Comprehensive analysis of OmpR phosphorylation, dimerization, and DNA binding supports a canonical model for activation.
about
Prokaryotic 2-component systems and the OmpR/PhoB superfamilyA biochemical characterization of the DNA binding activity of the response regulator VicR from Streptococcus mutansDual-site phosphorylation of the control of virulence regulator impacts group a streptococcal global gene expression and pathogenesisBioluminescence resonance energy transfer system for measuring dynamic protein-protein interactions in bacteriaThe influence of repressor DNA binding site architecture on transcriptional controlTranscriptional regulation of the Aggregatibacter actinomycetemcomitans ygiW-qseBC operon by QseB and integration host factor proteinsDNA consensus sequence motif for binding response regulator PhoP, a virulence regulator of Mycobacterium tuberculosis.The Escherichia coli NarL receiver domain regulates transcription through promoter specific functions.The Response Regulator BfmR Is a Potential Drug Target for Acinetobacter baumannii.Unexpected properties of sRNA promoters allow feedback control via regulation of a two-component system.Large-scale identification of coevolution signals across homo-oligomeric protein interfaces by direct coupling analysis.Use of a Phosphorylation Site Mutant To Identify Distinct Modes of Gene Repression by the Control of Virulence Regulator (CovR) in Streptococcus pyogenes.Allosteric activation of bacterial response regulators: the role of the cognate histidine kinase beyond phosphorylation.An Adaptive Mutation in Enterococcus faecium LiaR Associated with Antimicrobial Peptide Resistance Mimics Phosphorylation and Stabilizes LiaR in an Activated State.Characterization of the CrbS/R Two-Component System in Pseudomonas fluorescens Reveals a New Set of Genes under Its Control and a DNA Motif Required for CrbR-Mediated Transcriptional Activation.Computational Studies of the Active and Inactive Regulatory Domains of Response Regulator PhoP Using Molecular Dynamics Simulations.The structure of the biofilm-controlling response regulator BfmR from Acinetobacter baumannii reveals details of its DNA-binding mechanism.Stochastic simulation of prokaryotic two-component signalling indicates stochasticity-induced active-state locking and growth-rate dependent bistability.The EnvZ-OmpR Two-Component Signaling System Is Inactivated in a Mutant Devoid of Osmoregulated Periplasmic Glucans in Dickeya dadantii
P2860
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P2860
Comprehensive analysis of OmpR phosphorylation, dimerization, and DNA binding supports a canonical model for activation.
description
2013 nî lūn-bûn
@nan
2013 թուականի Փետրուարին հրատարակուած գիտական յօդուած
@hyw
2013 թվականի փետրվարին հրատարակված գիտական հոդված
@hy
2013年の論文
@ja
2013年論文
@yue
2013年論文
@zh-hant
2013年論文
@zh-hk
2013年論文
@zh-mo
2013年論文
@zh-tw
2013年论文
@wuu
name
Comprehensive analysis of OmpR ...... anonical model for activation.
@ast
Comprehensive analysis of OmpR ...... anonical model for activation.
@en
type
label
Comprehensive analysis of OmpR ...... anonical model for activation.
@ast
Comprehensive analysis of OmpR ...... anonical model for activation.
@en
prefLabel
Comprehensive analysis of OmpR ...... anonical model for activation.
@ast
Comprehensive analysis of OmpR ...... anonical model for activation.
@en
P2860
P1476
Comprehensive analysis of OmpR ...... anonical model for activation.
@en
P2093
Christopher M Barbieri
P2860
P304
P356
10.1016/J.JMB.2013.02.003
P407
P50
P577
2013-02-08T00:00:00Z