Structural adaptations in the specialized bacteriophage T4 co-chaperonin Gp31 expand the size of the Anfinsen cage
about
Probing the interface in a human co-chaperonin heptamer: residues disrupting oligomeric unfolded state identifiedBacteriophage T4 GenomeMycobacterium tuberculosis Chaperonin 10 Heptamers Self-Associate through Their Biologically Active LoopsIdentification of in vivo substrates of the yeast mitochondrial chaperonins reveals overlapping but non-identical requirement for hsp60 and hsp10.P. falciparum cpn20 is a bona fide co-chaperonin that can replace GroES in E. coliChaperoninsOligomeric interfaces under the lens: geminiOverview of protein structural and functional folds.Bacteriophage-encoded cochaperonins can substitute for Escherichia coli's essential GroES proteinThe T4-encoded cochaperonin, gp31, has unique properties that explain its requirement for the folding of the T4 major capsid protein.The unfolding story of the chaperonins.GroEL is involved in activation of Escherichia coli RNA polymerase devoid of the omega subunit in vivo.Residues in substrate proteins that interact with GroEL in the capture process are buried in the native stateGenetic analysis of the bacteriophage T4-encoded cochaperonin Gp31Identification of important amino acid residues that modulate binding of Escherichia coli GroEL to its various cochaperonesAn ORFan no more: the bacteriophage T4 39.2 gene product, NwgI, modulates GroEL chaperone functionExpression and functional characterization of the first bacteriophage-encoded chaperonin.A mobile loop order-disorder transition modulates the speed of chaperonin cycling.The GroEL/GroES cis cavity as a passive anti-aggregation device.Chaperonin complex with a newly folded protein encapsulated in the folding chamber.Chaperonin cofactors, Cpn10 and Cpn20, of green algae and plants function as hetero-oligomeric ring complexes.Pseudo-T-even bacteriophage RB49 encodes CocO, a cochaperonin for GroEL, which can substitute for Escherichia coli's GroES and bacteriophage T4's Gp31.Structural basis for helper T-cell and antibody epitope immunodominance in bacteriophage T4 Hsp10. Role of disordered loops.Thermal activation of the co-chaperonins GroES and gp31 probed by mass spectrometry.On the maximum size of proteins to stay and fold in the cavity of GroEL underneath GroES.Chloroplasts have a novel Cpn10 in addition to Cpn20 as co-chaperonins in Arabidopsis thaliana.Assembly and infection process of bacteriophage T4.Monitoring macromolecular complexes involved in the chaperonin-assisted protein folding cycle by mass spectrometry
P2860
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P2860
Structural adaptations in the specialized bacteriophage T4 co-chaperonin Gp31 expand the size of the Anfinsen cage
description
1997 nî lūn-bûn
@nan
1997 թուականի Յուլիսին հրատարակուած գիտական յօդուած
@hyw
1997 թվականի հուլիսին հրատարակված գիտական հոդված
@hy
1997年の論文
@ja
1997年論文
@yue
1997年論文
@zh-hant
1997年論文
@zh-hk
1997年論文
@zh-mo
1997年論文
@zh-tw
1997年论文
@wuu
name
Structural adaptations in the ...... the size of the Anfinsen cage
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Structural adaptations in the ...... the size of the Anfinsen cage
@en
Structural adaptations in the ...... the size of the Anfinsen cage
@nl
type
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Structural adaptations in the ...... the size of the Anfinsen cage
@ast
Structural adaptations in the ...... the size of the Anfinsen cage
@en
Structural adaptations in the ...... the size of the Anfinsen cage
@nl
prefLabel
Structural adaptations in the ...... the size of the Anfinsen cage
@ast
Structural adaptations in the ...... the size of the Anfinsen cage
@en
Structural adaptations in the ...... the size of the Anfinsen cage
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P2093
P1433
P1476
Structural adaptations in the ...... the size of the Anfinsen cage
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P2093
S M van der Vies
P304
P356
10.1016/S0092-8674(00)80343-8
P407
P577
1997-07-25T00:00:00Z