A ribosome-associated peptidyl-prolyl cis/trans isomerase identified as the trigger factor.
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Interconversion of red opsin isoforms by the cyclophilin-related chaperone protein Ran-binding protein 2Promiscuous Substrate Recognition in Folding and Assembly Activities of the Trigger Factor ChaperoneFK506-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 proteinsChaperone domains convert prolyl isomerases into generic catalysts of protein folding.Identification of a potential hydrophobic peptide binding site in the C-terminal arm of trigger factor.Classification of rice (Oryza sativa L. Japonica nipponbare) immunophilins (FKBPs, CYPs) and expression patterns under water stress.A role for trigger factor and an rgg-like regulator in the transcription, secretion and processing of the cysteine proteinase of Streptococcus pyogenes.Binding specificity of Escherichia coli trigger factor.Transcriptional regulation of the cpr gene cluster in ortho-chlorophenol-respiring Desulfitobacterium dehalogenansCatalysis of cis/trans isomerization in native HIV-1 capsid by human cyclophilin AQuantitative proteomic analysis of cell cycle of the dinoflagellate Prorocentrum donghaiense (Dinophyceae).Dimeric Structure of the Bacterial Extracellular Foldase PrsA.Cross-linking measurements of in vivo protein complex topologies.Involvement of the DnaK-DnaJ-GrpE chaperone team in protein secretion in Escherichia coliCarbon source-dependent synthesis of SecB, a cytosolic chaperone involved in protein translocation across Escherichia coli membranes.Protein secretion and surface display in Gram-positive bacteria.Secretion genes as determinants of Bacillus anthracis chain length.Assisted folding of D-glyceraldehyde-3-phosphate dehydrogenase by trigger factor.Biogenesis of respiratory cytochromes in bacteria.Trigger factor is induced upon cold shock and enhances viability of Escherichia coli at low temperatures.Comprehensive analysis of the effects of Escherichia coli ORFs on protein translation reactionThe crystal structure of ribosomal chaperone trigger factor from Vibrio cholerae.Escherichia coli trigger factor is a prolyl isomerase that associates with nascent polypeptide chains.FKBP10 depletion enhances glucocerebrosidase proteostasis in Gaucher disease fibroblasts.Overexpression of trigger factor prevents aggregation of recombinant proteins in Escherichia coli.Biochemical and genetic characterization of an FK506-sensitive peptidyl prolyl cis-trans isomerase from a thermophilic archaeon, Methanococcus thermolithotrophicus.FK506 binding protein from the hyperthermophilic archaeon Pyrococcus horikoshii suppresses the aggregation of proteins in Escherichia coli.The YSIRK-G/S motif of staphylococcal protein A and its role in efficiency of signal peptide processing.Biochemical and functional analyses of the Mip protein: influence of the N-terminal half and of peptidylprolyl isomerase activity on the virulence of Legionella pneumophila.Proteome of Salmonella typhimurium SL1344: identification of novel abundant cell envelope proteins and assignment to a two-dimensional reference map.Acceleration of protein folding by four orders of magnitude through a single amino acid substitution.Functional dissection of Escherichia coli trigger factor: unraveling the function of individual domains.You got to know when to hold (or unfold) 'em….Trigger factor chaperone acts as a mechanical foldase.Metal-dependent nucleotide binding to the Escherichia coli rotamase SlyD.Aspergillus oryzae CsyB catalyzes the condensation of two β-ketoacyl-CoAs to form 3-acetyl-4-hydroxy-6-alkyl-α-pyroneInterplay of signal recognition particle and trigger factor at L23 near the nascent chain exit site on the Escherichia coli ribosome.Effective cotranslational folding of firefly luciferase without chaperones of the Hsp70 family.An RpoS-dependent sRNA regulates the expression of a chaperone involved in protein foldingRole of the DnaK and HscA homologs of Hsp70 chaperones in protein folding in E.coli.
P2860
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P2860
A ribosome-associated peptidyl-prolyl cis/trans isomerase identified as the trigger factor.
description
1995 nî lūn-bûn
@nan
1995年の論文
@ja
1995年学术文章
@wuu
1995年学术文章
@zh-cn
1995年学术文章
@zh-hans
1995年学术文章
@zh-my
1995年学术文章
@zh-sg
1995年學術文章
@yue
1995年學術文章
@zh
1995年學術文章
@zh-hant
name
A ribosome-associated peptidyl ...... ntified as the trigger factor.
@en
type
label
A ribosome-associated peptidyl ...... ntified as the trigger factor.
@en
prefLabel
A ribosome-associated peptidyl ...... ntified as the trigger factor.
@en
P2093
P2860
P1433
P1476
A ribosome-associated peptidyl ...... entified as the trigger factor
@en
P2093
Nierhaus KH
Rahfeld JU
Rücknagel KP
P2860
P304
P356
10.1002/J.1460-2075.1995.TB00177.X
P407
P577
1995-10-01T00:00:00Z