13383. doi:10.1073/pnas.95.23.13363
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 13363-13383
    • Prusiner, S.B.1
  • 109
    • 33746824192 scopus 로고    scopus 로고
    • Neuronal SIRT1 activation as a novel mechanism underlying the prevention of Alzheimer disease amyloid neuropathology by calorie restriction
    • doi:10.1074/jbc.M602909200
    • Qin, W., T. Yang, L. Ho, Z. Zhao, J. Wang, L. Chen, W. Zhao, M. Thiyagarajan, D. MacGrogan, J.T. Rodgers, et al. 2006b. Neuronal SIRT1 activation as a novel mechanism underlying the prevention of Alzheimer disease amyloid neuropathology by calorie restriction. J. Biol. Chem. 281:21745-21754. doi:10.1074/jbc.M602909200
    • (2006) J. Biol. Chem. , vol.281 , pp. 21745-21754
    • Qin, W.1    Yang, T.2    Ho, L.3    Zhao, Z.4    Wang, J.5    Chen, L.6    Zhao, W.7    Thiyagarajan, M.8    MacGrogan, D.9    Rodgers, J.T.10
  • 110
    • 0036566266 scopus 로고    scopus 로고
    • Aggregate-prone proteins with polyglutamine and polyalanine expansions are degraded by autophagy
    • doi:10.1093/hmg/11.9.1107
    • Ravikumar, B., R. Duden, and D.C. Rubinsztein. 2002. Aggregate-prone proteins with polyglutamine and polyalanine expansions are degraded by autophagy. Hum. Mol. Genet. 11:1107-1117. doi:10.1093/hmg/11.9.1107
    • (2002) Hum. Mol. Genet. , vol.11 , pp. 1107-1117
    • Ravikumar, B.1    Duden, R.2    Rubinsztein, D.C.3
  • 112
    • 0013913695 scopus 로고
    • The biology of aging
    • Reichel, W. 1966. The biology of aging. J. Am. Geriatr. Soc. 14:431-446.
    • (1966) J. Am. Geriatr. Soc. , vol.14 , pp. 431-446
    • Reichel, W.1
  • 113
    • 2942536602 scopus 로고    scopus 로고
    • The paradox of the insulin/IGF-1 signaling pathway in longevity
    • doi:10.1016/j.mad.2004.03.006
    • Rincon, M., R. Muzumdar, G. Atzmon, and N. Barzilai. 2004. The paradox of the insulin/IGF-1 signaling pathway in longevity. Mech. Ageing Dev. 125:397-403. doi:10.1016/j.mad.2004.03.006
    • (2004) Mech. Ageing Dev. , vol.125 , pp. 397-403
    • Rincon, M.1    Muzumdar, R.2    Atzmon, G.3    Barzilai, N.4
  • 114
    • 0023340731 scopus 로고
    • Four genes responsible for a position effect on expression from HML and HMR in Saccharomyces cerevisiae
    • Rine, J., and I. Herskowitz. 1987. Four genes responsible for a position effect on expression from HML and HMR in Saccharomyces cerevisiae. Genetics. 116:9-22.
    • (1987) Genetics , vol.116 , pp. 9-22
    • Rine, J.1    Herskowitz, I.2
  • 115
    • 8644224064 scopus 로고    scopus 로고
    • Sir2 mediates longevity in the fly through a pathway related to calorie restriction
    • doi:10.1073/pnas.0404184101
    • Rogina, B., and S.L. Helfand. 2004. Sir2 mediates longevity in the fly through a pathway related to calorie restriction. Proc. Natl. Acad. Sci. USA. 101:15998-16003. doi:10.1073/pnas.0404184101
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 15998-16003
    • Rogina, B.1    Helfand, S.L.2
  • 116
    • 0037194897 scopus 로고    scopus 로고
    • Polyglutamine pathogenesis: Emergence of unifying mechanisms for Huntington's disease and related disorders
    • doi:10.1016/S0896-6273(02)00872-3
    • Ross, C.A. 2002. Polyglutamine pathogenesis: emergence of unifying mechanisms for Huntington's disease and related disorders. Neuron. 35:819-822. doi:10.1016/S0896-6273(02)00872-3
    • (2002) Neuron , vol.35 , pp. 819-822
    • Ross, C.A.1
  • 118
    • 0032475931 scopus 로고    scopus 로고
    • Huntingtin acts in the nucleus to induce apoptosis but death does not correlate with the formation of intranuclear inclusions
    • doi:10.1016/S0092-8674(00)81782-1
    • Saudou, F., S. Finkbeiner, D. Devys, and M.E. Greenberg. 1998. Huntingtin acts in the nucleus to induce apoptosis but death does not correlate with the formation of intranuclear inclusions. Cell. 95:55-66. doi:10.1016/S0092-8674(00) 81782-1
    • (1998) Cell , vol.95 , pp. 55-66
    • Saudou, F.1    Finkbeiner, S.2    Devys, D.3    Greenberg, M.E.4
  • 119
    • 5644239087 scopus 로고    scopus 로고
    • Alzheimer disease: Mechanistic understanding predicts novel therapies
    • American College of Physicians; American Physiological Society
    • Selkoe, D.J.; American College of Physicians; American Physiological Society. 2004. Alzheimer disease: mechanistic understanding predicts novel therapies. Ann. Intern. Med. 140:627-638.
    • (2004) Ann. Intern. Med. , vol.140 , pp. 627-638
    • Selkoe, D.J.1
  • 121
    • 0035139109 scopus 로고    scopus 로고
    • Cellular defenses against unfolded proteins: A cell biologist thinks about neurodegenerative diseases
    • doi:10.1016/S0896-6273(01)00177-5
    • Sherman, M.Y., and A.L. Goldberg. 2001. Cellular defenses against unfolded proteins: a cell biologist thinks about neurodegenerative diseases. Neuron. 29:15-32. doi:10.1016/S0896-6273(01)00177-5
    • (2001) Neuron , vol.29 , pp. 15-32
    • Sherman, M.Y.1    Goldberg, A.L.2
  • 122
    • 19544363062 scopus 로고    scopus 로고
    • Prions as adaptive conduits of memory and inheritance
    • doi:10.1038/nrg1616
    • Shorter, J., and S. Lindquist. 2005. Prions as adaptive conduits of memory and inheritance. Nat. Rev. Genet. 6:435-450. doi:10.1038/nrg1616
    • (2005) Nat. Rev. Genet. , vol.6 , pp. 435-450
    • Shorter, J.1    Lindquist, S.2
  • 126
    • 0036548070 scopus 로고    scopus 로고
    • Gamma-Secretase, Notch, Abeta and Alzheimer's disease: Where do the presenilins fit in?
    • doi:10.1038/nrn785
    • Sisodia, S.S., and P.H. St George-Hyslop. 2002. gamma-Secretase, Notch, Abeta and Alzheimer's disease: where do the presenilins fit in? Nat. Rev. Neurosci. 3:281-290. doi:10.1038/nrn785
    • (2002) Nat. Rev. Neurosci. , vol.3 , pp. 281-290
    • Sisodia, S.S.1    St George-Hyslop, P.H.2
  • 127
    • 43449138491 scopus 로고    scopus 로고
    • Dietary restriction suppresses proteotoxicity and enhances longevity by an hsf-1-dependent mechanism in Caenorhabditis elegans
    • doi:10.1111/j.1474-9726.2008.00385.x
    • Steinkraus, K.A., E.D. Smith, C. Davis, D. Carr, W.R. Pendergrass, G.L. Sutphin, B.K. Kennedy, and M. Kaeberlein. 2008. Dietary restriction suppresses proteotoxicity and enhances longevity by an hsf-1-dependent mechanism in Caenorhabditis elegans. Aging Cell. 7:394-404. doi:10.1111/j.1474-9726.2008. 00385.x
    • (2008) Aging Cell , vol.7 , pp. 394-404
    • Steinkraus, K.A.1    Smith, E.D.2    Davis, C.3    Carr, D.4    Pendergrass, W.R.5    Sutphin, G.L.6    Kennedy, B.K.7    Kaeberlein, M.8
  • 128
    • 69449084089 scopus 로고    scopus 로고
    • Rapamycin activation of 4E-BP prevents parkinsonian dopaminergic neuron loss
    • doi:10.1038/nn.2372
    • Tain, L.S., H. Mortiboys, R.N. Tao, E. Ziviani, O. Bandmann, and A.J. Whitworth. 2009. Rapamycin activation of 4E-BP prevents parkinsonian dopaminergic neuron loss. Nat. Neurosci. 12:1129-1135. doi:10.1038/nn.2372
    • (2009) Nat. Neurosci. , vol.12 , pp. 1129-1135
    • Tain, L.S.1    Mortiboys, H.2    Tao, R.N.3    Ziviani, E.4    Bandmann, O.5    Whitworth, A.J.6
  • 129
    • 0035815445 scopus 로고    scopus 로고
    • A mutant Drosophila insulin receptor homolog that extends life-span and impairs neuroendocrine function
    • doi:10.1126/science.1057987
    • Tatar, M., A. Kopelman, D. Epstein, M.P. Tu, C.M. Yin, and R.S. Garofalo. 2001. A mutant Drosophila insulin receptor homolog that extends life-span and impairs neuroendocrine function. Science. 292:107-110. doi:10.1126/science. 1057987
    • (2001) Science , vol.292 , pp. 107-110
    • Tatar, M.1    Kopelman, A.2    Epstein, D.3    Tu, M.P.4    Yin, C.M.5    Garofalo, R.S.6
  • 130
    • 0035826271 scopus 로고    scopus 로고
    • Increased dosage of a sir-2 gene extends lifespan in Caenorhabditis elegans
    • doi:10.1038/35065638
    • Tissenbaum, H.A., and L. Guarente. 2001. Increased dosage of a sir-2 gene extends lifespan in Caenorhabditis elegans. Nature. 410:227-230. doi:10.1038/35065638
    • (2001) Nature , vol.410 , pp. 227-230
    • Tissenbaum, H.A.1    Guarente, L.2
  • 131
    • 77950617631 scopus 로고    scopus 로고
    • 2010. A mouse model of amyloid beta oligomers: Their contribution to synaptic alteration, abnormal tau phosphorylation, glial activation, and neuronal loss in vivo
    • doi:10.1523/JNEUROSCI.5825-09.2010
    • Tomiyama, T., S. Matsuyama, H. Iso, T. Umeda, H. Takuma, K. Ohnishi, K. Ishibashi, R. Teraoka, N. Sakama, T. Yamashita, et al. 2010. A mouse model of amyloid beta oligomers: their contribution to synaptic alteration, abnormal tau phosphorylation, glial activation, and neuronal loss in vivo. J. Neurosci. 30:4845-4856. doi:10.1523/JNEUROSCI.5825-09.2010
    • J. Neurosci. , vol.30 , pp. 4845-4856
    • Tomiyama, T.1    Matsuyama, S.2    Iso, H.3    Umeda, T.4    Takuma, H.5    Ohnishi, K.6    Ishibashi, K.7    Teraoka, R.8    Sakama, N.9    Yamashita, T.10
  • 132
    • 4544235083 scopus 로고    scopus 로고
    • Epigenetic regulation of translation reveals hidden genetic variation to produce complex traits
    • doi:10.1038/nature02885
    • True, H.L., I. Berlin, and S.L. Lindquist. 2004. Epigenetic regulation of translation reveals hidden genetic variation to produce complex traits. Nature. 431:184-187. doi:10.1038/nature02885
    • (2004) Nature , vol.431 , pp. 184-187
    • True, H.L.1    Berlin, I.2    Lindquist, S.L.3
  • 134
    • 41949097891 scopus 로고    scopus 로고
    • C. elegans model identifies genetic modifiers of alpha-synuclein inclusion formation during aging
    • doi:10.1371/journal.pgen.1000027
    • van Ham, T.J., K.L. Thijssen, R. Breitling, R.M. Hofstra, R.H. Plasterk, and E.A. Nollen. 2008. C. elegans model identifies genetic modifiers of alpha-synuclein inclusion formation during aging. PLoS Genet. 4:e1000027. doi:10.1371/journal.pgen.1000027
    • (2008) PLoS Genet. , vol.4
    • Van Ham, T.J.1    Thijssen, K.L.2    Breitling, R.3    Hofstra, R.M.4    Plasterk, R.H.5    Nollen, E.A.6
  • 136
    • 0642367846 scopus 로고    scopus 로고
    • Genetics: Influence of TOR kinase on lifespan in C. elegans
    • doi:10.1038/426620a
    • Vellai, T., K. Takacs-Vellai, Y. Zhang, A.L. Kovacs, L. Orosz, and F. Müller. 2003. Genetics: influence of TOR kinase on lifespan in C. elegans. Nature. 426:620. doi:10.1038/426620a
    • (2003) Nature , vol.426 , pp. 620
    • Vellai, T.1    Takacs-Vellai, K.2    Zhang, Y.3    Kovacs, A.L.4    Orosz, L.5    Müller, F.6
  • 137
  • 138
    • 69949180640 scopus 로고    scopus 로고
    • TOR-mediated autophagy regulates cell death in Drosophila neurodegenerative disease
    • doi:10.1083/jcb.200904090
    • Wang, T., U. Lao, and B.A. Edgar. 2009. TOR-mediated autophagy regulates cell death in Drosophila neurodegenerative disease. J. Cell Biol. 186:703-711. doi:10.1083/jcb.200904090
    • (2009) J. Cell Biol. , vol.186 , pp. 703-711
    • Wang, T.1    Lao, U.2    Edgar, B.A.3
  • 139
    • 0041589248 scopus 로고    scopus 로고
    • Alpha-Synuclein is degraded by both autophagy and the proteasome
    • doi:10.1074/jbc.M300227200
    • Webb, J.L., B. Ravikumar, J. Atkins, J.N. Skepper, and D.C. Rubinsztein. 2003. Alpha-Synuclein is degraded by both autophagy and the proteasome. J. Biol. Chem. 278:25009-25013. doi:10.1074/jbc.M300227200
    • (2003) J. Biol. Chem. , vol.278 , pp. 25009-25013
    • Webb, J.L.1    Ravikumar, B.2    Atkins, J.3    Skepper, J.N.4    Rubinsztein, D.C.5
  • 140
    • 0024550204 scopus 로고
    • Identification, biogenesis, and localization of precursors of Alzheimer's disease A4 amyloid protein
    • doi:10.1016/0092-8674(89)90177-3
    • Weidemann, A., G. König, D. Bunke, P. Fischer, J.M. Salbaum, C.L. Masters, and K. Beyreuther. 1989. Identification, biogenesis, and localization of precursors of Alzheimer's disease A4 amyloid protein. Cell. 57:115-126. doi:10.1016/0092-8674(89)90177-3
    • (1989) Cell , vol.57 , pp. 115-126
    • Weidemann, A.1    König, G.2    Bunke, D.3    Fischer, P.4    Salbaum, J.M.5    Masters, C.L.6    Beyreuther, K.7
  • 141
    • 60749101582 scopus 로고    scopus 로고
    • Stress-inducible regulation of heat shock factor 1 by the deacetylase SIRT1
    • doi:10.1126/science.1165946
    • Westerheide, S.D., J. Anckar, S.M. Stevens Jr., L. Sistonen, and R.I. Morimoto. 2009. Stress-inducible regulation of heat shock factor 1 by the deacetylase SIRT1. Science. 323:1063-1066. doi:10.1126/science.1165946
    • (2009) Science , vol.323 , pp. 1063-1066
    • Westerheide, S.D.1    Anckar, J.2    Stevens Jr., S.M.3    Sistonen, L.4    Morimoto, R.I.5
  • 142
    • 0033535553 scopus 로고    scopus 로고
    • Two transmembrane aspartates in presenilin-1 required for presenilin endoproteolysis and gamma-secretase activity
    • doi:10.1038/19077
    • Wolfe, M.S., W. Xia, B.L. Ostaszewski, T.S. Diehl, W.T. Kimberly, and D.J. Selkoe. 1999. Two transmembrane aspartates in presenilin-1 required for presenilin endoproteolysis and gamma-secretase activity. Nature. 398:513-517. doi:10.1038/19077
    • (1999) Nature , vol.398 , pp. 513-517
    • Wolfe, M.S.1    Xia, W.2    Ostaszewski, B.L.3    Diehl, T.S.4    Kimberly, W.T.5    Selkoe, D.J.6
  • 143
    • 3943071801 scopus 로고    scopus 로고
    • Sirtuin activators mimic caloric restriction and delay ageing in metazoans
    • doi:10.1038/nature02789
    • Wood, J.G., B. Rogina, S. Lavu, K. Howitz, S.L. Helfand, M. Tatar, and D. Sinclair. 2004. Sirtuin activators mimic caloric restriction and delay ageing in metazoans. Nature. 430:686-689. doi:10.1038/nature02789
    • (2004) Nature , vol.430 , pp. 686-689
    • Wood, J.G.1    Rogina, B.2    Lavu, S.3    Howitz, K.4    Helfand, S.L.5    Tatar, M.6    Sinclair, D.7
  • 144
    • 0034094873 scopus 로고    scopus 로고
    • Glutamine repeats and neurodegeneration
    • doi:10.1146/annurev.neuro.23.1.217
    • Zoghbi, H.Y., and H.T. Orr. 2000. Glutamine repeats and neurodegeneration. Annu. Rev. Neurosci. 23:217-247. doi:10.1146/annurev.neuro. 23.1.217
    • (2000) Annu. Rev. Neurosci. , vol.23 , pp. 217-247
    • Zoghbi, H.Y.1    Orr, H.T.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.