Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
8
pubmed:dateCreated
2008-8-27
pubmed:abstractText
Platelets, specialized adhesive cells, play key roles in normal and pathological hemostasis through their ability to rapidly adhere to subendothelial matrix proteins (adhesion) and to other activated platelets (aggregation), functions which are inhibited by nitric oxide (NO). Platelets have been reported to be regulated not only by exogenous endothelium-derived NO, but also by two isoforms of NO synthase, endothelial (eNOS) and inducible (iNOS), endogenously expressed in platelets. however, data concerning expression, regulation and function of eNOS AND iNOS in platelets remain controversial.
pubmed:commentsCorrections
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/Cyclic GMP, http://linkedlifedata.com/resource/pubmed/chemical/Enzyme Inhibitors, http://linkedlifedata.com/resource/pubmed/chemical/Guanylate Cyclase, http://linkedlifedata.com/resource/pubmed/chemical/NG-Nitroarginine Methyl Ester, http://linkedlifedata.com/resource/pubmed/chemical/NOS2 protein, human, http://linkedlifedata.com/resource/pubmed/chemical/NOS3 protein, human, http://linkedlifedata.com/resource/pubmed/chemical/Nitric Oxide, http://linkedlifedata.com/resource/pubmed/chemical/Nitric Oxide Synthase, http://linkedlifedata.com/resource/pubmed/chemical/Nitric Oxide Synthase Type II, http://linkedlifedata.com/resource/pubmed/chemical/Nitric Oxide Synthase Type III, http://linkedlifedata.com/resource/pubmed/chemical/Nos2 protein, mouse, http://linkedlifedata.com/resource/pubmed/chemical/Nos3 protein, mouse, http://linkedlifedata.com/resource/pubmed/chemical/RNA, Messenger, http://linkedlifedata.com/resource/pubmed/chemical/Ristocetin, http://linkedlifedata.com/resource/pubmed/chemical/omega-N-Methylarginine, http://linkedlifedata.com/resource/pubmed/chemical/src-Family Kinases, http://linkedlifedata.com/resource/pubmed/chemical/von Willebrand Factor
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
1538-7836
pubmed:author
pubmed:issnType
Electronic
pubmed:volume
6
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1376-84
pubmed:dateRevised
2011-10-27
pubmed:meshHeading
pubmed-meshheading:18485089-Animals, pubmed-meshheading:18485089-Blood Platelets, pubmed-meshheading:18485089-Cyclic GMP, pubmed-meshheading:18485089-Enzyme Activation, pubmed-meshheading:18485089-Enzyme Inhibitors, pubmed-meshheading:18485089-Guanylate Cyclase, pubmed-meshheading:18485089-Humans, pubmed-meshheading:18485089-Mice, pubmed-meshheading:18485089-Mice, Knockout, pubmed-meshheading:18485089-NG-Nitroarginine Methyl Ester, pubmed-meshheading:18485089-Nitric Oxide, pubmed-meshheading:18485089-Nitric Oxide Synthase, pubmed-meshheading:18485089-Nitric Oxide Synthase Type II, pubmed-meshheading:18485089-Nitric Oxide Synthase Type III, pubmed-meshheading:18485089-Phosphorylation, pubmed-meshheading:18485089-RNA, Messenger, pubmed-meshheading:18485089-Ristocetin, pubmed-meshheading:18485089-Solubility, pubmed-meshheading:18485089-omega-N-Methylarginine, pubmed-meshheading:18485089-src-Family Kinases, pubmed-meshheading:18485089-von Willebrand Factor
pubmed:year
2008
pubmed:articleTitle
NO-synthase-/NO-independent regulation of human and murine platelet soluble guanylyl cyclase activity.
pubmed:affiliation
Institute of Clinical Biochemistry and Pathobiochemistry, University of Wuerzburg, Wuerzburg, Germany.
pubmed:publicationType
Journal Article, In Vitro, Research Support, Non-U.S. Gov't