메뉴 건너뛰기




Volumn 8, Issue 1, 2013, Pages

Mutation in E1, the Ubiquitin Activating Enzyme, Reduces Drosophila Lifespan and Results in Motor Impairment

Author keywords

[No Author keywords available]

Indexed keywords

GLYCOPROTEIN E1; RAS PROTEIN; UBIQUITIN PROTEIN LIGASE;

EID: 84873865668     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0032835     Document Type: Article
Times cited : (32)

References (78)
  • 1
    • 0141987860 scopus 로고    scopus 로고
    • The ubiquitin proteasome system in neurodegenerative diseases. Sometimes the chicken, sometimes the egg
    • Ciechanover A, Brundin P, (2003) The ubiquitin proteasome system in neurodegenerative diseases. Sometimes the chicken, sometimes the egg. Neuron 40: 427-446.
    • (2003) Neuron , vol.40 , pp. 427-446
    • Ciechanover, A.1    Brundin, P.2
  • 2
    • 3442900482 scopus 로고    scopus 로고
    • Human disorders of ubiquitination and proteasomal degradation
    • Jiang YH, Beaudet AL, (2004) Human disorders of ubiquitination and proteasomal degradation. Curr Opin Pediatr 16: 419-426.
    • (2004) Curr Opin Pediatr , vol.16 , pp. 419-426
    • Jiang, Y.H.1    Beaudet, A.L.2
  • 3
    • 0034829801 scopus 로고    scopus 로고
    • The molecular bases of Alzheimer's disease and other neurodegenerative disorders
    • Maccioni RB, Muñoz JP, Barbeito L, (2001) The molecular bases of Alzheimer's disease and other neurodegenerative disorders. Arch Med Res 32: 367-381.
    • (2001) Arch Med Res , vol.32 , pp. 367-381
    • Maccioni, R.B.1    Muñoz, J.P.2    Barbeito, L.3
  • 4
    • 67749133983 scopus 로고    scopus 로고
    • Cytoskeletal pathologies of Alzheimer disease
    • Bamburg JR, Bloom GS, (2009) Cytoskeletal pathologies of Alzheimer disease. Cell Motil Cytoskeleton 66: 635-649.
    • (2009) Cell Motil Cytoskeleton , vol.66 , pp. 635-649
    • Bamburg, J.R.1    Bloom, G.S.2
  • 6
    • 18244365872 scopus 로고    scopus 로고
    • Amyloid-beta, tau alterations and mitochondrial dysfunction in Alzheimer disease: the chickens or the eggs?
    • Smith MA, Drew KL, Nunomura A, Takeda A, Hirai K, et al. (2002) Amyloid-beta, tau alterations and mitochondrial dysfunction in Alzheimer disease: the chickens or the eggs? Neurochem Int 40: 527-531.
    • (2002) Neurochem Int , vol.40 , pp. 527-531
    • Smith, M.A.1    Drew, K.L.2    Nunomura, A.3    Takeda, A.4    Hirai, K.5
  • 8
    • 63849213978 scopus 로고    scopus 로고
    • Amyloid beta-peptide aggregation. What does it result in and how can it be prevented?
    • Nerelius C, Johansson J, Sandegren A, (2009) Amyloid beta-peptide aggregation. What does it result in and how can it be prevented? Front Biosci 14: 1716-1729.
    • (2009) Front Biosci , vol.14 , pp. 1716-1729
    • Nerelius, C.1    Johansson, J.2    Sandegren, A.3
  • 9
    • 66949152096 scopus 로고    scopus 로고
    • Parkinson's disease
    • Lees AJ, Hardy J, Revesz T, (2009) Parkinson's disease. Lancet 373: 2055-2066.
    • (2009) Lancet , vol.373 , pp. 2055-2066
    • Lees, A.J.1    Hardy, J.2    Revesz, T.3
  • 10
    • 34250641949 scopus 로고    scopus 로고
    • Introduction to Parkinson's disease
    • Pallone JA, (2007) Introduction to Parkinson's disease. Dis Mon 53: 195-199.
    • (2007) Dis Mon , vol.53 , pp. 195-199
    • Pallone, J.A.1
  • 11
    • 0027480960 scopus 로고
    • A novel gene containing a trinucleotide repeat that is expanded and unstable on Huntington's disease chromosomes
    • Huntington's Disease Collaborative Research Group
    • Huntington's Disease Collaborative Research Group (1993) A novel gene containing a trinucleotide repeat that is expanded and unstable on Huntington's disease chromosomes. Cell 72: 971-983.
    • (1993) Cell , vol.72 , pp. 971-983
  • 12
    • 68349108020 scopus 로고    scopus 로고
    • The ubiquitin proteasome system in neuropathology
    • Lehman NL, (2009) The ubiquitin proteasome system in neuropathology. Acta Neuropathol 118: 329-347.
    • (2009) Acta Neuropathol , vol.118 , pp. 329-347
    • Lehman, N.L.1
  • 13
    • 0037381710 scopus 로고    scopus 로고
    • Proteasome inhibition by paired helical filament-tau in brains of patients with Alzheimer's disease
    • Keck S, Nitsch R, Grune T, Ullrich O, (2003) Proteasome inhibition by paired helical filament-tau in brains of patients with Alzheimer's disease. J Neurochem 85: 115-122.
    • (2003) J Neurochem , vol.85 , pp. 115-122
    • Keck, S.1    Nitsch, R.2    Grune, T.3    Ullrich, O.4
  • 14
    • 50649112184 scopus 로고    scopus 로고
    • alpha-Synuclein protofibrils inhibit 26 S proteasome-mediated protein degradation: understanding the cytotoxicity of protein protofibrils in neurodegenerative disease pathogenesis
    • Zhang NY, Tang Z, Liu CW, (2008) alpha-Synuclein protofibrils inhibit 26 S proteasome-mediated protein degradation: understanding the cytotoxicity of protein protofibrils in neurodegenerative disease pathogenesis. J Biol Chem 283: 20288-20298.
    • (2008) J Biol Chem , vol.283 , pp. 20288-20298
    • Zhang, N.Y.1    Tang, Z.2    Liu, C.W.3
  • 15
    • 49849088116 scopus 로고    scopus 로고
    • Aggregopathy in neurodegenerative diseases: mechanisms and therapeutic implication
    • Dohm CP, Kermer P, Bähr M, (2008) Aggregopathy in neurodegenerative diseases: mechanisms and therapeutic implication. Neurodegener Dis 5: 321-338.
    • (2008) Neurodegener Dis , vol.5 , pp. 321-338
    • Dohm, C.P.1    Kermer, P.2    Bähr, M.3
  • 16
    • 24144489814 scopus 로고    scopus 로고
    • Proteasome inhibition and aggresome formation in sporadic inclusion-body myositis and in amyloid-beta precursor protein-overexpressing cultured human muscle fibers
    • Fratta P, Engel WK, McFerrin J, Davies KJ, Lin SW, Askanas V, (2005) Proteasome inhibition and aggresome formation in sporadic inclusion-body myositis and in amyloid-beta precursor protein-overexpressing cultured human muscle fibers. Am J Pathol 167: 517-526.
    • (2005) Am J Pathol , vol.167 , pp. 517-526
    • Fratta, P.1    Engel, W.K.2    McFerrin, J.3    Davies, K.J.4    Lin, S.W.5    Askanas, V.6
  • 17
    • 24044516868 scopus 로고    scopus 로고
    • Alpha-synuclein alters proteasome function, protein synthesis, and stationary phase viability
    • Chen Q, Thorpe J, Keller JN, (2005) Alpha-synuclein alters proteasome function, protein synthesis, and stationary phase viability. J Biol Chem 280: 30009-30017.
    • (2005) J Biol Chem , vol.280 , pp. 30009-30017
    • Chen, Q.1    Thorpe, J.2    Keller, J.N.3
  • 18
    • 7244260495 scopus 로고    scopus 로고
    • Alzheimer's disease meets the ubiquitin-proteasome system
    • Song S, Jung YK, (2004) Alzheimer's disease meets the ubiquitin-proteasome system. Trends Mol Med 10: 565-570.
    • (2004) Trends Mol Med , vol.10 , pp. 565-570
    • Song, S.1    Jung, Y.K.2
  • 19
    • 0035947372 scopus 로고    scopus 로고
    • Impairment of the ubiquitin-proteasome system by protein aggregation
    • Bence NF, Sampat RM, Kopito RR, (2001) Impairment of the ubiquitin-proteasome system by protein aggregation. Science 292: 1552-1555.
    • (2001) Science , vol.292 , pp. 1552-1555
    • Bence, N.F.1    Sampat, R.M.2    Kopito, R.R.3
  • 20
    • 69949170793 scopus 로고    scopus 로고
    • The pathogenic mechanisms of polyglutamine diseases and current therapeutic strategies
    • Bauer PO, Nukina N, (2009) The pathogenic mechanisms of polyglutamine diseases and current therapeutic strategies. Bauer PO, Nukina N. J Neurochem 110: 1737-1765.
    • (2009) Bauer PO, Nukina N. J Neurochem , vol.110 , pp. 1737-1765
    • Bauer, P.O.1    Nukina, N.2
  • 21
    • 52049093169 scopus 로고    scopus 로고
    • Polyglutamine neurodegeneration: protein misfolding revisited
    • Williams AJ, Paulson HL, (2008) Polyglutamine neurodegeneration: protein misfolding revisited. Trends Neurosci 31: 521-528.
    • (2008) Trends Neurosci , vol.31 , pp. 521-528
    • Williams, A.J.1    Paulson, H.L.2
  • 24
    • 33845531563 scopus 로고    scopus 로고
    • Parkinson's disease: diagnosis and treatment
    • Rao SS, Hofmann LA, Shakil A, (2006) Parkinson's disease: diagnosis and treatment. Am Fam Physician 74: 2046-2054.
    • (2006) Am Fam Physician , vol.74 , pp. 2046-2054
    • Rao, S.S.1    Hofmann, L.A.2    Shakil, A.3
  • 25
  • 26
    • 0031013848 scopus 로고    scopus 로고
    • Prevalence of parkinsonism and Parkinson's disease in Europe: the EUROPARKINSON Collaborative Study. European Community Concerted Action on the Epidemiology of Parkinson's disease
    • de Rijk MC, Tzourio C, Breteler MM, Dartigues JF, Amaducci L, et al. (1997) Prevalence of parkinsonism and Parkinson's disease in Europe: the EUROPARKINSON Collaborative Study. European Community Concerted Action on the Epidemiology of Parkinson's disease. J Neurol Neurosurg Psychiatry 62: 10-15.
    • (1997) J Neurol Neurosurg Psychiatry , vol.62 , pp. 10-15
    • de Rijk, M.C.1    Tzourio, C.2    Breteler, M.M.3    Dartigues, J.F.4    Amaducci, L.5
  • 27
    • 0035674445 scopus 로고    scopus 로고
    • Huntington's disease: a review of the literature on prevalence and treatment of neuropsychiatric phenomena
    • Naarding P, Kremer HPH, Zitman FG, (2001) Huntington's disease: a review of the literature on prevalence and treatment of neuropsychiatric phenomena. European Psychiatry 16: 439-445.
    • (2001) European Psychiatry , vol.16 , pp. 439-445
    • Naarding, P.1    Kremer, H.P.H.2    Zitman, F.G.3
  • 29
    • 0028898424 scopus 로고
    • Protein ubiquitination involving an E1-E2-E3 enzyme ubiquitin thioester cascade
    • Scheffner M, Nuber U, Huibregtse JM, (1995) Protein ubiquitination involving an E1-E2-E3 enzyme ubiquitin thioester cascade. Nature 373: 81-83.
    • (1995) Nature , vol.373 , pp. 81-83
    • Scheffner, M.1    Nuber, U.2    Huibregtse, J.M.3
  • 30
    • 65649115267 scopus 로고    scopus 로고
    • Recognition and processing of ubiquitin-protein conjugates by the proteasome
    • Finley D, (2009) Recognition and processing of ubiquitin-protein conjugates by the proteasome. Annu Rev Biochem 78: 477-513.
    • (2009) Annu Rev Biochem , vol.78 , pp. 477-513
    • Finley, D.1
  • 33
    • 33750354046 scopus 로고    scopus 로고
    • Parkin and defective ubiquitination in Parkinson's disease
    • Dawson TM (2006) Parkin and defective ubiquitination in Parkinson's disease. J Neural Transm Suppl (70): 209-213.
    • (2006) J Neural Transm Suppl , Issue.70 , pp. 209-213
    • Dawson, T.M.1
  • 34
    • 0038624450 scopus 로고    scopus 로고
    • Parkin's substrates and the pathways leading to neuronal damage
    • Cookson MR, (2003) Parkin's substrates and the pathways leading to neuronal damage. Neuromolecular Med 3: 1-13.
    • (2003) Neuromolecular Med , vol.3 , pp. 1-13
    • Cookson, M.R.1
  • 35
    • 0032499264 scopus 로고    scopus 로고
    • Mutations in the parkin gene cause autosomal recessive juvenile parkinsonism
    • Kitada T, Asakawa S, Hattori N, Matsumine H, Yamamura Y, et al. (1998) Mutations in the parkin gene cause autosomal recessive juvenile parkinsonism. Nature 392: 605-608.
    • (1998) Nature , vol.392 , pp. 605-608
    • Kitada, T.1    Asakawa, S.2    Hattori, N.3    Matsumine, H.4    Yamamura, Y.5
  • 36
    • 84880188650 scopus 로고    scopus 로고
    • Frameshift proteins in Alzheimer's disease and in other conformational disorders: time for the ubiquitin-proteasome system
    • van Leeuwen FW, Hol EM, Fischer DF, (2006) Frameshift proteins in Alzheimer's disease and in other conformational disorders: time for the ubiquitin-proteasome system. J Alzheimers Dis 9: 319-325.
    • (2006) J Alzheimers Dis , vol.9 , pp. 319-325
    • van Leeuwen, F.W.1    Hol, E.M.2    Fischer, D.F.3
  • 37
    • 0035203294 scopus 로고    scopus 로고
    • Mutant ubiquitin expressed in Alzheimer's disease causes neuronal death
    • De Vrij FM, Sluijs JA, Gregori L, Fischer DF, Hermens WT, et al. (2001) Mutant ubiquitin expressed in Alzheimer's disease causes neuronal death. FASEB J 15: 2680-2688.
    • (2001) FASEB J , vol.15 , pp. 2680-2688
    • De Vrij, F.M.1    Sluijs, J.A.2    Gregori, L.3    Fischer, D.F.4    Hermens, W.T.5
  • 38
    • 61449117889 scopus 로고    scopus 로고
    • Disease-associated mutant ubiquitin causes proteasomal impairment and enhances the toxicity of protein aggregates
    • Tank EM, True HL, (2009) Disease-associated mutant ubiquitin causes proteasomal impairment and enhances the toxicity of protein aggregates. PLoS Genet 5: e1000382.
    • (2009) PLoS Genet , vol.5
    • Tank, E.M.1    True, H.L.2
  • 39
    • 4444274236 scopus 로고    scopus 로고
    • Accumulation of aberrant ubiquitin induces aggregate formation and cell death in polyglutamine diseases
    • de Pril R, Fischer DF, Maat-Schieman ML, Hobo B, de Vos RA, et al. (2004) Accumulation of aberrant ubiquitin induces aggregate formation and cell death in polyglutamine diseases. Hum Mol Genet 13: 1803-1813.
    • (2004) Hum Mol Genet , vol.13 , pp. 1803-1813
    • de Pril, R.1    Fischer, D.F.2    Maat-Schieman, M.L.3    Hobo, B.4    de Vos, R.A.5
  • 40
    • 34249713085 scopus 로고    scopus 로고
    • Dose-dependent inhibition of proteasome activity by a mutant ubiquitin associated with neurodegenerative disease
    • van Tijn P, de Vrij FM, Schuurman KG, Dantuma NP, Fischer DF, et al. (2007) Dose-dependent inhibition of proteasome activity by a mutant ubiquitin associated with neurodegenerative disease. J Cell Sci 120: 1615-1623.
    • (2007) J Cell Sci , vol.120 , pp. 1615-1623
    • van Tijn, P.1    de Vrij, F.M.2    Schuurman, K.G.3    Dantuma, N.P.4    Fischer, D.F.5
  • 41
    • 0038155122 scopus 로고    scopus 로고
    • Alzheimer's associated variant ubiquitin causes inhibition of the 26S proteasome and chaperone expression
    • Hope AD, de Silva R, Fischer DF, Hol EM, van Leeuwen FW, et al. (2003) Alzheimer's associated variant ubiquitin causes inhibition of the 26S proteasome and chaperone expression. J Neurochem 86: 394-404.
    • (2003) J Neurochem , vol.86 , pp. 394-404
    • Hope, A.D.1    de Silva, R.2    Fischer, D.F.3    Hol, E.M.4    van Leeuwen, F.W.5
  • 42
    • 6844258835 scopus 로고    scopus 로고
    • Frameshift mutants of beta amyloid precursor protein and ubiquitin-B in Alzheimer's and Down patients
    • van Leeuwen FW, de Kleijn DP, van den Hurk HH, Neubauer A, Sonnemans GJ, et al. (1998) Frameshift mutants of beta amyloid precursor protein and ubiquitin-B in Alzheimer's and Down patients. Science 279: 242-247.
    • (1998) Science , vol.279 , pp. 242-247
    • van Leeuwen, F.W.1    de Kleijn, D.P.2    van den Hurk, H.H.3    Neubauer, A.4    Sonnemans, G.J.5
  • 43
    • 0034710151 scopus 로고    scopus 로고
    • A survey of the human disease gene counterparts in the Drosophilia genome
    • Fortini ME, Skupski MP, Boguski MS, Hariharan IK, (2000) A survey of the human disease gene counterparts in the Drosophilia genome. J Cell Biol 150: F23-40.
    • (2000) J Cell Biol , vol.150
    • Fortini, M.E.1    Skupski, M.P.2    Boguski, M.S.3    Hariharan, I.K.4
  • 44
    • 52949084018 scopus 로고    scopus 로고
    • Mutation of the Gene Encoding the Ubiquitin Activating Enzyme Uba1 Causes Tissue Overgrowth in Drosophila
    • Pfleger CM, Harvey KF, Yan H, Hariharan IK, (2007) Mutation of the Gene Encoding the Ubiquitin Activating Enzyme Uba1 Causes Tissue Overgrowth in Drosophila. Fly 1: 95-105.
    • (2007) Fly , vol.1 , pp. 95-105
    • Pfleger, C.M.1    Harvey, K.F.2    Yan, H.3    Hariharan, I.K.4
  • 45
    • 67650519590 scopus 로고    scopus 로고
    • Impairment of ubiquitylation by mutation in Drosophila E1 promotes both cell-autonomous and non-cell-autonomous Ras-ERK activation in vivo
    • Yan H, Chin M-L, Horvath EA, Kane EA, Pfleger CM, (2009) Impairment of ubiquitylation by mutation in Drosophila E1 promotes both cell-autonomous and non-cell-autonomous Ras-ERK activation in vivo. J Cell Sci 122: 1461-1470.
    • (2009) J Cell Sci , vol.122 , pp. 1461-1470
    • Yan, H.1    Chin, M.-L.2    Horvath, E.A.3    Kane, E.A.4    Pfleger, C.M.5
  • 46
    • 38749120297 scopus 로고    scopus 로고
    • Rare missense and synonymous variants in UBE1 are associated with X-linked infantile spinal muscular atrophy
    • Ramser J, Ahearn ME, Lenski C, Yariz KO, Hellebrand H, et al. (2008) Rare missense and synonymous variants in UBE1 are associated with X-linked infantile spinal muscular atrophy. Am J Hum Genet 82: 188-193.
    • (2008) Am J Hum Genet , vol.82 , pp. 188-193
    • Ramser, J.1    Ahearn, M.E.2    Lenski, C.3    Yariz, K.O.4    Hellebrand, H.5
  • 47
    • 0024568234 scopus 로고
    • A cost of mating in female fruitflies
    • Fowler K, Partridge L, (1989) A cost of mating in female fruitflies. Nature 338: 760-761.
    • (1989) Nature , vol.338 , pp. 760-761
    • Fowler, K.1    Partridge, L.2
  • 48
    • 13944262511 scopus 로고    scopus 로고
    • Sex peptide causes mating costs in female Drosophila melanogaster
    • Wigby S, Chapman T, (2005) Sex peptide causes mating costs in female Drosophila melanogaster. Current Biology 15: 316-321.
    • (2005) Current Biology , vol.15 , pp. 316-321
    • Wigby, S.1    Chapman, T.2
  • 49
    • 0034704752 scopus 로고    scopus 로고
    • A Drosophila model of Parkinson's disease
    • Feany MB, Bender WW, (2000) A Drosophila model of Parkinson's disease. Nature 404: 394-398.
    • (2000) Nature , vol.404 , pp. 394-398
    • Feany, M.B.1    Bender, W.W.2
  • 50
    • 0026528074 scopus 로고
    • Hypergravity and aging in Drosophila melanogaster. 4. Climbing activity
    • Le Bourg E, Lints FA, (1992) Hypergravity and aging in Drosophila melanogaster. 4. Climbing activity. Gerontology 38: 59-64.
    • (1992) Gerontology , vol.38 , pp. 59-64
    • Le Bourg, E.1    Lints, F.A.2
  • 51
    • 0029919640 scopus 로고    scopus 로고
    • Sternopleural is a regulatory mutation of wingless with both dominant and recessive effects on larval development of Drosophila melanogaster
    • Neumann CJ, Cohen SM, (1996) Sternopleural is a regulatory mutation of wingless with both dominant and recessive effects on larval development of Drosophila melanogaster. Genetics 142: 1147-1155.
    • (1996) Genetics , vol.142 , pp. 1147-1155
    • Neumann, C.J.1    Cohen, S.M.2
  • 52
    • 0028328631 scopus 로고
    • A gain-of-function mutation in Drosophila MAP kinase activates multiple receptor tyrosine kinase signaling pathways
    • Brunner D, Oellers N, Szabad J, Biggs WH, Zipursky SL, et al. (1994) A gain-of-function mutation in Drosophila MAP kinase activates multiple receptor tyrosine kinase signaling pathways. Cell 76: 875-888.
    • (1994) Cell , vol.76 , pp. 875-888
    • Brunner, D.1    Oellers, N.2    Szabad, J.3    Biggs, W.H.4    Zipursky, S.L.5
  • 53
    • 0028048762 scopus 로고
    • The function of argos in regulating cell fate decisions during Drosophila eye and wing vein development
    • Sawamoto K, Okano H, Kobayakawa Y, Hayashi S, Mikoshiba K, et al. (1994) The function of argos in regulating cell fate decisions during Drosophila eye and wing vein development. Dev Biol 164: 267-276.
    • (1994) Dev Biol , vol.164 , pp. 267-276
    • Sawamoto, K.1    Okano, H.2    Kobayakawa, Y.3    Hayashi, S.4    Mikoshiba, K.5
  • 54
    • 0030970264 scopus 로고    scopus 로고
    • who encodes a KH RNA binding protein that functions in muscle development
    • Baehrecke EH, (1997) who encodes a KH RNA binding protein that functions in muscle development. Development 124: 1323-1332.
    • (1997) Development , vol.124 , pp. 1323-1332
    • Baehrecke, E.H.1
  • 55
    • 0030959948 scopus 로고    scopus 로고
    • The held out wings (how) Drosophila gene encodes a putative RNA-binding protein involved in the control of muscular and cardiac activity
    • Zaffran S, Astier M, Gratecos D, Sémériva M, (1997) The held out wings (how) Drosophila gene encodes a putative RNA-binding protein involved in the control of muscular and cardiac activity. Development 124: 2087-2098.
    • (1997) Development , vol.124 , pp. 2087-2098
    • Zaffran, S.1    Astier, M.2    Gratecos, D.3    Sémériva, M.4
  • 56
    • 0034531580 scopus 로고    scopus 로고
    • Activated mitogenic signaling induces a process of dedifferentiation in Alzheimer's disease that eventually results in cell death
    • Arendt T, Holzer M, Stöbe A, Gärtner U, Lüth HJ, et al. (2000) Activated mitogenic signaling induces a process of dedifferentiation in Alzheimer's disease that eventually results in cell death. Ann N Y Acad Sci 920: 249-255.
    • (2000) Ann N Y Acad Sci , vol.920 , pp. 249-255
    • Arendt, T.1    Holzer, M.2    Stöbe, A.3    Gärtner, U.4    Lüth, H.J.5
  • 57
    • 59449095881 scopus 로고    scopus 로고
    • Genetic evidence linking age-dependent attenuation of the 26S proteasome with the aging process
    • Tonoki A, Kuranaga E, Tomioka T, Hamazaki J, Murata S, et al. (2009) Genetic evidence linking age-dependent attenuation of the 26S proteasome with the aging process. Mol Cell Biol 29: 1095-1106.
    • (2009) Mol Cell Biol , vol.29 , pp. 1095-1106
    • Tonoki, A.1    Kuranaga, E.2    Tomioka, T.3    Hamazaki, J.4    Murata, S.5
  • 59
    • 71849084532 scopus 로고    scopus 로고
    • Aging and dietary restriction alter proteasome biogenesis and composition in the brain and liver
    • Dasuri K, Zhang L, Ebenezer P, Liu Y, Fernandez-Kim SO, et al. (2009) Aging and dietary restriction alter proteasome biogenesis and composition in the brain and liver. Mech Ageing Dev 130: 777-783.
    • (2009) Mech Ageing Dev , vol.130 , pp. 777-783
    • Dasuri, K.1    Zhang, L.2    Ebenezer, P.3    Liu, Y.4    Fernandez-Kim, S.O.5
  • 60
    • 0027176364 scopus 로고
    • The relationship between trinucleotide (CAG) repeat length and clinical features of Huntington's disease
    • Andrew SE, Goldberg YP, Kremer B, Telenius H, Theilmann J, et al. (1993) The relationship between trinucleotide (CAG) repeat length and clinical features of Huntington's disease. Nat Genet 4: 398-403.
    • (1993) Nat Genet , vol.4 , pp. 398-403
    • Andrew, S.E.1    Goldberg, Y.P.2    Kremer, B.3    Telenius, H.4    Theilmann, J.5
  • 61
    • 0030935035 scopus 로고    scopus 로고
    • The likelihood of being affected with Huntington disease by a particular age, for a specific CAG size
    • Brinkman RR, Mezei MM, Theilmann J, Almqvist E, Hayden MR, (1997) The likelihood of being affected with Huntington disease by a particular age, for a specific CAG size. Am J Hum Genet 60: 1202-1210.
    • (1997) Am J Hum Genet , vol.60 , pp. 1202-1210
    • Brinkman, R.R.1    Mezei, M.M.2    Theilmann, J.3    Almqvist, E.4    Hayden, M.R.5
  • 62
    • 0027377151 scopus 로고
    • Correlation between the onset age of Huntington's disease and length of the trinucleotide repeat in IT-15
    • Stine OC, Pleasant N, Franz ML, Abbott MH, Folstein SE, et al. (1993) Correlation between the onset age of Huntington's disease and length of the trinucleotide repeat in IT-15. Hum Mol Genet 2: 1547-1549.
    • (1993) Hum Mol Genet , vol.2 , pp. 1547-1549
    • Stine, O.C.1    Pleasant, N.2    Franz, M.L.3    Abbott, M.H.4    Folstein, S.E.5
  • 63
    • 77951252744 scopus 로고    scopus 로고
    • Huntington's disease: the case for genetic modifiers
    • Gusella J, MacDonald ME, (2009) Huntington's disease: the case for genetic modifiers. Genome Med 1: 80.1-80.6.
    • (2009) Genome Med , vol.1 , pp. 1-6
    • Gusella, J.1    MacDonald, M.E.2
  • 64
    • 33746961204 scopus 로고    scopus 로고
    • Genetic analysis of candidate genes modifying the age-at-onset in Huntington's disease
    • Metzger S, Bauer P, Tomiuk J, Laccone F, Didonato S, et al. (2006) Genetic analysis of candidate genes modifying the age-at-onset in Huntington's disease. Hum Genet 120: 285-292.
    • (2006) Hum Genet , vol.120 , pp. 285-292
    • Metzger, S.1    Bauer, P.2    Tomiuk, J.3    Laccone, F.4    Didonato, S.5
  • 66
    • 0038240721 scopus 로고    scopus 로고
    • Causative and susceptibility genes for Alzheimer's disease: a review
    • Rocchi A, Pellegrini S, Siciliano G, Murri L, (2003) Causative and susceptibility genes for Alzheimer's disease: a review. Brain Res Bull 61: 1-24.
    • (2003) Brain Res Bull , vol.61 , pp. 1-24
    • Rocchi, A.1    Pellegrini, S.2    Siciliano, G.3    Murri, L.4
  • 67
    • 0033392493 scopus 로고    scopus 로고
    • Ubiquitin ligase activity and tyrosine phosphorylation underlie suppression of growth factor signaling by c-Cbl/Sli-1
    • Levkowitz G, Waterman H, Ettenberg SA, Katz M, Tsygankov, et al. (1999) Ubiquitin ligase activity and tyrosine phosphorylation underlie suppression of growth factor signaling by c-Cbl/Sli-1. Mol Cell 4: 1029-1040.
    • (1999) Mol Cell , vol.4 , pp. 1029-1040
    • Levkowitz, G.1    Waterman, H.2    Ettenberg, S.A.3    Katz, M.4    Tsygankov5
  • 68
    • 0033529537 scopus 로고    scopus 로고
    • The RING finger of c-Cbl mediates desensitization of the epidermal growth factor receptor
    • Waterman H, Levkowitz G, Alroy I, Yarden Y, (2000) The RING finger of c-Cbl mediates desensitization of the epidermal growth factor receptor. J Biol Chem 274: 22151-22154.
    • (2000) J Biol Chem , vol.274 , pp. 22151-22154
    • Waterman, H.1    Levkowitz, G.2    Alroy, I.3    Yarden, Y.4
  • 69
    • 0033615732 scopus 로고    scopus 로고
    • Ligand-induced ubiquitination of the epidermal growth factor receptor involves the interaction of the c-Cbl RING finger and UbcH7
    • Yokouchi M, Kondo T, Houghton A, Bartkiewicz M, Horne WC, et al. (1999) Ligand-induced ubiquitination of the epidermal growth factor receptor involves the interaction of the c-Cbl RING finger and UbcH7. J Biol Chem 274: 31707-31712.
    • (1999) J Biol Chem , vol.274 , pp. 31707-31712
    • Yokouchi, M.1    Kondo, T.2    Houghton, A.3    Bartkiewicz, M.4    Horne, W.C.5
  • 70
    • 33344475413 scopus 로고    scopus 로고
    • Differential modification of Ras proteins by ubiquitination
    • Jura N, Scotto-Lavino E, Sobczyk A, Bar-Sagi D, (2006) Differential modification of Ras proteins by ubiquitination. Mol Cell 21: 679-687.
    • (2006) Mol Cell , vol.21 , pp. 679-687
    • Jura, N.1    Scotto-Lavino, E.2    Sobczyk, A.3    Bar-Sagi, D.4
  • 72
    • 0033537306 scopus 로고    scopus 로고
    • Signal transduction abnormalities in Alzheimer's disease: evidence of a pathogenic stimuli
    • McShea A, Zelasko DA, Gerst JL, Smith MA, (1999) Signal transduction abnormalities in Alzheimer's disease: evidence of a pathogenic stimuli. Brain Res 815: 237-242.
    • (1999) Brain Res , vol.815 , pp. 237-242
    • McShea, A.1    Zelasko, D.A.2    Gerst, J.L.3    Smith, M.A.4
  • 73
    • 0032588815 scopus 로고    scopus 로고
    • Elevated expression of p21ras is an early event in Alzheimer's disease and precedes neurofibrillary degeneration
    • Gärtner U, Holzer M, Arendt T, (1999) Elevated expression of p21ras is an early event in Alzheimer's disease and precedes neurofibrillary degeneration. Neuroscience 91: 1-5.
    • (1999) Neuroscience , vol.91 , pp. 1-5
    • Gärtner, U.1    Holzer, M.2    Arendt, T.3
  • 74
    • 0033516947 scopus 로고    scopus 로고
    • Activation of neuronal extracellular receptor kinase (ERK) in Alzheimer disease links oxidative stress to abnormal phosphorylation
    • Perry G, Roder H, Nunomura A, Takeda A, Friedlich AL, et al. (1999) Activation of neuronal extracellular receptor kinase (ERK) in Alzheimer disease links oxidative stress to abnormal phosphorylation. Neuroreport 10: 2411-2415.
    • (1999) Neuroreport , vol.10 , pp. 2411-2415
    • Perry, G.1    Roder, H.2    Nunomura, A.3    Takeda, A.4    Friedlich, A.L.5
  • 75
    • 33750900598 scopus 로고    scopus 로고
    • Distribution, levels and phosphorylation of Raf-1 in Alzheimer's disease
    • Mei M, Su B, Harrison K, Chao M, Siedlak SL, et al. (2006) Distribution, levels and phosphorylation of Raf-1 in Alzheimer's disease. J Neurochem 99: 1377-1388.
    • (2006) J Neurochem , vol.99 , pp. 1377-1388
    • Mei, M.1    Su, B.2    Harrison, K.3    Chao, M.4    Siedlak, S.L.5
  • 76
    • 0031887528 scopus 로고    scopus 로고
    • The origin and loss of the ubiquitin activating enzyme gene on the mammalian Y chromosome
    • Mitchell MJ, Wilcox SA, Watson JM, Lerner JL, Woods DR, et al. (1998) The origin and loss of the ubiquitin activating enzyme gene on the mammalian Y chromosome. Hum Mol Genet 7: 429-434.
    • (1998) Hum Mol Genet , vol.7 , pp. 429-434
    • Mitchell, M.J.1    Wilcox, S.A.2    Watson, J.M.3    Lerner, J.L.4    Woods, D.R.5
  • 77
    • 33846260694 scopus 로고    scopus 로고
    • X-linked infantile spinal muscular atrophy: clinical definition and molecular mapping
    • Dressman D, Ahearn ME, Yariz KO, Basterrecha H, Martínez F, et al. (2007) X-linked infantile spinal muscular atrophy: clinical definition and molecular mapping. Genet Med 9: 52-60.
    • (2007) Genet Med , vol.9 , pp. 52-60
    • Dressman, D.1    Ahearn, M.E.2    Yariz, K.O.3    Basterrecha, H.4    Martínez, F.5
  • 78
    • 0029009458 scopus 로고
    • A gene for a severe lethal form of X-linked arthrogryposis (X-linked infantile spinal muscular atrophy) maps to human chromosome Xp11.3-q11.2
    • Kobayashi H, Baumbach L, Matise TC, Schiavi A, Greenberg F, Hoffman EP, (1995) A gene for a severe lethal form of X-linked arthrogryposis (X-linked infantile spinal muscular atrophy) maps to human chromosome Xp11.3-q11.2. Hum Mol Genet 4: 1213-1216.
    • (1995) Hum Mol Genet , vol.4 , pp. 1213-1216
    • Kobayashi, H.1    Baumbach, L.2    Matise, T.C.3    Schiavi, A.4    Greenberg, F.5    Hoffman, E.P.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.