Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
5186
pubmed:dateCreated
1994-12-7
pubmed:abstractText
The EPH-related transmembrane tyrosine kinases constitute the largest known family of receptor-like tyrosine kinases, with many members displaying specific patterns of expression in the developing and adult nervous system. A family of cell surface-bound ligands exhibiting distinct, but overlapping, specificities for these EPH-related kinases was identified. These ligands were unable to act as conventional soluble factors. However, they did function when presented in membrane-bound form, suggesting that they require direct cell-to-cell contact to activate their receptors. Membrane attachment may serve to facilitate ligand dimerization or aggregation, because antibody-mediated clustering activated previously inactive soluble forms of these ligands.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/DNA-Binding Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Ephrin-A1, http://linkedlifedata.com/resource/pubmed/chemical/Ephrin-B1, http://linkedlifedata.com/resource/pubmed/chemical/Ligands, http://linkedlifedata.com/resource/pubmed/chemical/Membrane Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Proto-Oncogene Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Receptor, EphA5, http://linkedlifedata.com/resource/pubmed/chemical/Receptor Protein-Tyrosine Kinases, http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Fusion Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Retroviridae Proteins, Oncogenic, http://linkedlifedata.com/resource/pubmed/chemical/Transcription Factors, http://linkedlifedata.com/resource/pubmed/chemical/ets-Domain Protein Elk-1
pubmed:status
MEDLINE
pubmed:month
Nov
pubmed:issn
0036-8075
pubmed:author
pubmed:issnType
Print
pubmed:day
4
pubmed:volume
266
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
816-9
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed-meshheading:7973638-Amino Acid Sequence, pubmed-meshheading:7973638-Animals, pubmed-meshheading:7973638-Cell Line, pubmed-meshheading:7973638-Cell Membrane, pubmed-meshheading:7973638-DNA-Binding Proteins, pubmed-meshheading:7973638-Ephrin-A1, pubmed-meshheading:7973638-Ephrin-B1, pubmed-meshheading:7973638-Humans, pubmed-meshheading:7973638-Ligands, pubmed-meshheading:7973638-Membrane Proteins, pubmed-meshheading:7973638-Molecular Sequence Data, pubmed-meshheading:7973638-Neurons, pubmed-meshheading:7973638-Phosphorylation, pubmed-meshheading:7973638-Proteins, pubmed-meshheading:7973638-Proto-Oncogene Proteins, pubmed-meshheading:7973638-Receptor, EphA5, pubmed-meshheading:7973638-Receptor Protein-Tyrosine Kinases, pubmed-meshheading:7973638-Recombinant Fusion Proteins, pubmed-meshheading:7973638-Retroviridae Proteins, Oncogenic, pubmed-meshheading:7973638-Solubility, pubmed-meshheading:7973638-Transcription Factors, pubmed-meshheading:7973638-Transfection, pubmed-meshheading:7973638-Tumor Cells, Cultured, pubmed-meshheading:7973638-ets-Domain Protein Elk-1
pubmed:year
1994
pubmed:articleTitle
Ligands for EPH-related receptor tyrosine kinases that require membrane attachment or clustering for activity.
pubmed:affiliation
Regeneron Pharmaceuticals, Tarrytown, NY 10591.
pubmed:publicationType
Journal Article