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Volumn 27, Issue 2, 2003, Pages 291-301

Proapoptotic protein glyceraldehyde-3-phosphate dehydrogenase: A possible site of action of antiapoptotic drugs

Author keywords

Aggregate formation; Antiapoptotic drugs; Apoptosis; Functional domains; Glyceraldehyde 3 phosphate dehydrogenase; Neurodegenerative disorders; Nuclear translocation; Pathogenesis; Promoter region

Indexed keywords

1 [N (4 CHLOROBENZYL)SUCCINAMOYL]PROLINAL; 10 (N METHYL N PROPARGYLAMINOMETHYL)DIBENZO[B,F]OXEPIN; ANTIPARKINSON AGENT; CHOLINESTERASE INHIBITOR; COMPLEMENTARY DNA; CYCLOHEXIMIDE; DACTINOMYCIN; DONEPEZIL; GLYCERALDEHYDE 3 PHOSPHATE DEHYDROGENASE; MONOAMINE OXIDASE INHIBITOR; N (2 HEPTYL) N METHYLPROPARGYLAMINE; NOOTROPIC AGENT; RASAGILINE; SELEGILINE; TACRINE; UNCLASSIFIED DRUG;

EID: 0345268748     PISSN: 02785846     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0278-5846(03)00024-1     Document Type: Review
Times cited : (50)

References (89)
  • 1
    • 0019972810 scopus 로고
    • The cholinergic hypothesis of geriatric memory dysfunction
    • Bartus R.T., Dean R.L. III, Beer B., Lippa A.S. The cholinergic hypothesis of geriatric memory dysfunction. Science. 217:1982;408-417.
    • (1982) Science , vol.217 , pp. 408-417
    • Bartus, R.T.1    Dean R.L. III2    Beer, B.3    Lippa, A.S.4
  • 3
    • 0035947372 scopus 로고    scopus 로고
    • Impairment of the ubiquitin-proteasome system by protein aggregation
    • Bence N.F., Sampat R.M., Kopito R.R. Impairment of the ubiquitin-proteasome system by protein aggregation. Science. 292:2001;1552-1555.
    • (2001) Science , vol.292 , pp. 1552-1555
    • Bence, N.F.1    Sampat, R.M.2    Kopito, R.R.3
  • 4
    • 0032881811 scopus 로고    scopus 로고
    • R-2HMP, an orally active agent combining independent anti-apoptotic and MAO-B inhibitory activities
    • Berry M.D. R-2HMP, an orally active agent combining independent anti-apoptotic and MAO-B inhibitory activities. CNS Drug Rev. 5:1999;105-124.
    • (1999) CNS Drug Rev. , vol.5 , pp. 105-124
    • Berry, M.D.1
  • 5
    • 0018226855 scopus 로고
    • Report of the committee on the genetic constitution of chromosomes 2, 3, 4, 5, 7, 8, 10, 11, and 12
    • Bootsma D., Ruddle F.H. Report of the committee on the genetic constitution of chromosomes 2, 3, 4, 5, 7, 8, 10, 11, and 12. Cytogenet. Cell Genet. 22:1978;74-91.
    • (1978) Cytogenet. Cell Genet. , vol.22 , pp. 74-91
    • Bootsma, D.1    Ruddle, F.H.2
  • 7
    • 0034603520 scopus 로고    scopus 로고
    • Vascular risk factors for Alzheimer's disease: An epidemiologic perspective
    • Breteler M.M.B. Vascular risk factors for Alzheimer's disease: an epidemiologic perspective. Neurobiol. Aging. 21:2000;153-160.
    • (2000) Neurobiol. Aging , vol.21 , pp. 153-160
    • Breteler, M.M.B.1
  • 9
    • 0032211790 scopus 로고    scopus 로고
    • Demonstration of a RNA-dependent nuclear interaction between the promyelocytic leukaemia protein and glyceraldehyde-3-phosphate dehydrogenase
    • Carlile G.W., Tatton W.G., Borden K.L.B. Demonstration of a RNA-dependent nuclear interaction between the promyelocytic leukaemia protein and glyceraldehyde-3-phosphate dehydrogenase. Biochem. J. 335:1998;691-696.
    • (1998) Biochem. J. , vol.335 , pp. 691-696
    • Carlile, G.W.1    Tatton, W.G.2    Borden, K.L.B.3
  • 10
    • 0033989493 scopus 로고    scopus 로고
    • Reduced apoptosis after nerve growth factor and serum withdrawal: Conversion of tetrameric glyceraldehyde-3-phosphate dehydrogenase to a dimer
    • Carlile G.W., Chalmers-Redman R.M.E., Tatton N.A., Pong A., Borden K.L.B., Tatton W.G. Reduced apoptosis after nerve growth factor and serum withdrawal: conversion of tetrameric glyceraldehyde-3-phosphate dehydrogenase to a dimer. Mol. Pharmacol. 57:2000;2-12.
    • (2000) Mol. Pharmacol. , vol.57 , pp. 2-12
    • Carlile, G.W.1    Chalmers-Redman, R.M.E.2    Tatton, N.A.3    Pong, A.4    Borden, K.L.B.5    Tatton, W.G.6
  • 11
    • 0021804407 scopus 로고
    • Interaction of glyceraldehyde-3-phosphate dehydrogenase with isolated microsomal subfractions of skeletal muscle
    • Caswell A.H., Corbett A.M. Interaction of glyceraldehyde-3-phosphate dehydrogenase with isolated microsomal subfractions of skeletal muscle. J. Biol. Chem. 260:1985;6892-6898.
    • (1985) J. Biol. Chem. , vol.260 , pp. 6892-6898
    • Caswell, A.H.1    Corbett, A.M.2
  • 12
    • 0033232529 scopus 로고    scopus 로고
    • Involvement of glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and p53 in neuronal apoptosis: Evidence that GAPDH is up-regulated by p53
    • Chen R.-W., Saunders P.A., Wei H., Li Z., Seth P., Chuang D.-M. Involvement of glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and p53 in neuronal apoptosis: evidence that GAPDH is up-regulated by p53. J. Neurosci. 19:1999;9654-9662.
    • (1999) J. Neurosci. , vol.19 , pp. 9654-9662
    • Chen, R.-W.1    Saunders, P.A.2    Wei, H.3    Li, Z.4    Seth, P.5    Chuang, D.-M.6
  • 13
    • 0032563246 scopus 로고    scopus 로고
    • Crystallographic analysis of the recognition of a nuclear localization signal by the nuclear import factor karyopherin α
    • Conti E., Uy M., Leighton L., Blobel G., Kuriyan J. Crystallographic analysis of the recognition of a nuclear localization signal by the nuclear import factor karyopherin α Cell. 94:1998;193-204.
    • (1998) Cell , vol.94 , pp. 193-204
    • Conti, E.1    Uy, M.2    Leighton, L.3    Blobel, G.4    Kuriyan, J.5
  • 15
    • 0032501740 scopus 로고    scopus 로고
    • Are neuronal intranuclear inclusions the common neuropathology of triplet-repeat disorders with polyglutamine-repeat expansions?
    • Davies S.W., Beardsall K., Turmaine M., DiFiglia M., Aronin N., Bates G.P. Are neuronal intranuclear inclusions the common neuropathology of triplet-repeat disorders with polyglutamine-repeat expansions? Lancet. 351:1998;131-133.
    • (1998) Lancet , vol.351 , pp. 131-133
    • Davies, S.W.1    Beardsall, K.2    Turmaine, M.3    DiFiglia, M.4    Aronin, N.5    Bates, G.P.6
  • 16
    • 0030752709 scopus 로고    scopus 로고
    • Aggregation of huntingtin in neuronal intranuclear inclusions and dystrophic neurites in brain
    • DiFiglia M., Sapp E., Chase K.O., Davies S.W., Bates G.P., Vonsattel J.P., Aronin N. Aggregation of huntingtin in neuronal intranuclear inclusions and dystrophic neurites in brain. Science. 277:1997;1990-1993.
    • (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
  • 17
    • 0033679283 scopus 로고    scopus 로고
    • Polyglutamine expansions: Proteolysis, chaperones, and the dangers of promiscuity
    • Ferrigno P., Silver P.A. Polyglutamine expansions: proteolysis, chaperones, and the dangers of promiscuity. Neuron. 26:2000;9-12.
    • (2000) Neuron , vol.26 , pp. 9-12
    • Ferrigno, P.1    Silver, P.A.2
  • 18
    • 0022423216 scopus 로고
    • Various rat adult tissues express only one major mRNA species from the glyceraldehyde-3-phosphate-dehydrogenase multigenic family
    • Fort Ph., Marty L., Piechaczyk M., El Sabrouty S., Dani Ch. , Jeanteur Ph. , Blanchard J.M. Various rat adult tissues express only one major mRNA species from the glyceraldehyde-3-phosphate-dehydrogenase multigenic family. Nucleic Acids Res. 13:1985;1431-1442.
    • (1985) Nucleic Acids Res. , vol.13 , pp. 1431-1442
    • Fort, Ph.1    Marty, L.2    Piechaczyk, M.3    El Sabrouty, S.4    Dani, Ch.5    Jeanteur, Ph.6    Blanchard, J.M.7
  • 19
    • 0025907011 scopus 로고
    • Tacrine: A pharmacological review
    • Freeman S.E., Dawson R.M. Tacrine: a pharmacological review. Prog. Neurobiol. 36:1991;257-277.
    • (1991) Prog. Neurobiol. , vol.36 , pp. 257-277
    • Freeman, S.E.1    Dawson, R.M.2
  • 21
    • 0344951409 scopus 로고    scopus 로고
    • GAPDH antisense oligonucleotide protects dopaminergic neuronal death occurring with exposure of the cerebrospinal fluid from PD patients
    • Fukuhara Y., Takeshima T., Kashiwaya Y., Mishima K., Ishitani R., Nakashima K. GAPDH antisense oligonucleotide protects dopaminergic neuronal death occurring with exposure of the cerebrospinal fluid from PD patients. Soc. Neurosci. Abstr. 27:2001;198.17.
    • (2001) Soc. Neurosci. Abstr. , vol.27 , pp. 19817
    • Fukuhara, Y.1    Takeshima, T.2    Kashiwaya, Y.3    Mishima, K.4    Ishitani, R.5    Nakashima, K.6
  • 22
    • 0029972551 scopus 로고    scopus 로고
    • Contacts in context: Promoter specificity and macromolecular interactions in transcription
    • Goodrich J.A., Cutler G., Tjian R. Contacts in context: promoter specificity and macromolecular interactions in transcription. Cell. 84:1996;825-830.
    • (1996) Cell , vol.84 , pp. 825-830
    • Goodrich, J.A.1    Cutler, G.2    Tjian, R.3
  • 23
    • 0035829720 scopus 로고    scopus 로고
    • Disruption of axonal transport and neuronal viability by amyloid precursor protein mutations in Drosophila
    • Gunawardena S., Goldstein L.S.B. Disruption of axonal transport and neuronal viability by amyloid precursor protein mutations in Drosophila. Neuron. 32:2001;389-401.
    • (2001) Neuron , vol.32 , pp. 389-401
    • Gunawardena, S.1    Goldstein, L.S.B.2
  • 24
    • 0031052381 scopus 로고    scopus 로고
    • Amyloid, the presenilins and Alzheimer's disease
    • Hardy J. Amyloid, the presenilins and Alzheimer's disease. Trends Neurosci. 20:1997;154-159.
    • (1997) Trends Neurosci. , vol.20 , pp. 154-159
    • Hardy, J.1
  • 25
    • 0032491408 scopus 로고    scopus 로고
    • Genetic classification of primary neurodegenerative disease
    • Hardy J., Gwinn-Hardy K. Genetic classification of primary neurodegenerative disease. Science. 282:1998;1075-1079.
    • (1998) Science , vol.282 , pp. 1075-1079
    • Hardy, J.1    Gwinn-Hardy, K.2
  • 26
    • 0032888789 scopus 로고    scopus 로고
    • Alpha-synuclein in Lewy body disease and Alzheimer's disease
    • Hashimoto M., Masliah E. Alpha-synuclein in Lewy body disease and Alzheimer's disease. Brain Pathol. 9:1999;707-720.
    • (1999) Brain Pathol. , vol.9 , pp. 707-720
    • Hashimoto, M.1    Masliah, E.2
  • 28
    • 0029838525 scopus 로고    scopus 로고
    • Glyceraldehyde-3-phosphate dehydrogenase antisense oligodeoxynucleotides protect against cytosine arabinonucleoside-induced apoptosis in cultured cerebellar neurons
    • Ishitani R., Chuang D.-M. Glyceraldehyde-3-phosphate dehydrogenase antisense oligodeoxynucleotides protect against cytosine arabinonucleoside-induced apoptosis in cultured cerebellar neurons. Proc. Natl. Acad. Sci. U.S.A. 93:1996;9937-9941.
    • (1996) Proc. Natl. Acad. Sci. U.S.A. , vol.93 , pp. 9937-9941
    • Ishitani, R.1    Chuang, D.-M.2
  • 29
    • 0030045251 scopus 로고    scopus 로고
    • Evidence that glyceraldehyde-3-phosphate dehydrogenase is involved in age-induced apoptosis in mature cerebellar neurons in culture
    • Ishitani R., Sunaga K., Hirano A., Saunders P., Katsube N., Chuang D.-M. Evidence that glyceraldehyde-3-phosphate dehydrogenase is involved in age-induced apoptosis in mature cerebellar neurons in culture. J. Neurochem. 66:1996;928-935.
    • (1996) J. Neurochem. , vol.66 , pp. 928-935
    • Ishitani, R.1    Sunaga, K.2    Hirano, A.3    Saunders, P.4    Katsube, N.5    Chuang, D.-M.6
  • 30
    • 0030426279 scopus 로고    scopus 로고
    • An antisense oligodeoxynucleotide to glyceraldehyde-3-phosphate dehydrogenase blocks age-induced apoptosis of mature cerebrocortical neurons in culture
    • Ishitani R., Kimura M., Sunaga K., Katsube N., Tanaka M., Chuang D.-M. An antisense oligodeoxynucleotide to glyceraldehyde-3-phosphate dehydrogenase blocks age-induced apoptosis of mature cerebrocortical neurons in culture. J. Pharmacol. Exp. Ther. 278:1996;447-454.
    • (1996) J. Pharmacol. Exp. Ther. , vol.278 , pp. 447-454
    • Ishitani, R.1    Kimura, M.2    Sunaga, K.3    Katsube, N.4    Tanaka, M.5    Chuang, D.-M.6
  • 32
    • 0031968628 scopus 로고    scopus 로고
    • Nuclear localization of overexpressed glyceraldehyde-3-phosphate dehydrogenase in cultured cerebellar neurons undergoing apoptosis
    • Ishitani R., Tanaka M., Sunaga K., Katsube N., Chuang D.-M. Nuclear localization of overexpressed glyceraldehyde-3-phosphate dehydrogenase in cultured cerebellar neurons undergoing apoptosis. Mol. Pharmacol. 53:1998;701-707.
    • (1998) Mol. Pharmacol. , vol.53 , pp. 701-707
    • Ishitani, R.1    Tanaka, M.2    Sunaga, K.3    Katsube, N.4    Chuang, D.-M.5
  • 34
    • 0028071526 scopus 로고
    • Nuclear signaling pathways for polypeptide ligands and their membrane receptors?
    • Jans D.A. Nuclear signaling pathways for polypeptide ligands and their membrane receptors? FASEB J. 8:1994;841-847.
    • (1994) FASEB J. , vol.8 , pp. 841-847
    • Jans, D.A.1
  • 35
    • 0034073298 scopus 로고    scopus 로고
    • A review of the neurotrophic and neuroprotective properties of ONO-1603: Comparison with those of tetrahydroaminoacridine, an antidementia drug
    • Katsube N., Ishitani R. A review of the neurotrophic and neuroprotective properties of ONO-1603: comparison with those of tetrahydroaminoacridine, an antidementia drug. CNS Drug Rev. 6:2000;21-34.
    • (2000) CNS Drug Rev. , vol.6 , pp. 21-34
    • Katsube, N.1    Ishitani, R.2
  • 37
    • 0032935542 scopus 로고    scopus 로고
    • ONO-1603, a potential antidementia drug, delays age-induced apoptosis and suppresses overexpression of glyceraldehyde-3-phosphate dehydrogenase in cultured central nervous system neurons
    • Katsube N., Sunaga K., Aishita H., Chuang D.-M., Ishitani R. ONO-1603, a potential antidementia drug, delays age-induced apoptosis and suppresses overexpression of glyceraldehyde-3-phosphate dehydrogenase in cultured central nervous system neurons. J. Pharmacol. Exp. Ther. 288:1999;6-13.
    • (1999) J. Pharmacol. Exp. Ther. , vol.288 , pp. 6-13
    • Katsube, N.1    Sunaga, K.2    Aishita, H.3    Chuang, D.-M.4    Ishitani, R.5
  • 38
    • 0032191848 scopus 로고    scopus 로고
    • Neuronal intranuclear inclusions in polyglutamine diseases: Nuclear weapons or nuclear fallout?
    • Kim T.-W., Tanzi R.E. Neuronal intranuclear inclusions in polyglutamine diseases: nuclear weapons or nuclear fallout? Neuron. 21:1998;657-659.
    • (1998) Neuron , vol.21 , pp. 657-659
    • Kim, T.-W.1    Tanzi, R.E.2
  • 40
    • 0032475941 scopus 로고    scopus 로고
    • Ataxin-1 nuclear localization and aggregation: Role in polyglutamine-induced disease in SCA1 transgenic mice
    • Klement I.A., Skinner P.J., Kaytor M.D., Yi H., Hersch S.M., Clark H.B., Zoghbi H.Y., Orr H.T. Ataxin-1 nuclear localization and aggregation: role in polyglutamine-induced disease in SCA1 transgenic mice. Cell. 95:1998;41-53.
    • (1998) Cell , vol.95 , pp. 41-53
    • Klement, I.A.1    Skinner, P.J.2    Kaytor, M.D.3    Yi, H.4    Hersch, S.M.5    Clark, H.B.6    Zoghbi, H.Y.7    Orr, H.T.8
  • 41
    • 0032885515 scopus 로고    scopus 로고
    • A neurological disease caused by an expanded CAG trinucleotide repeat in the TATA-binding protein gene: A new polyglutamine disease?
    • Koide R., Kobayashi S., Shimohata T., Ikeuchi T., Maruyama M., Saito M., Yamada M., Takahashi H., Tsuji S. A neurological disease caused by an expanded CAG trinucleotide repeat in the TATA-binding protein gene: a new polyglutamine disease? Hum. Mol. Genet. 8:1999;2047-2053.
    • (1999) Hum. Mol. Genet. , vol.8 , pp. 2047-2053
    • Koide, R.1    Kobayashi, S.2    Shimohata, T.3    Ikeuchi, T.4    Maruyama, M.5    Saito, M.6    Yamada, M.7    Takahashi, H.8    Tsuji, S.9
  • 42
    • 0029833062 scopus 로고    scopus 로고
    • Spinocerebellar ataxia type-1 and spinobulbar muscular atrophy gene products interact with glyceraldehyde-3-phosphate dehydrogenase
    • Koshy B., Matilla T., Burright E.N., Merry D.E., Fischbeck K.H., Orr H.T., Zoghbi H.Y. Spinocerebellar ataxia type-1 and spinobulbar muscular atrophy gene products interact with glyceraldehyde-3-phosphate dehydrogenase. Hum. Mol. Genet. 5:1996;1311-1318.
    • (1996) Hum. Mol. Genet. , vol.5 , pp. 1311-1318
    • Koshy, B.1    Matilla, T.2    Burright, E.N.3    Merry, D.E.4    Fischbeck, K.H.5    Orr, H.T.6    Zoghbi, H.Y.7
  • 45
    • 0034884148 scopus 로고    scopus 로고
    • Transfection-enforced Bcl-2 overexpression and an anti-Parkinson drug, rasagiline, prevent nuclear accumulation of glyceraldehyde-3-phosphate dehydrogenase induced by an endogenous dopaminergic neurotoxin, N-methyl(R)salsolinol
    • Maruyama W., Akao Y., Youdim M.B.H., Davis B.A., Naoi M. Transfection-enforced Bcl-2 overexpression and an anti-Parkinson drug, rasagiline, prevent nuclear accumulation of glyceraldehyde-3-phosphate dehydrogenase induced by an endogenous dopaminergic neurotoxin, N-methyl(R)salsolinol. J. Neurochem. 78:2001;727-735.
    • (2001) J. Neurochem. , vol.78 , pp. 727-735
    • Maruyama, W.1    Akao, Y.2    Youdim, M.B.H.3    Davis, B.A.4    Naoi, M.5
  • 46
    • 0034329742 scopus 로고    scopus 로고
    • Apoptosis in neurodegenerative disorders
    • Mattson M.P. Apoptosis in neurodegenerative disorders. Nature Rev., Mol. Cell Biol. 1:2000;120-129.
    • (2000) Nature Rev., Mol. Cell Biol. , vol.1 , pp. 120-129
    • Mattson, M.P.1
  • 49
    • 0022535636 scopus 로고
    • Glyceraldehyde-3-phosphate dehydrogenase is a nonhistone protein and a possible activator of transcription in neurons
    • Morgenegg G., Winkler G.C., Hübscher U., Heizmann C.W., Mous J., Kuenzle C.C. Glyceraldehyde-3-phosphate dehydrogenase is a nonhistone protein and a possible activator of transcription in neurons. J. Neurochem. 47:1986;54-62.
    • (1986) J. Neurochem. , vol.47 , pp. 54-62
    • Morgenegg, G.1    Winkler, G.C.2    Hübscher, U.3    Heizmann, C.W.4    Mous, J.5    Kuenzle, C.C.6
  • 50
    • 0033556160 scopus 로고    scopus 로고
    • Generation of neuronal intranuclear inclusions by polyglutamine-GFP: Analysis of inclusion clearance and toxicity as a function of polyglutamine length
    • Moulder K.L., Onodera O., Burke J.R., Strittmatter W.J., Johnson E.M. Jr. Generation of neuronal intranuclear inclusions by polyglutamine-GFP: analysis of inclusion clearance and toxicity as a function of polyglutamine length. J. Neurosci. 19:1999;705-715.
    • (1999) J. Neurosci. , vol.19 , pp. 705-715
    • Moulder, K.L.1    Onodera, O.2    Burke, J.R.3    Strittmatter, W.J.4    Johnson E.M., Jr.5
  • 53
    • 0032936755 scopus 로고    scopus 로고
    • Etiology and pathogenesis of Parkinson's disease
    • Olanow C.W., Tatton W.G. Etiology and pathogenesis of Parkinson's disease. Annu. Rev. Neurosci. 22:1999;123-144.
    • (1999) Annu. Rev. Neurosci. , vol.22 , pp. 123-144
    • Olanow, C.W.1    Tatton, W.G.2
  • 54
    • 0026058318 scopus 로고
    • Cell death during development of the nervous system
    • Oppenheim R.W. Cell death during development of the nervous system. Annu. Rev. Neurosci. 14:1991;453-501.
    • (1991) Annu. Rev. Neurosci. , vol.14 , pp. 453-501
    • Oppenheim, R.W.1
  • 55
    • 0031914155 scopus 로고    scopus 로고
    • R-deprenyl and R-2-heptyl-N-methylpropargylamine prevent apoptosis in cerebellar granule neurons induced by cytosine arabinoside but not low extracellular potassium
    • Paterson I.A., Zhang D., Warrington R.C., Boulton A.A. R-deprenyl and R-2-heptyl-N-methylpropargylamine prevent apoptosis in cerebellar granule neurons induced by cytosine arabinoside but not low extracellular potassium. J. Neurochem. 70:1998;515-523.
    • (1998) J. Neurochem. , vol.70 , pp. 515-523
    • Paterson, I.A.1    Zhang, D.2    Warrington, R.C.3    Boulton, A.A.4
  • 57
    • 0033080367 scopus 로고    scopus 로고
    • Glutamine repeats and neurodegenerative diseases: Molecular aspects
    • Perutz M.F. Glutamine repeats and neurodegenerative diseases: molecular aspects. Trends Biochem. Sci. 24:1999;58-63.
    • (1999) Trends Biochem. Sci. , vol.24 , pp. 58-63
    • Perutz, M.F.1
  • 59
    • 0029072690 scopus 로고
    • Evidence for apoptotic cell death in Huntington disease and excitotoxic animal models
    • Portera-Cailliau C., Hedreen J.C., Price D.L., Koliatsos V.E. Evidence for apoptotic cell death in Huntington disease and excitotoxic animal models. J. Neurosci. 15:1995;3775-3787.
    • (1995) J. Neurosci. , vol.15 , pp. 3775-3787
    • Portera-Cailliau, C.1    Hedreen, J.C.2    Price, D.L.3    Koliatsos, V.E.4
  • 61
    • 0033009890 scopus 로고    scopus 로고
    • The central effectors of cell death in the immune system
    • Rathmell J.C., Thompson C.B. The central effectors of cell death in the immune system. Annu. Rev. Immunol. 17:1999;781-828.
    • (1999) Annu. Rev. Immunol. , vol.17 , pp. 781-828
    • Rathmell, J.C.1    Thompson, C.B.2
  • 62
    • 0029095105 scopus 로고
    • A mutation in glyceraldehyde-3-phosphate dehydrogenase alters endocytosis in CHO cells
    • Robbins A.R., Ward R.D., Oliver C. A mutation in glyceraldehyde-3-phosphate dehydrogenase alters endocytosis in CHO cells. J. Cell Biol. 130:1995;1093-1104.
    • (1995) J. Cell Biol. , vol.130 , pp. 1093-1104
    • Robbins, A.R.1    Ward, R.D.2    Oliver, C.3
  • 63
    • 10244259208 scopus 로고    scopus 로고
    • The efficacy and safety of donepezil in patients with Alzheimer's disease: Results of a US multicentre, randomized, double-blind, placebo-controlled trial
    • Rogers S.L., Friedhoff L.T. The efficacy and safety of donepezil in patients with Alzheimer's disease: results of a US multicentre, randomized, double-blind, placebo-controlled trial. Dementia. 7:1996;293-303.
    • (1996) Dementia , vol.7 , pp. 293-303
    • Rogers, S.L.1    Friedhoff, L.T.2
  • 64
    • 0032475931 scopus 로고    scopus 로고
    • Huntingtin acts in the nucleus to induce apoptosis but death does not correlate with the formation of intranuclear inclusions
    • Saudou F., Finkbeiner S., Devys D., Greenberg M.E. Huntingtin acts in the nucleus to induce apoptosis but death does not correlate with the formation of intranuclear inclusions. Cell. 95:1998;55-66.
    • (1998) Cell , vol.95 , pp. 55-66
    • Saudou, F.1    Finkbeiner, S.2    Devys, D.3    Greenberg, M.E.4
  • 65
    • 0030809974 scopus 로고    scopus 로고
    • Subcellular distribution of glyceraldehyde-3-phosphate dehydrogenase in cerebellar granule cells undergoing cytosine arabinoside-induced apoptosis
    • Saunders P.A., Chalecka-Franaszek E., Chuang D.-M. Subcellular distribution of glyceraldehyde-3-phosphate dehydrogenase in cerebellar granule cells undergoing cytosine arabinoside-induced apoptosis. J. Neurochem. 69:1997;1820-1828.
    • (1997) J. Neurochem. , vol.69 , pp. 1820-1828
    • Saunders, P.A.1    Chalecka-Franaszek, E.2    Chuang, D.-M.3
  • 66
    • 0032972037 scopus 로고    scopus 로고
    • Nuclear translocation of glyceraldehyde-3-phosphate dehydrogenase isoforms during neuronal apoptosis
    • Saunders P.A., Chen R.-W., Chuang D.-M. Nuclear translocation of glyceraldehyde-3-phosphate dehydrogenase isoforms during neuronal apoptosis. J. Neurochem. 72:1999;925-932.
    • (1999) J. Neurochem. , vol.72 , pp. 925-932
    • Saunders, P.A.1    Chen, R.-W.2    Chuang, D.-M.3
  • 67
    • 0030868934 scopus 로고    scopus 로고
    • Glyceraldehyde-3-phosphate dehydrogenase: Nuclear translocation participates in neuronal and nonneuronal cell death
    • Sawa A., Khan A.A., Hester L.D., Snyder S.H. Glyceraldehyde-3-phosphate dehydrogenase: nuclear translocation participates in neuronal and nonneuronal cell death. Proc. Natl. Acad. Sci. U.S.A. 94:1997;11669-11674.
    • (1997) Proc. Natl. Acad. Sci. U.S.A. , vol.94 , pp. 11669-11674
    • Sawa, A.1    Khan, A.A.2    Hester, L.D.3    Snyder, S.H.4
  • 68
    • 0027314334 scopus 로고
    • Rat brain glyceraldehyde-3-phosphate dehydrogenase interacts with the recombinant cytoplasmic domain of Alzheimer's β-amyloid precursor protein
    • Schulze H., Schuler A., Stüber D., Döbeli H., Langen H., Huber G. Rat brain glyceraldehyde-3-phosphate dehydrogenase interacts with the recombinant cytoplasmic domain of Alzheimer's β-amyloid precursor protein. J. Neurochem. 60:1993;1915-1922.
    • (1993) J. Neurochem. , vol.60 , pp. 1915-1922
    • Schulze, H.1    Schuler, A.2    Stüber, D.3    Döbeli, H.4    Langen, H.5    Huber, G.6
  • 69
    • 0035066332 scopus 로고    scopus 로고
    • Alzheimer's disease: Genes, proteins, and therapy
    • Selkoe D.J. Alzheimer's disease: genes, proteins, and therapy. Physiol. Rev. 81:2001;741-766.
    • (2001) Physiol. Rev. , vol.81 , pp. 741-766
    • Selkoe, D.J.1
  • 71
    • 0035139109 scopus 로고    scopus 로고
    • Cellular defenses against unfolded proteins: A cell biologist thinks about neurodegenerative diseases
    • Sherman M.Y., Goldberg A.L. Cellular defenses against unfolded proteins: a cell biologist thinks about neurodegenerative diseases. Neuron. 29:2001;15-32.
    • (2001) Neuron , vol.29 , pp. 15-32
    • Sherman, M.Y.1    Goldberg, A.L.2
  • 72
    • 0027518424 scopus 로고
    • Sequence-specific binding of transfer RNA by glyceraldehyde-3-phosphate dehydrogenase
    • Singh R., Green M.R. Sequence-specific binding of transfer RNA by glyceraldehyde-3-phosphate dehydrogenase. Science. 259:1993;365-368.
    • (1993) Science , vol.259 , pp. 365-368
    • Singh, R.1    Green, M.R.2
  • 73
    • 0032973950 scopus 로고    scopus 로고
    • New insights into an old protein: The functional diversity of mammalian glyceraldehyde-3-phosphate dehydrogenase
    • Sirover M.A. New insights into an old protein: the functional diversity of mammalian glyceraldehyde-3-phosphate dehydrogenase. Biochim. Biophys. Acta. 1432:1999;159-184.
    • (1999) Biochim. Biophys. Acta , vol.1432 , pp. 159-184
    • Sirover, M.A.1
  • 74
    • 0032475877 scopus 로고    scopus 로고
    • Nuclear inclusions in glutamine repeat disorders: Are they pernicious, coincidental, or beneficial?
    • Sisodia S.S. Nuclear inclusions in glutamine repeat disorders: are they pernicious, coincidental, or beneficial? Cell. 95:1998;1-4.
    • (1998) Cell , vol.95 , pp. 1-4
    • Sisodia, S.S.1
  • 75
    • 0030946552 scopus 로고    scopus 로고
    • An etiological role of amyloidogenic carboxyl-terminal fragments of the β-amyloid precursor protein in Alzheimer's disease
    • Suh Y.-H. An etiological role of amyloidogenic carboxyl-terminal fragments of the β-amyloid precursor protein in Alzheimer's disease. J. Neurochem. 68:1997;1781-1791.
    • (1997) J. Neurochem. , vol.68 , pp. 1781-1791
    • Suh, Y.-H.1
  • 76
    • 0022899577 scopus 로고
    • Oral tetrahydroaminoacridine in long-term treatment of senile dementia, Alzheimer type
    • Summers W.K., Majovski L.V., Marsch G.M., Tachiki K., Kling A. Oral tetrahydroaminoacridine in long-term treatment of senile dementia, Alzheimer type. N. Engl. J. Med. 315:1986;1241-1245.
    • (1986) N. Engl. J. Med. , vol.315 , pp. 1241-1245
    • Summers, W.K.1    Majovski, L.V.2    Marsch, G.M.3    Tachiki, K.4    Kling, A.5
  • 77
    • 0028865070 scopus 로고
    • Glyceraldehyde-3-phosphate dehydrogenase is over-expressed during apoptotic death of neuronal cultures and is recognized by a monoclonal antibody against amyloid plaques from Alzheimer's brain
    • Sunaga K., Takahashi H., Chuang D.-M., Ishitani R. Glyceraldehyde-3-phosphate dehydrogenase is over-expressed during apoptotic death of neuronal cultures and is recognized by a monoclonal antibody against amyloid plaques from Alzheimer's brain. Neurosci. Lett. 200:1995;133-136.
    • (1995) Neurosci. Lett. , vol.200 , pp. 133-136
    • Sunaga, K.1    Takahashi, H.2    Chuang, D.-M.3    Ishitani, R.4
  • 79
    • 0033551557 scopus 로고    scopus 로고
    • Over-expression of GAPDH induces apoptosis in COS-7 cells transfected with cloned GAPDH cDNAs
    • Tajima H., Tsuchiya K., Yamada M., Kondo K., Katsube N., Ishitani R. Over-expression of GAPDH induces apoptosis in COS-7 cells transfected with cloned GAPDH cDNAs. NeuroReport. 10:1999;2029-2033.
    • (1999) NeuroReport , vol.10 , pp. 2029-2033
    • Tajima, H.1    Tsuchiya, K.2    Yamada, M.3    Kondo, K.4    Katsube, N.5    Ishitani, R.6
  • 80
    • 0344520600 scopus 로고    scopus 로고
    • Overexpression of glyceraldehyde-3-phosphate dehydrogenase (GAPDH) induces apoptosis: Generation of inclusion bodies by GAPDH-GFP fusion protein
    • Tajima H., Tsuchiya K., Yamada M., Takata H., Katsube N., Ishitani R. Overexpression of glyceraldehyde-3-phosphate dehydrogenase (GAPDH) induces apoptosis: generation of inclusion bodies by GAPDH-GFP fusion protein. Soc. Neurosci. Abstr. 25:1999;906.11.
    • (1999) Soc. Neurosci. Abstr. , vol.25 , pp. 90611
    • Tajima, H.1    Tsuchiya, K.2    Yamada, M.3    Takata, H.4    Katsube, N.5    Ishitani, R.6
  • 81
    • 0036196375 scopus 로고    scopus 로고
    • Induction of glyceraldehyde-3-phosphate dehydrogenase (GAPDH) expression in rat brain after focal ischemia/reperfusion
    • Tanaka R., Mochizuki H., Suzuki A., Katsube N., Ishitani R., Mizuno Y., Urabe T. Induction of glyceraldehyde-3-phosphate dehydrogenase (GAPDH) expression in rat brain after focal ischemia/reperfusion. J. Cereb. Blood Flow Metab. 22:2002;280-288.
    • (2002) J. Cereb. Blood Flow Metab. , vol.22 , pp. 280-288
    • Tanaka, R.1    Mochizuki, H.2    Suzuki, A.3    Katsube, N.4    Ishitani, R.5    Mizuno, Y.6    Urabe, T.7
  • 82
    • 0033756901 scopus 로고    scopus 로고
    • Increased caspase 3 and Bax immunoreactivity accompany nuclear GAPDH translocation and neuronal apoptosis in Parkinson's disease
    • Tatton N.A. Increased caspase 3 and Bax immunoreactivity accompany nuclear GAPDH translocation and neuronal apoptosis in Parkinson's disease. Exp. Neurol. 166:2000;29-43.
    • (2000) Exp. Neurol. , vol.166 , pp. 29-43
    • Tatton, N.A.1
  • 83
    • 0028943734 scopus 로고
    • Apoptosis in the pathogenesis and treatment of disease
    • Thompson C.B. Apoptosis in the pathogenesis and treatment of disease. Science. 267:1995;1456-1462.
    • (1995) Science , vol.267 , pp. 1456-1462
    • Thompson, C.B.1
  • 84
    • 0022423245 scopus 로고
    • Isolation and characterization of rat and human glyceraldehyde-3-phosphate dehydrogenase cDNAs: Genomic complexity and molecular evolution of the gene
    • Tso J.Y., Sun X.-H., Kao T.-H., Reece K.S., Wu R. Isolation and characterization of rat and human glyceraldehyde-3-phosphate dehydrogenase cDNAs: genomic complexity and molecular evolution of the gene. Nucleic Acids Res. 13:1985;2485-2502.
    • (1985) Nucleic Acids Res. , vol.13 , pp. 2485-2502
    • Tso, J.Y.1    Sun, X.-H.2    Kao, T.-H.3    Reece, K.S.4    Wu, R.5
  • 85
    • 0345382956 scopus 로고    scopus 로고
    • Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) gene: Two upstream regions mediate its overexpression during cytosine arabinonucleoside-induced neuronal apoptosis
    • Tsuchiya K., Tajima H., Sunaga K., Katsube N., Ishitani R. Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) gene: two upstream regions mediate its overexpression during cytosine arabinonucleoside-induced neuronal apoptosis. Soc. Neurosci. Abstr. 26:2000;225.12.
    • (2000) Soc. Neurosci. Abstr. , vol.26 , pp. 22512
    • Tsuchiya, K.1    Tajima, H.2    Sunaga, K.3    Katsube, N.4    Ishitani, R.5
  • 87
    • 0021084784 scopus 로고
    • Prolyl endopeptidase
    • Wilk S. Prolyl endopeptidase. Life Sci. 33:1983;2149-2157.
    • (1983) Life Sci. , vol.33 , pp. 2149-2157
    • Wilk, S.1
  • 88
    • 0027996828 scopus 로고
    • Dynamic mutations hit double figures
    • Willems P.J. Dynamic mutations hit double figures. Nat. Genet. News Views. 8:1994;213-215.
    • (1994) Nat. Genet. News Views , vol.8 , pp. 213-215
    • Willems, P.J.1
  • 89
    • 0022261811 scopus 로고
    • Neuropeptides in human memory and learning processes
    • Zager E.L., Black P.M. Neuropeptides in human memory and learning processes. Neurosurgery. 17:1985;355-369.
    • (1985) Neurosurgery , vol.17 , pp. 355-369
    • Zager, E.L.1    Black, P.M.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.