Trigger factor: a soluble protein that folds pro-OmpA into a membrane-assembly-competent form - Wikidata - wikimedia - TriplyDB

Trigger factor: a soluble protein that folds pro-OmpA into a membrane-assembly-competent form

Trigger factor: a soluble protein that folds pro-OmpA into a membrane-assembly-competent form

http://www.wikidata.org/entity/Q34333215

about

SecD and SecF are required for the proton electrochemical gradient stimulation of preprotein translocation The Sec-dependent pathway Promiscuous Substrate Recognition in Folding and Assembly Activities of the Trigger Factor Chaperone The complete general secretory pathway in gram-negative bacteria Insights into the structure and assembly of Escherichia coli outer membrane protein A Selective ribosome profiling reveals the cotranslational chaperone action of trigger factor in vivo Rotational restriction of nascent peptides as an essential element of co-translational protein folding: possible molecular players and structural consequences.Chaperone domains convert prolyl isomerases into generic catalysts of protein folding.SecA protein, a peripheral protein of the Escherichia coli plasma membrane, is essential for the functional binding and translocation of proOmpA.Three pure chaperone proteins of Escherichia coli--SecB, trigger factor and GroEL--form soluble complexes with precursor proteins in vitro.SecA suppresses the temperature-sensitive SecY24 defect in protein translocation in Escherichia coli membrane vesicles.Purified secB protein of Escherichia coli retards folding and promotes membrane translocation of the maltose-binding protein in vitro.PrlA4 prevents the rejection of signal sequence defective preproteins by stabilizing the SecA-SecY interaction during the initiation of translocation.A role for trigger factor and an rgg-like regulator in the transcription, secretion and processing of the cysteine proteinase of Streptococcus pyogenes.ProOmpA contains secondary and tertiary structure prior to translocation and is shielded from aggregation by association with SecB protein The secD locus of E.coli codes for two membrane proteins required for protein export.Lon protease quality control of presecretory proteins in Escherichia coli and its dependence on the SecB and DnaJ (Hsp40) chaperones.Translocation can drive the unfolding of a preprotein domain.Trigger factor depletion or overproduction causes defective cell division but does not block protein export.In vivo analysis of the overlapping functions of DnaK and trigger factor Specific recognition of the leader region of precursor proteins is required for the activation of translocation ATPase of Escherichia coli.Detergent disruption of bacterial inner membranes and recovery of protein translocation activity.Physiological role during export for the retardation of folding by the leader peptide of maltose-binding protein.Immunoproteomic identification of immunogenic proteins in Cronobacter sakazakii strain BAA-894.Multitasking SecB chaperones in bacteria Trigger factor-mediated prolyl isomerization influences maturation of the Streptococcus pyogenes cysteine protease.Revisiting the interaction between the chaperone Skp and lipopolysaccharide Carbon source-dependent synthesis of SecB, a cytosolic chaperone involved in protein translocation across Escherichia coli membranes.A little help from my friends: quality control of presecretory proteins in bacteria The folding properties of the Escherichia coli maltose-binding protein influence its interaction with SecB in vitro.The mature portion of Escherichia coli maltose-binding protein (MBP) determines the dependence of MBP on SecB for export.Temperature-dependent insertion of prolipoprotein into Escherichia coli membrane vesicles and requirements for ATP, soluble factors, and functional SecY protein for the overall translocation process.Mutations that improve export of maltose-binding protein in SecB- cells of Escherichia coli.Requirement of heat-labile cytoplasmic protein factors for posttranslational translocation of OmpA protein precursors into Escherichia coli membrane vesicles.Synthesis of an Escherichia coli protein carrying a signal peptide mutation causes depolarization of the cytoplasmic membrane potential.In vitro insertion of leader peptidase into Escherichia coli membrane vesicles.Role of the leader peptide of maltose-binding protein in two steps of the export process Electrochemical potential releases a membrane-bound secretion intermediate of maltose-binding protein in Escherichia coli Interaction of SecB with intermediates along the folding pathway of maltose-binding protein.Assisted folding of D-glyceraldehyde-3-phosphate dehydrogenase by trigger factor.

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P2860

Trigger factor: a soluble protein that folds pro-OmpA into a membrane-assembly-competent form

http://www.wikidata.org/entity/Q34333215

description

1987 nî lūn-bûn

@nan

1987 թուականի Օգոստոսին հրատարակուած գիտական յօդուած

@hyw

1987 թվականի օգոստոսին հրատարակված գիտական հոդված

@hy

1987年の論文

@ja

1987年論文

@yue

1987年論文

@zh-hant

1987年論文

@zh-hk

1987年論文

@zh-mo

1987年論文

@zh-tw

1987年论文

@wuu

name

Trigger factor: a soluble prot ...... mbrane-assembly-competent form

@ast

Trigger factor: a soluble prot ...... mbrane-assembly-competent form

@en

Trigger factor: a soluble prot ...... mbrane-assembly-competent form

@nl

type

label

Trigger factor: a soluble prot ...... mbrane-assembly-competent form

@ast

Trigger factor: a soluble prot ...... mbrane-assembly-competent form

@en

Trigger factor: a soluble prot ...... mbrane-assembly-competent form

@nl

prefLabel

Trigger factor: a soluble prot ...... mbrane-assembly-competent form

@ast

Trigger factor: a soluble prot ...... mbrane-assembly-competent form

@en

Trigger factor: a soluble prot ...... mbrane-assembly-competent form

@nl

P1433

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P1476

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P2860

Q34333215-074E779E-EB8C-4BCE-BA53-0312A37B83CC

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P31

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P356

Q34333215-F1813950-20EC-430A-BB4F-9B0210D4A10E

P407

Q34333215-BB1C051D-0B36-4D38-B64E-B91A5579511B

P433

Q34333215-01BA2F6B-7CC7-408A-904E-D39E5F6D3A39

P478

Q34333215-AA9DD273-C00C-496A-AA96-7CAAF5A54C11

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Q34333215-CFCB6EF2-CB85-40F0-93EF-E16FB8367603

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Q34333215-6A76D626-EEB4-4D36-923E-AC6B4BC0C7B1

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P921

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P932

Q34333215-4864D874-C834-492C-92C0-0530E5274061

P356

PNAS.84.15.5216

P1433

Proceedings of the National Academy of Sciences of the United States of America

P1476

Trigger factor: a soluble prot ...... mbrane-assembly-competent form

@en

P2093

E Crooke

http://www.w3.org/2001/XMLSchema#string

W Wickner

http://www.w3.org/2001/XMLSchema#string

P2860

Protein measurement with the Folin phenol reagent

Correlation of competence for export with lack of tertiary structure of the mature species: a study in vivo of maltose-binding protein in E. coli

Trans-membrane translocation of proteins. The direct transfer model.

A purified precursor polypeptide requires a cytosolic protein fraction for import into mitochondria.

Both ATP and the electrochemical potential are required for optimal assembly of pro-OmpA into Escherichia coli inner membrane vesicles

Transfer of proteins across membranes. II. Reconstitution of functional rough microsomes from heterologous components.

Translocation of proteins across the endoplasmic reticulum III. Signal recognition protein (SRP) causes signal sequence-dependent and site-specific arrest of chain elongation that is released by microsomal membranes.

Alkaline phosphatase and OmpA protein can be translocated posttranslationally into membrane vesicles of Escherichia coli.

Energy-requiring translocation of the OmpA protein and alkaline phosphatase of Escherichia coli into inner membrane vesicles

Primary structure of major outer membrane protein II (ompA protein) of Escherichia coli K-12.

P304

5216-5220

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P31

scholarly article

P356

10.1073/PNAS.84.15.5216

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P407

P433

15

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P478

84

http://www.w3.org/2001/XMLSchema#string

P577

1987-08-01T00:00:00Z

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P5875

19857695

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P698

3299381

http://www.w3.org/2001/XMLSchema#string

P921

protein folding

P932

298825

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