Nonconserved active site residues modulate CheY autophosphorylation kinetics and phosphodonor preference.
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A Variable Active Site Residue Influences the Kinetics of Response Regulator Phosphorylation and Dephosphorylation.CheY's acetylation sites responsible for generating clockwise flagellar rotation in Escherichia coliAdaptation of the Agrobacterium tumefaciens VirG response regulator to activate transcription in plants.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.A link between dimerization and autophosphorylation of the response regulator PhoB.Regulation of signaling directionality revealed by 3D snapshots of a kinase:regulator complex in action.A tale of two machines: a review of the BLAST meeting, Tucson, AZ, 20-24 January 2013.Experimental Analysis of Functional Variation within Protein Families: Receiver Domain Autodephosphorylation Kinetics.
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Nonconserved active site residues modulate CheY autophosphorylation kinetics and phosphodonor preference.
description
article científic
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article scientifique
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articolo scientifico
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artigo científico
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bilimsel makale
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scientific article published on 19 March 2013
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vedecký článok
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vetenskaplig artikel
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videnskabelig artikel
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vědecký článek
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name
Nonconserved active site resid ...... s and phosphodonor preference.
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Nonconserved active site resid ...... s and phosphodonor preference.
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type
label
Nonconserved active site resid ...... s and phosphodonor preference.
@en
Nonconserved active site resid ...... s and phosphodonor preference.
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prefLabel
Nonconserved active site resid ...... s and phosphodonor preference.
@en
Nonconserved active site resid ...... s and phosphodonor preference.
@nl
P2093
P2860
P356
P1433
P1476
Nonconserved active site resid ...... s and phosphodonor preference.
@en
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Robert B Bourret
Robert M Immormino
Ruth E Silversmith
Stephanie A Thomas
P2860
P304
P356
10.1021/BI301654M
P407
P577
2013-03-19T00:00:00Z