AlphaB-crystallin, a small heat-shock protein, prevents the amyloid fibril growth of an amyloid beta-peptide and beta2-microglobulin. - Wikidata - awgldk - TriplyDB

AlphaB-crystallin, a small heat-shock protein, prevents the amyloid fibril growth of an amyloid beta-peptide and beta2-microglobulin.

AlphaB-crystallin, a small heat-shock protein, prevents the amyloid fibril growth of an amyloid beta-peptide and beta2-microglobulin.

http://www.wikidata.org/entity/Q40678915

about

N-terminal domain of Pyrococcus furiosus l-asparaginase functions as a non-specific, stable, molecular chaperone Historical and Current Concepts of Fibrillogenesis and In vivo Amyloidogenesis: Implications of Amyloid Tissue Targeting The structured core domain of B-crystallin can prevent amyloid fibrillation and associated toxicity The neuroendocrine protein 7B2 suppresses the aggregation of neurodegenerative disease-related proteins The extracellular chaperone clusterin sequesters oligomeric forms of the amyloid-β(1-40) peptide Specific chaperones and regulatory domains in control of amyloid formation.Behavioral defects in chaperone-deficient Alzheimer's disease model mice.Site-directed mutations in the C-terminal extension of human alphaB-crystallin affect chaperone function and block amyloid fibril formation Amyloidogenic and associated proteins in systemic amyloidosis proteome of adipose tissue.Amyloid beta-protein assembly as a therapeutic target of Alzheimer's disease.Interaction between oligomers of stefin B and amyloid-beta in vitro and in cells.The interaction of alphaB-crystallin with mature alpha-synuclein amyloid fibrils inhibits their elongation.Identifying the amylome, proteins capable of forming amyloid-like fibrils Small heat-shock proteins interact with a flanking domain to suppress polyglutamine aggregation.Challenges associated with metal chelation therapy in Alzheimer's disease Small heat shock proteins potentiate amyloid dissolution by protein disaggregases from yeast and humans αB-Crystallin inhibits the cell toxicity associated with amyloid fibril formation by κ-casein and the amyloid-β peptide.Monitoring the prevention of amyloid fibril formation by alpha-crystallin. Temperature dependence and the nature of the aggregating species.Humoral response against small heat shock proteins in Parkinson's disease.Sequestration of toxic oligomers by HspB1 as a cytoprotective mechanism.Binding of the molecular chaperone αB-crystallin to Aβ amyloid fibrils inhibits fibril elongation 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 Lipocalin-type prostaglandin D synthase/beta-trace is a major amyloid beta-chaperone in human cerebrospinal fluid.Kinetics and thermodynamics of amyloid formation from direct measurements of fluctuations in fibril mass AbetaPP-overexpression and proteasome inhibition increase alphaB-crystallin in cultured human muscle: relevance to inclusion-body myositis.Chaperone networks: tipping the balance in protein folding diseases Novel roles for α-crystallins in retinal function and disease.Crystallins and neuroinflammation: The glial side of the story.siRNA screen identifies QPCT as a druggable target for Huntington's disease.Structure, function, property, and role in neurologic diseases and other diseases of the sHsp22.Monitoring the interaction between β2-microglobulin and the molecular chaperone αB-crystallin by NMR and mass spectrometry: αB-crystallin dissociates β2-microglobulin oligomers.Interactive sequences in the molecular chaperone, human alphaB crystallin modulate the fibrillation of amyloidogenic proteins.Plasmodium falciparum merozoite surface protein 2 is unstructured and forms amyloid-like fibrils E. coli chaperones DnaK, Hsp33 and Spy inhibit bacterial functional amyloid assembly.Receptor-associated protein interacts with amyloid-beta peptide and promotes its cellular uptake.Mechanism of suppression of protein aggregation by α-crystallin.Biophysical approaches for the study of interactions between molecular chaperones and protein aggregates.Chaperones as Suppressors of Protein Misfolded Oligomer Toxicity Modulation of amyloid-β 1-42 structure and toxicity by proline-rich whey peptides.

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P2860

AlphaB-crystallin, a small heat-shock protein, prevents the amyloid fibril growth of an amyloid beta-peptide and beta2-microglobulin.

http://www.wikidata.org/entity/Q40678915

description

2005 nî lūn-bûn

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2005年の論文

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2005年論文

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2005年論文

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2005年論文

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2005年論文

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2005年論文

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2005年论文

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2005年论文

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2005年论文

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name

AlphaB-crystallin, a small hea ...... ptide and beta2-microglobulin.

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type

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AlphaB-crystallin, a small hea ...... ptide and beta2-microglobulin.

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AlphaB-crystallin, a small hea ...... ptide and beta2-microglobulin.

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P1433

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P1476

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P2860

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Q40678915-B7A2F7C6-BA01-43E5-AFF8-428BD9EA6607

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P1433

Biochemical Journal

P1476

AlphaB-crystallin, a small hea ...... ptide and beta2-microglobulin.

@en

P2093

Bakthisaran Raman

http://www.w3.org/2001/XMLSchema#string

Ch Mohan Rao

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Hironobu Naiki

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Miyo Sakai

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Saloni Y Pasta

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Tadato Ban

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Tangirala Ramakrishna

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Yuji Goto

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P2860

A missense mutation in the alphaB-crystallin chaperone gene causes a desmin-related myopathy

Unfolding and refolding of a quinone oxidoreductase: alpha-crystallin, a molecular chaperone, assists its reactivation

Structure and function of the small heat shock protein/alpha-crystallin family of molecular chaperones

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

Role of the C-terminal extensions of alpha-crystallins. Swapping the C-terminal extension of alpha-crystallin to alphaB-crystallin results in enhanced chaperone activity

Common structure of soluble amyloid oligomers implies common mechanism of pathogenesis

Alpha-crystallin can function as a molecular chaperone

From the globular to the fibrous state: protein structure and structural conversion in amyloid formation.

Small heat-shock proteins and their potential role in human disease.

Interaction of human recombinant alphaA- and alphaB-crystallins with early and late unfolding intermediates of citrate synthase on its thermal denaturation.

P304

573-581

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P31

scholarly article

P356

10.1042/BJ20050339

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P407

P433

Pt 3

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P478

392

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P577

2005-12-01T00:00:00Z

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P698

16053447

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P932

1316297

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