15324660

Source:http://linkedlifedata.com/resource/pubmed/id/15324660

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Predicate	Object
rdf:type	pubmed:Citation
lifeskim:mentions	umls-concept:C0010853, umls-concept:C0029246, umls-concept:C0090388, umls-concept:C0178539, umls-concept:C0205245, umls-concept:C0242210, umls-concept:C0851285, umls-concept:C0936012, umls-concept:C1314939, umls-concept:C1421563, umls-concept:C1515655
pubmed:issue	16
pubmed:dateCreated	2004-8-24
pubmed:abstractText	14-3-3 proteins are abundant and conserved polypeptides that mediate the cellular effects of basophilic protein kinases through their ability to bind specific peptide motifs phosphorylated on serine or threonine.
pubmed:grant	http://linkedlifedata.com/resource/pubmed/grant/DK44239
pubmed:language	eng
pubmed:journal	http://linkedlifedata.com/resource/pubmed/journal/9107782
pubmed:citationSubset	IM
pubmed:chemical	http://linkedlifedata.com/resource/pubmed/chemical/14-3-3 Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Actins, http://linkedlifedata.com/resource/pubmed/chemical/Cyclic AMP-Dependent Protein Kinases, http://linkedlifedata.com/resource/pubmed/chemical/DNA, Complementary, http://linkedlifedata.com/resource/pubmed/chemical/DNA Primers, http://linkedlifedata.com/resource/pubmed/chemical/GTP-Binding Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Guanine Nucleotide Exchange Factors, http://linkedlifedata.com/resource/pubmed/chemical/Protein-Serine-Threonine Kinases, http://linkedlifedata.com/resource/pubmed/chemical/Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Tyrosine 3-Monooxygenase, http://linkedlifedata.com/resource/pubmed/chemical/rho guanine nucleotide exchange...
pubmed:status	MEDLINE
pubmed:month	Aug
pubmed:issn	0960-9822
pubmed:author	pubmed-author:FawcettJames PJP, pubmed-author:JinJingJ, pubmed-author:KulkarniSarangS, pubmed-author:LangebergLorene KLK, pubmed-author:MetalnikovPavelP, pubmed-author:O'DonnellPaulP, pubmed-author:PawsonTonyT, pubmed-author:ScottJohn DJD, pubmed-author:SmithF DonelsonFD, pubmed-author:StarkChrisC, pubmed-author:TaylorLorneL, pubmed-author:TaylorPaulP, pubmed-author:WellsClark DCD, pubmed-author:WoodgettJames RJR, pubmed-author:ZougmanAlexandreA
pubmed:issnType	Print
pubmed:day	24
pubmed:volume	14
pubmed:owner	NLM
pubmed:authorsComplete	Y
pubmed:pagination	1436-50
pubmed:dateRevised	2008-9-11
pubmed:meshHeading	pubmed-meshheading:15324660-14-3-3 Proteins, pubmed-meshheading:15324660-Actins, pubmed-meshheading:15324660-Animals, pubmed-meshheading:15324660-Cell Differentiation, pubmed-meshheading:15324660-Cell Size, pubmed-meshheading:15324660-Cells, Cultured, pubmed-meshheading:15324660-Cluster Analysis, pubmed-meshheading:15324660-Computational Biology, pubmed-meshheading:15324660-Cyclic AMP-Dependent Protein Kinases, pubmed-meshheading:15324660-Cytoskeleton, pubmed-meshheading:15324660-DNA, Complementary, pubmed-meshheading:15324660-DNA Primers, pubmed-meshheading:15324660-Dogs, pubmed-meshheading:15324660-Fluorescent Antibody Technique, pubmed-meshheading:15324660-GTP-Binding Proteins, pubmed-meshheading:15324660-Guanine Nucleotide Exchange Factors, pubmed-meshheading:15324660-Humans, pubmed-meshheading:15324660-Mass Spectrometry, pubmed-meshheading:15324660-Mice, pubmed-meshheading:15324660-Phosphorylation, pubmed-meshheading:15324660-Precipitin Tests, pubmed-meshheading:15324660-Protein Structure, Tertiary, pubmed-meshheading:15324660-Protein-Serine-Threonine Kinases, pubmed-meshheading:15324660-Proteins, pubmed-meshheading:15324660-Proteomics, pubmed-meshheading:15324660-Transfection, pubmed-meshheading:15324660-Tyrosine 3-Monooxygenase
pubmed:year	2004
pubmed:articleTitle	Proteomic, functional, and domain-based analysis of in vivo 14-3-3 binding proteins involved in cytoskeletal regulation and cellular organization.
pubmed:affiliation	Samuel Lunenfeld Research Institute, Mount Sinai Hospital, 600 University Avenue, Toronto, Ontario M5G 1X5, Canada.
pubmed:publicationType	Journal Article, Comparative Study, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't