Two variable active site residues modulate response regulator phosphoryl group stability
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Negative control in two-component signal transduction by transmitter phosphatase activityMatching Biochemical Reaction Kinetics to the Timescales of Life: Structural Determinants That Influence the Autodephosphorylation Rate of Response Regulator ProteinsUsing Structural Information to Change the Phosphotransfer Specificity of a Two-Component Chemotaxis Signalling ComplexCrystal Structure of Activated CheY1 from Helicobacter pyloriLOV Histidine Kinase Modulates the General Stress Response System and Affects the virB Operon Expression in Brucella abortusThreonine phosphorylation prevents promoter DNA binding of the Group B Streptococcus response regulator CovR.A Variable Active Site Residue Influences the Kinetics of Response Regulator Phosphorylation and Dephosphorylation.A conserved helical capping hydrogen bond in PAS domains controls signaling kinetics in the superfamily prototype photoactive yellow protein.Modeling chemotaxis reveals the role of reversed phosphotransfer and a bi-functional kinase-phosphatase.Receiver domain structure and function in response regulator proteins.How important is the phosphatase activity of sensor kinases?Kinetic characterization of the WalRKSpn (VicRK) two-component system of Streptococcus pneumoniae: dependence of WalKSpn (VicK) phosphatase activity on its PAS domain.Phosphorylation and dephosphorylation among Dif chemosensory proteins essential for exopolysaccharide regulation in Myxococcus xanthusCheV: CheW-like coupling proteins at the core of the chemotaxis signaling networkConserved mechanism for sensor phosphatase control of two-component signaling revealed in the nitrate sensor NarX.Action at a distance: amino acid substitutions that affect binding of the phosphorylated CheY response regulator and catalysis of dephosphorylation can be far from the CheZ phosphatase active site.Fundamental constraints on the abundances of chemotaxis proteinsMethylatable Signaling Helix Coordinated Inhibitory Receiver Domain in Sensor Kinase Modulates Environmental Stress Response in Bacillus Cereus.Probing Mechanistic Similarities between Response Regulator Signaling Proteins and Haloacid Dehalogenase Phosphatases.Cross Talk Inhibition Nullified by a Receiver Domain Missense SubstitutionImidazole as a Small Molecule Analogue in Two-Component Signal Transduction.Signal transduction meets systems biology: deciphering specificity determinants for protein-protein interactions.A bifunctional kinase-phosphatase in bacterial chemotaxis.Colocalization of fast and slow timescale dynamics in the allosteric signaling protein CheYUpward mobility and alternative lifestyles: a report from the 10th biennial meeting on Bacterial Locomotion and Signal TransductionBiological insights from structures of two-component proteins.Nonconserved active site residues modulate CheY autophosphorylation kinetics and phosphodonor preference.Regulation of Virulence in Staphylococcus aureus: Molecular Mechanisms and Remaining Puzzles.Molecular Mechanisms of Two-Component Signal Transduction.Activation and inhibition of the receptor histidine kinase AgrC occurs through opposite helical transduction motions.Use of restrained molecular dynamics to predict the conformations of phosphorylated receiver domains in two-component signaling systems.Ligand-induced folding of a two-component signaling receiver domain.Experimental Analysis of Functional Variation within Protein Families: Receiver Domain Autodephosphorylation Kinetics.Oligomerization of the response regulator ComE from Streptococcus mutans is affected by phosphorylation.A novel "four-component" two-component signal transduction mechanism regulates developmental progression in Myxococcus xanthus.Interplay of RsbM and RsbK controls the σ(B) activity of Bacillus cereus.Dynamics of two Phosphorelays controlling cell cycle progression in Caulobacter crescentus.Neisseria meningitidis and Neisseria gonorrhoeae are differently adapted in the regulation of denitrification: single nucleotide polymorphisms that enable species-specific tuning of the aerobic-anaerobic switch.An Adaptive Mutation in Enterococcus faecium LiaR Associated with Antimicrobial Peptide Resistance Mimics Phosphorylation and Stabilizes LiaR in an Activated State.
P2860
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P2860
Two variable active site residues modulate response regulator phosphoryl group stability
description
article científic
@ca
article scientifique
@fr
articolo scientifico
@it
artigo científico
@pt
bilimsel makale
@tr
scientific article published on July 2008
@en
vedecký článok
@sk
vetenskaplig artikel
@sv
videnskabelig artikel
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vědecký článek
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name
Two variable active site residues modulate response regulator phosphoryl group stability
@en
Two variable active site residues modulate response regulator phosphoryl group stability.
@nl
type
label
Two variable active site residues modulate response regulator phosphoryl group stability
@en
Two variable active site residues modulate response regulator phosphoryl group stability.
@nl
prefLabel
Two variable active site residues modulate response regulator phosphoryl group stability
@en
Two variable active site residues modulate response regulator phosphoryl group stability.
@nl
P2093
P2860
P1476
Two variable active site residues modulate response regulator phosphoryl group stability
@en
P2093
Jocelyn A Brewster
Robert B Bourret
Stephanie A Thomas
P2860
P304
P356
10.1111/J.1365-2958.2008.06296.X
P407
P577
2008-07-01T00:00:00Z