The chaperone activity of α-synuclein: Utilizing deletion mutants to map its interaction with target proteins

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dc.contributor.authorRekas, Agata
dc.contributor.authorAhn, Keun Jae
dc.contributor.authorKim, Jongsun
dc.contributor.authorCarver, John
dc.date.accessioned2015-12-10T23:09:11Z
dc.date.issued2012
dc.date.updated2016-02-24T10:45:53Z
dc.description.abstractα-Synuclein is the principal component of the Lewy body deposits that are characteristic of Parkinson's disease. In vivo, and under physiological conditions in vitro, α-synuclein aggregates to form amyloid fibrils, a process that is likely to be associa
dc.identifier.issn1097-0134
dc.identifier.urihttp://hdl.handle.net/1885/63371
dc.publisherJohn Wiley & Sons Inc
dc.sourceProteins
dc.subjectKeywords: alpha synuclein; amyloid; chaperone; thioflavine; amino terminal sequence; article; beta sheet; binding site; carboxy terminal sequence; circular dichroism; correlation analysis; light scattering; mutational analysis; priority journal; protein aggregation Aggregation; Amyloid fibril; Binding site; Circular dichroism; Dynamic light scattering; Parkinson's disease; Thioflavin T
dc.titleThe chaperone activity of α-synuclein: Utilizing deletion mutants to map its interaction with target proteins
dc.typeJournal article
local.bibliographicCitation.issue5
local.bibliographicCitation.lastpage1325
local.bibliographicCitation.startpage1316
local.contributor.affiliationRekas, Agata, ANSTO
local.contributor.affiliationAhn, Keun Jae, Yonsei University
local.contributor.affiliationKim, Jongsun, Yonsei University
local.contributor.affiliationCarver, John, College of Physical and Mathematical Sciences, ANU
local.contributor.authoruidCarver, John, u1571001
local.description.embargo2037-12-31
local.description.notesImported from ARIES
local.identifier.absfor030406 - Proteins and Peptides
local.identifier.absseo970103 - Expanding Knowledge in the Chemical Sciences
local.identifier.ariespublicationU4217927xPUB798
local.identifier.citationvolume80
local.identifier.doi10.1002/prot.24028
local.identifier.scopusID2-s2.0-84862811649
local.identifier.thomsonID000302541900006
local.type.statusPublished Version

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