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Human TRiC complex purified from HeLa cells contains all eight CCT subunits and is active in vitroCrystal Structure of Group II Chaperonin in the Open StateDual Action of ATP Hydrolysis Couples Lid Closure to Substrate Release into the Group II Chaperonin ChamberChaperonins from an Antarctic archaeon are predominantly monomeric: crystal structure of an open state monomerFlexible interwoven termini determine the thermal stability of thermosomesDynamics, flexibility, and allostery in molecular chaperoninsThe structural basis of substrate recognition by the eukaryotic chaperonin TRiC/CCTxTract: software for characterizing conformational changes of protein complexes by quantitative cross-linking mass spectrometryThe cytosolic chaperonin CCT/TRiC and cancer cell proliferation.A Mutant Chaperonin That Is Functional at Lower Temperatures Enables Hyperthermophilic Archaea To Grow under Cold-Stress Conditions.Expression and functional characterization of the first bacteriophage-encoded chaperonin.A gradient of ATP affinities generates an asymmetric power stroke driving the chaperonin TRIC/CCT folding cycle.Human CCT4 and CCT5 chaperonin subunits expressed in Escherichia coli form biologically active homo-oligomers.Cellular chaperonin CCTγ contributes to rabies virus replication during infectionChaperonin TRiC/CCT Recognizes Fusion Oncoprotein AML1-ETO through Subunit-Specific Interactions.Internal (His)₆-tagging delivers a fully functional hetero-oligomeric class II chaperonin in high yield.The Mechanism and Function of Group II Chaperonins.Purification, crystallization, and preliminary X-ray crystallographic analysis of the Group III chaperonin from Carboxydothermus hydrogenoformans.The TCP1γ subunit of Leishmania donovani forms a biologically active homo-oligomeric complex.Differential conformational modulations of MreB folding upon interactions with GroEL/ES and TRiC chaperonin components.The group II chaperonin Mm-Cpn binds and refolds human γD crystallin.An information theoretic framework reveals a tunable allosteric network in group II chaperonins.Protein foldingUsing the dendritic polymer PAMAM to form gold nanoparticles in the protein cage thermosome.The TRiC chaperonin controls reovirus replication through outer-capsid folding.A chaperonin as protein nanoreactor for atom-transfer radical polymerization.Selective and responsive nanoreactors
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P2860
description
article científic
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article scientifique
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articolo scientifico
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artigo científico
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bilimsel makale
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scientific article published on 22 March 2008
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vedecký článok
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vetenskaplig artikel
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videnskabelig artikel
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vědecký článek
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name
Chaperonins: The hunt for the Group II mechanism.
@en
Chaperonins: The hunt for the Group II mechanism.
@nl
type
label
Chaperonins: The hunt for the Group II mechanism.
@en
Chaperonins: The hunt for the Group II mechanism.
@nl
prefLabel
Chaperonins: The hunt for the Group II mechanism.
@en
Chaperonins: The hunt for the Group II mechanism.
@nl
P1476
Chaperonins: The hunt for the Group II mechanism
@en
P2093
Anthony R Clarke
P304
P356
10.1016/J.ABB.2008.03.015
P407
P577
2008-03-22T00:00:00Z