Structural basis for methylesterase CheB regulation by a phosphorylation-activated domain - Wikidata - wikimedia - TriplyDB

Structural basis for methylesterase CheB regulation by a phosphorylation-activated domain

Structural basis for methylesterase CheB regulation by a phosphorylation-activated domain

http://www.wikidata.org/entity/Q27748852

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CHEMOTAXIS-GUIDED MOVEMENTS IN BACTERIA Structural basis of activity and allosteric control of diguanylate cyclase Prokaryotic 2-component systems and the OmpR/PhoB superfamily The trans-activation domain of the sporulation response regulator Spo0A revealed by X-ray crystallography The crystal structure of the phosphorylation domain in PhoP reveals a functional tandem association mediated by an asymmetric interface Structural Analysis of the Domain Interface in DrrB, a Response Regulator of the OmpR/PhoB Subfamily NMR structure of the pseudo-receiver domain of CikA Structure of an atypical orphan response regulator protein supports a new phosphorylation-independent regulatory mechanism Domain Orientation in the Inactive Response Regulator Mycobacterium tuberculosis MtrA Provides a Barrier to Activation † , ‡The structure of a full-length response regulator from Mycobacterium tuberculosis in a stabilized three-dimensional domain-swapped, activated state A structural model of anti-anti-σ inhibition by a two-component receiver domain: the PhyR stress response regulator Structural insights into the regulatory mechanism of the response regulator RocR from Pseudomonas aeruginosa in cyclic Di-GMP signaling.An insight into the interaction mode between CheB and chemoreceptor from two crystal structures of CheB methylesterase catalytic domain Structural insight into the low affinity between Thermotoga maritima CheA and CheB compared to their Escherichia coli/Salmonella typhimurium counterparts Signal transduction and regulatory mechanisms involved in control of the sigma(S) (RpoS) subunit of RNA polymerase Chemotaxis in Escherichia coli: a molecular model for robust precise adaptation The structural basis of signal transduction for the response regulator PrrA from Mycobacterium tuberculosis Information processing in bacteria: memory, computation, and statistical physics: a key issues review Making sense of it all: bacterial chemotaxis Phosphorylation-induced dimerization of the FixJ receiver domain.A Variable Active Site Residue Influences the Kinetics of Response Regulator Phosphorylation and Dephosphorylation.Bacterial locomotion and signal transduction.Strain-specific parallel evolution drives short-term diversification during Pseudomonas aeruginosa biofilm formation Evidence for phosphorylation-dependent conformational changes in methylesterase CheB.Inhibitors of bacterial two-component signalling systems.Structural classification of bacterial response regulators: diversity of output domains and domain combinations.Methylation of aquaporins in plant plasma membrane.Diversity of structure and function of response regulator output domains The receiver domain of hybrid histidine kinase VirA: an enhancing factor for vir gene expression in Agrobacterium tumefaciens.Multicomponent transcriptional regulation at the complex promoter of the exopolysaccharide I biosynthetic operon of Ralstonia solanacearum Carboxyl-terminal extensions beyond the conserved pentapeptide reduce rates of chemoreceptor adaptational modification.Genetic evidence that the alpha5 helix of the receiver domain of PhoB is involved in interdomain interactions How signals are heard during bacterial chemotaxis: protein-protein interactions in sensory signal propagation.A dynamic-signaling-team model for chemotaxis receptors in Escherichia coli Diversity in chemotaxis mechanisms among the bacteria and archaea.The protein interaction network of a taxis signal transduction system in a halophilic archaeon Amplification of signaling events in bacteria.Mutational analysis of RetS, an unusual sensor kinase-response regulator hybrid required for Pseudomonas aeruginosa virulence.Adapt locally and act globally: strategy to maintain high chemoreceptor sensitivity in complex environments.Response tuning in bacterial chemotaxis.

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P2860

Structural basis for methylesterase CheB regulation by a phosphorylation-activated domain

http://www.wikidata.org/entity/Q27748852

description

1998 nî lūn-bûn

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1998 թուականի Փետրուարին հրատարակուած գիտական յօդուած

@hyw

1998 թվականի փետրվարին հրատարակված գիտական հոդված

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1998年の論文

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1998年学术文章

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1998年学术文章

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1998年学术文章

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1998年学术文章

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1998年学术文章

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1998年學術文章

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Structural basis for methylesterase CheB regulation by a phosphorylation-activated domain

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Structural basis for methylesterase CheB regulation by a phosphorylation-activated domain

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Structural basis for methylesterase CheB regulation by a phosphorylation-activated domain

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Structural basis for methylesterase CheB regulation by a phosphorylation-activated domain

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Structural basis for methylesterase CheB regulation by a phosphorylation-activated domain

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Structural basis for methylesterase CheB regulation by a phosphorylation-activated domain

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Structural basis for methylesterase CheB regulation by a phosphorylation-activated domain

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Structural basis for methylesterase CheB regulation by a phosphorylation-activated domain

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Structural basis for methylesterase CheB regulation by a phosphorylation-activated domain

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Proceedings of the National Academy of Sciences of the United States of America

P1476

Structural basis for methylesterase CheB regulation by a phosphorylation-activated domain

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P2093

A H West

http://www.w3.org/2001/XMLSchema#string

P N Goudreau

http://www.w3.org/2001/XMLSchema#string

Q Xu

http://www.w3.org/2001/XMLSchema#string

S Djordjevic

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P2860

Protein phosphorylation and regulation of adaptive responses in bacteria

Crystal structure of Escherichia coli CheY refined at 1.7-A resolution

Three-dimensional structure of CheY, the response regulator of bacterial chemotaxis

Crystal structure of the catalytic domain of the chemotaxis receptor methylesterase, CheB

Three-dimensional solution structure of the N-terminal receiver domain of NTRC

Structure of the Mg(2+)-bound form of CheY and mechanism of phosphoryl transfer in bacterial chemotaxis

Structure of the Escherichia coli response regulator NarL

Crystal structure of a phosphatase-resistant mutant of sporulation response regulator Spo0F from Bacillus subtilis

Crystal structures of CheY mutants Y106W and T87I/Y106W. CheY activation correlates with movement of residue 106

Crystal structure of the chemotaxis receptor methyltransferase CheR suggests a conserved structural motif for binding S-adenosylmethionine

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1381-1386

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scholarly article

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10.1073/PNAS.95.4.1381

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4

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13765896

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9465023

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P921

phosphorylation

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19010

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