about
Class IIa bacteriocins: diversity and new developmentsCrystal Structures of the Response Regulator DosR from Mycobacterium tuberculosis Suggest a Helix Rearrangement Mechanism for Phosphorylation Activation1.9 Å structure of the signal receiver domain of the putative response regulator NarL fromMycobacterium tuberculosisCrystal Structure of the -Kinase Domain of Dictyostelium Myosin Heavy Chain Kinase AStructure and binding specificity of the receiver domain of sensor histidine kinase CKI1 from Arabidopsis thalianaStructural Basis of a Physical Blockage Mechanism for the Interaction of Response Regulator PmrA with Connector Protein PmrD fromKlebsiella pneumoniaePhosphorylated Ssk1 prevents unphosphorylated Ssk1 from activating the Ssk2 mitogen-activated protein kinase kinase kinase in the yeast high-osmolarity glycerol osmoregulatory pathwayDual control of Sinorhizobium meliloti RpoE2 sigma factor activity by two PhyR-type two-component response regulatorsStructural classification of bacterial response regulators: diversity of output domains and domain combinations.Functional analysis of the VirSR phosphorelay from Clostridium perfringens.Regulation of the AbrA1/A2 two-component system in Streptomyces coelicolor and the potential of its deletion strain as a heterologous host for antibiotic production.CitB is required for full virulence of Xanthomonas oryzae pv. oryzae.The continuing story of class IIa bacteriocinsCrystal structures of beryllium fluoride-free and beryllium fluoride-bound CheY in complex with the conserved C-terminal peptide of CheZ reveal dual binding modes specific to CheY conformation.Structural analysis and solution studies of the activated regulatory domain of the response regulator ArcA: a symmetric dimer mediated by the alpha4-beta5-alpha5 face.Molecular dynamics of the FixJ receiver domain: movement of the beta4-alpha4 loop correlates with the in and out flip of Phe101.Mapping essential domains of Mycobacterium smegmatis WhmD: insights into WhiB structure and function.Mutations altering the N-terminal receiver domain of NRI (NtrC) That prevent dephosphorylation by the NRII-PII complex in Escherichia coli.The Campylobacter jejuni RacRS system regulates fumarate utilization in a low oxygen environment.Phosphorylation-independent dimer-dimer interactions by the enhancer-binding activator NtrC of Escherichia coli: a third function for the C-terminal domain.The Campylobacter jejuni PhosS/PhosR operon represents a non-classical phosphate-sensitive two-component system.Evolution of the genetic code by incorporation of amino acids that improved or changed protein function.Fmoc-chemistry of a stable phosphohistidine analogue.
P2860
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P2860
description
2001 nî lūn-bûn
@nan
2001 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած
@hyw
2001 թվականի դեկտեմբերին հրատարակված գիտական հոդված
@hy
2001年の論文
@ja
2001年論文
@yue
2001年論文
@zh-hant
2001年論文
@zh-hk
2001年論文
@zh-mo
2001年論文
@zh-tw
2001年论文
@wuu
name
Phosphoaspartates in bacterial signal transduction.
@ast
Phosphoaspartates in bacterial signal transduction.
@en
Phosphoaspartates in bacterial signal transduction.
@nl
type
label
Phosphoaspartates in bacterial signal transduction.
@ast
Phosphoaspartates in bacterial signal transduction.
@en
Phosphoaspartates in bacterial signal transduction.
@nl
prefLabel
Phosphoaspartates in bacterial signal transduction.
@ast
Phosphoaspartates in bacterial signal transduction.
@en
Phosphoaspartates in bacterial signal transduction.
@nl
P2093
P1476
Phosphoaspartates in bacterial signal transduction.
@en
P2093
P304
P356
10.1016/S0959-440X(01)00271-8
P577
2001-12-01T00:00:00Z