Trigger Factor can antagonize both SecB and DnaK/DnaJ chaperone functions in Escherichia coli.
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Structural Basis for Protein Antiaggregation Activity of the Trigger Factor ChaperoneStructural basis for the antifolding activity of a molecular chaperoneSelective ribosome profiling reveals the cotranslational chaperone action of trigger factor in vivoComparison of strand-specific transcriptomes of enterohemorrhagic Escherichia coli O157:H7 EDL933 (EHEC) under eleven different environmental conditions including radish sprouts and cattle feces.Lon protease quality control of presecretory proteins in Escherichia coli and its dependence on the SecB and DnaJ (Hsp40) chaperones.Multitasking SecB chaperones in bacteriaTrigger factor from the psychrophilic bacterium Psychrobacter frigidicola is a monomeric chaperoneSecB-like chaperone controls a toxin-antitoxin stress-responsive system in Mycobacterium tuberculosis.Semiquantitative analysis of clinical heat stress in Clostridium difficile strain 630 using a GeLC/MS workflow with emPAI quantitationLarge-scale evolutionary analyses on SecB subunits of bacterial sec system.Conserved, disordered C terminus of DnaK enhances cellular survival upon stress and DnaK in vitro chaperone activityQuantitative proteomic analysis of host--pathogen interactions: a study of Acinetobacter baumannii responses to host airwaysThe C-tail anchored TssL subunit, an essential protein of the enteroaggregative Escherichia coli Sci-1 Type VI secretion system, is inserted by YidCHsp33 controls elongation factor-Tu stability and allows Escherichia coli growth in the absence of the major DnaK and trigger factor chaperonesTAC from Mycobacterium tuberculosis: a paradigm for stress-responsive toxin-antitoxin systems controlled by SecB-like chaperones.The Hsp70 chaperone machines of Escherichia coli: a paradigm for the repartition of chaperone functions.Secretion of GOB metallo-beta-lactamase in Escherichia coli depends strictly on the cooperation between the cytoplasmic DnaK chaperone system and the Sec machinery: completion of folding and Zn(II) ion acquisition occur in the bacterial periplasm.Subcellular proteomic characterization of the high-temperature stress response of the cyanobacterium Spirulina platensisSecA Cotranslationally Interacts with Nascent Substrate Proteins In Vivo.The chaperone toolbox at the single-molecule level: From clamping to confining.Global Analysis of the Impact of Deleting Trigger Factor on the Transcriptome Profile of Escherichia coli.The rate of folding dictates substrate secretion by the Escherichia coli hemolysin type 1 secretion system.Determination of the intracellular concentration of the export chaperone SecB in Escherichia coli.Chaperone addiction of toxin-antitoxin systems.Recent advances in the expression, evolution, and dynamics of prokaryotic genomes.Physical map and dynamics of the chaperone network in Escherichia coli.Directed evolution of SecB chaperones toward toxin-antitoxin systems.Unraveling the effects of static magnetic field stress on cytosolic proteins of Salmonella by using a proteomic approach.The way is the goal: how SecA transports proteins across the cytoplasmic membrane in bacteria.Oligomerization of a molecular chaperone modulates its activity.
P2860
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P2860
Trigger Factor can antagonize both SecB and DnaK/DnaJ chaperone functions in Escherichia coli.
description
2007 nî lūn-bûn
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name
Trigger Factor can antagonize ...... functions in Escherichia coli.
@ast
Trigger Factor can antagonize ...... functions in Escherichia coli.
@en
type
label
Trigger Factor can antagonize ...... functions in Escherichia coli.
@ast
Trigger Factor can antagonize ...... functions in Escherichia coli.
@en
prefLabel
Trigger Factor can antagonize ...... functions in Escherichia coli.
@ast
Trigger Factor can antagonize ...... functions in Escherichia coli.
@en
P2093
P2860
P356
P1476
Trigger Factor can antagonize ...... functions in Escherichia coli
@en
P2093
Costa Georgopoulos
Debbie Ang
Françoise Schwager
Ronald S Ullers
P2860
P304
P356
10.1073/PNAS.0608232104
P407
P577
2007-02-20T00:00:00Z