메뉴 건너뛰기




Volumn 113, Issue 2, 2010, Pages 402-417

Identification and characterization of a novel endogenous murine parkin mutation

Author keywords

C3H mouse; E3 ligase; Mutation; Parkin; Parkinson's disease; Recessive

Indexed keywords

BRAIN EXTRACT; MESSENGER RNA; MONOCLONAL ANTIBODY; MONOCLONAL ANTIBODY PRK109; MONOCLONAL ANTIBODY PRK28; MONOCLONAL ANTIBODY PRK8; PARKIN; UBIQUITIN CONJUGATING ENZYME E2; UBIQUITIN CONJUGATING ENZYME E2 UBCH7; UBIQUITIN CONJUGATING ENZYME E2 UBCH8; UNCLASSIFIED DRUG;

EID: 77949747845     PISSN: 00223042     EISSN: 14714159     Source Type: Journal    
DOI: 10.1111/j.1471-4159.2010.06605.x     Document Type: Article
Times cited : (3)

References (72)
  • 1
    • 0034805921 scopus 로고    scopus 로고
    • The genomic structure and promoter region of the human parkin gene
    • Asakawa S., Tsunematsu K., Takayanagi A. et al. (2001) The genomic structure and promoter region of the human parkin gene. Biochem. Biophys. Res. Commun. 286, 863 868.
    • (2001) Biochem. Biophys. Res. Commun. , vol.286 , pp. 863-868
    • Asakawa, S.1    Tsunematsu, K.2    Takayanagi, A.3
  • 2
    • 58349114656 scopus 로고    scopus 로고
    • Molecular analysis of the parkin gene in South African patients diagnosed with Parkinson's disease
    • Bardien S., Keyser R., Yako Y., Lombard D. Carr J. (2009) Molecular analysis of the parkin gene in South African patients diagnosed with Parkinson's disease. Parkinsonism Relat. Disord. 15, 116 121.
    • (2009) Parkinsonism Relat. Disord. , vol.15 , pp. 116-121
    • Bardien, S.1    Keyser, R.2    Yako, Y.3    Lombard, D.4    Carr, J.5
  • 3
    • 38949210720 scopus 로고    scopus 로고
    • Genetics of parkinsonism
    • Bonifati V. (2007) Genetics of parkinsonism. Parkinsonism Relat. Disord. 13 (Suppl. 3 S233 S241.
    • (2007) Parkinsonism Relat. Disord. , vol.13 , Issue.SUPPL. 3
    • Bonifati, V.1
  • 4
    • 4444255628 scopus 로고    scopus 로고
    • Alpha-internexin aggregates are abundant in neuronal intermediate filament inclusion disease (NIFID) but rare in other neurodegenerative diseases
    • Cairns N. J., Uryu K., Bigio E. H. et al. (2004) Alpha-internexin aggregates are abundant in neuronal intermediate filament inclusion disease (NIFID) but rare in other neurodegenerative diseases. Acta Neuropathol. 108, 213 223.
    • (2004) Acta Neuropathol. , vol.108 , pp. 213-223
    • Cairns, N.J.1    Uryu, K.2    Bigio, E.H.3
  • 7
    • 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. (2001) Parkin ubiquitinates the alpha-synuclein-interacting protein, synphilin- 1: implications for Lewy-body formation in Parkinson disease. Nat. Med. 7, 1144 1150.
    • (2001) Nat. Med. , vol.7 , 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
  • 9
    • 0034770604 scopus 로고    scopus 로고
    • Linking ubiquitin, parkin and synphilin-1
    • Ciechanover A. (2001) Linking ubiquitin, parkin and synphilin-1. Nat. Med. 7, 1108 1109.
    • (2001) Nat. Med. , vol.7 , pp. 1108-1109
    • Ciechanover, A.1
  • 12
    • 33645558938 scopus 로고    scopus 로고
    • Inclusion body formation and neurodegeneration are parkin independent in a mouse model of alpha-synucleinopathy
    • von Coelln R., Thomas B., Andrabi S. A. et al. (2006) Inclusion body formation and neurodegeneration are parkin independent in a mouse model of alpha-synucleinopathy. J. Neurosci. 26, 3685 3696.
    • (2006) J. Neurosci. , vol.26 , pp. 3685-3696
    • Von Coelln, R.1    Thomas, B.2    Andrabi, S.A.3
  • 13
    • 10744220754 scopus 로고    scopus 로고
    • The p38 subunit of the aminoacyl-tRNA synthetase complex is a Parkin substrate: Linking protein biosynthesis and neurodegeneration
    • Corti O., Hampe C., Koutnikova H. et al. (2003) The p38 subunit of the aminoacyl-tRNA synthetase complex is a Parkin substrate: linking protein biosynthesis and neurodegeneration. Hum. Mol. Genet. 12, 1427 1437.
    • (2003) Hum. Mol. Genet. , vol.12 , pp. 1427-1437
    • Corti, O.1    Hampe, C.2    Koutnikova, H.3
  • 14
    • 34249937901 scopus 로고    scopus 로고
    • Pink1, Parkin, DJ-1 and mitochondrial dysfunction in Parkinson's disease
    • Dodson M. W. Guo M. (2007) Pink1, Parkin, DJ-1 and mitochondrial dysfunction in Parkinson's disease. Curr. Opin. Neurobiol. 17, 331 337.
    • (2007) Curr. Opin. Neurobiol. , vol.17 , pp. 331-337
    • Dodson, M.W.1    Guo, M.2
  • 15
    • 55949128232 scopus 로고    scopus 로고
    • Emerging pathways in genetic Parkinson's disease: Autosomal-recessive genes in Parkinson's disease - A common pathway?
    • Fitzgerald J. C. Plun-Favreau H. (2008) Emerging pathways in genetic Parkinson's disease: autosomal-recessive genes in Parkinson's disease - a common pathway? FEBS J. 275, 5758 5766.
    • (2008) FEBS J. , vol.275 , pp. 5758-5766
    • Fitzgerald, J.C.1    Plun-Favreau, H.2
  • 16
    • 69949115593 scopus 로고    scopus 로고
    • Parkin deficiency delays motor decline and disease manifestation in a mouse model of synucleinopathy
    • Fournier M., Vitte J., Garrigue J. et al. (2009) Parkin deficiency delays motor decline and disease manifestation in a mouse model of synucleinopathy. PLoS ONE 4, e6629.
    • (2009) PLoS ONE , vol.4 , pp. 6629
    • Fournier, M.1    Vitte, J.2    Garrigue, J.3
  • 17
    • 58149149970 scopus 로고    scopus 로고
    • Parkin deficiency increases vulnerability to inflammation-related nigral degeneration
    • Frank-Cannon T. C., Tran T., Ruhn K. A. et al. (2008) Parkin deficiency increases vulnerability to inflammation-related nigral degeneration. J. Neurosci. 28, 10825 10834.
    • (2008) J. Neurosci. , vol.28 , pp. 10825-10834
    • Frank-Cannon, T.C.1    Tran, T.2    Ruhn, K.A.3
  • 18
    • 0030803667 scopus 로고    scopus 로고
    • The NR2B-specific interactions of polyamines and protons with the N-methyl-D-aspartate receptor
    • Gallagher M. J., Huang H., Grant E. R. Lynch D. R. (1997) The NR2B-specific interactions of polyamines and protons with the N-methyl-D-aspartate receptor. J. Biol. Chem. 272, 24971 24979.
    • (1997) J. Biol. Chem. , vol.272 , pp. 24971-24979
    • Gallagher, M.J.1    Huang, H.2    Grant, E.R.3    Lynch, D.R.4
  • 19
    • 0141891953 scopus 로고    scopus 로고
    • Parkin-deficient mice exhibit nigrostriatal deficits but not loss of dopaminergic neurons
    • Goldberg M. S., Fleming S. M., Palacino J. J. et al. (2003) Parkin-deficient mice exhibit nigrostriatal deficits but not loss of dopaminergic neurons. J. Biol. Chem. 278, 43628 43635.
    • (2003) J. Biol. Chem. , vol.278 , pp. 43628-43635
    • Goldberg, M.S.1    Fleming, S.M.2    Palacino, J.J.3
  • 20
    • 10744227945 scopus 로고    scopus 로고
    • The C289G and C418R missense mutations cause rapid sequestration of human Parkin into insoluble aggregates
    • Gu W. J., Corti O., Araujo F. et al. (2003) The C289G and C418R missense mutations cause rapid sequestration of human Parkin into insoluble aggregates. Neurobiol. Dis. 14, 357 364.
    • (2003) Neurobiol. Dis. , vol.14 , pp. 357-364
    • Gu, W.J.1    Corti, O.2    Araujo, F.3
  • 21
    • 57049185760 scopus 로고    scopus 로고
    • Mutation analysis of Parkin, PINK1, DJ-1 and ATP13A2 genes in Chinese patients with autosomal recessive early-onset Parkinsonism
    • Guo J. F., Xiao B., Liao B. et al. (2008) Mutation analysis of Parkin, PINK1, DJ-1 and ATP13A2 genes in Chinese patients with autosomal recessive early-onset Parkinsonism. Mov. Disord. 23, 2074 2079.
    • (2008) Mov. Disord. , vol.23 , pp. 2074-2079
    • Guo, J.F.1    Xiao, B.2    Liao, B.3
  • 22
    • 33745280651 scopus 로고    scopus 로고
    • Biochemical analysis of Parkinson's disease-causing variants of Parkin, an E3 ubiquitin-protein ligase with monoubiquitylation capacity
    • Hampe C., Ardila-Osorio H., Fournier M., Brice A. Corti O. (2006) Biochemical analysis of Parkinson's disease-causing variants of Parkin, an E3 ubiquitin-protein ligase with monoubiquitylation capacity. Hum. Mol. Genet. 13, 2059 2075.
    • (2006) Hum. Mol. Genet. , vol.13 , pp. 2059-2075
    • Hampe, C.1    Ardila-Osorio, H.2    Fournier, M.3    Brice, A.4    Corti, O.5
  • 23
    • 7244261867 scopus 로고    scopus 로고
    • Distribution, type, and origin of Parkin mutations: Review and case studies
    • Hedrich K., Eskelson C., Wilmot B. et al. (2004) Distribution, type, and origin of Parkin mutations: review and case studies. Mov. Disord. 19, 1146 1157.
    • (2004) Mov. Disord. , vol.19 , pp. 1146-1157
    • Hedrich, K.1    Eskelson, C.2    Wilmot, B.3
  • 24
    • 33847191686 scopus 로고    scopus 로고
    • Parkin mediates neuroprotection through activation of IkappaB kinase/nuclear factor-kappaB signaling
    • Henn I. H., Bouman L., Schlehe J. S. et al. (2007) Parkin mediates neuroprotection through activation of IkappaB kinase/nuclear factor-kappaB signaling. J. Neurosci. 27, 1868 1878.
    • (2007) J. Neurosci. , vol.27 , pp. 1868-1878
    • Henn, I.H.1    Bouman, L.2    Schlehe, J.S.3
  • 25
    • 0141995596 scopus 로고    scopus 로고
    • The autosomal recessive juvenile Parkinson disease gene product, parkin, interacts with and ubiquitinates synaptotagmin XI
    • Huynh D. P., Scoles D. R., Nguyen D. Pulst S. M. (2003) The autosomal recessive juvenile Parkinson disease gene product, parkin, interacts with and ubiquitinates synaptotagmin XI. Hum. Mol. Genet. 12, 2587 2597.
    • (2003) Hum. Mol. Genet. , vol.12 , pp. 2587-2597
    • Huynh, D.P.1    Scoles, D.R.2    Nguyen, D.3    Pulst, S.M.4
  • 26
    • 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. (2000) Parkin suppresses unfolded protein stress-induced cell death through its E3 ubiquitin-protein ligase activity. J. Biol. Chem. 275, 35661 35664.
    • (2000) J. Biol. Chem. , vol.275 , pp. 35661-35664
    • Imai, Y.1    Soda, M.2    Takahashi, R.3
  • 27
    • 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. (2001) An unfolded putative transmembrane polypeptide, which can lead to endoplasmic reticulum stress, is a substrate of Parkin. Cell 105, 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
  • 28
    • 10744221310 scopus 로고    scopus 로고
    • Parkin gene inactivation alters behaviour and dopamine neurotransmission in the mouse
    • Itier J. M., Ibanez P., Mena M. A. et al. (2003) Parkin gene inactivation alters behaviour and dopamine neurotransmission in the mouse. Hum. Mol. Genet. 12, 2277 2291.
    • (2003) Hum. Mol. Genet. , vol.12 , pp. 2277-2291
    • Itier, J.M.1    Ibanez, P.2    Mena, M.A.3
  • 29
    • 0034266806 scopus 로고    scopus 로고
    • RING finger proteins: Mediators of ubiquitin ligase activity
    • Joazeiro C. A. Weissman A. M. (2000) RING finger proteins: mediators of ubiquitin ligase activity. Cell 102, 549 552.
    • (2000) Cell , vol.102 , pp. 549-552
    • Joazeiro, C.A.1    Weissman, A.M.2
  • 30
    • 63349087613 scopus 로고    scopus 로고
    • Regulation of DNA repair by parkin
    • Kao S. Y. (2009) Regulation of DNA repair by parkin. Biochem. Biophys. Res. Commun. 382, 321 325.
    • (2009) Biochem. Biophys. Res. Commun. , vol.382 , pp. 321-325
    • Kao, S.Y.1
  • 32
    • 0032818824 scopus 로고    scopus 로고
    • Positional cloning of the autosomal recessive juvenile parkinsonism (AR-JP) gene and its diversity in deletion mutations
    • Kitada T., Asakawa S., Matsumine H., Hattori N., Minoshima S., Shimizu N. Mizuno Y. (1999) Positional cloning of the autosomal recessive juvenile parkinsonism (AR-JP) gene and its diversity in deletion mutations. Parkinsonism Relat Disord 5, 163 168.
    • (1999) Parkinsonism Relat Disord , vol.5 , pp. 163-168
    • Kitada, T.1    Asakawa, S.2    Matsumine, H.3    Hattori, N.4    Minoshima, S.5    Shimizu, N.6    Mizuno, Y.7
  • 33
    • 0034044667 scopus 로고    scopus 로고
    • Molecular cloning, gene expression, and identification of a splicing variant of the mouse parkin gene
    • Kitada T., Asakawa S., Minoshima S., Mizuno Y. Shimizu N. (2000) Molecular cloning, gene expression, and identification of a splicing variant of the mouse parkin gene. Mamm. Genome 11, 417 421.
    • (2000) Mamm. Genome , vol.11 , pp. 417-421
    • Kitada, T.1    Asakawa, S.2    Minoshima, S.3    Mizuno, Y.4    Shimizu, N.5
  • 34
    • 33846511271 scopus 로고    scopus 로고
    • Pael receptor induces death of dopaminergic neurons in the substantia nigra via endoplasmic reticulum stress and dopamine toxicity, which is enhanced under condition of parkin inactivation
    • Kitao Y., Imai Y., Ozawa K. et al. (2007) Pael receptor induces death of dopaminergic neurons in the substantia nigra via endoplasmic reticulum stress and dopamine toxicity, which is enhanced under condition of parkin inactivation. Hum. Mol. Genet. 16, 50 60.
    • (2007) Hum. Mol. Genet. , vol.16 , pp. 50-60
    • Kitao, Y.1    Imai, Y.2    Ozawa, K.3
  • 35
    • 24144497601 scopus 로고    scopus 로고
    • Accumulation of the authentic parkin substrate aminoacyl-tRNA synthetase cofactor, p38/JTV-1, leads to catecholaminergic cell death
    • Ko H. S., von Coelln R., Sriram S. R. et al. (2005) Accumulation of the authentic parkin substrate aminoacyl-tRNA synthetase cofactor, p38/JTV-1, leads to catecholaminergic cell death. J. Neurosci. 25, 7968 7978.
    • (2005) J. Neurosci. , vol.25 , pp. 7968-7978
    • Ko, H.S.1    Von Coelln, R.2    Sriram, S.R.3
  • 36
    • 33745220302 scopus 로고    scopus 로고
    • Identification of far up stream element binding protein-1 as an authentic parkin substrate
    • Ko H. S., Kim S. W., Sriram S. R., Dawson V. L. Dawson T. M. (2006) Identification of far up stream element binding protein-1 as an authentic parkin substrate. J. Biol. Chem. 281, 16193 16196.
    • (2006) J. Biol. Chem. , vol.281 , pp. 16193-16196
    • Ko, H.S.1    Kim, S.W.2    Sriram, S.R.3    Dawson, V.L.4    Dawson, T.M.5
  • 39
    • 65649118144 scopus 로고    scopus 로고
    • Protein degradation in Parkinson disease revisited: It's complex
    • Li H. Guo M. (2009) Protein degradation in Parkinson disease revisited: it's complex. J. Clin. Invest. 119, 442 445.
    • (2009) J. Clin. Invest. , vol.119 , pp. 442-445
    • Li, H.1    Guo, M.2
  • 40
    • 20044386298 scopus 로고    scopus 로고
    • Parkin mediates nonclassical, proteasomal-independent ubiquitination of synphilin-1: Implications for Lewy body formation
    • Lim K. L., Chew K. C., Tan J. M. et al. (2005) Parkin mediates nonclassical, proteasomal-independent ubiquitination of synphilin-1: implications for Lewy body formation. J. Neurosci. 25, 2002 2009.
    • (2005) J. Neurosci. , vol.25 , pp. 2002-2009
    • Lim, K.L.1    Chew, K.C.2    Tan, J.M.3
  • 41
    • 0342368772 scopus 로고    scopus 로고
    • Association between early-onset Parkinson's disease and mutations in the parkin gene. French Parkinson's Disease Genetics Study Group
    • Lucking C. B., Durr A., Bonifati V. et al. (2000) Association between early-onset Parkinson's disease and mutations in the parkin gene. French Parkinson's Disease Genetics Study Group. N. Engl. J. Med. 342, 1560 1567.
    • (2000) N. Engl. J. Med. , vol.342 , pp. 1560-1567
    • Lucking, C.B.1    Durr, A.2    Bonifati, V.3
  • 42
    • 61649104022 scopus 로고    scopus 로고
    • Genotypic and phenotypic characteristics of Dutch patients with early onset Parkinson's disease
    • Macedo M. G., Verbaan D., Fang Y. et al. (2009) Genotypic and phenotypic characteristics of Dutch patients with early onset Parkinson's disease. Mov. Disord. 24, 196 203.
    • (2009) Mov. Disord. , vol.24 , pp. 196-203
    • MacEdo, M.G.1    Verbaan, D.2    Fang, Y.3
  • 43
    • 3142675793 scopus 로고    scopus 로고
    • Parkin and relatives: The RBR family of ubiquitin ligases
    • Marin I., Lucas J. I., Gradilla A. C. Ferrus A. (2004) Parkin and relatives: the RBR family of ubiquitin ligases. Physiol. Genomics 17, 253 263.
    • (2004) Physiol. Genomics , vol.17 , pp. 253-263
    • Marin, I.1    Lucas, J.I.2    Gradilla, A.C.3    Ferrus, A.4
  • 44
    • 1842455356 scopus 로고    scopus 로고
    • Parkin genetics: One model for Parkinson's disease
    • Mata I. F., Lockhart P. J. Farrer M. J. (2004) Parkin genetics: one model for Parkinson's disease. Hum. Mol. Genet. 13 (Spec No 1 R127 R133.
    • (2004) Hum. Mol. Genet. , vol.13 , Issue.SPEC NO. 1
    • Mata, I.F.1    Lockhart, P.J.2    Farrer, M.J.3
  • 45
    • 43549116100 scopus 로고    scopus 로고
    • Parkin mediates the degradation-independent ubiquitination of Hsp70
    • Moore D. J., West A. B., Dikeman D. A., Dawson V. L. Dawson T. M. (2008) Parkin mediates the degradation-independent ubiquitination of Hsp70. J. Neurochem. 105, 1806 1819.
    • (2008) J. Neurochem. , vol.105 , pp. 1806-1819
    • Moore, D.J.1    West, A.B.2    Dikeman, D.A.3    Dawson, V.L.4    Dawson, T.M.5
  • 46
    • 0033151716 scopus 로고    scopus 로고
    • A novel transactivation domain in parkin
    • Morett E. Bork P. (1999) A novel transactivation domain in parkin. Trends Biochem. Sci. 24, 229 231.
    • (1999) Trends Biochem. Sci. , vol.24 , pp. 229-231
    • Morett, E.1    Bork, P.2
  • 49
    • 10744224951 scopus 로고    scopus 로고
    • Novel monoclonal antibodies demonstrate biochemical variation of brain parkin with age
    • Pawlyk A. C., Giasson B. I., Sampathu D. M. et al. (2003) Novel monoclonal antibodies demonstrate biochemical variation of brain parkin with age. J. Biol. Chem. 278, 48120 48128.
    • (2003) J. Biol. Chem. , vol.278 , pp. 48120-48128
    • Pawlyk, A.C.1    Giasson, B.I.2    Sampathu, D.M.3
  • 50
    • 13844313915 scopus 로고    scopus 로고
    • Parkin-deficient mice are not a robust model of parkinsonism
    • Perez F. A. Palmiter R. D. (2005) Parkin-deficient mice are not a robust model of parkinsonism. Proc. Natl Acad. Sci. USA 102, 2174 2179.
    • (2005) Proc. Natl Acad. Sci. USA , vol.102 , pp. 2174-2179
    • Perez, F.A.1    Palmiter, R.D.2
  • 51
    • 30344450813 scopus 로고    scopus 로고
    • Parkin-deficient mice are not more sensitive to 6-hydroxydopamine or methamphetamine neurotoxicity
    • Perez F. A., Curtis W. R. Palmiter R. D. (2005) Parkin-deficient mice are not more sensitive to 6-hydroxydopamine or methamphetamine neurotoxicity. BMC Neurosci. 6, 71.
    • (2005) BMC Neurosci. , vol.6 , pp. 71
    • Perez, F.A.1    Curtis, W.R.2    Palmiter, R.D.3
  • 52
    • 0037648357 scopus 로고    scopus 로고
    • Parkin mutations are frequent in patients with isolated early-onset parkinsonism
    • Periquet M., Latouche M., Lohmann E. et al. (2003) Parkin mutations are frequent in patients with isolated early-onset parkinsonism. Brain 126, 1271 1278.
    • (2003) Brain , vol.126 , pp. 1271-1278
    • Periquet, M.1    Latouche, M.2    Lohmann, E.3
  • 54
    • 0034834665 scopus 로고    scopus 로고
    • E3 ubiquitin-protein ligase activity of Parkin is dependent on cooperative interaction of RING finger (TRIAD) elements
    • Rankin C. A., Joazeiro C. A., Floor E. Hunter T. (2001) E3 ubiquitin-protein ligase activity of Parkin is dependent on cooperative interaction of RING finger (TRIAD) elements. J. Biomed. Sci. 8, 421 429.
    • (2001) J. Biomed. Sci. , vol.8 , pp. 421-429
    • Rankin, C.A.1    Joazeiro, C.A.2    Floor, E.3    Hunter, T.4
  • 55
    • 0037738525 scopus 로고    scopus 로고
    • Parkin binds to alpha/beta tubulin and increases their ubiquitination and degradation
    • Ren Y., Zhao J. Feng J. (2003) Parkin binds to alpha/beta tubulin and increases their ubiquitination and degradation. J. Neurosci. 23, 3316 3324.
    • (2003) J. Neurosci. , vol.23 , pp. 3316-3324
    • Ren, Y.1    Zhao, J.2    Feng, J.3
  • 56
    • 33750480508 scopus 로고    scopus 로고
    • Decline of striatal dopamine release in parkin-deficient mice shown by ex vivo autoradiography
    • Sato S., Chiba T., Nishiyama S. et al. (2006) Decline of striatal dopamine release in parkin-deficient mice shown by ex vivo autoradiography. J. Neurosci. Res. 84, 1350 1357.
    • (2006) J. Neurosci. Res. , vol.84 , pp. 1350-1357
    • Sato, S.1    Chiba, T.2    Nishiyama, S.3
  • 57
    • 0033933048 scopus 로고    scopus 로고
    • Familial Parkinson disease gene product, parkin, is a ubiquitin-protein ligase
    • Shimura H., Hattori N., Kubo S. et al. (2000) Familial Parkinson disease gene product, parkin, is a ubiquitin-protein ligase. Nat. Genet. 25, 302 305.
    • (2000) Nat. Genet. , vol.25 , pp. 302-305
    • Shimura, H.1    Hattori, N.2    Kubo, S.3
  • 59
    • 24144470504 scopus 로고    scopus 로고
    • Familial-associated mutations differentially disrupt the solubility, localization, binding and ubiquitination properties of parkin
    • Sriram S. R., Li X., Ko H. S., Chung K. K., Wong E., Lim K. L., Dawson V. L. Dawson T. M. (2005) Familial-associated mutations differentially disrupt the solubility, localization, binding and ubiquitination properties of parkin. Hum. Mol. Genet. 14, 2571 2586.
    • (2005) Hum. Mol. Genet. , vol.14 , pp. 2571-2586
    • Sriram, S.R.1    Li, X.2    Ko, H.S.3    Chung, K.K.4    Wong, E.5    Lim, K.L.6    Dawson, V.L.7    Dawson, T.M.8
  • 60
    • 0037422010 scopus 로고    scopus 로고
    • Parkin is a component of an SCF-like ubiquitin ligase complex and protects postmitotic neurons from kainate excitotoxicity
    • Staropoli J. F., McDermott C., Martinat C., Schulman B., Demireva E. Abeliovich A. (2003) Parkin is a component of an SCF-like ubiquitin ligase complex and protects postmitotic neurons from kainate excitotoxicity. Neuron 37, 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
  • 61
    • 33745091901 scopus 로고    scopus 로고
    • Influence of heterozygosity for parkin mutation on onset age in familial Parkinson disease: The GenePD study
    • Sun M., Latourelle J. C., Wooten G. F. et al. (2006) Influence of heterozygosity for parkin mutation on onset age in familial Parkinson disease: the GenePD study. Arch. Neurol. 63, 826 832.
    • (2006) Arch. Neurol. , vol.63 , pp. 826-832
    • Sun, M.1    Latourelle, J.C.2    Wooten, G.F.3
  • 62
    • 34447289622 scopus 로고    scopus 로고
    • Pathogenic mutations in Parkinson disease
    • Tan E. K. Skipper L. M. (2007) Pathogenic mutations in Parkinson disease. Hum. Mutat. 28, 641 653.
    • (2007) Hum. Mutat. , vol.28 , pp. 641-653
    • Tan, E.K.1    Skipper, L.M.2
  • 64
    • 34147171101 scopus 로고    scopus 로고
    • MPTP and DSP-4 susceptibility of substantia nigra and locus coeruleus catecholaminergic neurons in mice is independent of parkin activity
    • Thomas B., von Coelln R., Mandir A. S. et al. (2007) MPTP and DSP-4 susceptibility of substantia nigra and locus coeruleus catecholaminergic neurons in mice is independent of parkin activity. Neurobiol. Dis. 26, 312 322.
    • (2007) Neurobiol. Dis. , vol.26 , pp. 312-322
    • Thomas, B.1    Von Coelln, R.2    Mandir, A.S.3
  • 65
    • 33645640622 scopus 로고    scopus 로고
    • Parkin ubiquitinates and promotes the degradation of RanBP2
    • Um J. W., Min D. S., Rhim H., Kim J., Paik S. R. Chung K. C. (2006) Parkin ubiquitinates and promotes the degradation of RanBP2. J. Biol. Chem. 281, 3595 3603.
    • (2006) J. Biol. Chem. , vol.281 , pp. 3595-3603
    • Um, J.W.1    Min, D.S.2    Rhim, H.3    Kim, J.4    Paik, S.R.5    Chung, K.C.6
  • 66
    • 30044434872 scopus 로고    scopus 로고
    • Similar patterns of mitochondrial vulnerability and rescue induced by genetic modification of alpha-synuclein, parkin, and DJ-1 in Caenorhabditis elegans
    • Ved R., Saha S., Westlund B. et al. (2005) Similar patterns of mitochondrial vulnerability and rescue induced by genetic modification of alpha-synuclein, parkin, and DJ-1 in Caenorhabditis elegans. J. Biol. Chem. 280, 42655 42668.
    • (2005) J. Biol. Chem. , vol.280 , pp. 42655-42668
    • Ved, R.1    Saha, S.2    Westlund, B.3
  • 67
    • 29644448325 scopus 로고    scopus 로고
    • Stress-induced alterations in parkin solubility promote parkin aggregation and compromise parkin's protective function
    • Wang C., Ko H. S., Thomas B. et al. (2005a) Stress-induced alterations in parkin solubility promote parkin aggregation and compromise parkin's protective function. Hum. Mol. Genet. 14, 3885 3897.
    • (2005) Hum. Mol. Genet. , vol.14 , pp. 3885-3897
    • Wang, C.1    Ko, H.S.2    Thomas, B.3
  • 68
    • 20244370595 scopus 로고    scopus 로고
    • Alterations in the solubility and intracellular localization of parkin by several familial Parkinson's disease-linked point mutations
    • Wang C., Tan J. M., Ho M. W. et al. (2005b) Alterations in the solubility and intracellular localization of parkin by several familial Parkinson's disease-linked point mutations. J. Neurochem. 93, 422 431.
    • (2005) J. Neurochem. , vol.93 , pp. 422-431
    • Wang, C.1    Tan, J.M.2    Ho, M.W.3
  • 69
    • 0344875488 scopus 로고    scopus 로고
    • Inactivation of parkin by oxidative stress and C-terminal truncations: A protective role of molecular chaperones
    • Winklhofer K. F., Henn I. H., Kay-Jackson P. C., Heller U. Tatzelt J. (2003) Inactivation of parkin by oxidative stress and C-terminal truncations: a protective role of molecular chaperones. J. Biol. Chem. 278, 47199 47208.
    • (2003) J. Biol. Chem. , vol.278 , pp. 47199-47208
    • Winklhofer, K.F.1    Henn, I.H.2    Kay-Jackson, P.C.3    Heller, U.4    Tatzelt, J.5
  • 71
    • 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. (2000) Parkin functions as an E2-dependent ubiquitin- protein ligase and promotes the degradation of the synaptic vesicle-associated protein, CDCrel-1. Proc. Natl Acad. Sci. USA 97, 13354 13359.
    • (2000) Proc. Natl Acad. Sci. 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


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.