18355002

Source:http://linkedlifedata.com/resource/pubmed/id/18355002

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Predicate	Object
rdf:type	pubmed:Citation
lifeskim:mentions	umls-concept:C0006826, umls-concept:C0033684, umls-concept:C1292734, umls-concept:C1522326
pubmed:issue	3
pubmed:dateCreated	2008-3-21
pubmed:abstractText	Multiprotein complexes figure prominently in all cellular processes. Disrupting formation of these complexes can modulate key cellular pathways and offers new possibilities for therapeutic intervention. A new study illustrates an efficient approach for developing high-affinity mimics that inhibit protein-protein interactions.
pubmed:language	eng
pubmed:journal	http://linkedlifedata.com/resource/pubmed/journal/101282906
pubmed:citationSubset	IM
pubmed:chemical	http://linkedlifedata.com/resource/pubmed/chemical/Proteins
pubmed:status	MEDLINE
pubmed:month	Mar
pubmed:issn	1554-8937
pubmed:author	pubmed-author:LohStewart NSN
pubmed:issnType	Electronic
pubmed:day	20
pubmed:volume	3
pubmed:owner	NLM
pubmed:authorsComplete	Y
pubmed:pagination	140-1
pubmed:meshHeading	pubmed-meshheading:18355002-Animals, pubmed-meshheading:18355002-Humans, pubmed-meshheading:18355002-Models, Molecular, pubmed-meshheading:18355002-Neoplasms, pubmed-meshheading:18355002-Proteins
pubmed:year	2008
pubmed:articleTitle	Disrupting proteins to treat cancer.
pubmed:affiliation	Department of Biochemistry and Molecular Biology, State University of New York, Upstate Medical University, 750 East Adams Street, Syracuse, New York 13210, USA. lohs@upstate.edu
pubmed:publicationType	Journal Article