Results 181 to 190 of about 40,447 (213)

Biotin analogs activate guanylate cyclase

Molecular and Cellular Biochemistry, 1984
The sulfur atom in the vitamin biotin has previously been suggested to be essential in biotin's mechanism of action. In a series of investigations on structure-function relationships with biotin analogs not containing the sulfur atom, the biotin analogs, azabiotin, bisnorazabiotin, carbobiotin and isoazabiotin enhanced guanylate cyclase, an enzyme that
D L, Vesely, H C, Wormser, H N, Abramson
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Soluble guanylate cyclase

Emerging Therapeutic Targets, 2000
Soluble guanylate cyclase (sGC) is a heterodimeric haemoprotein, which represents the intracellular receptor for the ubiquitous biological messenger nitric oxide (NO). Activation of the enzyme facilitates conversion of GTP to the intracellular second messenger cGMP, and it is this molecule which mediates the majority of biological actions attributed to
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Biochemistry of Soluble Guanylate Cyclase

2009
Nitric 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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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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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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Phencyclidine stimulates guanylate cyclase activity

Biochemical and Biophysical Research Communications, 1979
Abstract The hallucinogenic agents, phencylidine (Angel's Dust), TCP ∗ and their morpholine analogs enhanced the activity of guanylate cyclase {E.C.4.6.1.2}, the enzyme that catalyzes the production of guanosine 3′, 5′-monophosphate. This activation of guanylate cyclase by hencyclidine and TCP was observed over the concentration range of .00001 mM ...
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BROMOCRIPTINE ENHANCES GUANYLATE CYCLASE ACTIVITY

Endocrinology, 1981
Bromocriptine and its parent compound alpha-ergocryptine were investigated with respect to their ability to interact with the guanylate cyclase (E.C.4.6.1.2)-cyclic GMP system in vitro in the rat pituitary and ovary. Both bromocriptine and alpha-ergocryptine enhanced guanylate cyclase two- to threefold in both of these tissues over a concentration ...
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Biotin Enhances Guanylate Cyclase Activity

Science, 1982
Biotin and its analog, (+)-biotin- p -nitrophenyl ester enhanced guanylate cyclase activity two- to threefold in rat liver, kidney, colon, cerebellum, and heart. Dose-response relationships revealed that at concentrations as low as 1 micromolar, both biotin and its analog caused maximal augmentation of guanylate ...
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Plasma Membrane Guanylate Cyclase

1997
Cyclic GMP was discovered in rat urine (Ashman et al., 1963) at almost the same time the remarkable discovery of cyclic AMP was made (Sutherland and Rall, 1960). Mimicking the conceptual framework formulated for the second messenger role of cyclic AMP, cyclic GMP was also proposed to act as a second messenger of certain hormonal signals (reviewed in ...
Rameshwar K. Sharma, Teresa Duda
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Soluble guanylate cyclases in the retina

Molecular and Cellular Biochemistry, 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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