Results 121 to 130 of about 139,639 (149)

A Conserved Scaffold With Heterogeneous Metal Ion Binding Site: The Multifaceted Example of HD-GYP Proteins

open access: yesCoordination Chemistry Reviews, 2022
The control of the intracellular level of cyclic dinucleotides is a major strategy to transduce external signals into a cellular response, particularly in bacteria.
Alessandro Paiardini   +2 more
exaly   +4 more sources
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The HD-GYP domain protein of Shewanella putrefaciens YZ08 regulates biofilm formation and spoilage activities

Food Research International, 2022
Shewanella putrefaciens is an important spoilage bacteria in seafood and its ability to form biofilms in food processing environments increases the chances of food spoilage. Exploring the regulatory factors associated with biofilm formation and spoilage activity in S. putrefaciens is of great significance for extending the shelf life of seafood.
Zhengkai Yi   +3 more
openaire   +2 more sources

Structure and Function of HD-GYP Phosphodiesterases

2020
HD-GYPs represent the least abundant, and somewhat mysterious, class of dedicated cyclic di-GMP phosphodiesterases (PDE). They are metal dependent enzymes, belonging to the HD phosphohydrolase superfamily, and are evolutionarily unrelated to the EAL class of cyclic di-GMP dedicated PDEs.
Rinaldo S.   +4 more
openaire   +2 more sources

Phenotypic–genotypic analysis of GGDEF/EAL/HD‐GYP domain‐encoding genes in Pseudomonas putida

Environmental Microbiology Reports, 2019
Summary Cyclic diguanylate (c‐di‐GMP) is a broadly conserved bacterial signalling molecule that modulates diverse cellular processes, such as biofilm formation, colony morphology and swimming motility. The intracellular level of c‐di‐GMP is controlled by diguanylate cyclases (DGCs) with GGDEF domain and ...
Hailing Nie   +6 more
openaire   +2 more sources

The HD-GYP Domain and Cyclic Di-GMP Signaling

2014
A role for the HD-GYP domain in c-di-GMP hydrolysis was then proposed based on examination of the distribution and numbers of GGDEF, EAL, and HD-GYP domains encoded by different bacterial genomes, coupled with the known activities of other members of the HD superfamily of enzymes as metal-dependent hydrolases.
Robert P. Ryan   +2 more
openaire   +1 more source

Cyclic di-GMP Signaling Gone Astray: Cyclic GAMP Signaling via Hypr GGDEF and HD-GYP Enzymes

2020
GGDEF domain and HD-GYP enzymes are classically associated with cyclic di-GMP signaling. Here we describe our current knowledge of variants of these enzyme classes that instead are involved in cyclic GMP-AMP (cGAMP) signaling, including their discovery, recent elucidation of signature active site residues, specific phenotypes, and regulatory mechanisms.
Todd A. Wright   +2 more
openaire   +1 more source

HD-GYP domain structure solved

Nature Reviews Microbiology, 2013
openaire   +1 more source

Toxicity of Diclofenac to Gyps Vultures

Biology Letters, 2006
Rhys E Green   +2 more
exaly  

HD-GYP Domain Structure Solved

Nature Reviews Microbiology, 2014
Sheilagh Molloy
exaly  

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