Results 251 to 260 of about 148,798 (282)

A primer for measuring cGMP signaling and cGMP-mediated vascular relaxation

Nitric Oxide, 2021
Soluble guanylyl cyclase (sGC, also called GC1) is the main receptor for nitric oxide (NO) that catalyzes the production of the second messenger molecule, 3'5' cyclic guanosine monophosphate (cGMP) leading to vasorelaxation, and inhibition of leukocyte recruitment and platelet aggregation.
Adam C. Straub, Annie Beuve
openaire   +3 more sources

Specific cGMP binding by the cGMP binding domains of cGMP-binding cGMP specific phosphodiesterase

Cellular Signalling, 2002
The structure of cyclic GMP (cGMP)-binding (cGB), cGMP specific phosphodiesterase (PDE5) comprises several domains. We have used RT-PCR methods to clone the noncatalytic cGB domains of PDE5 from human colon cancer cell RNA and constructed glutathione-S-transferase (GST) fusion proteins to express and study the domains.
W. Joseph Thompson, Li Liu, Tashandra Underwood, Rifat Pamukcu, Han Li   +4 more
openaire   +3 more sources

Allosteric Activation of cGMP-Specific, cGMP-Binding Phosphodiesterase (PDE5) by cGMP

Biochemistry, 2002
The effects of cGMP binding on the catalytic activity of cGMP-specific, cGMP-binding phosphodiesterase (PDE5) are unclear because cGMP interacts with both allosteric and catalytic sites specifically. We studied the effects of cGMP on the hydrolysis of a fluorescent substrate analogue, 2'-O-anthraniloyl cGMP, by PDE5 partially purified from rat ...
Shigeki Asakawa, Daisuke Okada
openaire   +3 more sources

The cGMP system: components and function

Biological chemistry, 2019
The cyclic guanosine monophosphate (cGMP) signaling system is one of the most prominent regulators of a variety of physiological and pathophysiological processes in many mammalian and non-mammalian tissues.
F. Hofmann
semanticscholar   +1 more source

The GAF Domain of the cGMP-Binding, cGMP-Specific Phosphodiesterase (PDE5) Is a Sensor and a Sink for cGMP

Biochemistry, 2008
We describe here a novel sensor for cGMP based on the GAF domain of the cGMP-binding, cGMP-specific phosphodiesterase 5 (PDE5) using bioluminescence resonance energy transfer (BRET). The wild type GAFa domain, capable of binding cGMP with high affinity, and a mutant (GAFa F163A) unable to bind cGMP were cloned as fusions between GFP and Rluc for BRET ...
Biswas, Kabir Hassan, Sopory, Shailaja, Visweswariah, Sandhya S   +2 more
openaire   +3 more sources

Regulation of metabolism by cGMP

Pharmacology & Therapeutics, 2013
The second messenger cyclic guanosine monophosphate (cGMP) mediates the physiological effects of nitric oxide and natriuretic peptides in a broad spectrum of tissues and cells. So far, the major focus of research on cGMP lay on the cardiovascular system.
Ana Kilić, Alexander Pfeifer, Linda S. Hoffmann   +2 more
openaire   +2 more sources

cGMP in the Vasculature

2009
Cyclic guanosine 3', 5'-monophosphate (cGMP) plays an integral role in the control of vascular function. Generated from guanylate cyclases in response to the endogenous ligands, nitric oxide (NO) and natriuretic peptides (NPs), cGMP influences a number of vascular cell types and regulates vasomotor tone, endothelial permeability, cell growth and ...
Barbara K Kemp-Harper, Harald H.H.W. Schmidt   +1 more
openaire   +3 more sources

Modulation of synaptic function by cGMP and cGMP-gated cation channels

Neurochemistry International, 2004
Cyclic nucleotide-gated cation channels have been studied intensively in the primary sensory neurons of the visual and olfactory systems. Using both anatomical and physiological methods we have shown that they have a much more widespread distribution in the nervous system.
Ji Ye Wei, Colin J. Barnstable, Ming Hu Han   +2 more
openaire   +3 more sources

Negative feedback in NO/cGMP signalling [PDF]

Biochemical Society Transactions, 2005
Most of the effects of the signalling molecule nitric oxide (NO) are mediated by the stimulation of the NO-sensitive GC (guanylate cyclase) and the subsequent increase in cGMP formation. The enzyme contains a prosthetic haem group, which mediates NO stimulation.
Michael Russwurm, Doris Koesling, Andreas Friebe, Alexander Lange, Florian Mullershausen, Evanthia Mergia, Corina Wagner   +6 more
openaire   +2 more sources