Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:dateCreated
2003-10-29
pubmed:abstractText
The C-terminal four amino acids (GEEV) of human alpha1A-adrenergic receptors (ARs) have been reported to interact with the PDZ domain of neuronal nitric oxide synthase (nNOS) in a yeast two-hybrid system. The other two alpha1-AR subtypes have no sequence homology in this region, raising the possibility of subtype-specific protein-protein interactions.
pubmed:commentsCorrections
http://linkedlifedata.com/resource/pubmed/commentcorrection/12184796-10221915, http://linkedlifedata.com/resource/pubmed/commentcorrection/12184796-10349848, http://linkedlifedata.com/resource/pubmed/commentcorrection/12184796-10364559, http://linkedlifedata.com/resource/pubmed/commentcorrection/12184796-10443582, http://linkedlifedata.com/resource/pubmed/commentcorrection/12184796-10510297, http://linkedlifedata.com/resource/pubmed/commentcorrection/12184796-10681501, http://linkedlifedata.com/resource/pubmed/commentcorrection/12184796-11283303, http://linkedlifedata.com/resource/pubmed/commentcorrection/12184796-12065700, http://linkedlifedata.com/resource/pubmed/commentcorrection/12184796-1328250, http://linkedlifedata.com/resource/pubmed/commentcorrection/12184796-7746284, http://linkedlifedata.com/resource/pubmed/commentcorrection/12184796-8396931, http://linkedlifedata.com/resource/pubmed/commentcorrection/12184796-8625413, http://linkedlifedata.com/resource/pubmed/commentcorrection/12184796-9199503, http://linkedlifedata.com/resource/pubmed/commentcorrection/12184796-9733758, http://linkedlifedata.com/resource/pubmed/commentcorrection/12184796-9931481
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/ADRA1A protein, human, http://linkedlifedata.com/resource/pubmed/chemical/ADRA1B protein, human, http://linkedlifedata.com/resource/pubmed/chemical/Adra1a protein, rat, http://linkedlifedata.com/resource/pubmed/chemical/Adra1b protein, rat, http://linkedlifedata.com/resource/pubmed/chemical/Antibodies, http://linkedlifedata.com/resource/pubmed/chemical/Enzyme Inhibitors, http://linkedlifedata.com/resource/pubmed/chemical/Mitogen-Activated Protein Kinases, http://linkedlifedata.com/resource/pubmed/chemical/NG-Nitroarginine Methyl Ester, http://linkedlifedata.com/resource/pubmed/chemical/NOS1 protein, human, http://linkedlifedata.com/resource/pubmed/chemical/Nitric Oxide Synthase, http://linkedlifedata.com/resource/pubmed/chemical/Nitric Oxide Synthase Type I, http://linkedlifedata.com/resource/pubmed/chemical/Nos1 protein, rat, http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Adrenergic, alpha-1
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
1471-2210
pubmed:author
pubmed:issnType
Electronic
pubmed:day
16
pubmed:volume
2
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
17
pubmed:dateRevised
2010-11-18
pubmed:meshHeading
pubmed-meshheading:12184796-Animals, pubmed-meshheading:12184796-Antibodies, pubmed-meshheading:12184796-Cells, Cultured, pubmed-meshheading:12184796-Enzyme Activation, pubmed-meshheading:12184796-Enzyme Inhibitors, pubmed-meshheading:12184796-Humans, pubmed-meshheading:12184796-Mitogen-Activated Protein Kinases, pubmed-meshheading:12184796-NG-Nitroarginine Methyl Ester, pubmed-meshheading:12184796-Nitric Oxide Synthase, pubmed-meshheading:12184796-Nitric Oxide Synthase Type I, pubmed-meshheading:12184796-PC12 Cells, pubmed-meshheading:12184796-Precipitin Tests, pubmed-meshheading:12184796-Protein Binding, pubmed-meshheading:12184796-Protein Structure, Tertiary, pubmed-meshheading:12184796-Rats, pubmed-meshheading:12184796-Receptors, Adrenergic, alpha-1, pubmed-meshheading:12184796-Transfection
pubmed:year
2002
pubmed:articleTitle
Interaction of neuronal nitric oxide synthase with alpha1-adrenergic receptor subtypes in transfected HEK-293 cells.
pubmed:affiliation
Department of Pharmacology, Emory University, Atlanta, GA 30322, USA. aspupo@ibb.unesp.br
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't