Identification and characterization of protease-resistant SecA fragments: secA has two membrane-integral forms.
about
Phospholipids induce conformational changes of SecA to form membrane-specific domains: AFM structures and implication on protein-conducting channelsSecA alone can promote protein translocation and ion channel activity: SecYEG increases efficiency and signal peptide specificityRole of lipids in the translocation of proteins across membranes.Electrophysiological studies in Xenopus oocytes for the opening of Escherichia coli SecA-dependent protein-conducting channels.Ring-like pore structures of SecA: implication for bacterial protein-conducting channels.SecA: a potential antimicrobial target.Evaluation of small molecule SecA inhibitors against methicillin-resistant Staphylococcus aureus.Dissecting structures and functions of SecA-only protein-conducting channels: ATPase, pore structure, ion channel activity, protein translocation, and interaction with SecYEG/SecDF•YajC.Complex behavior in solution of homodimeric SecA.Design, Synthesis and Evaluation of Triazole-Pyrimidine Analogues as SecA Inhibitors.Membrane anchoring stabilizes and favors secretion of New Delhi metallo-β-lactamaseStoichiometry of SecYEG in the active translocase of Escherichia coli varies with precursor species.The first low microM SecA inhibitorsThe SecA subunit of Escherichia coli preprotein translocase is exposed to the periplasm.Mechanisms of Rose Bengal inhibition on SecA ATPase and ion channel activities.Fluorescein analogues inhibit SecA ATPase: the first sub-micromolar inhibitor of bacterial protein translocation.The dispensability and requirement of SecA N-terminal aminoacyl residues for complementation, membrane binding, lipid-specific domains and channel activities.Sites of interaction between SecA and the chaperone SecB, two proteins involved in export.Penetration into Membrane of Amino-terminal Region of SecA when Associated with SecYEG in Active Complexes.The Sec System: Protein Export in Escherichia coli.The SecA protein deeply penetrates into the SecYEG channel during insertion, contacting most channel transmembrane helices and periplasmic regions.
P2860
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P2860
Identification and characterization of protease-resistant SecA fragments: secA has two membrane-integral forms.
description
1998 nî lūn-bûn
@nan
1998 թուականի Փետրուարին հրատարակուած գիտական յօդուած
@hyw
1998 թվականի փետրվարին հրատարակված գիտական հոդված
@hy
1998年の論文
@ja
1998年論文
@yue
1998年論文
@zh-hant
1998年論文
@zh-hk
1998年論文
@zh-mo
1998年論文
@zh-tw
1998年论文
@wuu
name
Identification and characteriz ...... s two membrane-integral forms.
@ast
Identification and characteriz ...... s two membrane-integral forms.
@en
type
label
Identification and characteriz ...... s two membrane-integral forms.
@ast
Identification and characteriz ...... s two membrane-integral forms.
@en
prefLabel
Identification and characteriz ...... s two membrane-integral forms.
@ast
Identification and characteriz ...... s two membrane-integral forms.
@en
P2093
P2860
P1476
Identification and characteriz ...... as two membrane-integral forms
@en
P2093
P2860
P304
P407
P577
1998-02-01T00:00:00Z