Results 241 to 250 of about 40,840 (280)

Target Recognition of Guanylate Cyclase By Guanylate Cyclase-Activating Proteins

2002
Guanylate 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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Inhibition of Soluble Guanylate Cyclase by ODQ

Biochemistry, 2000
The heme in soluble guanylate cyclases (sGC) as isolated is ferrous, high-spin, and 5-coordinate. [1H-[1,2,4]oxadiazolo-[4, 3-a]quinoxalin-1-one] (ODQ) has been used extensively as a specific inhibitor for sGC and as a diagnostic tool for identifying a role for sGC in signal transduction events.
Y, Zhao, P E, Brandish, M, Di Valentin, M, DiValentin, J P, Schelvis, G T, Babcock, M A, Marletta   +6 more
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Structure and Regulation of Soluble Guanylate Cyclase

Annual Review of Biochemistry, 2012
Nitric oxide (NO) is an essential signaling molecule in biological systems. In mammals, the diatomic gas is critical to the cyclic guanosine monophosphate (cGMP) pathway as it functions as the primary activator of soluble guanylate cyclase (sGC). NO is synthesized from l-arginine and oxygen (O2) by the enzyme nitric oxide synthase (NOS). Once produced,
Michael A. Marletta, Emily R. Derbyshire
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Characterization of guanylate cyclase in squid photoreceptors

Visual Neuroscience, 1989
AbstractLight causes a rapid, 1.7-fold increase in cyclic GMP concentration in intact squid retinas (Johnson et al. (1986)). To determine whether light-induced changes in cyclic GMP concentration result from activation of guanylate cyclase, we have studied the regulation of guanylate cyclase activity in squid (Loligo pealei) photoreceptors.
Robinson, Phylis R, Cote, Rick H.
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Soluble guanylate cyclases in the retina

2002
Soluble guanylate cyclase catalyzes the formation of cyclic GMP using GTP as substrate. It is now well established that soluble guanylate cyclase is highly activated by nitric oxide, and that many of the effects of nitric oxide on various cells and tissues are mediated through increased production of cyclic GMP.
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The guanylate cyclase/receptor family of proteins

The FASEB Journal, 1989
Guanylate cyclase, which catalyzes the formation of cGMP from GTP, exists in both the soluble and particulate fractions of cells. At least two different cellular compartments for the particulate enzyme exist: the plasma membrane and cytoskeleton. The enzyme form found in the soluble fraction is a heterodimer that can be regulated by free radicals and ...
Michael Chinkers, David L. Garbers, Stephanie Schulz   +2 more
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Nicotine decreases guanylate cyclase activity

Bulletin of Environmental Contamination and Toxicology, 1978
The cyclic nucleotide, guanosine 3',5'-monophosphate (cyclic GMP) appears to serve a critical role in normal cell growth, DNA synthesis, and carcinogenesis (GOLDBERG et al. 1977). Tobacco smoke and hydrazine, a carcinogen which occurs in tobacco and tobacco smoke, have been shown to stimulate guanylate cyclase [E.C.
David L. Vesely, Gerald S. Levey
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Adenylate and Guanylate Cyclase Assays

Current Protocols in Pharmacology, 1998
AbstractThis unit presents two basic protocols to determine adenylate cyclase and guanylate cyclase activity in tissue and cell homogenates, permeabilized cells, or subcellular fractions. Two parts are presented for each method. First, the enzyme reaction that causes the formation of the labeled cyclic nucleotide is performed. Second, the separation of
W. Joseph Thompson, Troy Stevens, John J. Kelly   +2 more
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Guanylate Cyclase Receptor Family

1990
The plasma membrane forms of guanylate cyclase contain a highly conserved catalytic domain, which is also conserved in the soluble form of the enzyme and in mammalian adenylate cyclase. A protein kinase-like domain lies to the amino-terminal side of the catalytic domain and appears to be required for signaling via cGMP; it might also signal, itself ...
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A simple and sensitive assay for guanylate cyclase

Analytical Biochemistry, 1976
A simple and highly sensitive method for the assay of guanylate cyclase has been developed which is capable of measuring cyclic 3′–5′ GMP (cGMP) formation in picomole quantities. In the method, 10–100 μg of enzyme protein is incubated with 1m m [α-32P]GTP, 40 m m Tris-HCl buffer (pH 7.4), 3.3 m m Mn2+, 10 m m theophylline, and 1 m m cGMP.
N. Krishnan, Gopal Krishna
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