15604398

Source:http://linkedlifedata.com/resource/pubmed/id/15604398

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Predicate	Object
rdf:type	pubmed:Citation
lifeskim:mentions	umls-concept:C0031715, umls-concept:C0037083, umls-concept:C0127400, umls-concept:C1363844
pubmed:issue	5704
pubmed:dateCreated	2004-12-17
pubmed:commentsCorrections	http://linkedlifedata.com/resource/pubmed/commentcorrection/15604398-15604408
pubmed:language	eng
pubmed:journal	http://linkedlifedata.com/resource/pubmed/journal/0404511
pubmed:citationSubset	IM
pubmed:chemical	http://linkedlifedata.com/resource/pubmed/chemical/1-diphosphoinositol..., http://linkedlifedata.com/resource/pubmed/chemical/Inositol, http://linkedlifedata.com/resource/pubmed/chemical/Inositol Phosphates, http://linkedlifedata.com/resource/pubmed/chemical/NSR1 protein, S cerevisiae, http://linkedlifedata.com/resource/pubmed/chemical/Nuclear Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Phosphates, http://linkedlifedata.com/resource/pubmed/chemical/Phosphatidylinositols, http://linkedlifedata.com/resource/pubmed/chemical/Phosphotransferases (Phosphate..., http://linkedlifedata.com/resource/pubmed/chemical/Proteins, http://linkedlifedata.com/resource/pubmed/chemical/RNA-Binding Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Saccharomyces cerevisiae Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Serine
pubmed:status	MEDLINE
pubmed:month	Dec
pubmed:issn	1095-9203
pubmed:author	pubmed-author:HunterTonyT, pubmed-author:YorkJohn DJD
pubmed:issnType	Electronic
pubmed:day	17
pubmed:volume	306
pubmed:owner	NLM
pubmed:authorsComplete	Y
pubmed:pagination	2053-5
pubmed:dateRevised	2007-3-19
pubmed:meshHeading	pubmed-meshheading:15604398-Cell Membrane, pubmed-meshheading:15604398-Inositol, pubmed-meshheading:15604398-Inositol Phosphates, pubmed-meshheading:15604398-Models, Biological, pubmed-meshheading:15604398-Molecular Conformation, pubmed-meshheading:15604398-Nuclear Proteins, pubmed-meshheading:15604398-Phosphates, pubmed-meshheading:15604398-Phosphatidylinositols, pubmed-meshheading:15604398-Phosphorylation, pubmed-meshheading:15604398-Phosphotransferases (Phosphate Group Acceptor), pubmed-meshheading:15604398-Proteins, pubmed-meshheading:15604398-RNA-Binding Proteins, pubmed-meshheading:15604398-Saccharomyces cerevisiae, pubmed-meshheading:15604398-Saccharomyces cerevisiae Proteins, pubmed-meshheading:15604398-Second Messenger Systems, pubmed-meshheading:15604398-Serine, pubmed-meshheading:15604398-Signal Transduction
pubmed:year	2004
pubmed:articleTitle	Signal transduction. Unexpected mediators of protein phosphorylation.
pubmed:affiliation	Department of Pharmacology and Cancer Biology, Howard Hughes Medical Institute, Duke University Medical Center, Durham, NC 27710, USA. yorkj@duke.edu
pubmed:publicationType	Journal Article, Comment