Three pure chaperone proteins of Escherichia coli--SecB, trigger factor and GroEL--form soluble complexes with precursor proteins in vitro.
about
SecD and SecF are required for the proton electrochemical gradient stimulation of preprotein translocationA microbial sensor for discovering structural probes of protein misfolding and aggregationFimC is a periplasmic PapD-like chaperone that directs assembly of type 1 pili in bacteriaSeveral proteins imported into chloroplasts form stable complexes with the GroEL-related chloroplast molecular chaperoneReversible formation of on-pathway macroscopic aggregates during the folding of maltose binding proteinMultiple roles of the pilus biogenesis protein pilD: involvement of pilD in excretion of enzymes from Pseudomonas aeruginosaThe complete general secretory pathway in gram-negative bacteriaCloning and characterization of the groESL operon from Bacillus subtilis.Protein targeting to the bacterial cytoplasmic membrane.Dimeric SecA couples the preprotein translocation in an asymmetric manner.Identification of a groES-like chaperonin in mitochondria that facilitates protein folding.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 proteinInteractive surface in the PapD chaperone cleft is conserved in pilus chaperone superfamily and essential in subunit recognition and assembly.Catabolic repression of secB expression is positively controlled by cyclic AMP (cAMP) receptor protein-cAMP complexes at the transcriptional levelTranslocation can drive the unfolding of a preprotein domain.Sec-dependent protein export and the involvement of the molecular chaperone SecB.Trigger factor depletion or overproduction causes defective cell division but does not block protein export.Asp3 mediates multiple protein-protein interactions within the accessory Sec system of Streptococcus gordonii.Detergent disruption of bacterial inner membranes and recovery of protein translocation activity.Major stable peptides of Yersinia pestis synthesized during the low-calcium responseHuman and guinea pig immune responses to Legionella pneumophila protein antigens OmpS and Hsp60.Multitasking SecB chaperones in bacteriaLegionella pneumophila htpAB heat shock operon: nucleotide sequence and expression of the 60-kilodalton antigen in L. pneumophila-infected HeLa cells.Use of starvation promoters to limit growth and selectively enrich expression of trichloroethylene- and phenol-transforming activity in recombinant Escherichia coli [corrected]Adhesin presentation in bacteria requires molecular chaperones and ushers.pH-regulated activation and release of a bacteria-associated phospholipase C during intracellular infection by Listeria monocytogenes.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.Regulation by proteolysis: energy-dependent proteases and their targets.Characterization of the Heat Shock Response in Lactococcus lactis subsp. lactis.Targeting of GroEL to SecA on the cytoplasmic membrane of Escherichia coliThe bacterial Sec-translocase: structure and mechanism.The Trigger Factor Chaperone Encapsulates and Stabilizes Partial Folds of Substrate Proteins.In vitro interactions of the aphid endosymbiotic SymL chaperonin with barley yellow dwarf virus.Heat-shock proteins can substitute for SecB function during protein export in Escherichia coli.A little help from my friends: quality control of presecretory proteins in bacteriaBinding of SecB to ribosome-bound polypeptides has the same characteristics as binding to full-length, denatured proteins.Structures of chaperonins from an intracellular symbiont and their functional expression in Escherichia coli groE mutantsExport of the outer membrane lipoprotein is defective in secD, secE, and secF mutants of Escherichia coli.
P2860
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P2860
Three pure chaperone proteins of Escherichia coli--SecB, trigger factor and GroEL--form soluble complexes with precursor proteins in vitro.
description
1989 nî lūn-bûn
@nan
1989 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած
@hyw
1989 թվականի սեպտեմբերին հրատարակված գիտական հոդված
@hy
1989年の論文
@ja
1989年論文
@yue
1989年論文
@zh-hant
1989年論文
@zh-hk
1989年論文
@zh-mo
1989年論文
@zh-tw
1989年论文
@wuu
name
Three pure chaperone proteins ...... h precursor proteins in vitro.
@ast
Three pure chaperone proteins ...... h precursor proteins in vitro.
@en
Three pure chaperone proteins ...... h precursor proteins in vitro.
@nl
type
label
Three pure chaperone proteins ...... h precursor proteins in vitro.
@ast
Three pure chaperone proteins ...... h precursor proteins in vitro.
@en
Three pure chaperone proteins ...... h precursor proteins in vitro.
@nl
prefLabel
Three pure chaperone proteins ...... h precursor proteins in vitro.
@ast
Three pure chaperone proteins ...... h precursor proteins in vitro.
@en
Three pure chaperone proteins ...... h precursor proteins in vitro.
@nl
P2093
P2860
P1433
P1476
Three pure chaperone proteins ...... h precursor proteins in vitro.
@en
P2093
Bassford PJ Jr
Georgopoulos C
Kumamoto CA
Ziegelhoffer T
P2860
P304
P407
P577
1989-09-01T00:00:00Z