메뉴 건너뛰기




Volumn 12, Issue 11, 2006, Pages 521-528

Understanding the molecular causes of Parkinson's disease

Author keywords

[No Author keywords available]

Indexed keywords

ALPHA SYNUCLEIN; LEUCIN RICH REPEAT KINASE 2; PARKIN; PTEN INDUCED PUTATIVE KINASE 1; UNCLASSIFIED DRUG;

EID: 33750370804     PISSN: 14714914     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.molmed.2006.09.007     Document Type: Review
Times cited : (264)

References (90)
  • 1
    • 0030744876 scopus 로고    scopus 로고
    • Mutation in the α-synuclein gene identified in families with Parkinson's disease
    • Polymeropoulos M.H., et al. Mutation in the α-synuclein gene identified in families with Parkinson's disease. Science 276 (1997) 2045-2047
    • (1997) Science , vol.276 , pp. 2045-2047
    • Polymeropoulos, M.H.1
  • 2
    • 22244442489 scopus 로고    scopus 로고
    • The biochemistry of Parkinson's disease
    • Cookson M.R. The biochemistry of Parkinson's disease. Annu. Rev. Biochem. 74 (2005) 29-52
    • (2005) Annu. Rev. Biochem. , vol.74 , pp. 29-52
    • Cookson, M.R.1
  • 3
    • 10744227740 scopus 로고    scopus 로고
    • Comparison of kindreds with parkinsonism and α-synuclein genomic multiplications
    • Farrer M., et al. Comparison of kindreds with parkinsonism and α-synuclein genomic multiplications. Ann. Neurol. 55 (2004) 174-179
    • (2004) Ann. Neurol. , vol.55 , pp. 174-179
    • Farrer, M.1
  • 4
    • 32044453611 scopus 로고    scopus 로고
    • Clinical heterogeneity of α-synuclein gene duplication in Parkinson's disease
    • Nishioka K., et al. Clinical heterogeneity of α-synuclein gene duplication in Parkinson's disease. Ann. Neurol. 59 (2006) 298-309
    • (2006) Ann. Neurol. , vol.59 , pp. 298-309
    • Nishioka, K.1
  • 5
    • 0242300619 scopus 로고    scopus 로고
    • α-Synuclein locus triplication causes Parkinson's disease
    • Singleton A.B., et al. α-Synuclein locus triplication causes Parkinson's disease. Science 302 (2003) 841
    • (2003) Science , vol.302 , pp. 841
    • Singleton, A.B.1
  • 6
    • 33746869343 scopus 로고    scopus 로고
    • Collaborative analysis of α-synuclein gene promoter variability and Parkinson disease
    • Maraganore D.M., et al. Collaborative analysis of α-synuclein gene promoter variability and Parkinson disease. JAMA 296 (2006) 661-670
    • (2006) JAMA , vol.296 , pp. 661-670
    • Maraganore, D.M.1
  • 7
    • 0028985267 scopus 로고
    • The precursor protein of non-A β component of Alzheimer's disease amyloid is a presynaptic protein of the central nervous system
    • Iwai A., et al. The precursor protein of non-A β component of Alzheimer's disease amyloid is a presynaptic protein of the central nervous system. Neuron 14 (1995) 467-475
    • (1995) Neuron , vol.14 , pp. 467-475
    • Iwai, A.1
  • 8
    • 0028277520 scopus 로고
    • Identification of two distinct synucleins from human brain
    • Jakes R., et al. Identification of two distinct synucleins from human brain. FEBS Lett. 345 (1994) 27-32
    • (1994) FEBS Lett. , vol.345 , pp. 27-32
    • Jakes, R.1
  • 9
    • 0036315240 scopus 로고    scopus 로고
    • Demonstration of α-synuclein immunoreactivity in neuronal and glial cytoplasm in normal human brain tissue using proteinase K and formic acid pretreatment
    • Mori F., et al. Demonstration of α-synuclein immunoreactivity in neuronal and glial cytoplasm in normal human brain tissue using proteinase K and formic acid pretreatment. Exp. Neurol. 176 (2002) 98-104
    • (2002) Exp. Neurol. , vol.176 , pp. 98-104
    • Mori, F.1
  • 10
    • 0036884733 scopus 로고    scopus 로고
    • Pathogenesis of Parkinson's disease: dopamine, vesicles and α-synuclein
    • Lotharius J., and Brundin P. Pathogenesis of Parkinson's disease: dopamine, vesicles and α-synuclein. Nat. Rev. Neurosci. 3 (2002) 932-942
    • (2002) Nat. Rev. Neurosci. , vol.3 , pp. 932-942
    • Lotharius, J.1    Brundin, P.2
  • 11
    • 14944348552 scopus 로고    scopus 로고
    • The role of (-synuclein in both neuroprotection and neurodegeneration
    • Sidhu A., et al. The role of (-synuclein in both neuroprotection and neurodegeneration. Ann. N. Y. Acad. Sci. 1035 (2004) 250-270
    • (2004) Ann. N. Y. Acad. Sci. , vol.1035 , pp. 250-270
    • Sidhu, A.1
  • 12
    • 0034077041 scopus 로고    scopus 로고
    • Mice lacking α-synuclein display functional deficits in the nigrostriatal dopamine system
    • Abeliovich A., et al. Mice lacking α-synuclein display functional deficits in the nigrostriatal dopamine system. Neuron 25 (2000) 239-252
    • (2000) Neuron , vol.25 , pp. 239-252
    • Abeliovich, A.1
  • 13
    • 0037109727 scopus 로고    scopus 로고
    • Synaptic vesicle depletion correlates with attenuated synaptic responses to prolonged repetitive stimulation in mice lacking α-synuclein
    • Cabin D.E., et al. Synaptic vesicle depletion correlates with attenuated synaptic responses to prolonged repetitive stimulation in mice lacking α-synuclein. J. Neurosci. 22 (2002) 8797-8807
    • (2002) J. Neurosci. , vol.22 , pp. 8797-8807
    • Cabin, D.E.1
  • 14
    • 6944227811 scopus 로고    scopus 로고
    • Double-knockout mice for α- and β-synucleins: effect on synaptic functions
    • Chandra S., et al. Double-knockout mice for α- and β-synucleins: effect on synaptic functions. Proc. Natl. Acad. Sci. U. S. A. 101 (2004) 14966-14971
    • (2004) Proc. Natl. Acad. Sci. U. S. A. , vol.101 , pp. 14966-14971
    • Chandra, S.1
  • 15
    • 5144234034 scopus 로고    scopus 로고
    • Alpha-synuclein and transgenic mouse models
    • Fernagut P.O., and Chesselet M.F. Alpha-synuclein and transgenic mouse models. Neurobiol. Dis. 17 (2004) 123-130
    • (2004) Neurobiol. Dis. , vol.17 , pp. 123-130
    • Fernagut, P.O.1    Chesselet, M.F.2
  • 16
    • 0037155197 scopus 로고    scopus 로고
    • Lipid droplet binding and oligomerization properties of the Parkinson's disease protein α-synuclein
    • Cole N.B., et al. Lipid droplet binding and oligomerization properties of the Parkinson's disease protein α-synuclein. J. Biol. Chem. 277 (2002) 6344-6352
    • (2002) J. Biol. Chem. , vol.277 , pp. 6344-6352
    • Cole, N.B.1
  • 17
    • 0345189364 scopus 로고    scopus 로고
    • Yeast cells provide insight into α-synuclein biology and pathobiology
    • Outeiro T.F., and Lindquist S. Yeast cells provide insight into α-synuclein biology and pathobiology. Science 302 (2003) 1772-1775
    • (2003) Science , vol.302 , pp. 1772-1775
    • Outeiro, T.F.1    Lindquist, S.2
  • 18
    • 15244347219 scopus 로고    scopus 로고
    • Helix periodicity, topology, and dynamics of membrane-associated α-synuclein
    • Bussell Jr. R., et al. Helix periodicity, topology, and dynamics of membrane-associated α-synuclein. Protein Sci. 14 (2005) 862-872
    • (2005) Protein Sci. , vol.14 , pp. 862-872
    • Bussell Jr., R.1
  • 19
    • 24744432079 scopus 로고    scopus 로고
    • A combinatorial code for the interaction of α-synuclein with membranes
    • Kubo S., et al. A combinatorial code for the interaction of α-synuclein with membranes. J. Biol. Chem. 280 (2005) 31664-31672
    • (2005) J. Biol. Chem. , vol.280 , pp. 31664-31672
    • Kubo, S.1
  • 20
    • 12144267004 scopus 로고    scopus 로고
    • Fluorescence studies suggest a role for α-synuclein in the phosphatidylinositol lipid signaling pathway
    • Narayanan V., et al. Fluorescence studies suggest a role for α-synuclein in the phosphatidylinositol lipid signaling pathway. Biochemistry 44 (2005) 462-470
    • (2005) Biochemistry , vol.44 , pp. 462-470
    • Narayanan, V.1
  • 21
    • 1642264194 scopus 로고    scopus 로고
    • Structural determinants of PLD2 inhibition by α-synuclein
    • Payton J.E., et al. Structural determinants of PLD2 inhibition by α-synuclein. J. Mol. Biol. 337 (2004) 1001-1009
    • (2004) J. Mol. Biol. , vol.337 , pp. 1001-1009
    • Payton, J.E.1
  • 22
    • 20444362984 scopus 로고    scopus 로고
    • Fatty acid incorporation is decreased in astrocytes cultured from α-synuclein gene-ablated mice
    • Castagnet P.I., et al. Fatty acid incorporation is decreased in astrocytes cultured from α-synuclein gene-ablated mice. J. Neurochem. 94 (2005) 839-849
    • (2005) J. Neurochem. , vol.94 , pp. 839-849
    • Castagnet, P.I.1
  • 23
    • 20444400627 scopus 로고    scopus 로고
    • Alpha-synuclein gene deletion decreases brain palmitate uptake and alters the palmitate metabolism in the absence of α-synuclein palmitate binding
    • Golovko M.Y., et al. Alpha-synuclein gene deletion decreases brain palmitate uptake and alters the palmitate metabolism in the absence of α-synuclein palmitate binding. Biochemistry 44 (2005) 8251-8259
    • (2005) Biochemistry , vol.44 , pp. 8251-8259
    • Golovko, M.Y.1
  • 24
    • 27644578107 scopus 로고    scopus 로고
    • Mitochondrial lipid abnormality and electron transport chain impairment in mice lacking α-synuclein
    • Ellis C.E., et al. Mitochondrial lipid abnormality and electron transport chain impairment in mice lacking α-synuclein. Mol. Cell. Biol. 25 (2005) 10190-10201
    • (2005) Mol. Cell. Biol. , vol.25 , pp. 10190-10201
    • Ellis, C.E.1
  • 25
    • 27544507306 scopus 로고    scopus 로고
    • Alpha-synuclein cooperates with CSPα in preventing neurodegeneration
    • Chandra S., et al. Alpha-synuclein cooperates with CSPα in preventing neurodegeneration. Cell 123 (2005) 383-396
    • (2005) Cell , vol.123 , pp. 383-396
    • Chandra, S.1
  • 26
    • 0030882856 scopus 로고    scopus 로고
    • Alpha-synuclein in Lewy bodies
    • Spillantini M.G., et al. Alpha-synuclein in Lewy bodies. Nature 388 (1997) 839-840
    • (1997) Nature , vol.388 , pp. 839-840
    • Spillantini, M.G.1
  • 27
    • 0034646391 scopus 로고    scopus 로고
    • Fibrils formed in vitro from α-synuclein and two mutant forms linked to Parkinson's disease are typical amyloid
    • Conway K.A., et al. Fibrils formed in vitro from α-synuclein and two mutant forms linked to Parkinson's disease are typical amyloid. Biochemistry 39 (2000) 2552-2563
    • (2000) Biochemistry , vol.39 , pp. 2552-2563
    • Conway, K.A.1
  • 28
    • 0034712918 scopus 로고    scopus 로고
    • Fiber diffraction of synthetic α-synuclein filaments shows amyloid-like cross-β conformation
    • Serpell L.C., et al. Fiber diffraction of synthetic α-synuclein filaments shows amyloid-like cross-β conformation. Proc. Natl. Acad. Sci. U. S. A. 97 (2000) 4897-4902
    • (2000) Proc. Natl. Acad. Sci. U. S. A. , vol.97 , pp. 4897-4902
    • Serpell, L.C.1
  • 29
    • 2442700253 scopus 로고    scopus 로고
    • Alpha-synuclein in blood and brain from familial Parkinson disease with SNCA locus triplication
    • Miller D.W., et al. Alpha-synuclein in blood and brain from familial Parkinson disease with SNCA locus triplication. Neurology 62 (2004) 1835-1838
    • (2004) Neurology , vol.62 , pp. 1835-1838
    • Miller, D.W.1
  • 30
    • 26844527655 scopus 로고    scopus 로고
    • Genetic mouse models of parkinsonism: strengths and limitations
    • Fleming S.M., et al. Genetic mouse models of parkinsonism: strengths and limitations. NeuroRx. 2 (2005) 495-503
    • (2005) NeuroRx. , vol.2 , pp. 495-503
    • Fleming, S.M.1
  • 31
    • 0034704752 scopus 로고    scopus 로고
    • A Drosophila model of Parkinson's disease
    • Feany M.B., and Bender W.W. A Drosophila model of Parkinson's disease. Nature 404 (2000) 394-398
    • (2000) Nature , vol.404 , pp. 394-398
    • Feany, M.B.1    Bender, W.W.2
  • 32
    • 17844406856 scopus 로고    scopus 로고
    • Alpha-synuclein phosphorylation controls neurotoxicity and inclusion formation in a Drosophila model of Parkinson disease
    • Chen L., and Feany M.B. Alpha-synuclein phosphorylation controls neurotoxicity and inclusion formation in a Drosophila model of Parkinson disease. Nat. Neurosci. 8 (2005) 657-663
    • (2005) Nat. Neurosci. , vol.8 , pp. 657-663
    • Chen, L.1    Feany, M.B.2
  • 33
    • 0036174010 scopus 로고    scopus 로고
    • α-Synuclein is phosphorylated in synucleinopathy lesions
    • Fujiwara H., et al. α-Synuclein is phosphorylated in synucleinopathy lesions. Nat. Cell Biol. 4 (2002) 160-164
    • (2002) Nat. Cell Biol. , vol.4 , pp. 160-164
    • Fujiwara, H.1
  • 34
    • 14844335694 scopus 로고    scopus 로고
    • The E46K mutation in α-synuclein increases amyloid fibril formation
    • Greenbaum E.A., et al. The E46K mutation in α-synuclein increases amyloid fibril formation. J. Biol. Chem. 280 (2005) 7800-7807
    • (2005) J. Biol. Chem. , vol.280 , pp. 7800-7807
    • Greenbaum, E.A.1
  • 35
    • 0035800097 scopus 로고    scopus 로고
    • Vesicle permeabilization by protofibrillar α-synuclein: implications for the pathogenesis and treatment of Parkinson's disease
    • Volles M.J., et al. Vesicle permeabilization by protofibrillar α-synuclein: implications for the pathogenesis and treatment of Parkinson's disease. Biochemistry 40 (2001) 7812-7819
    • (2001) Biochemistry , vol.40 , pp. 7812-7819
    • Volles, M.J.1
  • 36
    • 33750284754 scopus 로고    scopus 로고
    • Interaction of α-synuclein and dopamine metabolites in the pathogenesis of Parkinson's disease: a case for the selective vulnerability of the substantia nigra
    • Galvin J.E. Interaction of α-synuclein and dopamine metabolites in the pathogenesis of Parkinson's disease: a case for the selective vulnerability of the substantia nigra. Acta Neuropathol. (Berl.) 112 (2006) 115-126
    • (2006) Acta Neuropathol. (Berl.) , vol.112 , pp. 115-126
    • Galvin, J.E.1
  • 37
    • 0036278335 scopus 로고    scopus 로고
    • Dopamine-dependent neurotoxicity of α-synuclein: a mechanism for selective neurodegeneration in Parkinson disease
    • Xu J., et al. Dopamine-dependent neurotoxicity of α-synuclein: a mechanism for selective neurodegeneration in Parkinson disease. Nat. Med. 8 (2002) 600-606
    • (2002) Nat. Med. , vol.8 , pp. 600-606
    • Xu, J.1
  • 38
    • 0035834360 scopus 로고    scopus 로고
    • Kinetic stabilization of the α-synuclein protofibril by a dopamine-α-synuclein adduct
    • Conway K.A., et al. Kinetic stabilization of the α-synuclein protofibril by a dopamine-α-synuclein adduct. Science 294 (2001) 1346-1349
    • (2001) Science , vol.294 , pp. 1346-1349
    • Conway, K.A.1
  • 39
    • 8844266996 scopus 로고    scopus 로고
    • Cloning of the gene containing mutations that cause PARK8-linked Parkinson's disease
    • Paisan-Ruiz C., et al. Cloning of the gene containing mutations that cause PARK8-linked Parkinson's disease. Neuron 44 (2004) 595-600
    • (2004) Neuron , vol.44 , pp. 595-600
    • Paisan-Ruiz, C.1
  • 40
    • 8844233579 scopus 로고    scopus 로고
    • Mutations in LRRK2 cause autosomal-dominant parkinsonism with pleomorphic pathology
    • Zimprich A., et al. Mutations in LRRK2 cause autosomal-dominant parkinsonism with pleomorphic pathology. Neuron 44 (2004) 601-607
    • (2004) Neuron , vol.44 , pp. 601-607
    • Zimprich, A.1
  • 41
    • 28544441181 scopus 로고    scopus 로고
    • Mutations in the gene LRRK2 encoding dardarin (PARK8) cause familial Parkinson's disease: clinical, pathological, olfactory and functional imaging and genetic data
    • Khan N.L., et al. Mutations in the gene LRRK2 encoding dardarin (PARK8) cause familial Parkinson's disease: clinical, pathological, olfactory and functional imaging and genetic data. Brain 128 (2005) 2786-2796
    • (2005) Brain , vol.128 , pp. 2786-2796
    • Khan, N.L.1
  • 42
    • 16444380313 scopus 로고    scopus 로고
    • LRRK2 mutations and Parkinsonism
    • Albrecht M. LRRK2 mutations and Parkinsonism. Lancet 365 (2005) 1230
    • (2005) Lancet , vol.365 , pp. 1230
    • Albrecht, M.1
  • 43
    • 19944432921 scopus 로고    scopus 로고
    • A common LRRK2 mutation in idiopathic Parkinson's disease
    • Gilks W.P., et al. A common LRRK2 mutation in idiopathic Parkinson's disease. Lancet 365 (2005) 415-416
    • (2005) Lancet , vol.365 , pp. 415-416
    • Gilks, W.P.1
  • 44
    • 31344432937 scopus 로고    scopus 로고
    • LRRK2 G2019S as a cause of Parkinson's disease in North African Arabs
    • Lesage S., et al. LRRK2 G2019S as a cause of Parkinson's disease in North African Arabs. N. Engl. J. Med. 354 (2006) 422-423
    • (2006) N. Engl. J. Med. , vol.354 , pp. 422-423
    • Lesage, S.1
  • 45
    • 31344439221 scopus 로고    scopus 로고
    • LRRK2 G2019S as a cause of Parkinson's disease in Ashkenazi Jews
    • Ozelius L.J., et al. LRRK2 G2019S as a cause of Parkinson's disease in Ashkenazi Jews. N. Engl. J. Med. 354 (2006) 424-425
    • (2006) N. Engl. J. Med. , vol.354 , pp. 424-425
    • Ozelius, L.J.1
  • 46
    • 33645790701 scopus 로고    scopus 로고
    • LRRK2 expression linked to dopamine-innervated areas
    • Galter D., et al. LRRK2 expression linked to dopamine-innervated areas. Ann. Neurol. 59 (2006) 714-719
    • (2006) Ann. Neurol. , vol.59 , pp. 714-719
    • Galter, D.1
  • 47
    • 33646146878 scopus 로고    scopus 로고
    • Anatomical localization of leucine-rich repeat kinase 2 in mouse brain
    • Melrose H., et al. Anatomical localization of leucine-rich repeat kinase 2 in mouse brain. Neuroscience (2006)
    • (2006) Neuroscience
    • Melrose, H.1
  • 48
    • 33644934224 scopus 로고    scopus 로고
    • LRRK2 is expressed in areas affected by Parkinson's disease in the adult mouse brain
    • Simon-Sanchez J., et al. LRRK2 is expressed in areas affected by Parkinson's disease in the adult mouse brain. Eur. J. Neurosci. 23 (2006) 659-666
    • (2006) Eur. J. Neurosci. , vol.23 , pp. 659-666
    • Simon-Sanchez, J.1
  • 49
    • 31144443248 scopus 로고    scopus 로고
    • The Parkinson disease causing LRRK2 mutation I2020T is associated with increased kinase activity
    • Gloeckner C.J., et al. The Parkinson disease causing LRRK2 mutation I2020T is associated with increased kinase activity. Hum. Mol. Genet. 15 (2006) 223-232
    • (2006) Hum. Mol. Genet. , vol.15 , pp. 223-232
    • Gloeckner, C.J.1
  • 50
    • 28044460070 scopus 로고    scopus 로고
    • Parkinson's disease-associated mutations in leucine-rich repeat kinase 2 augment kinase activity
    • West A.B., et al. Parkinson's disease-associated mutations in leucine-rich repeat kinase 2 augment kinase activity. Proc. Natl. Acad. Sci. U. S. A. 102 (2005) 16842-16847
    • (2005) Proc. Natl. Acad. Sci. U. S. A. , vol.102 , pp. 16842-16847
    • West, A.B.1
  • 51
    • 32044432395 scopus 로고    scopus 로고
    • Biochemical and pathological characterization of Lrrk2
    • Giasson B.I., et al. Biochemical and pathological characterization of Lrrk2. Ann. Neurol. 59 (2006) 315-322
    • (2006) Ann. Neurol. , vol.59 , pp. 315-322
    • Giasson, B.I.1
  • 52
    • 33750317653 scopus 로고    scopus 로고
    • LRRK2 protein is a component of lewy bodies
    • Zhu X., et al. LRRK2 protein is a component of lewy bodies. Ann. Neurol. (2006)
    • (2006) Ann. Neurol.
    • Zhu, X.1
  • 53
    • 0032499264 scopus 로고    scopus 로고
    • Mutations in the parkin gene cause autosomal recessive juvenile parkinsonism
    • Kitada T., et al. Mutations in the parkin gene cause autosomal recessive juvenile parkinsonism. Nature 392 (1998) 605-608
    • (1998) Nature , vol.392 , pp. 605-608
    • Kitada, T.1
  • 54
    • 0342368772 scopus 로고    scopus 로고
    • Association between early-onset Parkinson's disease and mutations in the parkin gene
    • Lucking C.B., et al. Association between early-onset Parkinson's disease and mutations in the parkin gene. N. Engl. J. Med. 342 (2000) 1560-1567
    • (2000) N. Engl. J. Med. , vol.342 , pp. 1560-1567
    • Lucking, C.B.1
  • 55
    • 1542285483 scopus 로고    scopus 로고
    • Genetics of parkin-linked disease
    • West A.B., and Maidment N.T. Genetics of parkin-linked disease. Hum. Genet. 114 (2004) 327-336
    • (2004) Hum. Genet. , vol.114 , pp. 327-336
    • West, A.B.1    Maidment, N.T.2
  • 56
    • 24644462201 scopus 로고    scopus 로고
    • Lewy body Parkinson's disease in a large pedigree with 77 Parkin mutation carriers
    • Pramstaller P.P., et al. Lewy body Parkinson's disease in a large pedigree with 77 Parkin mutation carriers. Ann. Neurol. 58 (2005) 411-422
    • (2005) Ann. Neurol. , vol.58 , pp. 411-422
    • Pramstaller, P.P.1
  • 57
    • 5444236802 scopus 로고    scopus 로고
    • Parkin-associated Parkinson's disease
    • von Coelln R., et al. Parkin-associated Parkinson's disease. Cell Tissue Res. 318 (2004) 175-184
    • (2004) Cell Tissue Res. , vol.318 , pp. 175-184
    • von Coelln, R.1
  • 58
    • 0033933048 scopus 로고    scopus 로고
    • Familial Parkinson disease gene product, parkin, is a ubiquitin-protein ligase
    • Shimura H., et al. Familial Parkinson disease gene product, parkin, is a ubiquitin-protein ligase. Nat. Genet. 25 (2000) 302-305
    • (2000) Nat. Genet. , vol.25 , pp. 302-305
    • Shimura, H.1
  • 59
    • 10444241856 scopus 로고    scopus 로고
    • BAG5 inhibits parkin and enhances dopaminergic neuron degeneration
    • Kalia S.K., et al. BAG5 inhibits parkin and enhances dopaminergic neuron degeneration. Neuron 44 (2004) 931-945
    • (2004) Neuron , vol.44 , pp. 931-945
    • Kalia, S.K.1
  • 60
    • 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., et al. Parkin and CASK/LIN-2 associate via a PDZ-mediated interaction and are co-localized in lipid rafts and postsynaptic densities in brain. J. Biol. Chem. 277 (2002) 486-491
    • (2002) J. Biol. Chem. , vol.277 , pp. 486-491
    • Fallon, L.1
  • 61
    • 24144470504 scopus 로고    scopus 로고
    • Familial-associated mutations differentially disrupt the solubility, localization, binding and ubiquitination properties of parkin
    • Sriram S.R., et al. Familial-associated mutations differentially disrupt the solubility, localization, binding and ubiquitination properties of parkin. Hum. Mol. Genet. 14 (2005) 2571-2586
    • (2005) Hum. Mol. Genet. , vol.14 , pp. 2571-2586
    • Sriram, S.R.1
  • 62
    • 0141891953 scopus 로고    scopus 로고
    • Parkin-deficient mice exhibit nigrostriatal deficits but not loss of dopaminergic neurons
    • Goldberg M.S., et al. Parkin-deficient mice exhibit nigrostriatal deficits but not loss of dopaminergic neurons. J. Biol. Chem. 278 (2003) 43628-43635
    • (2003) J. Biol. Chem. , vol.278 , pp. 43628-43635
    • Goldberg, M.S.1
  • 63
    • 10744221310 scopus 로고    scopus 로고
    • Parkin gene inactivation alters behaviour and dopamine neurotransmission in the mouse
    • Itier J.M., et al. Parkin gene inactivation alters behaviour and dopamine neurotransmission in the mouse. Hum. Mol. Genet. 12 (2003) 2277-2291
    • (2003) Hum. Mol. Genet. , vol.12 , pp. 2277-2291
    • Itier, J.M.1
  • 64
    • 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., et al. Accumulation of the authentic parkin substrate aminoacyl-tRNA synthetase cofactor, p38/JTV-1, leads to catecholaminergic cell death. J. Neurosci. 25 (2005) 7968-7978
    • (2005) J. Neurosci. , vol.25 , pp. 7968-7978
    • Ko, H.S.1
  • 65
    • 2442481789 scopus 로고    scopus 로고
    • Mitochondrial dysfunction and oxidative damage in parkin-deficient mice
    • Palacino J.J., et al. Mitochondrial dysfunction and oxidative damage in parkin-deficient mice. J. Biol. Chem. 279 (2004) 18614-18622
    • (2004) J. Biol. Chem. , vol.279 , pp. 18614-18622
    • Palacino, J.J.1
  • 66
    • 0037386532 scopus 로고    scopus 로고
    • Mitochondrial pathology and apoptotic muscle degeneration in Drosophila parkin mutants
    • Greene J.C., et al. Mitochondrial pathology and apoptotic muscle degeneration in Drosophila parkin mutants. Proc. Natl. Acad. Sci. U. S. A. 100 (2003) 4078-4083
    • (2003) Proc. Natl. Acad. Sci. U. S. A. , vol.100 , pp. 4078-4083
    • Greene, J.C.1
  • 67
    • 2542560342 scopus 로고    scopus 로고
    • Drosophila parkin mutants have decreased mass and cell size and increased sensitivity to oxygen radical stress
    • Pesah Y., et al. Drosophila parkin mutants have decreased mass and cell size and increased sensitivity to oxygen radical stress. Development 131 (2004) 2183-2194
    • (2004) Development , vol.131 , pp. 2183-2194
    • Pesah, Y.1
  • 68
    • 33644778845 scopus 로고    scopus 로고
    • Parkin enhances mitochondrial biogenesis in proliferating cells
    • Kuroda Y., et al. Parkin enhances mitochondrial biogenesis in proliferating cells. Hum. Mol. Genet. 15 (2006) 883-895
    • (2006) Hum. Mol. Genet. , vol.15 , pp. 883-895
    • Kuroda, Y.1
  • 69
    • 2542534741 scopus 로고    scopus 로고
    • S-nitrosylation of parkin regulates ubiquitination and compromises parkin's protective function
    • Chung K.K., et al. S-nitrosylation of parkin regulates ubiquitination and compromises parkin's protective function. Science 304 (2004) 1328-1331
    • (2004) Science , vol.304 , pp. 1328-1331
    • Chung, K.K.1
  • 70
    • 0344875488 scopus 로고    scopus 로고
    • Inactivation of parkin by oxidative stress and C-terminal truncations: a protective role of molecular chaperones
    • Winklhofer K.F., et al. Inactivation of parkin by oxidative stress and C-terminal truncations: a protective role of molecular chaperones. J. Biol. Chem. 278 (2003) 47199-47208
    • (2003) J. Biol. Chem. , vol.278 , pp. 47199-47208
    • Winklhofer, K.F.1
  • 71
    • 3242733689 scopus 로고    scopus 로고
    • Nitrosative stress linked to sporadic Parkinson's disease: S-nitrosylation of parkin regulates its E3 ubiquitin ligase activity
    • 101, 10810-10814
    • Yao D., et al. Nitrosative stress linked to sporadic Parkinson's disease: S-nitrosylation of parkin regulates its E3 ubiquitin ligase activity. Proc. Natl. Acad. Sci. U. S. A. 20 (2004) 101, 10810-10814
    • (2004) Proc. Natl. Acad. Sci. U. S. A. , vol.20
    • Yao, D.1
  • 72
    • 30744443484 scopus 로고    scopus 로고
    • Dopamine covalently modifies and functionally inactivates parkin
    • LaVoie M.J., et al. Dopamine covalently modifies and functionally inactivates parkin. Nat. Med. 11 (2005) 1214-1221
    • (2005) Nat. Med. , vol.11 , pp. 1214-1221
    • LaVoie, M.J.1
  • 73
    • 4444237208 scopus 로고    scopus 로고
    • Novel PINK1 mutations in early-onset parkinsonism
    • Hatano Y., et al. Novel PINK1 mutations in early-onset parkinsonism. Ann. Neurol. 56 (2004) 424-427
    • (2004) Ann. Neurol. , vol.56 , pp. 424-427
    • Hatano, Y.1
  • 74
    • 2442668926 scopus 로고    scopus 로고
    • Hereditary early-onset Parkinson's disease caused by mutations in PINK1
    • Valente E.M., et al. Hereditary early-onset Parkinson's disease caused by mutations in PINK1. Science 304 (2004) 1158-1160
    • (2004) Science , vol.304 , pp. 1158-1160
    • Valente, E.M.1
  • 75
    • 33644610520 scopus 로고    scopus 로고
    • The genetics of Parkinson disease: implications for neurological care
    • Klein C., and Schlossmacher M.G. The genetics of Parkinson disease: implications for neurological care. Nat. Clin. Pract. Neurol. 2 (2006) 136-146
    • (2006) Nat. Clin. Pract. Neurol. , vol.2 , pp. 136-146
    • Klein, C.1    Schlossmacher, M.G.2
  • 76
    • 27944444154 scopus 로고    scopus 로고
    • Mitochondrial import and enzymatic activity of PINK1 mutants associated to recessive parkinsonism
    • Silvestri L., et al. Mitochondrial import and enzymatic activity of PINK1 mutants associated to recessive parkinsonism. Hum. Mol. Genet. 14 (2005) 3477-3492
    • (2005) Hum. Mol. Genet. , vol.14 , pp. 3477-3492
    • Silvestri, L.1
  • 77
    • 33750598457 scopus 로고    scopus 로고
    • Abou-Sleiman, P. M. et al. (2006) A heterozygous effect for PINK1 mutations in Parkinson's disease? Ann. Neurol. (in press)
  • 78
    • 17644365438 scopus 로고    scopus 로고
    • Mutations in PTEN-induced putative kinase 1 associated with recessive parkinsonism have differential effects on protein stability
    • Beilina A., et al. Mutations in PTEN-induced putative kinase 1 associated with recessive parkinsonism have differential effects on protein stability. Proc. Natl. Acad. Sci. U. S. A. 102 (2005) 5703-5708
    • (2005) Proc. Natl. Acad. Sci. U. S. A. , vol.102 , pp. 5703-5708
    • Beilina, A.1
  • 79
    • 33745087689 scopus 로고    scopus 로고
    • PINK1 protein in normal human brain and Parkinson's disease
    • Gandhi S., et al. PINK1 protein in normal human brain and Parkinson's disease. Brain 129 (2006) 1720-1731
    • (2006) Brain , vol.129 , pp. 1720-1731
    • Gandhi, S.1
  • 80
    • 26644440926 scopus 로고    scopus 로고
    • Wild-type PINK1 prevents basal and induced neuronal apoptosis, a protective effect abrogated by Parkinson disease-related mutations
    • Petit A., et al. Wild-type PINK1 prevents basal and induced neuronal apoptosis, a protective effect abrogated by Parkinson disease-related mutations. J. Biol. Chem. 280 (2005) 34025-34032
    • (2005) J. Biol. Chem. , vol.280 , pp. 34025-34032
    • Petit, A.1
  • 81
    • 33745589773 scopus 로고    scopus 로고
    • Drosophila pink1 is required for mitochondrial function and interacts genetically with parkin
    • Clark I.E., et al. Drosophila pink1 is required for mitochondrial function and interacts genetically with parkin. Nature 441 (2006) 1162-1166
    • (2006) Nature , vol.441 , pp. 1162-1166
    • Clark, I.E.1
  • 82
    • 33745602748 scopus 로고    scopus 로고
    • Mitochondrial dysfunction in Drosophila PINK1 mutants is complemented by parkin
    • Park J., et al. Mitochondrial dysfunction in Drosophila PINK1 mutants is complemented by parkin. Nature 441 (2006) 1157-1161
    • (2006) Nature , vol.441 , pp. 1157-1161
    • Park, J.1
  • 83
    • 1642379155 scopus 로고    scopus 로고
    • Linking DJ-1 to neurodegeneration offers novel insights for understanding the pathogenesis of Parkinson's disease
    • Bonifati V., et al. Linking DJ-1 to neurodegeneration offers novel insights for understanding the pathogenesis of Parkinson's disease. J. Mol. Med. 82 (2004) 163-174
    • (2004) J. Mol. Med. , vol.82 , pp. 163-174
    • Bonifati, V.1
  • 84
    • 24944534660 scopus 로고    scopus 로고
    • Mitochondrial localization of the Parkinson's disease related protein DJ-1: implications for pathogenesis
    • Zhang L., et al. Mitochondrial localization of the Parkinson's disease related protein DJ-1: implications for pathogenesis. Hum. Mol. Genet. 14 (2005) 2063-2073
    • (2005) Hum. Mol. Genet. , vol.14 , pp. 2063-2073
    • Zhang, L.1
  • 85
    • 31344464179 scopus 로고    scopus 로고
    • The oxidation state of DJ-1 regulates its chaperone activity toward α-synuclein
    • Zhou W., et al. The oxidation state of DJ-1 regulates its chaperone activity toward α-synuclein. J. Mol. Biol. 356 (2006) 1036-1048
    • (2006) J. Mol. Biol. , vol.356 , pp. 1036-1048
    • Zhou, W.1
  • 86
    • 33646826619 scopus 로고    scopus 로고
    • Oxidative damage of DJ-1 is linked to sporadic Parkinson and Alzheimer diseases
    • Choi J., et al. Oxidative damage of DJ-1 is linked to sporadic Parkinson and Alzheimer diseases. J. Biol. Chem. 281 (2006) 10816-10824
    • (2006) J. Biol. Chem. , vol.281 , pp. 10816-10824
    • Choi, J.1
  • 87
    • 13844253723 scopus 로고    scopus 로고
    • Nigrostriatal dopaminergic deficits and hypokinesia caused by inactivation of the familial Parkinsonism-linked gene DJ-1
    • Goldberg M.S., et al. Nigrostriatal dopaminergic deficits and hypokinesia caused by inactivation of the familial Parkinsonism-linked gene DJ-1. Neuron 45 (2005) 489-496
    • (2005) Neuron , vol.45 , pp. 489-496
    • Goldberg, M.S.1
  • 88
    • 26444489693 scopus 로고    scopus 로고
    • Inactivation of Drosophila DJ-1 leads to impairments of oxidative stress response and phosphatidylinositol 3-kinase/Akt signalling
    • 102, 13670-13675
    • Yang Y., et al. Inactivation of Drosophila DJ-1 leads to impairments of oxidative stress response and phosphatidylinositol 3-kinase/Akt signalling. Proc. Natl. Acad. Sci. U. S. A. 20 (2005) 102, 13670-13675
    • (2005) Proc. Natl. Acad. Sci. U. S. A. , vol.20
    • Yang, Y.1
  • 89
    • 25144433763 scopus 로고    scopus 로고
    • Dopaminergic function in a family with the PARK6 form of autosomal recessive Parkinson's syndrome
    • Kessler K.R., et al. Dopaminergic function in a family with the PARK6 form of autosomal recessive Parkinson's syndrome. J. Neural. Transm. 112 (2005) 1345-1353
    • (2005) J. Neural. Transm. , vol.112 , pp. 1345-1353
    • Kessler, K.R.1
  • 90
    • 11444265305 scopus 로고    scopus 로고
    • Dopaminergic dysfunction in unrelated, asymptomatic carriers of a single parkin mutation
    • Khan N.L., et al. Dopaminergic dysfunction in unrelated, asymptomatic carriers of a single parkin mutation. Neurology 64 (2005) 134-136
    • (2005) Neurology , vol.64 , pp. 134-136
    • Khan, N.L.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.