Results 11 to 20 of about 40,840 (280)

Photoreceptor Guanylate Cyclase (GUCY2D) Mutations Cause Retinal Dystrophies by Severe Malfunction of Ca2+-Dependent Cyclic GMP Synthesis

open access: yesFrontiers in Molecular Neuroscience, 2018
Over 100 mutations in GUCY2D that encodes the photoreceptor guanylate cyclase GC-E are known to cause two major diseases: autosomal recessive Leber congenital amaurosis (arLCA) or autosomal dominant cone-rod dystrophy (adCRD) with a poorly understood ...
Dorit Lev, Karl-wilhelm Koch
exaly   +3 more sources

Adenylate Cyclase and Guanylate Cyclase in Myxococcus xanthus [PDF]

open access: bronzeMicrobiology, 1984
Myxococcus xanthus M300 vegetative cells contained significant amounts of adenylate and guanylate cyclase activity. The latter was distributed between the 100000 g supernatant and pellet fractions, required divalent cations for activity and exhibited an apparent Km of 1 mm.
A. L. DEVI, Howard D. McCurdy
openalex   +3 more sources

Editorial: Multi-limbed membrane guanylate cyclase cellular signaling pathways [PDF]

open access: yesFrontiers in Molecular Neuroscience, 2023
Rameshwar K. Sharma   +3 more
doaj   +2 more sources

Inhaled mosliciguat (BAY 1237592): targeting pulmonary vasculature via activating apo-sGC

open access: yesRespiratory Research, 2022
Background Oxidative stress associated with severe cardiopulmonary diseases leads to impairment in the nitric oxide/soluble guanylate cyclase signaling pathway, shifting native soluble guanylate cyclase toward heme-free apo-soluble guanylate cyclase ...
Eva M. Becker-Pelster   +18 more
doaj   +1 more source

Analysis of Rare Variants in 470,000 Exome-Sequenced UK Biobank Participants Implicates Novel Genes Affecting Risk of Hypertension

open access: yesPulse, 2023
Introduction: A previous study of 200,000 exome-sequenced UK Biobank participants to test for association of rare coding variants with hypertension implicated two genes at exome-wide significance, DNMT3A and FES.
David Curtis
doaj   +1 more source

Identification of bacterial guanylate cyclases [PDF]

open access: yesProteins: Structure, Function, and Bioinformatics, 2017
The ability of bacteria to use cGMP as a second messenger has been controversial for decades. Recently, nucleotide cyclases from Rhodospirillum centenum, GcyA, and Xanthomonas campestris, GuaX, have been shown to possess guanylate cyclase activities. Enzymatic activities of these guanylate cyclases measured in vitro were low, which makes interpretation
Hwan Youn   +3 more
openaire   +4 more sources

Crystal structures of the catalytic domain of human soluble guanylate cyclase. [PDF]

open access: yesPLoS ONE, 2013
Soluble guanylate cyclase (sGC) catalyses the synthesis of cyclic GMP in response to nitric oxide. The enzyme is a heterodimer of homologous α and β subunits, each of which is composed of multiple domains.
Charles K Allerston   +2 more
doaj   +1 more source

Nitric oxide — soluble guanylate cyclase — cyclic guanosine monophosphate signaling pathway in the pathogenesis of heart failure and search for novel therapeutic targets

open access: yesКардиоваскулярная терапия и профилактика, 2021
Heart failure is a severe disease with an unfavorable prognosis, which requires intensification of therapy and the search for novel approaches to treatment.
Zh. D. Kobalava, P. V. Lazarev
doaj   +1 more source

Cytoglobin regulates NO-dependent cilia motility and organ laterality during development

open access: yesNature Communications, 2023
Cytoglobin is a heme protein with unresolved physiological function. Genetic deletion of zebrafish cytoglobin (cygb2) causes developmental defects in left-right cardiac determination, which in humans is associated with defects in ciliary function and low
Elizabeth R. Rochon   +12 more
doaj   +1 more source

Amyloid-β inhibits No-cGMP signaling in a CD36- and CD47-dependent manner. [PDF]

open access: yesPLoS ONE, 2010
Amyloid-β interacts with two cell surface receptors, CD36 and CD47, through which the matricellular protein thrombospondin-1 inhibits soluble guanylate cyclase activation. Here we examine whether amyloid-β shares this inhibitory activity.
Thomas W Miller   +4 more
doaj   +1 more source

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