Trigger factor depletion or overproduction causes defective cell division but does not block protein export.
about
Signal peptide-dependent protein transport in Bacillus subtilis: a genome-based survey of the secretomeThe complete general secretory pathway in gram-negative bacteriaSelective ribosome profiling reveals the cotranslational chaperone action of trigger factor in vivoGlobal analysis of host response to induction of a latent bacteriophage.High-affinity binding of Escherichia coli SecB to the signal sequence region of a presecretory protein.A role for trigger factor and an rgg-like regulator in the transcription, secretion and processing of the cysteine proteinase of Streptococcus pyogenes.In vivo analysis of the overlapping functions of DnaK and trigger factorMultitasking SecB chaperones in bacteriaA homolog of Bacillus subtilis trigger factor in Listeria monocytogenes is involved in stress tolerance and bacterial virulence.Carbon source-dependent synthesis of SecB, a cytosolic chaperone involved in protein translocation across Escherichia coli membranes.Regulation by proteolysis: energy-dependent proteases and their targets.A little help from my friends: quality control of presecretory proteins in bacteriaThe Clp proteins: proteolysis regulators or molecular chaperones?Inhibition of cell division in hupA hupB mutant bacteria lacking HU protein.Assisted folding of D-glyceraldehyde-3-phosphate dehydrogenase by trigger factor.Analysis of Spo0M function in Bacillus subtilisTrigger factor is induced upon cold shock and enhances viability of Escherichia coli at low temperatures.Functions of the gene products of Escherichia coli.Trigger factor is involved in GroEL-dependent protein degradation in Escherichia coli and promotes binding of GroEL to unfolded proteinsEscherichia coli trigger factor is a prolyl isomerase that associates with nascent polypeptide chains.Early events in preprotein recognition in E. coli: interaction of SRP and trigger factor with nascent polypeptides.Functional analysis of the cyclophilin PpiB role in bacterial cell division.Overexpression of trigger factor prevents aggregation of recombinant proteins in Escherichia coli.The Oenococcus oeni clpX homologue is a heat shock gene preferentially expressed in exponential growth phase.Disruption of the genes for ClpXP protease in Salmonella enterica serovar Typhimurium results in persistent infection in mice, and development of persistence requires endogenous gamma interferon and tumor necrosis factor alpha.Proteome of Salmonella typhimurium SL1344: identification of novel abundant cell envelope proteins and assignment to a two-dimensional reference map.Global Analysis of the Impact of Deleting Trigger Factor on the Transcriptome Profile of Escherichia coli.A ribosome-associated peptidyl-prolyl cis/trans isomerase identified as the trigger factor.Functional dissection of Escherichia coli trigger factor: unraveling the function of individual domains.The Escherichia coli trigger factor.Role of SufI (FtsP) in cell division of Escherichia coli: evidence for its involvement in stabilizing the assembly of the divisome.The early interaction of the outer membrane protein phoe with the periplasmic chaperone Skp occurs at the cytoplasmic membrane.The chaperone activity of trigger factor is distinct from its isomerase activity during co-expression with adenylate kinase in Escherichia coli.Gene expression profiling of Escherichia coli growth transitions: an expanded stringent response model.Chaperone and antichaperone activities of trigger factor.Trigger factor peptidyl-prolyl cis/trans isomerase activity is not essential for the folding of cytosolic proteins in Escherichia coli.Functional characterization of the trigger factor protein PceT of tetrachloroethene-dechlorinating Desulfitobacterium hafniense Y51.High level accumulation of soluble diphtheria toxin mutant (CRM197) with co-expression of chaperones in recombinant Escherichia coli.DnaK promotes the selective export of outer membrane protein precursors in SecA-deficient Escherichia coli.Trigger factor retards protein export in Escherichia coli.
P2860
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P2860
Trigger factor depletion or overproduction causes defective cell division but does not block protein export.
description
1990 nî lūn-bûn
@nan
1990 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած
@hyw
1990 թվականի հոտեմբերին հրատարակված գիտական հոդված
@hy
1990年の論文
@ja
1990年論文
@yue
1990年論文
@zh-hant
1990年論文
@zh-hk
1990年論文
@zh-mo
1990年論文
@zh-tw
1990年论文
@wuu
name
Trigger factor depletion or ov ...... does not block protein export.
@ast
Trigger factor depletion or ov ...... does not block protein export.
@en
Trigger factor depletion or ov ...... does not block protein export.
@nl
type
label
Trigger factor depletion or ov ...... does not block protein export.
@ast
Trigger factor depletion or ov ...... does not block protein export.
@en
Trigger factor depletion or ov ...... does not block protein export.
@nl
prefLabel
Trigger factor depletion or ov ...... does not block protein export.
@ast
Trigger factor depletion or ov ...... does not block protein export.
@en
Trigger factor depletion or ov ...... does not block protein export.
@nl
P2860
P1476
Trigger factor depletion or ov ...... does not block protein export.
@en
P2093
P2860
P304
P356
10.1128/JB.172.10.5555-5562.1990
P407
P577
1990-10-01T00:00:00Z