16707553

Source:http://linkedlifedata.com/resource/pubmed/id/16707553

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Predicate	Object
rdf:type	pubmed:Citation
lifeskim:mentions	umls-concept:C0001443, umls-concept:C0006826, umls-concept:C0007102, umls-concept:C0085536, umls-concept:C0205234, umls-concept:C0205314, umls-concept:C0282639, umls-concept:C0334227, umls-concept:C0392756, umls-concept:C0441655, umls-concept:C0679622, umls-concept:C1158592, umls-concept:C1366487, umls-concept:C1366765, umls-concept:C1414141, umls-concept:C1704259, umls-concept:C1705987, umls-concept:C1948023
pubmed:issue	3
pubmed:dateCreated	2006-8-9
pubmed:commentsCorrections	http://linkedlifedata.com/resource/pubmed/commentcorrection/16707553-16611738
pubmed:language	eng
pubmed:journal	http://linkedlifedata.com/resource/pubmed/journal/100901225
pubmed:citationSubset	IM
pubmed:chemical	http://linkedlifedata.com/resource/pubmed/chemical/Adenosine, http://linkedlifedata.com/resource/pubmed/chemical/Adenosine Deaminase, http://linkedlifedata.com/resource/pubmed/chemical/Dipeptidyl Peptidase 4, http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Purinergic P1
pubmed:status	MEDLINE
pubmed:month	Sep
pubmed:issn	0363-6143
pubmed:author	pubmed-author:LindenJoelJ
pubmed:issnType	Print
pubmed:volume	291
pubmed:owner	NLM
pubmed:authorsComplete	Y
pubmed:pagination	C405-6
pubmed:dateRevised	2010-11-18
pubmed:meshHeading	pubmed-meshheading:16707553-Adenosine, pubmed-meshheading:16707553-Adenosine Deaminase, pubmed-meshheading:16707553-Animals, pubmed-meshheading:16707553-Dipeptidyl Peptidase 4, pubmed-meshheading:16707553-Down-Regulation, pubmed-meshheading:16707553-HT29 Cells, pubmed-meshheading:16707553-Humans, pubmed-meshheading:16707553-Neoplasms, pubmed-meshheading:16707553-Neovascularization, Pathologic, pubmed-meshheading:16707553-Receptors, Purinergic P1, pubmed-meshheading:16707553-Tumor Escape
pubmed:year	2006
pubmed:articleTitle	Adenosine metabolism and cancer. Focus on "Adenosine downregulates DPPIV on HT-29 colon cancer cells by stimulating protein tyrosine phosphatases and reducing ERK1/2 activity via a novel pathway".
pubmed:publicationType	Editorial, Comment