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rdf:type |
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lifeskim:mentions |
umls-concept:C0033681,
umls-concept:C0033684,
umls-concept:C0037791,
umls-concept:C0080298,
umls-concept:C0205250,
umls-concept:C0439849,
umls-concept:C0445223,
umls-concept:C0812303,
umls-concept:C0919478,
umls-concept:C1334043,
umls-concept:C1514562,
umls-concept:C1552599,
umls-concept:C1704675,
umls-concept:C1704787,
umls-concept:C1880389,
umls-concept:C1883204,
umls-concept:C1883221,
umls-concept:C2697616
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pubmed:issue |
2
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pubmed:dateCreated |
1994-3-15
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pubmed:abstractText |
As an approach toward identification and isolation of cellular proteins that may act as substrates or effectors of the SRC-family of protein-tyrosine kinases, fusion proteins containing noncatalytic elements of two highly related SRC-family members were tested for their ability to recognize distinct molecules present in lysates of cells known to normally express both enzymes. Our results demonstrate differences of protein binding between the SH2 elements of FYN and FGR kinases, but do not discriminate proteins binding to their SH3 domains.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/FYN protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Fyn protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphotyrosine,
http://linkedlifedata.com/resource/pubmed/chemical/Protein-Tyrosine Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/Proto-Oncogene Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Proto-Oncogene Proteins c-fyn,
http://linkedlifedata.com/resource/pubmed/chemical/Proto-Oncogene Proteins pp60(c-src),
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Fusion Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Tyrosine,
http://linkedlifedata.com/resource/pubmed/chemical/proto-oncogene proteins c-fgr,
http://linkedlifedata.com/resource/pubmed/chemical/src-Family Kinases
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pubmed:status |
MEDLINE
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pubmed:month |
Jan
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pubmed:issn |
0014-5793
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
31
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pubmed:volume |
338
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
183-6
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:7508405-3T3 Cells,
pubmed-meshheading:7508405-Animals,
pubmed-meshheading:7508405-Binding Sites,
pubmed-meshheading:7508405-Cell Line, Transformed,
pubmed-meshheading:7508405-Humans,
pubmed-meshheading:7508405-Mice,
pubmed-meshheading:7508405-Phosphorylation,
pubmed-meshheading:7508405-Phosphotyrosine,
pubmed-meshheading:7508405-Protein Binding,
pubmed-meshheading:7508405-Protein-Tyrosine Kinases,
pubmed-meshheading:7508405-Proto-Oncogene Proteins,
pubmed-meshheading:7508405-Proto-Oncogene Proteins c-fyn,
pubmed-meshheading:7508405-Proto-Oncogene Proteins pp60(c-src),
pubmed-meshheading:7508405-Recombinant Fusion Proteins,
pubmed-meshheading:7508405-Tumor Cells, Cultured,
pubmed-meshheading:7508405-Tyrosine,
pubmed-meshheading:7508405-src-Family Kinases
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pubmed:year |
1994
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pubmed:articleTitle |
Specificity of protein interactions with highly related SRC homology (SH) domains of FGR and FYN protein-tyrosine kinases.
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pubmed:affiliation |
Laboratory of Cellular Development and Oncology, National Institute of Dental Research, National Institutes of Health, Bethesda, MD 20892.
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pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, U.S. Gov't, Non-P.H.S.,
Research Support, Non-U.S. Gov't
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