The GroEL/GroES cis cavity as a passive anti-aggregation device.
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GroEL/ES Chaperonin Modulates the Mechanism and Accelerates the Rate of TIM-Barrel Domain FoldingB-Cell Epitopes in GroEL of Francisella tularensisMultiple chaperonins in bacteria--novel functions and non-canonical behaviorsDynamics, flexibility, and allostery in molecular chaperoninsCrystallization and preliminary X-ray crystallographic analysis of the XoGroEL chaperonin from Xanthomonas oryzae pv. oryzae.GroEL actively stimulates folding of the endogenous substrate protein PepQThe nucleotide exchange factor Ric-8A is a chaperone for the conformationally dynamic nucleotide-free state of Gαi1.Conditional disorder in chaperone action.Archaeal-like chaperonins in bacteria.Chaperones divide yeast proteins into classes of expression level and evolutionary rateExpression and functional characterization of the first bacteriophage-encoded chaperonin.Engineering Escherichia coli for soluble expression and single step purification of active human lysozyme.Production of the catalytic core of human peptidylglycine α-hydroxylating monooxygenase (hPHMcc) in Escherichia coliPutting handcuffs on the chaperonin GroEL.Super Spy variants implicate flexibility in chaperone action.Integrating protein homeostasis strategies in prokaryotes.Chaperonin 60: a paradoxical, evolutionarily conserved protein family with multiple moonlighting functions.The chaperone toolbox at the single-molecule level: From clamping to confining.Chaperone-client interactions: Non-specificity engenders multifunctionality.Replacement of GroEL in Escherichia coli by the Group II Chaperonin from the Archaeon Methanococcus maripaludis.Role of nonspecific interactions in molecular chaperones through model-based bioinformatics.The N-terminal domain of Aliivibrio fischeri LuxR is a target of the GroEL chaperonin.Effects of C-terminal Truncation of Chaperonin GroEL on the Yield of In-cage Folding of the Green Fluorescent Protein.Folding of maltose binding protein outside of and in GroEL.Comparative genomic analysis of mollicutes with and without a chaperonin system.The Chaperonin GroEL: A Versatile Tool for Applied Biotechnology Platforms.Single-Ring Intermediates Are Essential for Some Chaperonins.
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P2860
The GroEL/GroES cis cavity as a passive anti-aggregation device.
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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 03 July 2009
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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
The GroEL/GroES cis cavity as a passive anti-aggregation device.
@en
The GroEL/GroES cis cavity as a passive anti-aggregation device.
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type
label
The GroEL/GroES cis cavity as a passive anti-aggregation device.
@en
The GroEL/GroES cis cavity as a passive anti-aggregation device.
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prefLabel
The GroEL/GroES cis cavity as a passive anti-aggregation device.
@en
The GroEL/GroES cis cavity as a passive anti-aggregation device.
@nl
P2860
P1433
P1476
The GroEL/GroES cis cavity as a passive anti-aggregation device.
@en
P2093
Adrian C Apetri
Wayne A Fenton
P2860
P304
P356
10.1016/J.FEBSLET.2009.06.049
P407
P577
2009-07-03T00:00:00Z