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http://purl.uniprot.org/citations/22315227http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/22315227http://www.w3.org/2000/01/rdf-schema#comment"Since the discovery and isolation of α-synuclein (α-syn) from human brains, it has been widely accepted that it exists as an intrinsically disordered monomeric protein. Two recent studies suggested that α-syn produced in Escherichia coli or isolated from mammalian cells and red blood cells exists predominantly as a tetramer that is rich in α-helical structure (Bartels, T., Choi, J. G., and Selkoe, D. J. (2011) Nature 477, 107-110; Wang, W., Perovic, I., Chittuluru, J., Kaganovich, A., Nguyen, L. T. T., Liao, J., Auclair, J. R., Johnson, D., Landeru, A., Simorellis, A. K., Ju, S., Cookson, M. R., Asturias, F. J., Agar, J. N., Webb, B. N., Kang, C., Ringe, D., Petsko, G. A., Pochapsky, T. C., and Hoang, Q. Q. (2011) Proc. Natl. Acad. Sci. 108, 17797-17802). However, it remains unknown whether or not this putative tetramer is the main physiological form of α-syn in the brain. In this study, we investigated the oligomeric state of α-syn in mouse, rat, and human brains. To assess the conformational and oligomeric state of native α-syn in complex mixtures, we generated α-syn standards of known quaternary structure and conformational properties and compared the behavior of endogenously expressed α-syn to these standards using native and denaturing gel electrophoresis techniques, size-exclusion chromatography, and an oligomer-specific ELISA. Our findings demonstrate that both human and rodent α-syn expressed in the central nervous system exist predominantly as an unfolded monomer. Similar results were observed when human α-syn was expressed in mouse and rat brains as well as mammalian cell lines (HEK293, HeLa, and SH-SY5Y). Furthermore, we show that α-syn expressed in E. coli and purified under denaturing or nondenaturing conditions, whether as a free protein or as a fusion construct with GST, is monomeric and adopts a disordered conformation after GST removal. These results do not rule out the possibility that α-syn becomes structured upon interaction with other proteins and/or biological membranes."xsd:string
http://purl.uniprot.org/citations/22315227http://purl.org/dc/terms/identifier"doi:10.1074/jbc.m111.318949"xsd:string
http://purl.uniprot.org/citations/22315227http://purl.uniprot.org/core/author"Masliah E."xsd:string
http://purl.uniprot.org/citations/22315227http://purl.uniprot.org/core/author"Michael S."xsd:string
http://purl.uniprot.org/citations/22315227http://purl.uniprot.org/core/author"Schneider B."xsd:string
http://purl.uniprot.org/citations/22315227http://purl.uniprot.org/core/author"Moore D.J."xsd:string
http://purl.uniprot.org/citations/22315227http://purl.uniprot.org/core/author"Tsika E."xsd:string
http://purl.uniprot.org/citations/22315227http://purl.uniprot.org/core/author"Mbefo M.K."xsd:string
http://purl.uniprot.org/citations/22315227http://purl.uniprot.org/core/author"Eliezer D."xsd:string
http://purl.uniprot.org/citations/22315227http://purl.uniprot.org/core/author"Lashuel H.A."xsd:string
http://purl.uniprot.org/citations/22315227http://purl.uniprot.org/core/author"Fauvet B."xsd:string
http://purl.uniprot.org/citations/22315227http://purl.uniprot.org/core/author"Aebischer P."xsd:string
http://purl.uniprot.org/citations/22315227http://purl.uniprot.org/core/author"El-Agnaf O.M."xsd:string
http://purl.uniprot.org/citations/22315227http://purl.uniprot.org/core/author"Ardah M.T."xsd:string
http://purl.uniprot.org/citations/22315227http://purl.uniprot.org/core/author"Coune P."xsd:string
http://purl.uniprot.org/citations/22315227http://purl.uniprot.org/core/author"Desobry C."xsd:string
http://purl.uniprot.org/citations/22315227http://purl.uniprot.org/core/author"Fares M.B."xsd:string
http://purl.uniprot.org/citations/22315227http://purl.uniprot.org/core/author"Lion N."xsd:string
http://purl.uniprot.org/citations/22315227http://purl.uniprot.org/core/author"Prudent M."xsd:string
http://purl.uniprot.org/citations/22315227http://purl.uniprot.org/core/date"2012"xsd:gYear
http://purl.uniprot.org/citations/22315227http://purl.uniprot.org/core/name"J Biol Chem"xsd:string
http://purl.uniprot.org/citations/22315227http://purl.uniprot.org/core/pages"15345-15364"xsd:string
http://purl.uniprot.org/citations/22315227http://purl.uniprot.org/core/title"alpha-Synuclein in central nervous system and from erythrocytes, mammalian cells, and Escherichia coli exists predominantly as disordered monomer."xsd:string
http://purl.uniprot.org/citations/22315227http://purl.uniprot.org/core/volume"287"xsd:string
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