Results 131 to 140 of about 1,778 (147)
Some of the next articles are maybe not open access.

HD‐GYP domain proteins regulate biofilm formation and virulence in Pseudomonas aeruginosa

Environmental Microbiology, 2009
Summary HD‐GYP is a protein domain involved in the hydrolysis of the bacterial second messenger cyclic‐di‐GMP. The genome of the human pathogen Pseudomonas aeruginosa PAO1 encodes two proteins (PA4108, PA4781) with an HD‐GYP domain and a third protein, PA2572, which contains
Ryan, Robert P   +6 more
openaire   +3 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

Identification and Characterization of a Redox Sensor Phosphodiesterase from Ferrovum sp. PN-J185 Containing Bacterial Hemerythrin and HD-GYP Domains

Biochemistry, 2020
The second messenger bis(3',5')-cyclic dimeric guanosine monophosphate (c-di-GMP) regulates numerous important physiological functions in bacteria. In this study, we identified and characterized the first dimeric, full-length, non-heme iron-bound phosphodiesterase (PDE) containing bacterial hemerythrin and HD-GYP domains (Bhr-HD-GYP). We found that the
Kenichi Kitanishi   +3 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

Faculty Opinions recommendation of Dynamic complex formation between HD-GYP, GGDEF and PilZ domain proteins regulates motility in Xanthomonas campestris.

Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature, 2013
Brendan Wren, Ozan Gundogdu
openaire   +1 more source

Home - About - Disclaimer - Privacy