Escherichia coli trigger factor is a prolyl isomerase that associates with nascent polypeptide chains.
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Signal peptide-dependent protein transport in Bacillus subtilis: a genome-based survey of the secretomeComplexes between nascent polypeptides and their molecular chaperones in the cytosol of mammalian cellsProtein quality control in the bacterial periplasmPromiscuous Substrate Recognition in Folding and Assembly Activities of the Trigger Factor ChaperoneZuotin, a ribosome-associated DnaJ molecular chaperoneRole of the mitochondrial DnaJ homolog Mdj1p as a chaperone for mitochondrially synthesized and imported proteins.The molecular chaperone Ssb from Saccharomyces cerevisiae is a component of the ribosome-nascent chain complex.L25 functions as a conserved ribosomal docking site shared by nascent chain-associated complex and signal-recognition particle.FK506-binding protein of the hyperthermophilic archaeum, Thermococcus sp. KS-1, a cold-shock-inducible peptidyl-prolyl cis-trans isomerase with activities to trap and refold denatured proteinsEvaluation of similarities in the cis/trans isomerase function of trigger factor and DnaK.The periplasmic Escherichia coli peptidylprolyl cis,trans-isomerase FkpA. I. Increased functional expression of antibody fragments with and without cis-prolines.Chaperone function of FkpA, a heat shock prolyl isomerase, in the periplasm of Escherichia coli.Identification 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 actionBinding specificity of Escherichia coli trigger factor.Molecular basis for interactions of the DnaK chaperone with substrates.In vivo analysis of the overlapping functions of DnaK and trigger factorTrigger factor binds to ribosome-signal-recognition particle (SRP) complexes and is excluded by binding of the SRP receptor.Immunoproteomic identification of immunogenic proteins in Cronobacter sakazakii strain BAA-894.Quantitative proteomic analysis of cell cycle of the dinoflagellate Prorocentrum donghaiense (Dinophyceae).Proteomic profiling of Burkholderia cenocepacia clonal isolates with different virulence potential retrieved from a cystic fibrosis patient during chronic lung infection.The ribosome and YidC. New insights into the biogenesis of Escherichia coli inner membrane proteins.Carbon source-dependent synthesis of SecB, a cytosolic chaperone involved in protein translocation across Escherichia coli membranes.Functional Subunits of Eukaryotic Chaperonin CCT/TRiC in Protein Folding.Chaperone-assisted folding of newly synthesized proteins in the cytosol.Assisted folding of D-glyceraldehyde-3-phosphate dehydrogenase by trigger factor.Ligand crowding at a nascent signal sequence.Convergent evolution of clamp-like binding sites in diverse chaperones.Requirements for surface expression and function of adhesin P1 from Streptococcus mutans.The crystal structure of ribosomal chaperone trigger factor from Vibrio cholerae.Integrating protein homeostasis strategies in prokaryotes.Ribosome purification approaches for studying interactions of regulatory proteins and RNAs with the ribosome.Chaperone discovery.Overexpression of trigger factor prevents aggregation of recombinant proteins in Escherichia coli.Identification of nascent chain interaction sites on trigger factor.Functional dissection of Escherichia coli trigger factor: unraveling the function of individual domains.GroEL-mediated protein folding.Improving Acetic Acid Production by Over-Expressing PQQ-ADH in Acetobacter pasteurianus.Cotranslational protein folding.An RpoS-dependent sRNA regulates the expression of a chaperone involved in protein folding
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Escherichia coli trigger factor is a prolyl isomerase that associates with nascent polypeptide chains.
description
article científic
@ca
article scientifique
@fr
articolo scientifico
@it
artigo científico
@pt
bilimsel makale
@tr
scientific article published on April 1996
@en
vedecký článok
@sk
vetenskaplig artikel
@sv
videnskabelig artikel
@da
vědecký článek
@cs
name
Escherichia coli trigger facto ...... th nascent polypeptide chains.
@en
Escherichia coli trigger facto ...... th nascent polypeptide chains.
@nl
type
label
Escherichia coli trigger facto ...... th nascent polypeptide chains.
@en
Escherichia coli trigger facto ...... th nascent polypeptide chains.
@nl
prefLabel
Escherichia coli trigger facto ...... th nascent polypeptide chains.
@en
Escherichia coli trigger facto ...... th nascent polypeptide chains.
@nl
P2093
P2860
P356
P1476
Escherichia coli trigger facto ...... ith nascent polypeptide chains
@en
P2093
P2860
P304
P356
10.1073/PNAS.93.9.4437
P407
P50
P577
1996-04-01T00:00:00Z