Matching Biochemical Reaction Kinetics to the Timescales of Life: Structural Determinants That Influence the Autodephosphorylation Rate of Response Regulator Proteins - Wikidata - wikimedia - TriplyDB

Matching Biochemical Reaction Kinetics to the Timescales of Life: Structural Determinants That Influence the Autodephosphorylation Rate of Response Regulator Proteins

Matching Biochemical Reaction Kinetics to the Timescales of Life: Structural Determinants That Influence the Autodephosphorylation Rate of Response Regulator Proteins

http://www.wikidata.org/entity/Q27656808

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Crystal Structure of Activated CheY1 from Helicobacter pylori Structure and binding specificity of the receiver domain of sensor histidine kinase CKI1 from Arabidopsis thaliana Structural Basis of a Rationally Rewired Protein-Protein Interface Critical to Bacterial Signaling Conformational barrier of CheY3 and inability of CheY4 to bind FliM control the flagellar motor action in Vibrio cholerae LOV Histidine Kinase Modulates the General Stress Response System and Affects the virB Operon Expression in Brucella abortus A Variable Active Site Residue Influences the Kinetics of Response Regulator Phosphorylation and Dephosphorylation.Receiver domain structure and function in response regulator proteins.Design and implementation of a biomolecular concentration tracker Probing Mechanistic Similarities between Response Regulator Signaling Proteins and Haloacid Dehalogenase Phosphatases.Cross Talk Inhibition Nullified by a Receiver Domain Missense Substitution Imidazole as a Small Molecule Analogue in Two-Component Signal Transduction.Probing kinase and phosphatase activities of two-component systems in vivo with concentration-dependent phosphorylation profiling.Nonconserved active site residues modulate CheY autophosphorylation kinetics and phosphodonor preference.Molecular Mechanisms of Two-Component Signal Transduction.Use of restrained molecular dynamics to predict the conformations of phosphorylated receiver domains in two-component signaling systems.Experimental Analysis of Functional Variation within Protein Families: Receiver Domain Autodephosphorylation Kinetics.Sirt7 promotes adipogenesis in the mouse by inhibiting autocatalytic activation of Sirt1.Identification of Regions in the Receiver Domain of the ETHYLENE RESPONSE1 Ethylene Receptor of Arabidopsis Important for Functional Divergence.

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Matching Biochemical Reaction Kinetics to the Timescales of Life: Structural Determinants That Influence the Autodephosphorylation Rate of Response Regulator Proteins

http://www.wikidata.org/entity/Q27656808

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2009 nî lūn-bûn

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2009 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած

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2009 թվականի հոտեմբերին հրատարակված գիտական հոդված

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2009年の論文

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2009年論文

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2009年論文

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2009年論文

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2009年論文

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2009年論文

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2009年论文

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Matching Biochemical Reaction ...... of Response Regulator Proteins

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Matching Biochemical Reaction ...... of Response Regulator Proteins

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Matching Biochemical Reaction ...... of Response Regulator Proteins

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Matching Biochemical Reaction ...... of Response Regulator Proteins

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Matching Biochemical Reaction ...... of Response Regulator Proteins

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J.JMB.2009.07.064

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Journal of Molecular Biology

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Matching Biochemical Reaction ...... of Response Regulator Proteins

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Amy C Wollish

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Edward J Collins

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Peter J Miller

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Robert B Bourret

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Ruth E Silversmith

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Stephanie A Thomas

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Yael Pazy

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P2860

Ras-catalyzed hydrolysis of GTP: a new perspective from model studies

BeF(3)(-) acts as a phosphate analog in proteins phosphorylated on aspartate: structure of a BeF(3)(-) complex with phosphoserine phosphatase

Correlated switch binding and signaling in bacterial chemotaxis

Crystal structure of an activated response regulator bound to its target

Crystal structure of activated CheY. Comparison with other activated receiver domains

A dimeric two-component receiver domain inhibits the sigma54-dependent ATPase in DctD

A distinct meta-active conformation in the 1.1-A resolution structure of wild-type ApoCheY

Structural characterization of the reaction pathway in phosphoserine phosphatase: crystallographic "snapshots" of intermediate states

Structure and catalytic mechanism of the E. coli chemotaxis phosphatase CheZ

CheZ-Mediated Dephosphorylation of the Escherichia coli Chemotaxis Response Regulator CheY: Role for CheY Glutamate 89

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1205-20

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10.1016/J.JMB.2009.07.064

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