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Rationalizing the evolution of EAL domain-based cyclic di-GMP-specific phosphodiesterases

Rationalizing the evolution of EAL domain-based cyclic di-GMP-specific phosphodiesterases

http://www.wikidata.org/entity/Q41906114

about

Cyclic di-GMP: the first 25 years of a universal bacterial second messenger Structural insight of a concentration-dependent mechanism by which YdiV inhibits Escherichia coli flagellum biogenesis and motility Complex c-di-GMP signaling networks mediate transition between virulence properties and biofilm formation in Salmonella enterica serovar Typhimurium.Comparative genomics reveals adaptation by Alteromonas sp. SN2 to marine tidal-flat conditions: cold tolerance and aromatic hydrocarbon metabolism Comparative genomics reveals a deep-sea sediment-adapted life style of Pseudoalteromonas sp. SM9913.The EAL-like protein STM1697 regulates virulence phenotypes, motility and biofilm formation in Salmonella typhimurium.Stand-Alone EAL Domain Proteins Form a Distinct Subclass of EAL Proteins Involved in Regulation of Cell Motility and Biofilm Formation in Enterobacteria.The EAL domain containing protein STM2215 (rtn) is needed during Salmonella infection and has cyclic di-GMP phosphodiesterase activity.Dissecting the cyclic di-guanylate monophosphate signalling network regulating motility in Salmonella enterica serovar Typhimurium.Cyclic diguanylate turnover mediated by the sole GGDEF/EAL response regulator in Pseudomonas putida: its role in the rhizosphere and an analysis of its target processes Functional Characterization of c-di-GMP Signaling-Related Genes in the Probiotic

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Rationalizing the evolution of EAL domain-based cyclic di-GMP-specific phosphodiesterases

http://www.wikidata.org/entity/Q41906114

description

2009 nî lūn-bûn

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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

@zh-hk

2009年論文

@zh-mo

2009年論文

@zh-tw

2009年论文

@wuu

2009年论文

@zh

2009年论文

@zh-cn

name

Rationalizing the evolution of EAL domain-based cyclic di-GMP-specific phosphodiesterases

@en

type

label

Rationalizing the evolution of EAL domain-based cyclic di-GMP-specific phosphodiesterases

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prefLabel

Rationalizing the evolution of EAL domain-based cyclic di-GMP-specific phosphodiesterases

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P1433

Journal of Bacteriology

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Rationalizing the evolution of EAL domain-based cyclic di-GMP-specific phosphodiesterases

@en

P2860

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

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

The EAL domain protein VieA is a cyclic diguanylate phosphodiesterase

Roles of cyclic diguanylate in the regulation of bacterial pathogenesis

Structural biochemistry of a bacterial checkpoint protein reveals diadenylate cyclase activity regulated by DNA recombination intermediates

Crystal Structures of YkuI and Its Complex with Second Messenger Cyclic Di-GMP Suggest Catalytic Mechanism of Phosphodiester Bond Cleavage by EAL Domains

Structure and mechanism of a bacterial light-regulated cyclic nucleotide phosphodiesterase

GGDEF and EAL domains inversely regulate cyclic di-GMP levels and transition from sessility to motility

Cyclic nucleotide phosphodiesterases: molecular regulation to clinical use

Omega loops: nonregular secondary structures significant in protein function and stability

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4697-4700

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scholarly article

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10.1128/JB.00651-09

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15

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191

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2009-05-29T00:00:00Z

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19482927

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2715715

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