Three-state equilibrium of Escherichia coli trigger factor.
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Promiscuous Substrate Recognition in Folding and Assembly Activities of the Trigger Factor ChaperoneStructural Basis for Protein Antiaggregation Activity of the Trigger Factor ChaperoneSelective ribosome profiling reveals the cotranslational chaperone action of trigger factor in vivoIdentification of a potential hydrophobic peptide binding site in the C-terminal arm of trigger factor.Structure of trigger factor binding domain in biologically homologous complex with eubacterial ribosome reveals its chaperone actionTrigger factor binds to ribosome-signal-recognition particle (SRP) complexes and is excluded by binding of the SRP receptor.Hydrophobic collapse of trigger factor monomer in solutionTrigger factor from the psychrophilic bacterium Psychrobacter frigidicola is a monomeric chaperoneSelective ribosome profiling as a tool for studying the interaction of chaperones and targeting factors with nascent polypeptide chains and ribosomes.Expression and in vitro functional analyses of recombinant Gam1 proteinChaperone-assisted folding of newly synthesized proteins in the cytosol.Ligand crowding at a nascent signal sequence.Conformational dynamics of bacterial trigger factor in apo and ribosome-bound states.Flexibility of the bacterial chaperone trigger factor in microsecond-timescale molecular dynamics simulations.Use of folding modulators to improve heterologous protein production in Escherichia coli.Structural characterization of the interaction of α-synuclein nascent chains with the ribosomal surface and trigger factorThe crystal structure of ribosomal chaperone trigger factor from Vibrio cholerae.Protein folding on the ribosome studied using NMR spectroscopy.Global Analysis of the Impact of Deleting Trigger Factor on the Transcriptome Profile of Escherichia coli.Structural and molecular comparison of bacterial and eukaryotic trigger factorsTrigger factor chaperone acts as a mechanical foldase.Confined dynamics of a ribosome-bound nascent globin: Cone angle analysis of fluorescence depolarization decays in the presence of two local motions.Dimeric trigger factor stably binds folding-competent intermediates and cooperates with the DnaK-DnaJ-GrpE chaperone system to allow refolding.The dynamic dimer structure of the chaperone Trigger Factor.Single-molecule dynamics of the molecular chaperone trigger factor in living cells.Oligomerization of a molecular chaperone modulates its activity.Complexome of Escherichia coli cytosolic proteins under normal native conditions.Molecular biology: triggering positive competition.Real-time observation of trigger factor function on translating ribosomes.The C-terminal domain of Escherichia coli trigger factor represents the central module of its chaperone activity.Dissecting functional similarities of ribosome-associated chaperones from Saccharomyces cerevisiae and Escherichia coli.Ribosome-based protein folding systems are structurally divergent but functionally universal across biological kingdoms.
P2860
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P2860
Three-state equilibrium of Escherichia coli trigger factor.
description
2002 nî lūn-bûn
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2002年の論文
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2002年学术文章
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2002年学术文章
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2002年学术文章
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2002年学术文章
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2002年學術文章
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name
Three-state equilibrium of Escherichia coli trigger factor.
@en
Three-state equilibrium of Escherichia coli trigger factor.
@nl
type
label
Three-state equilibrium of Escherichia coli trigger factor.
@en
Three-state equilibrium of Escherichia coli trigger factor.
@nl
prefLabel
Three-state equilibrium of Escherichia coli trigger factor.
@en
Three-state equilibrium of Escherichia coli trigger factor.
@nl
P2093
P2860
P50
P356
P1433
P1476
Three-state equilibrium of Escherichia coli trigger factor.
@en
P2093
Günter Kramer
Hans-Joachim Schönfeld
Thomas Rauch
P2860
P304
P356
10.1515/BC.2002.182
P577
2002-10-01T00:00:00Z