Modulation of folding pathways of exported proteins by the leader sequence
about
SecD and SecF are required for the proton electrochemical gradient stimulation of preprotein translocationThe Sec-dependent pathwayThe complete general secretory pathway in gram-negative bacteriaSubstrate specificity of the SecB chaperone.SecA-dependent quality control of intracellular protein localization.Protein targeting to the bacterial cytoplasmic membrane.Tight folding of a passenger protein can interfere with the targeting function of a mitochondrial presequence.Three pure chaperone proteins of Escherichia coli--SecB, trigger factor and GroEL--form soluble complexes with precursor proteins in vitro.The structure of multiple polypeptide domains determines the signal recognition particle targeting requirement of Escherichia coli inner membrane proteins.Signal peptides are allosteric activators of the protein translocase.Purified secB protein of Escherichia coli retards folding and promotes membrane translocation of the maltose-binding protein in vitro.Identification of a sequence motif that confers SecB dependence on a SecB-independent secretory protein in vivo.The Tat protein export pathway.Peculiar properties of DsbA in its export across the Escherichia coli cytoplasmic membraneProOmpA contains secondary and tertiary structure prior to translocation and is shielded from aggregation by association with SecB proteinEscherichia coli translocase: the unravelling of a molecular machine.Translocation can drive the unfolding of a preprotein domain.A signal sequence is not required for protein export in prlA mutants of Escherichia coliAmino acid residues important for folding of thioredoxin are revealed only by study of the physiologically relevant reduced form of the protein.Specific recognition of the leader region of precursor proteins is required for the activation of translocation ATPase of Escherichia coli.Physiological role during export for the retardation of folding by the leader peptide of maltose-binding protein.Folding of a mutant maltose-binding protein of Escherichia coli which forms inclusion bodies.Escherichia coli alkaline phosphatase localized to the cytoplasm slowly acquires enzymatic activity in cells whose growth has been suspended: a caution for gene fusion studies.Glycine residues in the hydrophobic core of the GspB signal sequence route export toward the accessory Sec pathway.Targeting of signal sequenceless proteins for export in Escherichia coli with altered protein translocase.PrlA and PrlG suppressors reduce the requirement for signal sequence recognitionThe folding properties of the Escherichia coli maltose-binding protein influence its interaction with SecB in vitro.Mutations that improve export of maltose-binding protein in SecB- cells of Escherichia coli.Sec-dependent protein translocation across biological membranes: evolutionary conservation of an essential protein transport pathway (review).Role of the leader peptide of maltose-binding protein in two steps of the export processEscherichia coli alkaline phosphatase fails to acquire disulfide bonds when retained in the cytoplasmComprehensive Spatial Analysis of the Borrelia burgdorferi Lipoproteome Reveals a Compartmentalization Bias toward the Bacterial SurfaceInteraction of SecB with intermediates along the folding pathway of maltose-binding protein.prl mutations in the Escherichia coli secG gene.Mitochondrial import and processing of mutant human ornithine transcarbamylase precursors in cultured cellsProtein transport across the parasitophorous vacuole of Plasmodium falciparum: into the great wide open.Insertion of proteins into bacterial membranes: mechanism, characteristics, and comparisons with the eucaryotic process.Protein secretion in Bacillus species.Involvement of a chloroplast HSP70 heat shock protein in the integration of a protein (light-harvesting complex protein precursor) into the thylakoid membrane.Identification of a post-targeting step required for efficient cotranslational translocation of proteins across the Escherichia coli inner membrane.
P2860
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P2860
Modulation of folding pathways of exported proteins by the leader sequence
description
1988 nî lūn-bûn
@nan
1988 թուականի Փետրուարին հրատարակուած գիտական յօդուած
@hyw
1988 թվականի փետրվարին հրատարակված գիտական հոդված
@hy
1988年の論文
@ja
1988年論文
@yue
1988年論文
@zh-hant
1988年論文
@zh-hk
1988年論文
@zh-mo
1988年論文
@zh-tw
1988年论文
@wuu
name
Modulation of folding pathways of exported proteins by the leader sequence
@ast
Modulation of folding pathways of exported proteins by the leader sequence
@en
Modulation of folding pathways of exported proteins by the leader sequence
@nl
type
label
Modulation of folding pathways of exported proteins by the leader sequence
@ast
Modulation of folding pathways of exported proteins by the leader sequence
@en
Modulation of folding pathways of exported proteins by the leader sequence
@nl
prefLabel
Modulation of folding pathways of exported proteins by the leader sequence
@ast
Modulation of folding pathways of exported proteins by the leader sequence
@en
Modulation of folding pathways of exported proteins by the leader sequence
@nl
P2093
P3181
P356
P1433
P1476
Modulation of folding pathways of exported proteins by the leader sequence
@en
P2093
P304
P3181
P356
10.1126/SCIENCE.3278378
P407
P577
1988-02-26T00:00:00Z