Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
6
pubmed:dateCreated
2002-7-12
pubmed:abstractText
ErbB4 is a member of the epidermal growth factor receptor(EGFR) family of tyrosine kinases, which includes EGFR/ErbB1, ErbB2/HER2/Neu, and ErbB3/HER3. These receptors play important roles both in normal development and in neoplasia. For example, deregulated signaling by ErbB1 and ErbB2 is observed in many human malignancies. In contrast, the roles that ErbB4 plays in tumorigenesis and normal biological processes have not been clearly defined. To identify the biological responses that are coupled to ErbB4, we have constructed three constitutively active ErbB4 mutants. Unlike a constitutively active ErbB2 mutant, the ErbB4 mutants are not coupled to increased cell proliferation, loss of contact inhibition, or anchorage independence in a rodent fibroblast cell line. This suggests that ErbB2 and ErbB4 may play distinct roles in tumorigenesis in vivo.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jun
pubmed:issn
1044-9523
pubmed:author
pubmed:issnType
Print
pubmed:volume
13
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
247-56
pubmed:dateRevised
2011-11-2
pubmed:meshHeading
pubmed-meshheading:12114214-Cell Adhesion, pubmed-meshheading:12114214-Cell Division, pubmed-meshheading:12114214-Cells, Cultured, pubmed-meshheading:12114214-Colony-Forming Units Assay, pubmed-meshheading:12114214-Contact Inhibition, pubmed-meshheading:12114214-DNA Primers, pubmed-meshheading:12114214-Fibroblasts, pubmed-meshheading:12114214-Humans, pubmed-meshheading:12114214-Immunoblotting, pubmed-meshheading:12114214-Mutagenesis, Site-Directed, pubmed-meshheading:12114214-Phosphorylation, pubmed-meshheading:12114214-Plasmids, pubmed-meshheading:12114214-Polymerase Chain Reaction, pubmed-meshheading:12114214-Receptor, Epidermal Growth Factor, pubmed-meshheading:12114214-Receptor, erbB-2, pubmed-meshheading:12114214-Retroviridae, pubmed-meshheading:12114214-Signal Transduction, pubmed-meshheading:12114214-Tyrosine
pubmed:year
2002
pubmed:articleTitle
Constitutively active ErbB4 and ErbB2 mutants exhibit distinct biological activities.
pubmed:affiliation
Department of Medicinal Chemistry and Molecular Pharmacology, Purdue University, West Lafayette, Indiana 47907-1333, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't