Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
31
pubmed:dateCreated
1993-11-29
pubmed:abstractText
Phosphotyrosine-containing synthetic peptides were used to identify the binding sites for cellular polypeptides involved in nerve growth factor receptor/Trk-mediated signal transduction. In vitro association of SHC and the p85 subunit of phosphatidylinositol 3'-kinase with the Trk tyrosine kinase was prevented only by phosphorylated Y-490- and Y-751-containing peptides, respectively. In spite of the close proximity of the p85 binding site to that of phospholipase C gamma (Y-785), both target proteins are able to interact with the same receptor molecule simultaneously.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/Macromolecular Substances, http://linkedlifedata.com/resource/pubmed/chemical/Oligodeoxyribonucleotides, http://linkedlifedata.com/resource/pubmed/chemical/Peptide Fragments, http://linkedlifedata.com/resource/pubmed/chemical/Phosphatidylinositol 3-Kinases, http://linkedlifedata.com/resource/pubmed/chemical/Phosphoproteins, http://linkedlifedata.com/resource/pubmed/chemical/Phosphotransferases (Alcohol Group..., http://linkedlifedata.com/resource/pubmed/chemical/Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Proto-Oncogene Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Receptor, trkA, http://linkedlifedata.com/resource/pubmed/chemical/Receptor Protein-Tyrosine Kinases, http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Nerve Growth Factor
pubmed:status
MEDLINE
pubmed:month
Nov
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
5
pubmed:volume
268
pubmed:geneSymbol
trk
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
22963-6
pubmed:dateRevised
2010-11-18
pubmed:meshHeading
pubmed-meshheading:8226808-Amino Acid Sequence, pubmed-meshheading:8226808-Base Sequence, pubmed-meshheading:8226808-Binding, Competitive, pubmed-meshheading:8226808-Binding Sites, pubmed-meshheading:8226808-Cell Line, pubmed-meshheading:8226808-Humans, pubmed-meshheading:8226808-Macromolecular Substances, pubmed-meshheading:8226808-Molecular Sequence Data, pubmed-meshheading:8226808-Mutagenesis, Site-Directed, pubmed-meshheading:8226808-Oligodeoxyribonucleotides, pubmed-meshheading:8226808-Peptide Fragments, pubmed-meshheading:8226808-Phosphatidylinositol 3-Kinases, pubmed-meshheading:8226808-Phosphoproteins, pubmed-meshheading:8226808-Phosphotransferases (Alcohol Group Acceptor), pubmed-meshheading:8226808-Proteins, pubmed-meshheading:8226808-Proto-Oncogene Proteins, pubmed-meshheading:8226808-Receptor, trkA, pubmed-meshheading:8226808-Receptor Protein-Tyrosine Kinases, pubmed-meshheading:8226808-Receptors, Nerve Growth Factor, pubmed-meshheading:8226808-Signal Transduction, pubmed-meshheading:8226808-Structure-Activity Relationship
pubmed:year
1993
pubmed:articleTitle
Identification of Trk binding sites for SHC and phosphatidylinositol 3'-kinase and formation of a multimeric signaling complex.
pubmed:affiliation
Department of Molecular Biology, Max-Planck-Institut für Biochemie, Martinsried, Germany.
pubmed:publicationType
Journal Article, In Vitro, Research Support, Non-U.S. Gov't