Binding of the molecular chaperone αB-crystallin to Aβ amyloid fibrils inhibits fibril elongation
about
Fibrillogenic propensity of the GroEL apical domain: a Janus-faced minichaperoneN-terminal domain of Pyrococcus furiosus l-asparaginase functions as a non-specific, stable, molecular chaperoneHuman small heat shock proteins: protein interactomes of homo- and hetero-oligomeric complexes: an updateThe structured core domain of B-crystallin can prevent amyloid fibrillation and associated toxicityInteraction of the molecular chaperone DNAJB6 with growing amyloid-beta 42 (Aβ42) aggregates leads to sub-stoichiometric inhibition of amyloid formationAmyloid-β oligomers are sequestered by both intracellular and extracellular chaperonesThe extracellular chaperone clusterin sequesters oligomeric forms of the amyloid-β(1-40) peptideSingle molecule characterization of the interactions between amyloid-β peptides and the membranes of hippocampal cells.Probing small molecule binding to amyloid fibrils.Amyloid fibrils composed of hexameric peptides attenuate neuroinflammation.Interaction of amyloid inhibitor proteins with amyloid beta peptides: insight from molecular dynamics simulationsRescue of αB Crystallin (HSPB5) Mutants Associated Protein Aggregation by Co-Expression of HSPB5 PartnersOligomers of Heat-Shock Proteins: Structures That Don't Imply Function.NMNAT2:HSP90 Complex Mediates Proteostasis in Proteinopathies.Fluorescent filter-trap assay for amyloid fibril formation kinetics in complex solutions.Small heat shock proteins and α-crystallins: dynamic proteins with flexible functions.Novel roles for α-crystallins in retinal function and disease.Chaperone activity of small heat shock proteins underlies therapeutic efficacy in experimental autoimmune encephalomyelitis.Crystallins and neuroinflammation: The glial side of the story.The small heat shock proteins αB-crystallin and Hsp27 suppress SOD1 aggregation in vitro.Co-fibrillogenesis of Wild-type and D76N β2-Microglobulin: THE CRUCIAL ROLE OF FIBRILLAR SEEDS.Monitoring the interaction between β2-microglobulin and the molecular chaperone αB-crystallin by NMR and mass spectrometry: αB-crystallin dissociates β2-microglobulin oligomers.Physical activity delays hippocampal neurodegeneration and rescues memory deficits in an Alzheimer disease mouse modelAmyloid fiber formation in human γD-Crystallin induced by UV-B photodamageIdentification of proteins that interact with alpha A-crystallin using a human proteome microarray.A novel function for proSAAS as an amyloid anti-aggregant in Alzheimer's disease.Protein Quality Control by Molecular Chaperones in Neurodegeneration.Protein interactomes of three stress inducible small heat shock proteins: HspB1, HspB5 and HspB8.The physical chemistry of the amyloid phenomenon: thermodynamics and kinetics of filamentous protein aggregation.Small heat-shock proteins: important players in regulating cellular proteostasis.On the lag phase in amyloid fibril formation.Molecular chaperones and neuronal proteostasis.Medical implications of understanding the functions of human small heat shock proteins.Biophysical approaches for the study of interactions between molecular chaperones and protein aggregates.Charge dependent retardation of amyloid β aggregation by hydrophilic proteins.Expanding role of molecular chaperones in regulating α-synuclein misfolding; implications in Parkinson's disease.Small heat shock proteins in ageing and age-related diseases.Chaperones as Suppressors of Protein Misfolded Oligomer ToxicityKinetic analysis reveals the diversity of microscopic mechanisms through which molecular chaperones suppress amyloid formationC-terminal interactions mediate the quaternary dynamics of αB-crystallin.
P2860
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P2860
Binding of the molecular chaperone αB-crystallin to Aβ amyloid fibrils inhibits fibril elongation
description
2011 nî lūn-bûn
@nan
2011 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած
@hyw
2011 թվականի հոտեմբերին հրատարակված գիտական հոդված
@hy
2011年の論文
@ja
2011年論文
@yue
2011年論文
@zh-hant
2011年論文
@zh-hk
2011年論文
@zh-mo
2011年論文
@zh-tw
2011年论文
@wuu
name
Binding of the molecular chape ...... ils inhibits fibril elongation
@ast
Binding of the molecular chape ...... ils inhibits fibril elongation
@en
type
label
Binding of the molecular chape ...... ils inhibits fibril elongation
@ast
Binding of the molecular chape ...... ils inhibits fibril elongation
@en
prefLabel
Binding of the molecular chape ...... ils inhibits fibril elongation
@ast
Binding of the molecular chape ...... ils inhibits fibril elongation
@en
P2093
P2860
P50
P1433
P1476
Binding of the molecular chape ...... ils inhibits fibril elongation
@en
P2093
Mark E Welland
Sarah L Shammas
Sarah Meehan
Shuyu Wang
Tuomas P J Knowles
P2860
P304
P356
10.1016/J.BPJ.2011.07.056
P407
P577
2011-10-01T00:00:00Z