2004
DOI: 10.1016/j.neuint.2004.03.011
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Nitric oxide-sensitive guanylyl cyclase: structure and regulation

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Cited by 137 publications
(116 citation statements)
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“…Once released, NO diffuses through the cell membrane and enters the cytosol, where it meets the target protein, such as sGC (19,20). NO may bind to the protoporphyrin ring of sGC, causing activation of the enzyme and leading to the formation of cGMP (21,22). As an intracellular signaling molecule, cGMP plays an important role in the regulation of various cellular events and may exert its effects through PKGs, which catalyze the phosphorylation at serine/threonine residues on substrate proteins, thereby altering their activities (23).…”
Section: Discussionmentioning
confidence: 99%
“…Once released, NO diffuses through the cell membrane and enters the cytosol, where it meets the target protein, such as sGC (19,20). NO may bind to the protoporphyrin ring of sGC, causing activation of the enzyme and leading to the formation of cGMP (21,22). As an intracellular signaling molecule, cGMP plays an important role in the regulation of various cellular events and may exert its effects through PKGs, which catalyze the phosphorylation at serine/threonine residues on substrate proteins, thereby altering their activities (23).…”
Section: Discussionmentioning
confidence: 99%
“…It is composed of a cytosolic heterodimer of sGCa and sGCb subunits. 28 Among these subunits, sGCb1 acts as the common dimerizing subunit for the two sGCa subunits and is crucial for the expression of sGC in cells. Knockdown of the sGCb1 subunit gene results in the lack of sGC expression.…”
Section: Discussionmentioning
confidence: 99%
“…NO-GC was initially thought to be entirely cytosolic and was thus named "soluble GC", however it has also been found associated to membranes (Zabel et al 2002). NO-GC is composed of an α and a β subunit and both subunits are required for catalytic activity (Koesling et al 2004). Each subunit has a regulatory domain which contains a prosthetic heme group that is the NO-binding site, a catalytic domain that shares sequence homology with the corresponding domains in pGC and adenylyl cyclases and a central domain which allows subunit dimerization (Foster et al 1999) (Fig.…”
Section: Guanylyl Cyclisesmentioning
confidence: 99%