The two-faced nature of milk casein proteins: amyloid fibril formation and chaperone-like activity

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dc.contributor.authorThorn, Davic C.
dc.contributor.authorEcroyd, Heath
dc.contributor.authorCarver, John
dc.date.accessioned2015-12-07T22:25:13Z
dc.date.issued2009
dc.date.updated2015-12-07T09:33:32Z
dc.description.abstractMolecular chaperones are a diverse group of proteins that stabilise partially folded target proteins to prevent their misfolding, aggregation and potential precipitation under conditions of cellular stress, e.g. elevated temperature. Protein aggregation,
dc.identifier.issn0004-9433
dc.identifier.urihttp://hdl.handle.net/1885/21165
dc.publisherDairy Industry Association of Australia
dc.sourceAustralian Journal of Dairy Technology
dc.titleThe two-faced nature of milk casein proteins: amyloid fibril formation and chaperone-like activity
dc.typeJournal article
local.bibliographicCitation.issue1
local.bibliographicCitation.lastpage40
local.bibliographicCitation.startpage34
local.contributor.affiliationThorn, Davic C., University of Adelaide
local.contributor.affiliationEcroyd, Heath, The University of Adelaide
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.ariespublicationu8801298xPUB15
local.identifier.citationvolume64
local.identifier.scopusID2-s2.0-63749124891
local.identifier.thomsonID000264662700010
local.type.statusPublished Version

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