Results 181 to 190 of about 39,412 (236)
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Soluble guanylate cyclase: the forgotten sibling
Trends in Pharmacological Sciences, 1997Despite widespread distribution in most mammalian cells, the role of soluble guanylate cyclase has, until recently, been poorly defined, especially when compared with its more illustrious sibling, adenylate cyclase. In this review Adrian Hobbs outlines some of the reasons why the soluble guanylate cyclase-cGMP pathway has remained outside the ...
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From adenylate cyclase to guanylate cyclase
Journal of Molecular Biology, 1992Antoine Danchin
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Guanyl cyclase of Bacilluslicheniformis
Biochemical and Biophysical Research Communications, 1972Abstract Guanyl cyclase activity was detected in extracts of Bacillus licheniformis strain A-5. The enzyme is associated with the 105,000 × g particulate fraction of the extract, requires Mn++ for full activity, has a pH optimum of 8.5, and has an apparent Km for GTP of 5mM.
V L, Clark, R W, Bernlohr
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Guanylate Cyclase Activating Proteins, Guanylate Cyclase and Disease
2002A range of cone and cone-rod dystrophies (CORD) have been observed in man, caused by mutations in retinal guanylate cyclase 1 (RetGC1) and guanylate cyclase activating protein 1 (GCAP 1). The CORD causing mutations in RetGC1 are located at a mutation "hot spot" within the dimerisation domain, where R838 is the key residue.
Richard J, Newbold +5 more
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Current Opinion in Structural Biology, 2006
Soluble guanylate cyclase (sGC) is a mammalian nitric oxide (NO) sensor. When NO binds to the sGC heme, its GTP cyclase activity markedly increases, thus generating cyclic GMP, which serves to regulate several cell signaling functions. A good deal is known about the kinetics and equilibrium of binding of NO to sGC, leading to a proposed multistep ...
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Soluble guanylate cyclase (sGC) is a mammalian nitric oxide (NO) sensor. When NO binds to the sGC heme, its GTP cyclase activity markedly increases, thus generating cyclic GMP, which serves to regulate several cell signaling functions. A good deal is known about the kinetics and equilibrium of binding of NO to sGC, leading to a proposed multistep ...
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Target Recognition of Guanylate Cyclase By Guanylate Cyclase-Activating Proteins
2002Guanylate cyclase-activating proteins (GCAPs) control the activity of membrane bound guanylate cyclases in vertebrate photoreceptor cells. They form a permanent complex with guanylate cyclase 1 (ROS-GC1) at low and high Ca2+-concentrations. Five different target regions of GCAP-1 have been identified in ROS-GC1 at rather distant sites.
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European Journal of Biochemistry, 1970
An enzyme system catalyzing the formation of guanosine cyclic 3′:5′‐monophosphate (Guo‐3′:5′‐P) from GTP has been found in various tissues of the rat including kidney, spleen, liver, brain, heart, skeletal muscle and adipose tissue. The highest guanyl cyclase activity was measured in the lung.
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An enzyme system catalyzing the formation of guanosine cyclic 3′:5′‐monophosphate (Guo‐3′:5′‐P) from GTP has been found in various tissues of the rat including kidney, spleen, liver, brain, heart, skeletal muscle and adipose tissue. The highest guanyl cyclase activity was measured in the lung.
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Activation of guanyl cyclase and adenyl cyclase by secretin
Biochimica et Biophysica Acta (BBA) - Enzymology, 1973Abstract Properties of rat liver guanyl cyclase and adenyl cyclase and the effects of hormones on the activity of these enzymes have been investigated. 1. 1. Secretin ( 2·10 −7 –60·10 −7 M ) stimulates guanyl cyclase activity of 18 000 × g supernantants of rat liver homogenates with no change in the Michaelis-Menten constant
W J, Thompson +2 more
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Both soluble guanylate cyclase and particulate guanylate cyclase regulate myometrial contractility
American Journal of Obstetrics and Gynecology, 1998Our purpose was to compare the effects of agents stimulating particulate and soluble guanylate cyclase with spontaneous rat uterine contractions at midgestation and term.Uterine rings from midgestation (day 13) and term nonlaboring (day 22) rats were positioned in organ chambers for isometric force recording.
A S, Syal +4 more
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Biochemistry of Soluble Guanylate Cyclase
2009Nitric oxide (NO) functions in biology as both a critical cytotoxic agent and an essential signaling molecule. The toxicity of the diatomic gas has long been accepted; however, it was not known to be a signaling molecule until it was identified as the endothelium-derived relaxing factor (EDRF). Since this discovery, the physiological signaling pathways
Emily R, Derbyshire, Michael A, Marletta
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