{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Fauvet B"],"funding":["NIA NIH HHS"],"pagination":["15345-64"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC3346117"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["287(19)"],"pubmed_abstract":["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 whethe"],"journal":["The Journal of biological chemistry"],"pubmed_title":["α-Synuclein in central nervous system and from erythrocytes, mammalian cells, and Escherichia coli exists predominantly as disordered monomer."],"pmcid":["PMC3346117"],"funding_grant_id":["AG019391","R01 AG019391","R37 AG019391","R37 AG018440"],"pubmed_authors":["Michael S","Mbefo MK","Lion N","Tsika E","El-Agnaf OM","Fauvet B","Moore DJ","Fares MB","Prudent M","Ardah MT","Aebischer P","Lashuel HA","Eliezer D","Schneider B","Desobry C","Masliah E","Coune P"],"additional_accession":[]},"is_claimable":false,"name":"α-Synuclein in central nervous system and from erythrocytes, mammalian cells, and Escherichia coli exists predominantly as disordered monomer.","description":"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 whethe","dates":{"release":"2012-01-01T00:00:00Z","publication":"2012 May","modification":"2026-05-03T07:34:43.018Z","creation":"2019-03-27T00:53:10Z"},"accession":"S-EPMC3346117","cross_references":{"pubmed":["22315227"],"doi":["10.1074/jbc.m111.318949","10.1074/jbc.M111.318949"]}}