Trigger factor peptidyl-prolyl cis/trans isomerase activity is not essential for the folding of cytosolic proteins in Escherichia coli.
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Keeping up with protein foldingMolecular mechanism and structure of Trigger Factor bound to the translating ribosomePromiscuous Substrate Recognition in Folding and Assembly Activities of the Trigger Factor ChaperoneStructural Analysis of Protein Folding by the Long-Chain Archaeal Chaperone FKBP26The Hsp90 cochaperones Cpr6, Cpr7, and Cns1 interact with the intact ribosomePolypeptide binding proteins: what remains to be discovered?Identification of a potential hydrophobic peptide binding site in the C-terminal arm of trigger factor.Microbial peptidyl-prolyl cis/trans isomerases (PPIases): virulence factors and potential alternative drug targets.The chaperone function of cyclophilin 40 maps to a cleft between the prolyl isomerase and tetratricopeptide repeat domains.Trigger factor from the psychrophilic bacterium Psychrobacter frigidicola is a monomeric chaperoneEffect of hsp70 chaperone on the folding and misfolding of polypeptides modeling an elongating protein chainBirth, life and death of nascent polypeptide chains.Trigger Factor can antagonize both SecB and DnaK/DnaJ chaperone functions in Escherichia coli.Trigger factor assisted soluble expression of recombinant spike protein of porcine epidemic diarrhea virus in Escherichia coliConformational dynamics of bacterial trigger factor in apo and ribosome-bound states.Stress wars: the direct role of host and bacterial molecular chaperones in bacterial infection.Convergent evolution of clamp-like binding sites in diverse chaperones.Requirements for surface expression and function of adhesin P1 from Streptococcus mutans.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.The crystal structure of ribosomal chaperone trigger factor from Vibrio cholerae.Psychrophily and catalysis.Integrating protein homeostasis strategies in prokaryotes.Proteomic methods unravel the protein quality control in Escherichia coli.Breaking on through to the other side: protein export through the bacterial Sec system.Peptidylprolyl cis-trans isomerases of Legionella pneumophila: virulence, moonlighting and novel therapeutic targets.Functional analysis of the cyclophilin PpiB role in bacterial cell division.Identification of nascent chain interaction sites on trigger factor.Sequence-specific interactions of nascent Escherichia coli polypeptides with trigger factor and signal recognition particle.Functional dissection of Escherichia coli trigger factor: unraveling the function of individual domains.Analysis of protein phosphatase-1 and aurora protein kinase suppressors reveals new aspects of regulatory protein function in Saccharomyces cerevisiae.Trigger factor lacking the PPIase domain can enhance the folding of eukaryotic multi-domain proteins in Escherichia coli.Functional adaptations of the bacterial chaperone trigger factor to extreme environmental temperatures.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.Trigger factor binding to ribosomes with nascent peptide chains of varying lengths and sequences.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.Trigger factor in complex with the ribosome forms a molecular cradle for nascent proteins.Structural insight into proline / isomerization of unfolded proteins catalyzed by the trigger factor chaperone
P2860
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P2860
Trigger factor peptidyl-prolyl cis/trans isomerase activity is not essential for the folding of cytosolic proteins in Escherichia coli.
description
2004 nî lūn-bûn
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2004年の論文
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2004年学术文章
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name
Trigger factor peptidyl-prolyl ...... proteins in Escherichia coli.
@en
Trigger factor peptidyl-prolyl ...... proteins in Escherichia coli.
@nl
type
label
Trigger factor peptidyl-prolyl ...... proteins in Escherichia coli.
@en
Trigger factor peptidyl-prolyl ...... proteins in Escherichia coli.
@nl
prefLabel
Trigger factor peptidyl-prolyl ...... proteins in Escherichia coli.
@en
Trigger factor peptidyl-prolyl ...... proteins in Escherichia coli.
@nl
P2093
P2860
P50
P356
P1476
Trigger factor peptidyl-prolyl ...... proteins in Escherichia coli.
@en
P2093
Günter Kramer
Sonja Vorderwülbecke
Thomas Rauch
Thorben A Kurz
P2860
P304
14165-14170
P356
10.1074/JBC.M313635200
P407
P577
2004-01-16T00:00:00Z