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Dissociation from the Oligomeric State Is the Rate-limiting Step in Fibril Formation by K-Casein

Ecroyd, Heath; Koudelka, Tomas; Thorn, Davic C.; Williams, Danielle M.; Devlin, Glyn; Hoffmann, Peter; Carver, John

Description

Amyloid fibrils are aggregated and precipitated forms of protein in which the protein exists in highly ordered, long, unbranching threadlike formations that are stable and resistant to degradation by proteases. Fibril formation is an ordered process that

dc.contributor.authorEcroyd, Heath
dc.contributor.authorKoudelka, Tomas
dc.contributor.authorThorn, Davic C.
dc.contributor.authorWilliams, Danielle M.
dc.contributor.authorDevlin, Glyn
dc.contributor.authorHoffmann, Peter
dc.contributor.authorCarver, John
dc.date.accessioned2015-12-10T23:08:07Z
dc.identifier.issn0021-9258
dc.identifier.urihttp://hdl.handle.net/1885/63151
dc.description.abstractAmyloid fibrils are aggregated and precipitated forms of protein in which the protein exists in highly ordered, long, unbranching threadlike formations that are stable and resistant to degradation by proteases. Fibril formation is an ordered process that
dc.publisherAmerican Society for Biochemistry and Molecular Biology Inc
dc.sourceJournal of Biological Chemistry
dc.subjectKeywords: Agglomeration; Casein; Dissociation; Glycoproteins; High performance liquid chromatography; Mass spectrometry; Nucleation; Self assembled monolayers; Steelmaking; Turbidity; Aggregation mechanisms; Amyloid fibrils; Fibril formations; Fluorescence intensit
dc.titleDissociation from the Oligomeric State Is the Rate-limiting Step in Fibril Formation by K-Casein
dc.typeJournal article
local.description.notesImported from ARIES
local.identifier.citationvolume283
dc.date.issued2008
local.identifier.absfor030406 - Proteins and Peptides
local.identifier.ariespublicationU4217927xPUB775
local.type.statusPublished Version
local.contributor.affiliationEcroyd, Heath, The University of Adelaide
local.contributor.affiliationKoudelka, Tomas, University of Adelaide
local.contributor.affiliationThorn, Davic C., University of Adelaide
local.contributor.affiliationWilliams, Danielle M., University of Adelaide
local.contributor.affiliationDevlin, Glyn, University of Cambridge
local.contributor.affiliationHoffmann, Peter, University of Cambridge
local.contributor.affiliationCarver, John, College of Physical and Mathematical Sciences, ANU
local.description.embargo2037-12-31
local.bibliographicCitation.issue14
local.bibliographicCitation.startpage9012
local.bibliographicCitation.lastpage9022
local.identifier.doi10.1074/jbc.M709928200
local.identifier.absseo970103 - Expanding Knowledge in the Chemical Sciences
dc.date.updated2015-12-10T09:04:48Z
local.identifier.scopusID2-s2.0-44049105911
local.identifier.thomsonID000254465800031
CollectionsANU Research Publications

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