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Volumn 287, Issue 39, 2012, Pages 32630-32639

Identification of protein interfaces between α-synuclein, the principal component of Lewy bodies in Parkinson disease, and the molecular chaperones human Hsc70 and the yeast Ssa1p

Author keywords

[No Author keywords available]

Indexed keywords

BINDING DOMAIN; CENTRAL NERVOUS SYSTEMS; CROSSLINKER; HEAT SHOCK PROTEIN 70; IDENTIFICATION OF PROTEINS; LEWY BODIES; MOLECULAR CHAPERONES; PARKINSON DISEASE; PHYSICOCHEMICAL PROPERTY; PRINCIPAL COMPONENTS; SURFACE INTERFACES; SYNUCLEIN; THERAPEUTIC AGENTS; THERAPEUTIC PROPERTIES;

EID: 84866556269     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M112.387530     Document Type: Article
Times cited : (36)

References (40)
  • 1
    • 0036777847 scopus 로고    scopus 로고
    • Synergistic effects of pesticides and metals on the fibrillation of α-synuclein: Implications for Parkinson's disease
    • DOI 10.1016/S0161-813X(02)00067-0, PII S0161813X02000670
    • Uversky, V. N., Li, J., Bower, K., and Fink, A. L. (2002) Synergistic effects of pesticides and metals on the fibrillation of α-synuclein: Implications for Parkinson disease. Neurotoxicology 23, 527-536 (Pubitemid 36527673)
    • (2002) NeuroToxicology , vol.23 , Issue.4-5 , pp. 527-536
    • Uversky, V.N.1    Li, J.2    Bower, K.3    Fink, A.L.4
  • 2
    • 38949091068 scopus 로고    scopus 로고
    • Gene-environment interactions in Parkinson disease
    • Ross, C. A., and Smith W. W. (2007) Gene-environment interactions in Parkinson disease Parkinsonism. Relat. Disord. 13, S309-15
    • (2007) Parkinsonism. Relat. Disord. , vol.13
    • Ross, C.A.1    Smith, W.W.2
  • 7
    • 0037333666 scopus 로고    scopus 로고
    • Staging of brain pathology related to sporadic Parkinson's disease
    • DOI 10.1016/S0197-4580(02)00065-9, PII S0197458002000659
    • Braak, H., Del Tredici, K., Rüb, U., de Vos, R. A., Jansen Steur, E. N., and Braak, E. (2003) Staging of brain pathology related to sporadic Parkinson disease. Neurobiol. Aging 24, 197-211 (Pubitemid 36007810)
    • (2003) Neurobiology of Aging , vol.24 , Issue.2 , pp. 197-211
    • Braak, H.1    Del, T.K.2    Rub, U.3    De Vos, R.A.I.4    Jansen, S.E.N.H.5    Braak, E.6
  • 8
    • 77949848854 scopus 로고    scopus 로고
    • Prion-like transmission of protein aggregates in neurodegenerative diseases
    • Brundin, P., Melki, R., and Kopito, R. (2010) Prion-like transmission of protein aggregates in neurodegenerative diseases. Nat. Rev. Mol. Cell Biol. 11, 301-307
    • (2010) Nat. Rev. Mol. Cell Biol. , vol.11 , pp. 301-307
    • Brundin, P.1    Melki, R.2    Kopito, R.3
  • 9
    • 84862701723 scopus 로고    scopus 로고
    • Fibrillar α-synuclein and huntingtin exon 1 assemblies are toxic to the cells
    • Pieri, L., Madiona, K., Bousset, L., and Melki, R. (2012) Fibrillar α-synuclein and huntingtin exon 1 assemblies are toxic to the cells. Biophys. J. 102, 2894-2905
    • (2012) Biophys. J. , vol.102 , pp. 2894-2905
    • Pieri, L.1    Madiona, K.2    Bousset, L.3    Melki, R.4
  • 11
    • 66849143696 scopus 로고    scopus 로고
    • Converging concepts of protein folding in vitro and in vivo
    • Hartl, F. U., and Hayer-Hartl, M. (2009) Converging concepts of protein folding in vitro and in vivo. Nat. Struct. Mol. Biol. 16, 574-581
    • (2009) Nat. Struct. Mol. Biol. , vol.16 , pp. 574-581
    • Hartl, F.U.1    Hayer-Hartl, M.2
  • 12
    • 56749117866 scopus 로고    scopus 로고
    • Interactions between Hsp70 and the hydrophobic core of α-synuclein inhibit fibril assembly
    • Luk, K. C., Mills, I. P., Trojanowski, J. Q., and Lee, V. M. (2008) Interactions between Hsp70 and the hydrophobic core of α-synuclein inhibit fibril assembly. Biochemistry 47, 12614-12625
    • (2008) Biochemistry , vol.47 , pp. 12614-12625
    • Luk, K.C.1    Mills, I.P.2    Trojanowski, J.Q.3    Lee, V.M.4
  • 13
    • 79251565507 scopus 로고    scopus 로고
    • Heat-shock protein 70 modulates toxic extracellular α-synuclein oligomers and rescues trans-synaptic toxicity
    • Danzer, K. M., Ruf, W. P., Putcha, P., Joyner, D., Hashimoto, T., Glabe, C., Hyman, B. T., and McLean, P. J. (2011) Heat-shock protein 70 modulates toxic extracellular α-synuclein oligomers and rescues trans-synaptic toxicity. FASEB J. 25, 326-336
    • (2011) FASEB J. , vol.25 , pp. 326-336
    • Danzer, K.M.1    Ruf, W.P.2    Putcha, P.3    Joyner, D.4    Hashimoto, T.5    Glabe, C.6    Hyman, B.T.7    McLean, P.J.8
  • 14
    • 17644383748 scopus 로고    scopus 로고
    • Heat shock protein 70 inhibits α-synuclein fibril formation via preferential binding to prefibrillar species
    • DOI 10.1074/jbc.M413024200
    • Dedmon, M. M., Christodoulou, J., Wilson, M. R., and Dobson, C. M. (2005) Heat shock protein 70 inhibits α-synuclein fibril formation via preferential binding to prefibrillar species. J. Biol. Chem. 280, 14733-14740 (Pubitemid 40562821)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.15 , pp. 14733-14740
    • Dedmon, M.M.1    Christodoulou, J.2    Wilson, M.R.3    Dobson, C.M.4
  • 15
    • 33750873994 scopus 로고    scopus 로고
    • Heat Shock Protein 70 Inhibits α-Synuclein Fibril Formation via Interactions with Diverse Intermediates
    • DOI 10.1016/j.jmb.2006.08.062, PII S0022283606011156
    • Huang, C., Cheng, H., Hao, S., Zhou, H., Zhang, X., Gao, J., Sun Q. H., Hu, H., and Wang, C. C. (2006) Heat shock protein 70 inhibits α-synuclein fibril formation via interactions with diverse intermediates. J. Mol. Biol. 364, 323-336 (Pubitemid 44717537)
    • (2006) Journal of Molecular Biology , vol.364 , Issue.3 , pp. 323-336
    • Huang, C.1    Cheng, H.2    Hao, S.3    Zhou, H.4    Zhang, X.5    Gao, J.6    Sun, Q.-H.7    Hu, H.8    Wang, C.-c.9
  • 17
    • 78649346692 scopus 로고    scopus 로고
    • The heat shock response: Life on the verge of death
    • Richter, K., Haslbeck, M., and Buchner, J. (2010) The heat shock response: Life on the verge of death. Mol. Cell. 40, 253-266
    • (2010) Mol. Cell. , vol.40 , pp. 253-266
    • Richter, K.1    Haslbeck, M.2    Buchner, J.3
  • 20
    • 84872430627 scopus 로고    scopus 로고
    • The interaction of Hsc70 protein with fibrillar α-synuclein and its therapeutic potential in Parkinson disease
    • Pemberton, S., and Melki, R. (2012) The interaction of Hsc70 protein with fibrillar α-synuclein and its therapeutic potential in Parkinson disease. Commun. Integr. Biol. 5, 94-95
    • (2012) Commun. Integr. Biol. , vol.5 , pp. 94-95
    • Pemberton, S.1    Melki, R.2
  • 21
    • 75149142186 scopus 로고    scopus 로고
    • Hsp70 molecular chaperones and Parkinson disease
    • Witt, S. N. (2010) Hsp70 molecular chaperones and Parkinson disease. Biopolymers 93, 218-228
    • (2010) Biopolymers , vol.93 , pp. 218-228
    • Witt, S.N.1
  • 22
    • 0014681836 scopus 로고
    • Autoimmunity in patients treated with levodopa
    • Cotzias, G. C., and Papavasiliou, P. S. (1969) Autoimmunity in patients treated with levodopa. JAMA 207, 1353-1354
    • (1969) JAMA , vol.207 , pp. 1353-1354
    • Cotzias, G.C.1    Papavasiliou, P.S.2
  • 23
  • 24
    • 0015910273 scopus 로고
    • Autoimmune hemolytic anemia due to levodopa therapy
    • Territo, M. C., Peters, R. W., and Tanaka, K. R. (1973) Autoimmune hemolytic anemia due to levodopa therapy. JAMA 226, 1347-1348
    • (1973) JAMA , vol.226 , pp. 1347-1348
    • Territo, M.C.1    Peters, R.W.2    Tanaka, K.R.3
  • 25
    • 0017309671 scopus 로고
    • Thrombocytopenia associated with long term levodopa therapy
    • Wanamaker, W. M., Wanamaker, S. J., Celesia, G. G., and Koeller, A. A. (1976) Thrombocytopenia associated with long term levodopa therapy. JAMA 235, 2217-2219
    • (1976) JAMA , vol.235 , pp. 2217-2219
    • Wanamaker, W.M.1    Wanamaker, S.J.2    Celesia, G.G.3    Koeller, A.A.4
  • 26
    • 23844531539 scopus 로고    scopus 로고
    • PA700, the regulatory complex of the 26S proteasome, interferes with α-synuclein assembly
    • DOI 10.1111/j.1742-4658.2005.04776.x
    • Ghee, M., Melki, R., Michot, N., and Mallet, J. (2005) PA700, the regulatory complex of the 26 S proteasome, interferes with α-synuclein assembly. FEBS J. 272, 4023-4033 (Pubitemid 41160911)
    • (2005) FEBS Journal , vol.272 , Issue.16 , pp. 4023-4033
    • Ghee, M.1    Melki, R.2    Michot, N.3    Mallet, J.4
  • 27
    • 0033785942 scopus 로고    scopus 로고
    • Mutation of the ATP-binding pocket of SSA1 indicates that a functional interaction between Ssa1p and Ydj1p is required for post-translational translocation into the yeast endoplasmic reticulum
    • McClellan, A. J., and Brodsky, J. L. (2000) Mutation of the ATP-binding pocket of SSA1 indicates that a functional interaction between Ssa1p and Ydj1p is required for post-translational translocation into the yeast endoplasmic reticulum. Genetics 156, 501-512
    • (2000) Genetics , vol.156 , pp. 501-512
    • McClellan, A.J.1    Brodsky, J.L.2
  • 28
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M. M. (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72, 248-254
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 29
    • 0025146397 scopus 로고
    • Direct evidence for GTP and GDP-P(i) intermediates in microtubule assembly
    • Melki, R., Carlier, M. F., Pantaloni, D. (1990) Direct evidence for GTP and GDP-Pi intermediates in microtubule assembly. Biochemistry 29, 8921-8932 (Pubitemid 20311966)
    • (1990) Biochemistry , vol.29 , Issue.38 , pp. 8921-8932
    • Melki, R.1    Carlier, M.-F.2    Pantaloni, D.3
  • 30
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. K. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227, 680-685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 31
    • 78649991956 scopus 로고    scopus 로고
    • A region within the C-terminal domain of Ure2p is shown to interact with the molecular chaperone Ssa1p by the use of cross-linkers and mass spectrometry
    • Redeker, V., Bonnefoy, J., Le Caer, J. P., Pemberton, S., Laprévote O., and Melki, R. (2010) A region within the C-terminal domain of Ure2p is shown to interact with the molecular chaperone Ssa1p by the use of cross-linkers and mass spectrometry. FEBS J. 277, 5112-5123
    • (2010) FEBS J. , vol.277 , pp. 5112-5123
    • Redeker, V.1    Bonnefoy, J.2    Le Caer, J.P.3    Pemberton, S.4    Laprévote, O.5    Melki, R.6
  • 32
    • 33646264529 scopus 로고    scopus 로고
    • Advances in proteomics data analysis and display using an accurate mass and time tag approach
    • Zimmer, J. S., Monroe, M. E., Qian, W. J., Smith, R. D. (2006) Advances in proteomics data analysis and display using an accurate mass and time tag approach. Mass Spectrom. Rev. 25, 450-482
    • (2006) Mass Spectrom. Rev. , vol.25 , pp. 450-482
    • Zimmer, J.S.1    Monroe, M.E.2    Qian, W.J.3    Smith, R.D.4
  • 33
    • 0035514030 scopus 로고    scopus 로고
    • GPMAW - A software tool for analyzing proteins and peptides
    • Peri, S., Steen, H., and Pandey, A. (2001) GPMAW - a software tool for analyzing proteins and peptides. Trends Biochem. Sci. 26, 687-689
    • (2001) Trends Biochem. Sci. , vol.26 , pp. 687-689
    • Peri, S.1    Steen, H.2    Pandey, A.3
  • 35
    • 66249146087 scopus 로고    scopus 로고
    • Chemical cross-linking with NHS esters: A systematic study on amino acid reactivities
    • Mädler, S., Bich, C., Touboul, D., Zenobi, R. (2009) Chemical cross-linking with NHS esters: A systematic study on amino acid reactivities. J. Mass Spectrom. 44, 694-706
    • (2009) J. Mass Spectrom. , vol.44 , pp. 694-706
    • Mädler, S.1    Bich, C.2    Touboul, D.3    Zenobi, R.4
  • 36
    • 33748328052 scopus 로고    scopus 로고
    • Protein cross-linking analysis using mass spectrometry, isotope-coded cross-linkers, and integrated computational data processing
    • DOI 10.1021/pr060154z
    • Seebacher, J., Mallick, P., Zhang, N., Eddes, J. S., Aebersold, R., and Gelb, M. H. (2006) Protein cross-linking analysis using mass spectrometry, isotope-coded cross-linkers, and integrated computational data processing. J. Proteome Res. 5, 2270-2282 (Pubitemid 44330820)
    • (2006) Journal of Proteome Research , vol.5 , Issue.9 , pp. 2270-2282
    • Seebacher, J.1    Mallick, P.2    Zhang, N.3    Eddes, J.S.4    Aebersold, R.5    Gelb, M.H.6


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