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Volumn 45, Issue 1, 2003, Pages 1-13

Part I: Parkin-associated proteins and Parkinson's disease

Author keywords

Alzheimer's disease; Neurodegeneration; Parkin; Parkinson's disease; PDZ; Protein protein interactions; UbcH7 8; Ubiquitination

Indexed keywords

ALPHA SYNUCLEIN; CYTOCHALASIN D; G PROTEIN COUPLED RECEPTOR; GUANOSINE TRIPHOSPHATASE; HYDROLASE; NOCODAZOLE; PARKIN; PROTEIN; PROTEIN PAEL; SYNPHILIN 1; UBIQUITIN; UBIQUITIN THIOLESTERASE; UNCLASSIFIED DRUG;

EID: 0038724238     PISSN: 00283908     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0028-3908(02)00337-4     Document Type: Short Survey
Times cited : (62)

References (103)
  • 2
    • 0034708480 scopus 로고    scopus 로고
    • The genome sequence of Drosophila melanogaster
    • Adams M.D., et al. The genome sequence of Drosophila melanogaster. Science. 287:2000;2185-2195.
    • (2000) Science , vol.287 , pp. 2185-2195
    • Adams, M.D.1
  • 4
    • 0035377241 scopus 로고    scopus 로고
    • Features of the parkin/ariadne-like ubiquitin ligase, HHARI, that regulate its interaction with the ubiquitin-conjugating enzyme, ubch7
    • Ardley H.C., Tan N.G., Rose S.A., Markham A.F., Robinson P.A. Features of the parkin/ariadne-like ubiquitin ligase, HHARI, that regulate its interaction with the ubiquitin-conjugating enzyme, ubch7. Journal of Biological Chemistry. 276:2001;19640-19647.
    • (2001) Journal of Biological Chemistry , vol.276 , pp. 19640-19647
    • Ardley, H.C.1    Tan, N.G.2    Rose, S.A.3    Markham, A.F.4    Robinson, P.A.5
  • 6
    • 0034237719 scopus 로고    scopus 로고
    • Energetics in the pathogenesis of neurodegenerative diseases
    • Beal M.F. Energetics in the pathogenesis of neurodegenerative diseases. Trends in Neuroscience. 23:2000;298-304.
    • (2000) Trends in Neuroscience , vol.23 , pp. 298-304
    • Beal, M.F.1
  • 7
  • 8
    • 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
  • 9
    • 0035140976 scopus 로고    scopus 로고
    • Ankyrins and cellular targeting of diverse membrane proteins to physiological sites
    • Bennett V., Chen L. Ankyrins and cellular targeting of diverse membrane proteins to physiological sites. Current Opinions in Cellular Biology. 13:2001;61-67.
    • (2001) Current Opinions in Cellular Biology , vol.13 , pp. 61-67
    • Bennett, V.1    Chen, L.2
  • 10
    • 0036144763 scopus 로고    scopus 로고
    • Regulatory functions of ubiquitination in the immune system
    • Ben-Neriah Y. Regulatory functions of ubiquitination in the immune system. Nature Immunology. 3:2002;20-26.
    • (2002) Nature Immunology , vol.3 , pp. 20-26
    • Ben-Neriah, Y.1
  • 11
    • 0028277934 scopus 로고
    • The p53-associated protein MDM2 contains a newly characterized zinc-binding domain called the RING finger
    • Boddy M.N., et al. The p53-associated protein MDM2 contains a newly characterized zinc-binding domain called the RING finger. Trends in Biochemical Science. 19:1994;198-199.
    • (1994) Trends in Biochemical Science , vol.19 , pp. 198-199
    • Boddy, M.N.1
  • 12
    • 0034602928 scopus 로고    scopus 로고
    • RING domains: Master builders of molecular scaffolds?
    • Borden K.L. RING domains: master builders of molecular scaffolds? Journal of Molecular Biology. 295:2000;1103-1112.
    • (2000) Journal of Molecular Biology , vol.295 , pp. 1103-1112
    • Borden, K.L.1
  • 14
    • 0034776095 scopus 로고    scopus 로고
    • Parkin ubiquitinates the alpha-synuclein-interacting protein, synphilin-1: Implications for Lewy-body formation in Parkinson disease
    • Chung K.K., Zhang Y., Lim K.L., Tanaka Y., Huang H., Gao J., Ross C.A., Dawson V.L., Dawson T.M. Parkin ubiquitinates the alpha-synuclein-interacting protein, synphilin-1: implications for Lewy-body formation in Parkinson disease. Nature Medicine. 10:2001;1144-1150.
    • (2001) Nature Medicine , vol.10 , pp. 1144-1150
    • Chung, K.K.1    Zhang, Y.2    Lim, K.L.3    Tanaka, Y.4    Huang, H.5    Gao, J.6    Ross, C.A.7    Dawson, V.L.8    Dawson, T.M.9
  • 15
    • 0032514259 scopus 로고    scopus 로고
    • Human CASK/LI N-2 binds syndecan-2 and protein 4.1 and iocalizes to the basoiaterai membrane of epithelial cells
    • Cohen A.R., et al. Human CASK/LI N-2 binds syndecan-2 and protein 4.1 and iocalizes to the basoiaterai membrane of epithelial cells. Journal of Cellular Biology. 142:1998;129-138.
    • (1998) Journal of Cellular Biology , vol.142 , pp. 129-138
    • Cohen, A.R.1
  • 16
    • 0031838352 scopus 로고    scopus 로고
    • Chaperone suppression of aggregation and altered subcellular proteasome localization imply protein misfolding in SCA1
    • Cummings C.J., Mancini M.A., Antalffy B., DeFranco D.B., Orr H.T., Zoghbi H.Y. Chaperone suppression of aggregation and altered subcellular proteasome localization imply protein misfolding in SCA1. Nature Genetics. 19:1998;148-154.
    • (1998) Nature Genetics , vol.19 , pp. 148-154
    • Cummings, C.J.1    Mancini, M.A.2    Antalffy, B.3    DeFranco, D.B.4    Orr, H.T.5    Zoghbi, H.Y.6
  • 18
    • 0034523581 scopus 로고    scopus 로고
    • PDZ proteins interacting with C-terminal GluR2/3 are involved in a PKC-dependent regulation of AMPA receptors at hippocampal synapses
    • Daw M.I., Chittajallu R., Bortolotto Z.A., Dev K.K., Duprat F., Henley J.M., Collingridge G.L., Isaac J.T. PDZ proteins interacting with C-terminal GluR2/3 are involved in a PKC-dependent regulation of AMPA receptors at hippocampal synapses. Neuron. 28:2000;873-886.
    • (2000) Neuron , vol.28 , pp. 873-886
    • Daw, M.I.1    Chittajallu, R.2    Bortolotto, Z.A.3    Dev, K.K.4    Duprat, F.5    Henley, J.M.6    Collingridge, G.L.7    Isaac, J.T.8
  • 19
    • 0033030234 scopus 로고    scopus 로고
    • The protein kinase C alpha binding protein PICK1 interacts with short but not long form alternative splice variants of AMPA receptor subunits
    • Dev K.K., Nishimure A., Henley J.M., Nakanishi S. The protein kinase C alpha binding protein PICK1 interacts with short but not long form alternative splice variants of AMPA receptor subunits. Neuropharmacology. 38:1999;635-644.
    • (1999) Neuropharmacology , vol.38 , pp. 635-644
    • Dev, K.K.1    Nishimure, A.2    Henley, J.M.3    Nakanishi, S.4
  • 20
    • 0035397915 scopus 로고    scopus 로고
    • Regulation of mGlu7 receptors by proteins that interact with the intracellular C-terminus
    • Dev K.K., Nakanishi S., Henley J.M. Regulation of mGlu7 receptors by proteins that interact with the intracellular C-terminus. Trends in Pharmacological Science. 22:2001;355-361.
    • (2001) Trends in Pharmacological Science , vol.22 , pp. 355-361
    • Dev, K.K.1    Nakanishi, S.2    Henley, J.M.3
  • 21
    • 0038460184 scopus 로고    scopus 로고
    • Part II: α-synuclein and its molecular pathophysiological role in neurodegenerative disease
    • this issue. PII: S0028-3908(03)00140-0.
    • Dev, K.K., Hofele, K., Barbieri, S., Buchman, V.L., van der Putten, H., 2003. Part II: α-synuclein and its molecular pathophysiological role in neurodegenerative disease. Neuropharmacology 45, this issue. PII: S0028-3908(03)00140-0.
    • (2003) Neuropharmacology , vol.45
    • Dev, K.K.1    Hofele, K.2    Barbieri, S.3    Buchman, V.L.4    Van Der Putten, H.5
  • 23
    • 0037016687 scopus 로고    scopus 로고
    • Parkin and CASK/LIN-2 associate via a PDZ-mediated interaction and are co-localized in lipid rafts and postsynaptic densities in brain
    • Fallon L., Moreau F., Croft B.G., Labib N., Gu W.J., Fon E.A. Parkin and CASK/LIN-2 associate via a PDZ-mediated interaction and are co-localized in lipid rafts and postsynaptic densities in brain. Journal of Biological Chemistry. 277:2002;486-491.
    • (2002) Journal of Biological Chemistry , vol.277 , pp. 486-491
    • Fallon, L.1    Moreau, F.2    Croft, B.G.3    Labib, N.4    Gu, W.J.5    Fon, E.A.6
  • 25
    • 0037431172 scopus 로고    scopus 로고
    • Parkin: A multipurpose neuroprotective agent?
    • Feany M.B., Pallanck L.J. Parkin: a multipurpose neuroprotective agent? Neuron. 38:2003;13-16.
    • (2003) Neuron , vol.38 , pp. 13-16
    • Feany, M.B.1    Pallanck, L.J.2
  • 26
    • 0033214990 scopus 로고    scopus 로고
    • Septins: Cytoskeletal polymers or signalling GTPases?
    • Field C.M., Kellogg D. Septins: cytoskeletal polymers or signalling GTPases? Trends in Cellular Biology. 9:1999;387-394.
    • (1999) Trends in Cellular Biology , vol.9 , pp. 387-394
    • Field, C.M.1    Kellogg, D.2
  • 29
    • 0034798193 scopus 로고    scopus 로고
    • Genetics of Parkinson's disease
    • Gasser T. Genetics of Parkinson's disease. Journal of Neurology. 248:2001;833-840.
    • (2001) Journal of Neurology , vol.248 , pp. 833-840
    • Gasser, T.1
  • 31
    • 17444433155 scopus 로고    scopus 로고
    • Cloning of rat parkin cDNA and distribution ofparkin in rat brain
    • Gu W.J., et al. Cloning of rat parkin cDNA and distribution ofparkin in rat brain. Journal of Neurochemistry. 74:2000;1773-1776.
    • (2000) Journal of Neurochemistry , vol.74 , pp. 1773-1776
    • Gu, W.J.1
  • 36
    • 0031682676 scopus 로고    scopus 로고
    • Biochemical aspects of Parkinson's disease
    • Hornykiewicz, O., 1998. Biochemical aspects of Parkinson's disease. Neurology S2-9.
    • (1998) Neurology
    • Hornykiewicz, O.1
  • 39
    • 0034680913 scopus 로고    scopus 로고
    • Parkin suppresses unfolded protein stress-induced cell death through its E3 ubiquitin-protein ligase activity
    • Imai Y., Soda M., Takahashi R. Parkin suppresses unfolded protein stress-induced cell death through its E3 ubiquitin-protein ligase activity. Journal of Biological Chemistry. 275:2000;35661-35664.
    • (2000) Journal of Biological Chemistry , vol.275 , pp. 35661-35664
    • Imai, Y.1    Soda, M.2    Takahashi, R.3
  • 40
    • 0035967883 scopus 로고    scopus 로고
    • An unfolded putative transmembrane polypeptide, which can lead to endoplasmic reticulum stress, is a substrate of Parkin
    • Imai Y., Soda M., Inoue H., Hattori N., Mizuno Y., Takahashi R. An unfolded putative transmembrane polypeptide, which can lead to endoplasmic reticulum stress, is a substrate of Parkin. Cell. 105:2001;891-902.
    • (2001) Cell , vol.105 , pp. 891-902
    • Imai, Y.1    Soda, M.2    Inoue, H.3    Hattori, N.4    Mizuno, Y.5    Takahashi, R.6
  • 41
    • 0036345454 scopus 로고    scopus 로고
    • CHIP is associated with parkin, a gene responsible for Familial Parkinson's Disease and enhances its ubiquitin ligase activity
    • Imai Y., Soda M., Hatakeyama S., Akagi T., Hashikawa T., Nakayama K.I., Takahashi R. CHIP is associated with parkin, a gene responsible for Familial Parkinson's Disease and enhances its ubiquitin ligase activity. Molecular Cell. 10:2002;55-67.
    • (2002) Molecular Cell , vol.10 , pp. 55-67
    • Imai, Y.1    Soda, M.2    Hatakeyama, S.3    Akagi, T.4    Hashikawa, T.5    Nakayama, K.I.6    Takahashi, R.7
  • 42
    • 0035341492 scopus 로고    scopus 로고
    • Parkinson's disease, pesticides and mitochondrial dysfunction
    • Jenner P. Parkinson's disease, pesticides and mitochondrial dysfunction. Trends in Neuroscience. 24:2001;245-247.
    • (2001) Trends in Neuroscience , vol.24 , pp. 245-247
    • Jenner, P.1
  • 43
    • 0032500599 scopus 로고    scopus 로고
    • Binding of alpha-synuclein to brain vesicles is abolished by familial Parkinson's disease mutation
    • Jensen P.H., Nielsen M.S., Jakes R., Dotti C.G., Goedert M. Binding of alpha-synuclein to brain vesicles is abolished by familial Parkinson's disease mutation. Journal of Biological Chemistry. 273:1998;26292-26294.
    • (1998) Journal of Biological Chemistry , vol.273 , pp. 26292-26294
    • Jensen, P.H.1    Nielsen, M.S.2    Jakes, R.3    Dotti, C.G.4    Goedert, M.5
  • 45
    • 0033536637 scopus 로고    scopus 로고
    • The tyrosine kinase negative regulator c-Cbl as a RING-type, E2-dependent ubiquitin-protein ligase
    • Joazeiro C.A., Wing S.S., Huang H., Leverson J.D., Hunter T., Liu Y.C. The tyrosine kinase negative regulator c-Cbl as a RING-type, E2-dependent ubiquitin-protein ligase. Science. 286:1999;309-312.
    • (1999) Science , vol.286 , pp. 309-312
    • Joazeiro, C.A.1    Wing, S.S.2    Huang, H.3    Leverson, J.D.4    Hunter, T.5    Liu, Y.C.6
  • 46
    • 0034266806 scopus 로고    scopus 로고
    • RING finger proteins: Mediators of ubiquitin ligase activity
    • Joazeiro C.A., Weissman A.M. RING finger proteins: mediators of ubiquitin ligase activity. Cell. 102:2000;549-552.
    • (2000) Cell , vol.102 , pp. 549-552
    • Joazeiro, C.A.1    Weissman, A.M.2
  • 47
    • 0034326934 scopus 로고    scopus 로고
    • Does failure of parkin-mediated ubiquitination cause juvenile parkinsonism?
    • Kahle P.J., Leimer U., Haass C. Does failure of parkin-mediated ubiquitination cause juvenile parkinsonism? Trends in Biochemical Science. 25:2000;524-527.
    • (2000) Trends in Biochemical Science , vol.25 , pp. 524-527
    • Kahle, P.J.1    Leimer, U.2    Haass, C.3
  • 48
    • 0035063573 scopus 로고    scopus 로고
    • Novel roles for mammalian septins: From vesicle trafficking to oncogenesis
    • Kartmann B., Roth D. Novel roles for mammalian septins: from vesicle trafficking to oncogenesis. Journal of Cellular Science. 114:2001;839-844.
    • (2001) Journal of Cellular Science , vol.114 , pp. 839-844
    • Kartmann, B.1    Roth, D.2
  • 50
    • 0032127179 scopus 로고    scopus 로고
    • Identification, expression, and chromosomal localization of ubiquitin conjugating enzyme 7 (UBE2G2), a human homologue of the saccharomyces cerevisiae UBC7 gene
    • Katsanis N., Fisher E.M. Identification, expression, and chromosomal localization of ubiquitin conjugating enzyme 7 (UBE2G2), a human homologue of the saccharomyces cerevisiae UBC7 gene. Genomics. 51:1998;128-131.
    • (1998) Genomics , vol.51 , pp. 128-131
    • Katsanis, N.1    Fisher, E.M.2
  • 54
    • 0034044667 scopus 로고    scopus 로고
    • Molecuiar cloning, gene expression, and identification of a splicing variant of the mouse parkin gene
    • Kitada T., et al. Molecuiar cloning, gene expression, and identification of a splicing variant of the mouse parkin gene. Mammal Genome. 11:2000;417-421.
    • (2000) Mammal Genome , vol.11 , pp. 417-421
    • Kitada, T.1
  • 55
    • 0034578389 scopus 로고    scopus 로고
    • Aggresomes, inclusion bodies and protein aggregation
    • Kopito R.R. Aggresomes, inclusion bodies and protein aggregation. Trends in Biochemical Science. 10:2000;524-530.
    • (2000) Trends in Biochemical Science , vol.10 , pp. 524-530
    • Kopito, R.R.1
  • 58
    • 0030908874 scopus 로고    scopus 로고
    • Physical interaction between specific E2 and Hect E3 enzymes determines functional cooperativity
    • Kumar S., Kao W.H., Howley P.M. Physical interaction between specific E2 and Hect E3 enzymes determines functional cooperativity. Journal of Biological Chemistry. 272:1997;13548-13554.
    • (1997) Journal of Biological Chemistry , vol.272 , pp. 13548-13554
    • Kumar, S.1    Kao, W.H.2    Howley, P.M.3
  • 60
    • 0031715849 scopus 로고    scopus 로고
    • Epidemiology versus genetics in Parkinson's disease: Progress in resolving an age-old debate
    • Langston J.W. Epidemiology versus genetics in Parkinson's disease: progress in resolving an age-old debate. Annals in Neurology. 44:1998;S45-52.
    • (1998) Annals in Neurology , vol.44 , pp. 45-52
    • Langston, J.W.1
  • 61
    • 0035066885 scopus 로고    scopus 로고
    • Direct binding and functional coupling of alpha-synuclein to the dopamine transporters accelerate dopamine-induced apoptosis
    • Lee F.J., Liu F., Pristupa Z.B., Niznik H.B. Direct binding and functional coupling of alpha-synuclein to the dopamine transporters accelerate dopamine-induced apoptosis. FASEB Journal. 15:2001;916-926.
    • (2001) FASEB Journal , vol.15 , pp. 916-926
    • Lee, F.J.1    Liu, F.2    Pristupa, Z.B.3    Niznik, H.B.4
  • 63
    • 0035949542 scopus 로고    scopus 로고
    • Effect of familial Parkinson's disease point mutations A30P and A53T on the structural properties, aggregation, and fibrillation of human alpha-synuclein
    • Li J., Uversky V.N., Fink A.L. Effect of familial Parkinson's disease point mutations A30P and A53T on the structural properties, aggregation, and fibrillation of human alpha-synuclein. Biochemistry. 40:2001;11604-11613.
    • (2001) Biochemistry , vol.40 , pp. 11604-11613
    • Li, J.1    Uversky, V.N.2    Fink, A.L.3
  • 64
    • 0025326719 scopus 로고
    • Ubiquitin carboxyl-terminal hydrolase (PGP 9.5) is selectively present in ubiquitinated inclusion bodies characteristic of human neurodegenerative diseases
    • Lowe J., McDermott H., Landon M., Mayer R.J., Wilkinson K.D. Ubiquitin carboxyl-terminal hydrolase (PGP 9.5) is selectively present in ubiquitinated inclusion bodies characteristic of human neurodegenerative diseases. Journal of Pathology. 161:1990;153-160.
    • (1990) Journal of Pathology , vol.161 , pp. 153-160
    • Lowe, J.1    McDermott, H.2    Landon, M.3    Mayer, R.J.4    Wilkinson, K.D.5
  • 68
    • 0031661170 scopus 로고    scopus 로고
    • The making of neurexins
    • Missier M., et al. The making of neurexins. Journal of Neurochemistry. 71:1998;1339-1347.
    • (1998) Journal of Neurochemistry , vol.71 , pp. 1339-1347
    • Missier, M.1
  • 69
    • 0031848638 scopus 로고    scopus 로고
    • Neurochemical and neurogenetic correlates of Parkinson's disease
    • Mizuno Y., Hattori N., Matsumine H. Neurochemical and neurogenetic correlates of Parkinson's disease. Journal of Neurochemistry. 71:1998;893-902.
    • (1998) Journal of Neurochemistry , vol.71 , pp. 893-902
    • Mizuno, Y.1    Hattori, N.2    Matsumine, H.3
  • 70
    • 0033151716 scopus 로고    scopus 로고
    • A novel transactivation domain in parkin
    • Morett E., Bork P. A novel transactivation domain in parkin. Trends in Biochemical Science. 24:1999;229-231.
    • (1999) Trends in Biochemical Science , vol.24 , pp. 229-231
    • Morett, E.1    Bork, P.2
  • 73
    • 0030023718 scopus 로고    scopus 로고
    • Detection of protein-protein interactions in the nervous system using the two-hybrid system
    • Nishimune A., et al. Detection of protein-protein interactions in the nervous system using the two-hybrid system. Trends in Neuroscience. 19:1996;261-266.
    • (1996) Trends in Neuroscience , vol.19 , pp. 261-266
    • Nishimune, A.1
  • 74
    • 0030043724 scopus 로고    scopus 로고
    • Cioning of human ubiquitin-conjugating enzymes UbcH6 and UbcH7 (E2-F1 ) and characterization of their interaction with E6-AP and RSP5
    • Nuber U., et al. Cioning of human ubiquitin-conjugating enzymes UbcH6 and UbcH7 (E2-F1 ) and characterization of their interaction with E6-AP and RSP5. Journal of Biological Chemistry. 271:1996;2795-2800.
    • (1996) Journal of Biological Chemistry , vol.271 , pp. 2795-2800
    • Nuber, U.1
  • 75
    • 0030727466 scopus 로고    scopus 로고
    • Cell cycle regulation by the ubiquitin pathway
    • Pagano M. Cell cycle regulation by the ubiquitin pathway. FASEB Journal. 11:1997;1067-1075.
    • (1997) FASEB Journal , vol.11 , pp. 1067-1075
    • Pagano, M.1
  • 76
    • 0036132908 scopus 로고    scopus 로고
    • The septin CDCrel-1 is dispensable for normal development and neurotransmitter release
    • Peng X.R., Jia Z., Zhang Y., Ware J., Trimble W.S. The septin CDCrel-1 is dispensable for normal development and neurotransmitter release. Molecular and Cellular Biology. 22:2002;378-387.
    • (2002) Molecular and Cellular Biology , vol.22 , pp. 378-387
    • Peng, X.R.1    Jia, Z.2    Zhang, Y.3    Ware, J.4    Trimble, W.S.5
  • 78
    • 0034915764 scopus 로고    scopus 로고
    • Mechanisms underlying ubiquitination
    • Pickart C.M. Mechanisms underlying ubiquitination. Annual Review of Biochemistry. 70:2001;503-533.
    • (2001) Annual Review of Biochemistry , vol.70 , pp. 503-533
    • Pickart, C.M.1
  • 80
    • 0031171361 scopus 로고    scopus 로고
    • PDZ domains: Targeting signalling molecules to sub-membranous sites
    • Ponting C.P., Phillips C., Davies K.E., Blake D.J. PDZ domains: targeting signalling molecules to sub-membranous sites. Bioessays. 19:1997;469-479.
    • (1997) Bioessays , vol.19 , pp. 469-479
    • Ponting, C.P.1    Phillips, C.2    Davies, K.E.3    Blake, D.J.4
  • 81
    • 0037738525 scopus 로고    scopus 로고
    • Parkin binds to a α/β tubulin and increases their ubiquitination and degredation
    • Ren Y., Zhao J., Feng J. Parkin binds to a α/β tubulin and increases their ubiquitination and degredation. Journal of Neuroscience. 23:2003;3316-3324.
    • (2003) Journal of Neuroscience , vol.23 , pp. 3316-3324
    • Ren, Y.1    Zhao, J.2    Feng, J.3
  • 82
    • 0035146933 scopus 로고    scopus 로고
    • PML and COP1 - Two proteins with much in common
    • Reyes J.C. PML and COP1 - two proteins with much in common. Trends in Biochemical Science. 26:2001;18-20.
    • (2001) Trends in Biochemical Science , vol.26 , pp. 18-20
    • Reyes, J.C.1
  • 84
    • 0034643336 scopus 로고    scopus 로고
    • Rapid degradation of a large fraction of newly synthesized proteins by proteasomes
    • Schubert U., Anton L.C., Gibbs J., Norbury C.C., Yewdell J.W., Bennink J.R. Rapid degradation of a large fraction of newly synthesized proteins by proteasomes. Nature. 404:2000;770-774.
    • (2000) Nature , vol.404 , pp. 770-774
    • Schubert, U.1    Anton, L.C.2    Gibbs, J.3    Norbury, C.C.4    Yewdell, J.W.5    Bennink, J.R.6
  • 85
    • 0034916230 scopus 로고    scopus 로고
    • PDZ domains and the organization of supramolecular complexes
    • Sheng M., Sala C. PDZ domains and the organization of supramolecular complexes. Annual Review in Neuroscience. 24:2001;1-29.
    • (2001) Annual Review in Neuroscience , vol.24 , pp. 1-29
    • Sheng, M.1    Sala, C.2
  • 91
    • 0037422010 scopus 로고    scopus 로고
    • Parkin is a component of an SCF-like ubiquitin ligase complex and protects neurons from kainate excitotoxicity
    • Staropoli J.F., McDermott C., Martinat C., Schulman B., Demireva E., Abeliovich A. Parkin is a component of an SCF-like ubiquitin ligase complex and protects neurons from kainate excitotoxicity. Neuron. 37:2003;735-749.
    • (2003) Neuron , vol.37 , pp. 735-749
    • Staropoli, J.F.1    McDermott, C.2    Martinat, C.3    Schulman, B.4    Demireva, E.5    Abeliovich, A.6
  • 92
    • 0024546234 scopus 로고
    • The role of environmental toxins in the etiology of Parkinson's disease
    • Tanner C.M. The role of environmental toxins in the etiology of Parkinson's disease. Trends in Neuroscience. 12:1989;49-54.
    • (1989) Trends in Neuroscience , vol.12 , pp. 49-54
    • Tanner, C.M.1
  • 93
    • 0035976835 scopus 로고    scopus 로고
    • Alpha-synuclein metabolism and aggregation is linked to ubiquitin-independent degradation by the proteasome
    • Tofaris G.K., Layfield R., Spillantini M.G. Alpha-synuclein metabolism and aggregation is linked to ubiquitin-independent degradation by the proteasome. FEBS Letters. 509:2001;22-26.
    • (2001) FEBS Letters , vol.509 , pp. 22-26
    • Tofaris, G.K.1    Layfield, R.2    Spillantini, M.G.3
  • 94
    • 0035026044 scopus 로고    scopus 로고
    • Functional interaction between monoamine plasma membrane transporters and the synaptic PDZ domain-containing protein PICK1
    • Torres G.E., Yao W.D., Mohn A.R., Quan H., Kim K.M., Levey A.I., Staudinger J., Caron M.G. Functional interaction between monoamine plasma membrane transporters and the synaptic PDZ domain-containing protein PICK1. Neuron. 30:2001;121-134.
    • (2001) Neuron , vol.30 , pp. 121-134
    • Torres, G.E.1    Yao, W.D.2    Mohn, A.R.3    Quan, H.4    Kim, K.M.5    Levey, A.I.6    Staudinger, J.7    Caron, M.G.8
  • 95
    • 0027489773 scopus 로고
    • Moiecular cloning of cDNA encoding an unrecognized component of amyloid in Alzheimer disease
    • Ueda K., et al. Moiecular cloning of cDNA encoding an unrecognized component of amyloid in Alzheimer disease. Proceedings of the National Academy Science of the USA. 90:1993;11282-11286.
    • (1993) Proceedings of the National Academy Science of the USA , vol.90 , pp. 11282-11286
    • Ueda, K.1
  • 96
    • 0032146362 scopus 로고    scopus 로고
    • Mutations in RNA: A first example of molecular misreading in Alzheimer's disease
    • van Leuven F.W., Burbach J.P., Hol E.M. Mutations in RNA: a first example of molecular misreading in Alzheimer's disease. Trends in Neuroscience. 21:1998;331-335.
    • (1998) Trends in Neuroscience , vol.21 , pp. 331-335
    • Van Leuven, F.W.1    Burbach, J.P.2    Hol, E.M.3
  • 97
    • 0032867676 scopus 로고    scopus 로고
    • The 26S proteasome: A molecular machine designed for controlled proteolysis
    • Voges D., Zwickl P., Baumeister W. The 26S proteasome: a molecular machine designed for controlled proteolysis. Annual Review of Biochemistry. 68:1999;1015-1068.
    • (1999) Annual Review of Biochemistry , vol.68 , pp. 1015-1068
    • Voges, D.1    Zwickl, P.2    Baumeister, W.3
  • 99
    • 0030854265 scopus 로고    scopus 로고
    • Altemative expression of platelet glycoprotein Ib(beta) mRNA from an adjacent 5' gene with an imperfect polyadenylation signal sequence
    • Ware J., Zieger B. Altemative expression of platelet glycoprotein Ib(beta) mRNA from an adjacent 5' gene with an imperfect polyadenylation signal sequence. Journal of Clinical Investigation. 99:1997;520-525.
    • (1997) Journal of Clinical Investigation , vol.99 , pp. 520-525
    • Ware, J.1    Zieger, B.2
  • 100
    • 0037468831 scopus 로고    scopus 로고
    • Parkin suppresses Dopaminergic neuron-selective neurotoxicity induced by Pael-R in Drosophila
    • Yang Y., Nishimura I., Imai Y., Takahashi R., Lu B. Parkin suppresses Dopaminergic neuron-selective neurotoxicity induced by Pael-R in Drosophila. Neuron. 37:2003;911-924.
    • (2003) Neuron , vol.37 , pp. 911-924
    • Yang, Y.1    Nishimura, I.2    Imai, Y.3    Takahashi, R.4    Lu, B.5
  • 101
    • 0031575918 scopus 로고    scopus 로고
    • A novei endothelin receptor type-B-Iike gene enriched in the brain
    • Zeng Z., et al. A novei endothelin receptor type-B-Iike gene enriched in the brain. Biochemistry and Biophysical Research Communications. 233:1997;559-567.
    • (1997) Biochemistry and Biophysical Research Communications , vol.233 , pp. 559-567
    • Zeng, Z.1
  • 102
    • 0034700158 scopus 로고    scopus 로고
    • Parkin functions as an E2-dependent ubiquitin-protein ligase and promotes the degradation of the synaptic vesicle-associated protein, CDCrel-1
    • Zhang Y., Gao J., Chung K.K., Huang H., Dawson V.L., Dawson T.M. Parkin functions as an E2-dependent ubiquitin-protein ligase and promotes the degradation of the synaptic vesicle-associated protein, CDCrel-1. Proceedings of the National Academy Science of the USA. 97:2000;13354-13359.
    • (2000) Proceedings of the National Academy Science of the USA , vol.97 , pp. 13354-13359
    • Zhang, Y.1    Gao, J.2    Chung, K.K.3    Huang, H.4    Dawson, V.L.5    Dawson, T.M.6
  • 103
    • 0034682718 scopus 로고    scopus 로고
    • Structure of a c-Cbl-UbcH7 complex: RING domain function in ubiquitin-protein ligases
    • Zheng N., Wang P., Jeffrey P.D., Pavletich N.P. Structure of a c-Cbl-UbcH7 complex: RING domain function in ubiquitin-protein ligases. Cell. 102:2000;533-539.
    • (2000) Cell , vol.102 , pp. 533-539
    • Zheng, N.1    Wang, P.2    Jeffrey, P.D.3    Pavletich, N.P.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.