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Condorelli2001_GuanylateCyclase


ABSTRACT: This model features the observations of <a href = "http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=11325714">Condorelli P, George SC. Biophys J. (2001) 80(5):2110-9</a>. They propose a in vivo mechanism for the binding of free NO to sGC based on in vitro data within both pulmonary and vascular smooth muscle. All the parameters used have been obtained from reported results based on experiments. One important conclusion they make is that control of sGC in vivo is most likely to be ultra-sensitive and that activation in vivo occurs at lower NO concentrations than reported.

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To cite BioModels Database, please use: Li C, Donizelli M, Rodriguez N, Dharuri H, Endler L, Chelliah V, Li L, He E, Henry A, Stefan MI, Snoep JL, Hucka M, Le Novère N, Laibe C (2010) BioModels Database: An enhanced, curated and annotated resource for published quantitative kinetic models. BMC Syst Biol., 4:92.

ORGANISM(S): Homo sapiens

SUBMITTER: Sharat Vayttaden 

PROVIDER: MODEL4780441670 | biostudies-other |

SECONDARY ACCESSION(S): 11325714

REPOSITORIES: biostudies-other

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Publications

In vivo control of soluble guanylate cyclase activation by nitric oxide: a kinetic analysis.

Condorelli P P   George S C SC  

Biophysical journal 20010501 5


Free nitric oxide (NO) activates soluble guanylate cyclase (sGC), an enzyme, within both pulmonary and vascular smooth muscle. sGC catalyzes the cyclization of guanosine 5'-triphosphate to guanosine 3',5'-cyclic monophosphate (cGMP). Binding rates of NO to the ferrous heme(s) of sGC have been measured in vitro. However, a missing link in our understanding of the control mechanism of sGC by NO is a comprehensive in vivo kinetic analysis. Available literature data suggests that NO dissociation fro  ...[more]

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