The secD locus of E.coli codes for two membrane proteins required for protein export.
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Comparative Genomic Analysis of Chlamydia trachomatis Oculotropic and Genitotropic StrainsSecD and SecF are required for the proton electrochemical gradient stimulation of preprotein translocationThe Sec-dependent pathwayThe complete general secretory pathway in gram-negative bacteriaKinetic analysis of the assembly of the outer membrane protein LamB in Escherichia coli mutants each lacking a secretion or targeting factor in a different cellular compartment.Cloning and sequencing of yajC and secD homologs of Brucella abortus and demonstration of immune responses to YajC in mice vaccinated with B. abortus RB51Molecular characterization of IS1541 insertions in the genome of Yersinia pestis.Identification of a sequence motif that confers SecB dependence on a SecB-independent secretory protein in vivo.Distinct catalytic roles of the SecYE, SecG and SecDFyajC subunits of preprotein translocase holoenzyme.The SecDFyajC domain of preprotein translocase controls preprotein movement by regulating SecA membrane cycling.The Cs sec mutants of Escherichia coli reflect the cold sensitivity of protein export itself.Translocation can drive the unfolding of a preprotein domain.A novel membrane protein involved in protein translocation across the cytoplasmic membrane of Escherichia coli.Mutations in Flavobacterium johnsoniae secDF result in defects in gliding motility and chitin utilizationArchaeal and bacterial SecD and SecF homologs exhibit striking structural and functional conservation.SecA proteins of Bacillus subtilis and Escherichia coli possess homologous amino-terminal ATP-binding domains regulating integration into the plasma membraneThe bacterial Sec-translocase: structure and mechanism.One of three transmembrane stretches is sufficient for the functioning of the SecE protein, a membrane component of the E. coli secretion machinery.Gene regulation of plasmid- and chromosome-determined inorganic ion transport in bacteriaA mutation of Escherichia coli SecA protein that partially compensates for the absence of SecB.Genetic and molecular characterization of the Escherichia coli secD operon and its productsIn vivo studies of the role of SecA during protein export in Escherichia coliExport of the outer membrane lipoprotein is defective in secD, secE, and secF mutants of Escherichia coli.Regions of maltose-binding protein that influence SecB-dependent and SecA-dependent export in Escherichia coliCytochromes c biogenesis in a photosynthetic bacterium requires a periplasmic thioredoxin-like proteinRegulation of Escherichia coli secA mRNA translation by a secretion-responsive element.SecA protein is required for translocation of a model precursor protein into inverted vesicles of Escherichia coli plasma membrane.Protein secretion in Bacillus species.Genetic suppressors and recovery of repressed biochemical memory.Reconstitution of a protein translocation system containing purified SecY, SecE, and SecA from Escherichia coli.SecD and SecF facilitate protein export in Escherichia coli.Disruption of the gene encoding p12 (SecG) reveals the direct involvement and important function of SecG in the protein translocation of Escherichia coli at low temperature.SecD is involved in the release of translocated secretory proteins from the cytoplasmic membrane of Escherichia coli.Preprotein translocation by a hybrid translocase composed of Escherichia coli and Bacillus subtilis subunits.Multicopy suppression of cold-sensitive sec mutations in Escherichia coli.Sequence analysis and overexpression of the Zymomonas mobilis tgt gene encoding tRNA-guanine transglycosylase: purification and biochemical characterization of the enzyme.SecF stabilizes SecD and SecY, components of the protein translocation machinery of the Escherichia coli cytoplasmic membrane.Multicopy suppression: an approach to understanding intracellular functioning of the protein export system.Alignment of genes from the 9-minute region (araJ to tsx) of the Escherichia coli K-12 linkage map to the physical map.Processing of lipid-modified prolipoprotein requires energy and sec gene products in vivo.
P2860
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P2860
The secD locus of E.coli codes for two membrane proteins required for protein export.
description
1990 nî lūn-bûn
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1990 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած
@hyw
1990 թվականի հոտեմբերին հրատարակված գիտական հոդված
@hy
1990年の論文
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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
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name
The secD locus of E.coli codes for two membrane proteins required for protein export.
@ast
The secD locus of E.coli codes for two membrane proteins required for protein export.
@en
type
label
The secD locus of E.coli codes for two membrane proteins required for protein export.
@ast
The secD locus of E.coli codes for two membrane proteins required for protein export.
@en
prefLabel
The secD locus of E.coli codes for two membrane proteins required for protein export.
@ast
The secD locus of E.coli codes for two membrane proteins required for protein export.
@en
P2093
P2860
P1433
P1476
The secD locus of E.coli codes for two membrane proteins required for protein export.
@en
P2093
P2860
P304
P407
P577
1990-10-01T00:00:00Z