Export of unprocessed precursor maltose-binding protein to the periplasm of Escherichia coli cells.
about
Structural, functional, and evolutionary relationships among extracellular solute-binding receptors of bacteriaP80, the HinT interacting membrane protein, is a secreted antigen of Mycoplasma hominisA Target-Based Whole Cell Screen Approach To Identify Potential Inhibitors of Mycobacterium tuberculosis Signal PeptidaseThe complete general secretory pathway in gram-negative bacteriaExtracellular transport of VirG protein in Shigella.Export of maltose-binding protein species with altered charge distribution surrounding the signal peptide hydrophobic core in Escherichia coli cells harboring prl suppressor mutations.An Escherichia coli mutation preventing degradation of abnormal periplasmic proteins.The SecB chaperone is involved in the secretion of the Serratia marcescens HasA protein through an ABC transporter.Green fluorescent protein functions as a reporter for protein localization in Escherichia coli.Maltose transport in membrane vesicles of Escherichia coli is linked to ATP hydrolysisUncoupling substrate transport from ATP hydrolysis in the Escherichia coli maltose transporter.Molecular and functional analysis of the lepB gene, encoding a type I signal peptidase from Rickettsia rickettsii and Rickettsia typhi.Tromp1, a putative rare outer membrane protein, is anchored by an uncleaved signal sequence to the Treponema pallidum cytoplasmic membrane.Regulation by proteolysis: energy-dependent proteases and their targets.Effects of temperature on Escherichia coli overproducing beta-lactamase or human epidermal growth factor.Evidence for high affinity binding-protein dependent transport systems in gram-positive bacteria and in MycoplasmaSelection of functional signal peptide cleavage sites from a library of random sequencesAlterations in the hydrophilic segment of the maltose-binding protein (MBP) signal peptide that affect either export or translation of MBP.The folding properties of the Escherichia coli maltose-binding protein influence its interaction with SecB in vitro.Active transport of maltose in membrane vesicles obtained from Escherichia coli cells producing tethered maltose-binding proteinAnalysis of mutational alterations in the hydrophilic segment of the maltose-binding protein signal peptide.Mutations that improve export of maltose-binding protein in SecB- cells of Escherichia coli.Nucleotide sequence of the iucD gene of the pColV-K30 aerobactin operon and topology of its product studied with phoA and lacZ gene fusionsSecB-independent export of Escherichia coli ribose-binding protein (RBP): some comparisons with export of maltose-binding protein (MBP) and studies with RBP-MBP hybrid proteins.Two regions of mature periplasmic maltose-binding protein of Escherichia coli involved in secretionMutational alterations affecting the export competence of a truncated but fully functional maltose-binding protein signal peptideDetermination of the binding frame within a physiological ligand for the chaperone SecB.Interaction of SecB with intermediates along the folding pathway of maltose-binding protein.The chemistry and enzymology of the type I signal peptidasesFull engagement of liganded maltose-binding protein stabilizes a semi-open ATP-binding cassette dimer in the maltose transporterCloning and nucleotide sequence of the pvdA gene encoding the pyoverdin biosynthetic enzyme L-ornithine N5-oxygenase in Pseudomonas aeruginosaAbility of MBP or RBP signal peptides to influence folding and in vitro translocation of wild-type and hybrid precursors.Folding-based suppression of extracytoplasmic toxicity conferred by processing-defective LamB.Maltose-binding protein is open in the catalytic transition state for ATP hydrolysis during maltose transport.Two modes of ligand binding in maltose-binding protein of Escherichia coli. Functional significance in active transport.Maltose-binding protein containing an interdomain disulfide bridge confers a dominant-negative phenotype for transport and chemotaxis.Membrane association and multimerization of secreton component pulCSignal sequence mutations as tools for the characterization of LamB folding intermediates.A mutation in either dsbA or dsbB, a gene encoding a component of a periplasmic disulfide bond-catalyzing system, is required for high-level expression of the Bacteroides fragilis metallo-beta-lactamase, CcrA, in Escherichia coli.Defective export in Escherichia coli caused by DsbA'-PhoA hybrid proteins whose DsbA' domain cannot fold into a conformation resistant to periplasmic proteases
P2860
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P2860
Export of unprocessed precursor maltose-binding protein to the periplasm of Escherichia coli cells.
description
1987 nî lūn-bûn
@nan
1987年の論文
@ja
1987年学术文章
@wuu
1987年学术文章
@zh-cn
1987年学术文章
@zh-hans
1987年学术文章
@zh-my
1987年学术文章
@zh-sg
1987年學術文章
@yue
1987年學術文章
@zh
1987年學術文章
@zh-hant
name
Export of unprocessed precurso ...... asm of Escherichia coli cells.
@ast
Export of unprocessed precurso ...... asm of Escherichia coli cells.
@en
type
label
Export of unprocessed precurso ...... asm of Escherichia coli cells.
@ast
Export of unprocessed precurso ...... asm of Escherichia coli cells.
@en
prefLabel
Export of unprocessed precurso ...... asm of Escherichia coli cells.
@ast
Export of unprocessed precurso ...... asm of Escherichia coli cells.
@en
P2860
P1476
Export of unprocessed precurso ...... asm of Escherichia coli cells.
@en
P2093
P J Bassford
P2860
P304
P356
10.1128/JB.169.6.2352-2359.1987
P407
P577
1987-06-01T00:00:00Z