Interaction of human recombinant alphaA- and alphaB-crystallins with early and late unfolding intermediates of citrate synthase on its thermal denaturation.
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Unfolding and refolding of a quinone oxidoreductase: alpha-crystallin, a molecular chaperone, assists its reactivationA new heat shock gene, AgsA, which encodes a small chaperone involved in suppressing protein aggregation in Salmonella enterica serovar typhimuriumRole of the C-terminal extensions of alpha-crystallins. Swapping the C-terminal extension of alpha-crystallin to alphaB-crystallin results in enhanced chaperone activityCataract-causing defect of a mutant γ-crystallin proceeds through an aggregation pathway which bypasses recognition by the α-crystallin chaperone.αA-Crystallin-derived mini-chaperone modulates stability and function of cataract causing αAG98R-crystallinThe function of the beta3 interactive domain in the small heat shock protein and molecular chaperone, human alphaB crystallinRescue of αB Crystallin (HSPB5) Mutants Associated Protein Aggregation by Co-Expression of HSPB5 PartnersConserved F84 and P86 residues in alphaB-crystallin are essential to effectively prevent the aggregation of substrate proteins.Alpha-crystallin binds to the aggregation-prone molten-globule state of alkaline protease: implications for preventing irreversible thermal denaturation.A novel small heat shock protein of Haliotis discus hannai: characterization, structure modeling, and expression profiles under environmental stresses.Mechanism of suppression of protein aggregation by α-crystallin.Structural and functional consequences of chaperone site deletion in αA-crystallin.Alphab-crystallin-assisted reactivation of glucose-6-phosphate dehydrogenase upon refolding.Trimethylamine N-oxide alleviates the severe aggregation and ER stress caused by G98R alphaA-crystallin.A small heat shock/alpha-crystallin protein from encysted Artemia embryos suppresses tubulin denaturation.AlphaB-crystallin, a small heat-shock protein, prevents the amyloid fibril growth of an amyloid beta-peptide and beta2-microglobulin.Hydroimidazolone modification of human alphaA-crystallin: Effect on the chaperone function and protein refolding ability.Mammalian Hsp22 is a heat-inducible small heat-shock protein with chaperone-like activity.Structural and functional roles for beta-strand 7 in the alpha-crystallin domain of p26, a polydisperse small heat shock protein from Artemia franciscana.Structural perturbation and enhancement of the chaperone-like activity of alpha-crystallin by arginine hydrochloride.Escherichia coli small heat shock proteins, IbpA and IbpB, protect enzymes from inactivation by heat and oxidants.Suppression of DTT-induced aggregation of abrin by alphaA- and alphaB-crystallins: a model aggregation assay for alpha-crystallin chaperone activity in vitro.Subunit exchange demonstrates a differential chaperone activity of calf alpha-crystallin toward beta LOW- and individual gamma-crystallins.The selective inhibition of serpin aggregation by the molecular chaperone, alpha-crystallin, indicates a nucleation-dependent specificity.Role of the conserved SRLFDQFFG region of alpha-crystallin, a small heat shock protein. Effect on oligomeric size, subunit exchange, and chaperone-like activity.Molecular mechanism of the Escherichia coli AhpC in the function of a chaperone under heat-shock conditions
P2860
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P2860
Interaction of human recombinant alphaA- and alphaB-crystallins with early and late unfolding intermediates of citrate synthase on its thermal denaturation.
description
2001 nî lūn-bûn
@nan
2001 թուականի Մայիսին հրատարակուած գիտական յօդուած
@hyw
2001 թվականի մայիսին հրատարակված գիտական հոդված
@hy
2001年の論文
@ja
2001年学术文章
@wuu
2001年学术文章
@zh-cn
2001年学术文章
@zh-hans
2001年学术文章
@zh-my
2001年学术文章
@zh-sg
2001年學術文章
@yue
name
Interaction of human recombina ...... e on its thermal denaturation.
@ast
Interaction of human recombina ...... e on its thermal denaturation.
@en
type
label
Interaction of human recombina ...... e on its thermal denaturation.
@ast
Interaction of human recombina ...... e on its thermal denaturation.
@en
prefLabel
Interaction of human recombina ...... e on its thermal denaturation.
@ast
Interaction of human recombina ...... e on its thermal denaturation.
@en
P2093
P2860
P1433
P1476
Interaction of human recombina ...... e on its thermal denaturation.
@en
P2093
P2860
P304
P356
10.1016/S0014-5793(01)02451-6
P407
P577
2001-05-01T00:00:00Z