about
Signal peptide-dependent protein transport in Bacillus subtilis: a genome-based survey of the secretomeThe crystal structure of the ttCsaA protein: an export-related chaperone from Thermus thermophilus.Structural basis for the antifolding activity of a molecular chaperoneCellular disulfide bond formation in bioactive peptides and proteinsBiophysical characterization of the influence of salt on tetrameric SecB.Strategies for successful recombinant expression of disulfide bond-dependent proteins in Escherichia coli.Functional characterization of recombinant chloroplast signal recognition particle.ClpS is an essential component of the N-end rule pathway in Escherichia coli.A scFv antibody mutant isolated in a genetic screen for improved export via the twin arginine transporter pathway exhibits faster folding.Studying protein-protein interactions using peptide arrays.Bacterial protein translocase: a unique molecular machine with an army of substrates.Lon protease quality control of presecretory proteins in Escherichia coli and its dependence on the SecB and DnaJ (Hsp40) chaperones.Coherent membrane supports for parallel microsynthesis and screening of bioactive peptides.Recognition between flexible protein molecules: induced and assisted folding.SecB is a bona fide generalized chaperone in Escherichia coliStructural characterization of the complex of SecB and metallothionein-labeled proOmpA by cryo-electron microscopy.The structural view of bacterial translocation-specific chaperone SecB: implications for function.Multitasking SecB chaperones in bacteriaAsp2 and Asp3 interact directly with GspB, the export substrate of the Streptococcus gordonii accessory Sec SystemLarge-scale evolutionary analyses on SecB subunits of bacterial sec system.Ligand recognition specificity of leukocyte integrin αMβ2 (Mac-1, CD11b/CD18) and its functional consequences.Trigger Factor can antagonize both SecB and DnaK/DnaJ chaperone functions in Escherichia coli.Position-dependent effects of polylysine on Sec protein transportA little help from my friends: quality control of presecretory proteins in bacteriaSec-dependent protein translocation across biological membranes: evolutionary conservation of an essential protein transport pathway (review).New Escherichia coli outer membrane proteins identified through prediction and experimental verificationCellulose-bound peptide arrays: preparation and applications.Secretion of GOB metallo-beta-lactamase in Escherichia coli depends strictly on the cooperation between the cytoplasmic DnaK chaperone system and the Sec machinery: completion of folding and Zn(II) ion acquisition occur in the bacterial periplasm.SecB--a chaperone dedicated to protein translocation.Using peptides to study protein-protein interactions.Coupling between codon usage, translation and protein export in Escherichia coli.Proteomic methods unravel the protein quality control in Escherichia coli.Breaking on through to the other side: protein export through the bacterial Sec system.The Sec translocon mediated protein transport in prokaryotes and eukaryotes.SecB dependence of an exported protein is a continuum influenced by the characteristics of the signal peptide or early mature region.Multiple binding sites in fibrinogen for integrin alphaMbeta2 (Mac-1).Determination of the intracellular concentration of the export chaperone SecB in Escherichia coli.A script to highlight hydrophobicity and charge on protein surfaces.Structure and conservation of the periplasmic targeting factor Tic22 protein from plants and cyanobacteria.Utilizing peptide SPOT arrays to identify protein interactions.
P2860
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P2860
description
1999 nî lūn-bûn
@nan
1999 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած
@hyw
1999 թվականի նոյեմբերին հրատարակված գիտական հոդված
@hy
1999年の論文
@ja
1999年論文
@yue
1999年論文
@zh-hant
1999年論文
@zh-hk
1999年論文
@zh-mo
1999年論文
@zh-tw
1999年论文
@wuu
name
Substrate specificity of the SecB chaperone.
@ast
Substrate specificity of the SecB chaperone.
@en
type
label
Substrate specificity of the SecB chaperone.
@ast
Substrate specificity of the SecB chaperone.
@en
prefLabel
Substrate specificity of the SecB chaperone.
@ast
Substrate specificity of the SecB chaperone.
@en
P2093
P2860
P356
P1476
Substrate specificity of the SecB chaperone.
@en
P2093
Driessen AJ
Knoblauch NT
Schneider-Mergener J
Schönfeld HJ
P2860
P304
34219-34225
P356
10.1074/JBC.274.48.34219
P407
P577
1999-11-01T00:00:00Z