The structural basis of substrate recognition by the eukaryotic chaperonin TRiC/CCT
about
Engineering and Evolution of Molecular Chaperones and Protein Disaggregases with Enhanced ActivityContribution of the Type II Chaperonin, TRiC/CCT, to OncogenesisSubstrate-binding domain conformational dynamics mediate Hsp70 allosteryCapturing a Dynamic Chaperone-Substrate Interaction Using NMR-Informed Molecular ModelingxTract: software for characterizing conformational changes of protein complexes by quantitative cross-linking mass spectrometryAsymmetry in the function and dynamics of the cytosolic group II chaperonin CCT/TRiCStructure of the human TRiC/CCT Subunit 5 associated with hereditary sensory neuropathy.Protein unfolding as a switch from self-recognition to high-affinity client bindingChaperonin TRiC/CCT Recognizes Fusion Oncoprotein AML1-ETO through Subunit-Specific Interactions.Expression and diagnostic value of CCT3 and IQGAP3 in hepatocellular carcinoma.Visualizing chaperone-assisted protein folding.A molecular mechanism of chaperone-client recognition.Internal (His)₆-tagging delivers a fully functional hetero-oligomeric class II chaperonin in high yield.The Mechanism and Function of Group II Chaperonins.Quantitative proteomics: challenges and opportunities in basic and applied research.Staggered ATP binding mechanism of eukaryotic chaperonin TRiC (CCT) revealed through high-resolution cryo-EM.Chaperone-client interactions: Non-specificity engenders multifunctionality.Folding while bound to chaperones.Replacement of GroEL in Escherichia coli by the Group II Chaperonin from the Archaeon Methanococcus maripaludis.Forces Driving Chaperone ActionMechanistic basis for a molecular triage reactionCCT complex restricts neuropathogenic protein aggregation via autophagy.Targeting chaperonin containing TCP1 (CCT) as a molecular therapeutic for small cell lung cancer.Intraring allostery controls the function and assembly of a hetero-oligomeric class II chaperonin.TRiC/CCT chaperonins are essential for maintaining myofibril organization, cardiac physiological rhythm, and lifespan.The TRiC chaperonin controls reovirus replication through outer-capsid folding.TRiC controls transcription resumption after UV damage by regulating Cockayne syndrome protein A.Quantitative analysis of the impact of a human pathogenic mutation on the CCT5 chaperonin subunit using a proxy archaeal ortholog.Single-Ring Intermediates Are Essential for Some Chaperonins.Inert and seed-competent tau monomers suggest structural origins of aggregation.
P2860
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P2860
The structural basis of substrate recognition by the eukaryotic chaperonin TRiC/CCT
description
2014 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած
@hyw
2014 թվականի նոյեմբերին հրատարակված գիտական հոդված
@hy
artículu científicu espublizáu en 2014
@ast
im November 2014 veröffentlichter wissenschaftlicher Artikel
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scientific journal article
@en
vedecký článok (publikovaný 2014/11/20)
@sk
vědecký článek publikovaný v roce 2014
@cs
wetenschappelijk artikel (gepubliceerd op 2014/11/20)
@nl
наукова стаття, опублікована в листопаді 2014
@uk
مقالة علمية (نشرت في 20-11-2014)
@ar
name
The structural basis of substrate recognition by the eukaryotic chaperonin TRiC/CCT
@ast
The structural basis of substrate recognition by the eukaryotic chaperonin TRiC/CCT
@en
The structural basis of substrate recognition by the eukaryotic chaperonin TRiC/CCT
@nl
type
label
The structural basis of substrate recognition by the eukaryotic chaperonin TRiC/CCT
@ast
The structural basis of substrate recognition by the eukaryotic chaperonin TRiC/CCT
@en
The structural basis of substrate recognition by the eukaryotic chaperonin TRiC/CCT
@nl
prefLabel
The structural basis of substrate recognition by the eukaryotic chaperonin TRiC/CCT
@ast
The structural basis of substrate recognition by the eukaryotic chaperonin TRiC/CCT
@en
The structural basis of substrate recognition by the eukaryotic chaperonin TRiC/CCT
@nl
P2093
P2860
P3181
P1433
P1476
The structural basis of substrate recognition by the eukaryotic chaperonin TRiC/CCT
@en
P2093
Corey W. Liu
Lukasz A. Joachimiak
Thomas Walzthoeni
P2860
P304
P3181
P356
10.1016/J.CELL.2014.10.042
P407
P577
2014-11-20T00:00:00Z