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