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Crystallin proteins and amyloid fibrils

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dc.contributor.authorEcroyd, Heath
dc.contributor.authorCarver, John
dc.date.accessioned2015-12-10T23:08:36Z
dc.date.issued2009
dc.date.updated2016-02-24T10:45:21Z
dc.description.abstractImproper protein folding (misfolding) can lead to the formation of disordered (amorphous) or ordered (amyloid fibril) aggregates. The major lens protein, α-crystallin, is a member of the small heat-shock protein (sHsp) family of intracellular molecular c
dc.identifier.issn1420-682X
dc.identifier.urihttp://hdl.handle.net/1885/63182
dc.publisherBirkhauser Verlag
dc.sourceCellular and Molecular Life Sciences
dc.subjectKeywords: alpha crystallin; alpha synuclein; amyloid; amyloid beta protein[25-35]; beta crystallin; biomaterial; chaperone; gamma crystallin; heat shock protein 20; heat shock protein 25; heat shock protein 27; small heat shock protein; Alzheimer disease; amino aci Alzheimer's disease; Amyloid fibril; Cataract; Crystallin; Lens; Molecular chaperone; Parkinson's disease; Protein aggregation; Protein folding; Small heat-shock protein
dc.titleCrystallin proteins and amyloid fibrils
dc.typeJournal article
local.bibliographicCitation.issue1
local.bibliographicCitation.lastpage81
local.bibliographicCitation.startpage62
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.ariespublicationU4217927xPUB778
local.identifier.citationvolume66
local.identifier.doi10.1007/s00018-008-8327-4
local.identifier.scopusID2-s2.0-58149506229
local.identifier.thomsonID000262433100005
local.type.statusPublished Version

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