The folding properties of the Escherichia coli maltose-binding protein influence its interaction with SecB in vitro.
about
The complete general secretory pathway in gram-negative bacteriaExport of maltose-binding protein species with altered charge distribution surrounding the signal peptide hydrophobic core in Escherichia coli cells harboring prl suppressor mutations.Laboratory evolution of fast-folding green fluorescent protein using secretory pathway quality control.The SecB chaperone is involved in the secretion of the Serratia marcescens HasA protein through an ABC transporter.A signal sequence is not required for protein export in prlA mutants of Escherichia coliProduction of active chimeric pediocin AcH in Escherichia coli in the absence of processing and secretion genes from the Pediococcus pap operon.Carbon source-dependent synthesis of SecB, a cytosolic chaperone involved in protein translocation across Escherichia coli membranes.Binding of SecB to ribosome-bound polypeptides has the same characteristics as binding to full-length, denatured proteins.PrlA and PrlG suppressors reduce the requirement for signal sequence recognitionSecB-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.Determination of the binding frame within a physiological ligand for the chaperone SecB.Calorimetric analyses of the interaction between SecB and its ligandsStromal factor plays an essential role in protein integration into thylakoids that cannot be replaced by unfolding or by heat shock protein Hsp70Protein secretion in Bacillus species.SecB--a chaperone dedicated to protein translocation.Ability of MBP or RBP signal peptides to influence folding and in vitro translocation of wild-type and hybrid precursors.Involvement of SecB, a chaperone, in the export of ribose-binding protein.The amino terminus of the F1-ATPase beta-subunit precursor functions as an intramolecular chaperone to facilitate mitochondrial protein importElectron spin resonance and fluorescence studies of the bound-state conformation of a model protein substrate to the chaperone SecB.The Sec System: Protein Export in Escherichia coli.Efficient insertion of odd-numbered transmembrane segments of the tetracycline resistance protein requires even-numbered segments.
P2860
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P2860
The folding properties of the Escherichia coli maltose-binding protein influence its interaction with SecB in vitro.
description
1990 nî lūn-bûn
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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
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name
The folding properties of the ...... nteraction with SecB in vitro.
@ast
The folding properties of the ...... nteraction with SecB in vitro.
@en
type
label
The folding properties of the ...... nteraction with SecB in vitro.
@ast
The folding properties of the ...... nteraction with SecB in vitro.
@en
prefLabel
The folding properties of the ...... nteraction with SecB in vitro.
@ast
The folding properties of the ...... nteraction with SecB in vitro.
@en
P2860
P1476
The folding properties of the ...... nteraction with SecB in vitro.
@en
P2093
P J Bassford
P2860
P304
P356
10.1128/JB.172.6.3023-3029.1990
P407
P577
1990-06-01T00:00:00Z