Topology, dimerization, and stability of the single-span membrane protein CadC
about
Structure-function analysis of the DNA-binding domain of a transmembrane transcriptional activator.Vibrio parahaemolyticus VtrA is a membrane-bound regulator and is activated via oligomerization.SecA mediates cotranslational targeting and translocation of an inner membrane protein.A Modular Receptor Platform To Expand the Sensing Repertoire of Bacteria.Bacterial transmembrane signalling systems and their engineering for biosensing.
P2860
Topology, dimerization, and stability of the single-span membrane protein CadC
description
2014 nî lūn-bûn
@nan
2014 թուականի Յունիսին հրատարակուած գիտական յօդուած
@hyw
2014 թվականի հունիսին հրատարակված գիտական հոդված
@hy
2014年の論文
@ja
2014年論文
@yue
2014年論文
@zh-hant
2014年論文
@zh-hk
2014年論文
@zh-mo
2014年論文
@zh-tw
2014年论文
@wuu
name
Topology, dimerization, and stability of the single-span membrane protein CadC
@ast
Topology, dimerization, and stability of the single-span membrane protein CadC
@en
Topology, dimerization, and stability of the single-span membrane protein CadC
@nl
type
label
Topology, dimerization, and stability of the single-span membrane protein CadC
@ast
Topology, dimerization, and stability of the single-span membrane protein CadC
@en
Topology, dimerization, and stability of the single-span membrane protein CadC
@nl
prefLabel
Topology, dimerization, and stability of the single-span membrane protein CadC
@ast
Topology, dimerization, and stability of the single-span membrane protein CadC
@en
Topology, dimerization, and stability of the single-span membrane protein CadC
@nl
P2860
P1476
Topology, dimerization, and stability of the single-span membrane protein CadC
@en
P2093
Eric Lindner
P2860
P304
P356
10.1016/J.JMB.2014.06.006
P407
P577
2014-06-16T00:00:00Z