Interactive sequences in the molecular chaperone, human alphaB crystallin modulate the fibrillation of amyloidogenic proteins.
about
Human small heat shock proteins: protein interactomes of homo- and hetero-oligomeric complexes: an updateCrystal structures of truncated alphaA and alphaB crystallins reveal structural mechanisms of polydispersity important for eye lens functionIn vivo substrates of the lens molecular chaperones αA-crystallin and αB-crystallinLens proteomics: analysis of rat crystallins when lenses are exposed to dexamethasone.Anti-chaperone betaA3/A1(102-117) peptide interacting sites in human alphaB-crystallinMultiple sites in αB-crystallin modulate its interactions with desmin filaments assembled in vitro.Interaction of amyloid inhibitor proteins with amyloid beta peptides: insight from molecular dynamics simulationsLens aging: effects of crystallins.beta(2)-microglobulin: from physiology to amyloidosis.Molecular chaperones and associated cellular clearance mechanisms against toxic protein conformers in Parkinson's disease.Protein interactomes of three stress inducible small heat shock proteins: HspB1, HspB5 and HspB8.HspB1, HspB5 and HspB4 in Human Cancers: Potent Oncogenic Role of Some of Their Client Proteins.αB-crystallin (HspB5) in familial amyloidotic polyneuropathy.Truncation of alphaB-crystallin by the myopathy-causing Q151X mutation significantly destabilizes the protein leading to aggregate formation in transfected cells.C-terminal interactions mediate the quaternary dynamics of αB-crystallin.Self-assembly of protein aggregates in ageing disorders: the lens and cataract model.The effect of nanoparticles on amyloid aggregation depends on the protein stability and intrinsic aggregation rate.Functional Amyloid Protection in the Eye Lens: Retention of α-Crystallin Molecular Chaperone Activity after Modification into Amyloid Fibrils.The taming of small heat-shock proteins: crystallization of the alpha-crystallin domain from human Hsp27.Effect of αB-crystallin on protein aggregation in Drosophila.
P2860
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P2860
Interactive sequences in the molecular chaperone, human alphaB crystallin modulate the fibrillation of amyloidogenic proteins.
description
2007 nî lūn-bûn
@nan
2007年の論文
@ja
2007年学术文章
@wuu
2007年学术文章
@zh-cn
2007年学术文章
@zh-hans
2007年学术文章
@zh-my
2007年学术文章
@zh-sg
2007年學術文章
@yue
2007年學術文章
@zh
2007年學術文章
@zh-hant
name
Interactive sequences in the m ...... ion of amyloidogenic proteins.
@en
Interactive sequences in the m ...... ion of amyloidogenic proteins.
@nl
type
label
Interactive sequences in the m ...... ion of amyloidogenic proteins.
@en
Interactive sequences in the m ...... ion of amyloidogenic proteins.
@nl
prefLabel
Interactive sequences in the m ...... ion of amyloidogenic proteins.
@en
Interactive sequences in the m ...... ion of amyloidogenic proteins.
@nl
P2093
P2860
P1476
Interactive sequences in the m ...... ion of amyloidogenic proteins.
@en
P2093
John I Clark
Joy G Ghosh
Scott A Houck
P2860
P304
P356
10.1016/J.BIOCEL.2007.10.035
P577
2007-11-13T00:00:00Z