Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
5
pubmed:dateCreated
2005-6-22
pubmed:abstractText
Ligand dependent activity of receptor tyrosine kinases is critical for modulating downstream signaling and cell proliferation. In normal cellular context, hepatocyte growth factor (HGF) regulates MET kinase activation and mediates cell proliferation, migration and motility. Recent elucidation of the MET extracellular domain suggests that the Sema domain, which bears structural similarity to other Semaphorins and Plexin family members, plays a critical role in ligand mediated receptor activation. Overexpression of MET which is observed in many cancers leads to ligand independent receptor dimerization and activation. Evidence to support a role for the Sema domain in cancer and therapeutic implications of targeting the Met Sema domain are discussed in this review.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
May
pubmed:issn
1551-4005
pubmed:author
pubmed:issnType
Electronic
pubmed:volume
4
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
683-5
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed:year
2005
pubmed:articleTitle
Met activation and receptor dimerization in cancer: a role for the Sema domain.
pubmed:affiliation
Molecular Oncology, Genentech Inc., South San Francisco, California 94080, USA. wickramasinghe.dineli@gene.com
pubmed:publicationType
Journal Article, Review