Results 41 to 50 of about 16,264 (303)

Socializing, networking and development: a report from the second ‘Young Microbiologists Symposium on Microbe Signalling, Organization and Pathogenesis’ [PDF]

open access: yes, 2012
In mid-June, the second Young Microbiologists Symposium took place under the broad title of ‘Microbe signalling, organization and pathogenesis’ on the picturesque campus of University College Cork, Ireland.
Barret   +48 more
core   +1 more source

The HD-GYP Domain, Cyclic Di-GMP Signaling, and Bacterial Virulence to Plants

open access: yesMolecular Plant-Microbe Interactions, 2006
Cyclic di-GMP is an almost ubiquitous second messenger in bacteria that was first described as an allosteric activator of cellulose synthase but is now known to regulate a range of functions, including virulence in human and animal pathogens. Two protein
J. Maxwell Dow   +3 more
doaj   +1 more source

Regulation of gingival epithelial cytokine response by bacterial cyclic dinucleotides

open access: yesJournal of Oral Microbiology, 2019
Background: Cyclic dinucleotides (cyclic di-guanosine monophosphate (c-di-GMP) and cyclic di-adenosine monophosphate (c-di-AMP)) and lipopolysaccharides (LPS) are pathogen-associated molecular patterns (PAMPs).
Samira Elmanfi   +5 more
doaj   +1 more source

Extraction and Quantification of Cyclic Di-GMP from Pseudomonas aeruginosa

open access: yesBio-Protocol, 2013
Cyclic di-GMP (c-di-GMP) has emerged as an important intracellular signaling molecule, controlling the transitions between planktonic (free-living) and sessile lifestyles, biofilm formation, and virulence in a wide variety of microorganisms.
Ankita Roy, Olga Petrova, Karin Sauer
doaj   +1 more source

Visualization of c-di-GMP in multicellular Dictyostelium stages

open access: yesFrontiers in Cell and Developmental Biology, 2023
The bacterial signaling molecule cyclic diguanosine monophosphate (c-di-GMP) is only synthesized and utilized by the cellular slime mold Dictyostelium discoideum among eukaryotes.
Hayato Ide   +3 more
doaj   +1 more source

Identification of the YfgF MASE1 domain as a modulator of bacterial responses to aspartate [PDF]

open access: yes, 2013
Complex 3'-5'-cyclic diguanylic acid (c-di-GMP) responsive regulatory networks that are modulated by the action of multiple diguanylate cyclases (DGC; GGDEF domain proteins) and phosphodiesterases (PDE; EAL domain proteins) have evolved in many bacteria.
Agasing, A.   +3 more
core   +1 more source

A cyclic‐di‐GMP receptor required for bacterial exopolysaccharide production [PDF]

open access: yesMolecular Microbiology, 2007
SummaryBis‐(3′,5′)‐cyclic‐dimeric‐guanosine monophosphate (c‐di‐GMP) has been shown to be a global regulatory molecule that modulates the reciprocal responses of bacteria to activate either virulence pathways or biofilm formation. The mechanism of c‐di‐GMP signal transduction, including recognition of c‐di‐GMP and subsequent phenotypic regulation ...
Lee, Vincent T.   +5 more
openaire   +3 more sources

Cellular levels and binding of c-di-GMP control subcellular localization and activity of the Vibrio cholerae transcriptional regulator VpsT. [PDF]

open access: yesPLoS Pathogens, 2012
The second messenger, cyclic diguanylate (c-di-GMP), regulates diverse cellular processes in bacteria. C-di-GMP is produced by diguanylate cyclases (DGCs), degraded by phosphodiesterases (PDEs), and receptors couple c-di-GMP production to cellular ...
Nicholas J Shikuma   +2 more
doaj   +1 more source

Cyclic di-GMP mediates a histidine kinase/phosphatase switch by noncovalent domain cross-linking [PDF]

open access: yes, 2016
Histidine kinases are key components of regulatory networks in bacteria. Although many of these enzymes are bifunctional, mediating both phosphorylation and dephosphorylation of downstream targets, the molecular details of this central regulatory switch ...
Dubey, Badri N.   +6 more
core   +2 more sources

Nucleotide binding by the widespread high-affinity cyclic di-GMP receptor MshEN domain

open access: yesNature Communications, 2016
Cyclic-di-GMP is a bacterial second messenger that binds to the regulatory domain of ATPases of some bacteria. Here, the authors report the crystal structure of this interaction, identify a cyclic-di-GMP binding mode, and show that this interaction might
Yu-Chuan Wang   +8 more
doaj   +1 more source

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