Binding of the molecular chaperone αB-crystallin to Aβ amyloid fibrils inhibits fibril elongation - Wikidata - wikimedia - TriplyDB

Binding of the molecular chaperone αB-crystallin to Aβ amyloid fibrils inhibits fibril elongation

Binding of the molecular chaperone αB-crystallin to Aβ amyloid fibrils inhibits fibril elongation

http://www.wikidata.org/entity/Q35246361

about

Fibrillogenic propensity of the GroEL apical domain: a Janus-faced minichaperone N-terminal domain of Pyrococcus furiosus l-asparaginase functions as a non-specific, stable, molecular chaperone Human small heat shock proteins: protein interactomes of homo- and hetero-oligomeric complexes: an update The structured core domain of B-crystallin can prevent amyloid fibrillation and associated toxicity Interaction of the molecular chaperone DNAJB6 with growing amyloid-beta 42 (Aβ42) aggregates leads to sub-stoichiometric inhibition of amyloid formation Amyloid-β oligomers are sequestered by both intracellular and extracellular chaperones The extracellular chaperone clusterin sequesters oligomeric forms of the amyloid-β(1-40) peptide Single 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 simulations Rescue of αB Crystallin (HSPB5) Mutants Associated Protein Aggregation by Co-Expression of HSPB5 Partners Oligomers 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 model Amyloid fiber formation in human γD-Crystallin induced by UV-B photodamage Identification 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 Toxicity Kinetic analysis reveals the diversity of microscopic mechanisms through which molecular chaperones suppress amyloid formation C-terminal interactions mediate the quaternary dynamics of αB-crystallin.

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P2860

Binding of the molecular chaperone αB-crystallin to Aβ amyloid fibrils inhibits fibril elongation

http://www.wikidata.org/entity/Q35246361

description

2011 nî lūn-bûn

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2011 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած

@hyw

2011 թվականի հոտեմբերին հրատարակված գիտական հոդված

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2011年の論文

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2011年論文

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2011年論文

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2011年論文

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2011年論文

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2011年論文

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2011年论文

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name

Binding of the molecular chape ...... ils inhibits fibril elongation

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Binding of the molecular chape ...... ils inhibits fibril elongation

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Binding of the molecular chape ...... ils inhibits fibril elongation

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Binding of the molecular chape ...... ils inhibits fibril elongation

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Binding of the molecular chape ...... ils inhibits fibril elongation

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Binding of the molecular chape ...... ils inhibits fibril elongation

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Binding of the molecular chape ...... ils inhibits fibril elongation

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Mark E Welland

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Sarah L Shammas

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Sarah Meehan

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Shuyu Wang

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Tuomas P J Knowles

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P2860

Forecasting the global burden of Alzheimer’s disease

alphaB-crystallin competes with Alzheimer's disease beta-amyloid peptide for peptide-peptide interactions and induces oxidation of Abeta-Met35

In vitro perturbation of aggregation processes in beta-amyloid peptides: a spectroscopic study

Crystal structures of truncated alphaA and alphaB crystallins reveal structural mechanisms of polydispersity important for eye lens function

Protein misfolding, functional amyloid, and human disease

Alzheimer's disease: genes, proteins, and therapy

Deranged expression of molecular chaperones in brains of patients with Alzheimer's disease

Protein folding and misfolding

alpha B subunit of lens-specific protein alpha-crystallin is present in other ocular and non-ocular tissues

Secreted amyloid beta-protein similar to that in the senile plaques of Alzheimer's disease is increased in vivo by the presenilin 1 and 2 and APP mutations linked to familial Alzheimer's disease

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10.1016/J.BPJ.2011.07.056

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7

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101

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Christopher A Waudby

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51683810

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molecular chaperones

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3183811

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