ProOmpA contains secondary and tertiary structure prior to translocation and is shielded from aggregation by association with SecB protein
about
SecD and SecF are required for the proton electrochemical gradient stimulation of preprotein translocationReversible formation of on-pathway macroscopic aggregates during the folding of maltose binding proteinThe complete general secretory pathway in gram-negative bacteriaProtein secretion and outer membrane assembly in AlphaproteobacteriaKinetic 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.Protein targeting to the bacterial cytoplasmic membrane.PrlA4 prevents the rejection of signal sequence defective preproteins by stabilizing the SecA-SecY interaction during the initiation of translocation.Interactive surface in the PapD chaperone cleft is conserved in pilus chaperone superfamily and essential in subunit recognition and assembly.Translocation can drive the unfolding of a preprotein domain.Structural characterization of the complex of SecB and metallothionein-labeled proOmpA by cryo-electron microscopy.Adhesin presentation in bacteria requires molecular chaperones and ushers.Regions of maltose-binding protein that influence SecB-dependent and SecA-dependent export in Escherichia coliProtein secretion in Bacillus species.Refolding and oriented insertion of a membrane protein into a lipid bilayer.Translocation of a folded protein across the outer membrane in Escherichia coli.A 30-residue-long "export initiation domain" adjacent to the signal sequence is critical for protein translocation across the inner membrane of Escherichia coliImmunoglobulin-like PapD chaperone caps and uncaps interactive surfaces of nascently translocated pilus subunits.The SecA and SecY subunits of translocase are the nearest neighbors of a translocating preprotein, shielding it from phospholipidsThe molecular chaperone SecB is released from the carboxy-terminus of SecA during initiation of precursor protein translocation.Preparation of a highly translocation-competent proOmpA/SecB complex.Selective extracellular release of cholera toxin B subunit by Escherichia coli: dissection of Neisseria Iga beta-mediated outer membrane transport.Preprotein mature domains contain translocase targeting signals that are essential for secretion.Driving Forces of Translocation Through Bacterial Translocon SecYEG.
P2860
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P2860
ProOmpA contains secondary and tertiary structure prior to translocation and is shielded from aggregation by association with SecB protein
description
1990 nî lūn-bûn
@nan
1990 թուականի Յուլիսին հրատարակուած գիտական յօդուած
@hyw
1990 թվականի հուլիսին հրատարակված գիտական հոդված
@hy
1990年の論文
@ja
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
@wuu
name
ProOmpA contains secondary and ...... association with SecB protein
@ast
ProOmpA contains secondary and ...... association with SecB protein
@en
type
label
ProOmpA contains secondary and ...... association with SecB protein
@ast
ProOmpA contains secondary and ...... association with SecB protein
@en
prefLabel
ProOmpA contains secondary and ...... association with SecB protein
@ast
ProOmpA contains secondary and ...... association with SecB protein
@en
P2093
P2860
P1433
P1476
ProOmpA contains secondary and ...... association with SecB protein
@en
P2093
P2860
P304
P407
P577
1990-07-01T00:00:00Z