Structural Insight into the Mechanism of c-di-GMP Hydrolysis by EAL Domain Phosphodiesterases - Wikidata - awgldk - TriplyDB

Structural Insight into the Mechanism of c-di-GMP Hydrolysis by EAL Domain Phosphodiesterases

Structural Insight into the Mechanism of c-di-GMP Hydrolysis by EAL Domain Phosphodiesterases

http://www.wikidata.org/entity/Q27663896

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Cyclic di-GMP: the first 25 years of a universal bacterial second messenger Expression and Genetic Activation of Cyclic Di-GMP-Specific Phosphodiesterases in Escherichia coli.Structural Basis for c-di-GMP-Mediated Inside-Out Signaling Controlling Periplasmic Proteolysis Structural insights into the regulatory mechanism of the response regulator RocR from Pseudomonas aeruginosa in cyclic Di-GMP signaling.Structural insight of a concentration-dependent mechanism by which YdiV inhibits Escherichia coli flagellum biogenesis and motility The Structure of an Unconventional HD-GYP Protein from Bdellovibrio Reveals the Roles of Conserved Residues in this Class of Cyclic-di-GMP Phosphodiesterases Crystal Structure of an EAL Domain in Complex with Reaction Product 5′-pGpG Crystal structure of an HD-GYP domain cyclic-di-GMP phosphodiesterase reveals an enzyme with a novel trinuclear catalytic iron centre Inherent Regulation of EAL Domain-catalyzed Hydrolysis of Second Messenger Cyclic di-GMP Structures of the catalytic EAL domain of the Escherichia coli direct oxygen sensor Formation and dimerization of the phosphodiesterase active site of the Pseudomonas aeruginosa MorA, a bi-functional c-di-GMP regulator Biofilms and Cyclic di-GMP (c-di-GMP) Signaling: Lessons from Pseudomonas aeruginosa and Other Bacteria C-di-GMP hydrolysis by Pseudomonas aeruginosa HD-GYP phosphodiesterases: analysis of the reaction mechanism and novel roles for pGpG Crystallization and preliminary X-ray diffraction characterization of the XccFimX(EAL)-c-di-GMP and XccFimX(EAL)-c-di-GMP-XccPilZ complexes from Xanthomonas campestris.Diversity of Cyclic Di-GMP-Binding Proteins and Mechanisms.Systematic Nomenclature for GGDEF and EAL Domain-Containing Cyclic Di-GMP Turnover Proteins of Escherichia coli.Nuclease-Resistant c-di-AMP Derivatives That Differentially Recognize RNA and Protein Receptors Identification of c-di-GMP derivatives resistant to an EAL domain phosphodiesterase Functional characterization of core components of the Bacillus subtilis cyclic-di-GMP signaling pathway.Active Site Metal Occupancy and Cyclic Di-GMP Phosphodiesterase Activity of Thermotoga maritima HD-GYP Sensing the messenger: the diverse ways that bacteria signal through c-di-GMP.Nucleotide, c-di-GMP, c-di-AMP, cGMP, cAMP, (p)ppGpp signaling in bacteria and implications in pathogenesis.Characterization of elements involved in allosteric light regulation of phosphodiesterase activity by comparison of different functional BlrP1 states.Progress in Understanding the Molecular Basis Underlying Functional Diversification of Cyclic Dinucleotide Turnover Proteins.Dimerisation induced formation of the active site and the identification of three metal sites in EAL-phosphodiesterases Thermoregulation of Biofilm Formation in Burkholderia pseudomallei Is Disrupted by Mutation of a Putative Diguanylate Cyclase.Cyclic diguanylate regulation of Bacillus cereus group biofilm formation.Membrane-anchored MucR mediates nitrate-dependent regulation of alginate production in Pseudomonas aeruginosa.Stand-Alone EAL Domain Proteins Form a Distinct Subclass of EAL Proteins Involved in Regulation of Cell Motility and Biofilm Formation in Enterobacteria.Bacterial rotary export ATPases are allosterically regulated by the nucleotide second messenger cyclic-di-GMP.Modification of a bi-functional diguanylate cyclase-phosphodiesterase to efficiently produce cyclic diguanylate monophosphate.Different evolutionary modifications as a guide to rewire two-component systems.Engineering of Bacillus subtilis strains to allow rapid characterization of heterologous diguanylate cyclases and phosphodiesterases.Finally! The structural secrets of a HD-GYP phosphodiesterase revealed.The extremophile Acidithiobacillus ferrooxidans possesses a c-di-GMP signalling pathway that could play a significant role during bioleaching of minerals.Structural polymorphism of c-di-GMP bound to an EAL domain and in complex with a type II PilZ-domain protein.Computational and NMR spectroscopy insights into the conformation of cyclic di-nucleotides.Insights into biofilm dispersal regulation from the crystal structure of the PAS-GGDEF-EAL region of RbdA from Pseudomonas aeruginosa.Analysis of proton wires in the enzyme active site suggests a mechanism of c-di-GMP hydrolysis by the EAL domain phosphodiesterases.Transmembrane redox control and proteolysis of PdeC, a novel type of c-di-GMP phosphodiesterase.

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Structural Insight into the Mechanism of c-di-GMP Hydrolysis by EAL Domain Phosphodiesterases

http://www.wikidata.org/entity/Q27663896

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2010 nî lūn-bûn

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2010 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած

@hyw

2010 թվականի սեպտեմբերին հրատարակված գիտական հոդված

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2010年の論文

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2010年論文

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2010年論文

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2010年論文

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2010年論文

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2010年論文

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2010年论文

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J.JMB.2010.07.050

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Journal of Molecular Biology

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Structural Insight into the Me ...... EAL Domain Phosphodiesterases

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Alexander Singer

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Anatoli Tchigvintsev

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Changsoo Chang

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Greg Brown

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Hong Cui

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Robert Flick

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Wayne F Anderson

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Xiaohui Xu

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P2860

Cyclic diguanylate is a ubiquitous signaling molecule in bacteria: insights into biochemistry of the GGDEF protein domain

The ubiquitous protein domain EAL is a cyclic diguanylate-specific phosphodiesterase: enzymatically active and inactive EAL domains

A general two-metal-ion mechanism for catalytic RNA

Cell cycle-dependent dynamic localization of a bacterial response regulator with a novel di-guanylate cyclase output domain

Structure of Thermotoga maritima stationary phase survival protein SurE: a novel acid phosphatase

Metal ion-mediated substrate-assisted catalysis in type II restriction endonucleases

The EAL domain protein VieA is a cyclic diguanylate phosphodiesterase

Roles of cyclic diguanylate in the regulation of bacterial pathogenesis

Get the message out: cyclic-Di-GMP regulates multiple levels of flagellum-based motility

The structural basis of cyclic diguanylate signal transduction by PilZ domains

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524-38

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2163114

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10.1016/J.JMB.2010.07.050

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402

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Andrzej Joachimiak

Michael Proudfoot

Alexei Savchenko

Michael Y. Galperin

Alexander F. Yakunin

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2010-09-24T00:00:00Z

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45535821

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