12809244

Source:http://linkedlifedata.com/resource/pubmed/id/12809244

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Predicate	Object
rdf:type	pubmed:Citation
lifeskim:mentions	umls-concept:C0178587, umls-concept:C0205245, umls-concept:C0243045, umls-concept:C1511131, umls-concept:C2603343
pubmed:issue	11
pubmed:dateCreated	2003-6-17
pubmed:abstractText	Density functional theory (DFT) calculations were carried out to study the molecular mechanism of the phosphoryl transfer reaction catalyzed by cyclin-dependent kinases (CDKs). The DFT study presented here shows that CDKs catalyze the phosphoryl transfer reaction from ATP to the serine substrate through a single step mechanism with a SN2-like transition state.
pubmed:language	eng
pubmed:journal	http://linkedlifedata.com/resource/pubmed/journal/9610838
pubmed:citationSubset	IM
pubmed:chemical	http://linkedlifedata.com/resource/pubmed/chemical/Cyclin-Dependent Kinases
pubmed:status	MEDLINE
pubmed:month	Jun
pubmed:issn	1359-7345
pubmed:author	pubmed-author:CavalliAndreaA, pubmed-author:De VivoMarcoM, pubmed-author:RecanatiniMaurizioM
pubmed:issnType	Print
pubmed:day	7
pubmed:owner	NLM
pubmed:authorsComplete	Y
pubmed:pagination	1308-9
pubmed:dateRevised	2009-11-19
pubmed:meshHeading	pubmed-meshheading:12809244-Catalysis, pubmed-meshheading:12809244-Cyclin-Dependent Kinases, pubmed-meshheading:12809244-Models, Molecular
pubmed:year	2003
pubmed:articleTitle	Density functional study of the enzymatic reaction catalyzed by a cyclin-dependent kinase.
pubmed:affiliation	University of Bologna, Department of Pharmaceutical Sciences, Via Belmeloro 6, I-40126 Bologna, Italy.
pubmed:publicationType	Journal Article, Research Support, Non-U.S. Gov't