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PredicateObject
rdf:type
lifeskim:mentions
pubmed:dateCreated
1995-10-26
pubmed:abstractText
Microorganisms and plants are treasuries of secondary metabolites having unique structures and biological activities. We have isolated inhibitors of cellular signal transduction from them. Phosphatidylinositol turnover inhibitors include inostamycin, piericidins and echiguanines. Erbstatin and lavendustin A were isolated as tyrosine kinase inhibitors, and dephostatin was isolated as a tyrosine phosphatase inhibitor. Recently, we have isolated a new vinca alkaloid having anti-ras activity. These signal transduction inhibitors will be useful for mechanistic studies and suppression of cancer.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
0065-2571
pubmed:author
pubmed:issnType
Print
pubmed:volume
35
pubmed:geneSymbol
erb B, erb B1, erb B2, fms, hst, jun, myc, ras, sis, src, trk
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
43-53
pubmed:dateRevised
2010-11-18
pubmed:meshHeading
pubmed-meshheading:7572353-1-Phosphatidylinositol 4-Kinase, pubmed-meshheading:7572353-CDP-Diacylglycerol-Inositol 3-Phosphatidyltransferase, pubmed-meshheading:7572353-Enzyme Inhibitors, pubmed-meshheading:7572353-Fungi, pubmed-meshheading:7572353-Molecular Structure, pubmed-meshheading:7572353-Phosphatidylinositol 3-Kinases, pubmed-meshheading:7572353-Phosphatidylinositols, pubmed-meshheading:7572353-Phosphotransferases (Alcohol Group Acceptor), pubmed-meshheading:7572353-Plants, pubmed-meshheading:7572353-Protein Tyrosine Phosphatases, pubmed-meshheading:7572353-Protein-Tyrosine Kinases, pubmed-meshheading:7572353-Signal Transduction, pubmed-meshheading:7572353-Streptomyces, pubmed-meshheading:7572353-Transferases (Other Substituted Phosphate Groups), pubmed-meshheading:7572353-ras Proteins
pubmed:year
1995
pubmed:articleTitle
Isolation and biological activities of signal transduction inhibitors from microorganisms and plants.
pubmed:affiliation
Department of Applied Chemistry, Faculty of Science and Technology, Keio University, Yokohama, Japan.
pubmed:publicationType
Journal Article, Review