Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
6
pubmed:dateCreated
1997-8-26
pubmed:abstractText
Angiogenesis, the formation of new blood vessels, is essential for tumor growth. The inhibition of angiogenesis is therefore emerging as a promising therapy for cancer. Two natural products, fumagillin and ovalicin, were discovered to be potent inhibitors of angiogenesis due to their inhibition of endothelial cell proliferation. An analog of fumagillin, AGM-1470, is currently undergoing clinical trials for the treatment of a variety of cancers. The underlying molecular mechanism of the inhibition of angiogenesis by these natural drugs has remained unknown.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/Affinity Labels, http://linkedlifedata.com/resource/pubmed/chemical/Aminopeptidases, http://linkedlifedata.com/resource/pubmed/chemical/Antibiotics, Antineoplastic, http://linkedlifedata.com/resource/pubmed/chemical/Biotin, http://linkedlifedata.com/resource/pubmed/chemical/Cyclohexanes, http://linkedlifedata.com/resource/pubmed/chemical/Eukaryotic Initiation Factor-2, http://linkedlifedata.com/resource/pubmed/chemical/Fatty Acids, Unsaturated, http://linkedlifedata.com/resource/pubmed/chemical/Metalloendopeptidases, http://linkedlifedata.com/resource/pubmed/chemical/O-(chloroacetylcarbamoyl)fumagillol, http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Sesquiterpenes, http://linkedlifedata.com/resource/pubmed/chemical/fumagillin, http://linkedlifedata.com/resource/pubmed/chemical/methionine aminopeptidase 2, http://linkedlifedata.com/resource/pubmed/chemical/ovalicin
pubmed:status
MEDLINE
pubmed:month
Jun
pubmed:issn
1074-5521
pubmed:author
pubmed:issnType
Print
pubmed:volume
4
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
461-71
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed-meshheading:9224570-Affinity Labels, pubmed-meshheading:9224570-Amino Acid Sequence, pubmed-meshheading:9224570-Aminopeptidases, pubmed-meshheading:9224570-Animals, pubmed-meshheading:9224570-Antibiotics, Antineoplastic, pubmed-meshheading:9224570-Biotin, pubmed-meshheading:9224570-Cattle, pubmed-meshheading:9224570-Cells, Cultured, pubmed-meshheading:9224570-Cyclohexanes, pubmed-meshheading:9224570-Endothelium, Vascular, pubmed-meshheading:9224570-Eukaryotic Initiation Factor-2, pubmed-meshheading:9224570-Fatty Acids, Unsaturated, pubmed-meshheading:9224570-Metalloendopeptidases, pubmed-meshheading:9224570-Mice, pubmed-meshheading:9224570-Molecular Sequence Data, pubmed-meshheading:9224570-Molecular Structure, pubmed-meshheading:9224570-Neovascularization, Pathologic, pubmed-meshheading:9224570-Phosphorylation, pubmed-meshheading:9224570-Recombinant Proteins, pubmed-meshheading:9224570-Sesquiterpenes, pubmed-meshheading:9224570-Yeasts
pubmed:year
1997
pubmed:articleTitle
Methionine aminopeptidase (type 2) is the common target for angiogenesis inhibitors AGM-1470 and ovalicin.
pubmed:affiliation
Center for Cancer Research, Massachusetts Institute of Technology, Department of Biology, Cambridge, MA 02139, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, U.S. Gov't, Non-P.H.S., Research Support, Non-U.S. Gov't