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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
7
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pubmed:dateCreated |
1998-5-7
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pubmed:abstractText |
In Drosophila the function of the epidermal growth factor (EGF) receptor is modulated zygotically by three EGF-like proteins: Spitz (Spi), which is a potent activator; Vein (Vn), which is a moderate activator; and Argos (Aos), which is an inhibitor. Chimeric molecules were constructed in which the EGF domain of Vn was swapped with the EGF domain from each factor. The modified Vn proteins behaved both in vitro and in vivo with properties characteristic of the factor from which the EGF domain was derived. These results demonstrate that the EGF domain is the key determinant that gives DER inhibitors and activators their distinct properties.
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/9531530-1425355,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9531530-1606617,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9531530-1644292,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9531530-2500601,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9531530-7601354,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9531530-7651519,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9531530-7691414,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9531530-7779404,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9531530-7791898,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9531530-7833286,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9531530-7925030,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9531530-8026629,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9531530-8223268,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9531530-8413661,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9531530-8504935,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9531530-8565833,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9531530-8806825,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9531530-8824589,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9531530-8929534,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9531530-8951052,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9531530-9094709,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9531530-9106165,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9531530-9154002,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9531530-9200690,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9531530-9262480,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9531530-9334331
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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/Argos protein, Drosophila,
http://linkedlifedata.com/resource/pubmed/chemical/Drosophila Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Epidermal Growth Factor,
http://linkedlifedata.com/resource/pubmed/chemical/Eye Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Insect Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Nerve Tissue Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Neuregulins,
http://linkedlifedata.com/resource/pubmed/chemical/Receptor, Epidermal Growth Factor,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Fusion Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/spi protein, Drosophila,
http://linkedlifedata.com/resource/pubmed/chemical/vein protein, Drosophila
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pubmed:status |
MEDLINE
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pubmed:month |
Apr
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pubmed:issn |
0890-9369
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
1
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pubmed:volume |
12
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
908-13
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:9531530-Amino Acid Sequence,
pubmed-meshheading:9531530-Animals,
pubmed-meshheading:9531530-Drosophila,
pubmed-meshheading:9531530-Drosophila Proteins,
pubmed-meshheading:9531530-Epidermal Growth Factor,
pubmed-meshheading:9531530-Eye,
pubmed-meshheading:9531530-Eye Proteins,
pubmed-meshheading:9531530-Genetic Engineering,
pubmed-meshheading:9531530-Insect Proteins,
pubmed-meshheading:9531530-Membrane Proteins,
pubmed-meshheading:9531530-Molecular Sequence Data,
pubmed-meshheading:9531530-Nerve Tissue Proteins,
pubmed-meshheading:9531530-Neuregulins,
pubmed-meshheading:9531530-Phenotype,
pubmed-meshheading:9531530-Receptor, Epidermal Growth Factor,
pubmed-meshheading:9531530-Recombinant Fusion Proteins,
pubmed-meshheading:9531530-Sequence Alignment,
pubmed-meshheading:9531530-Sequence Homology, Amino Acid,
pubmed-meshheading:9531530-Wing
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pubmed:year |
1998
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pubmed:articleTitle |
EGF domain swap converts a drosophila EGF receptor activator into an inhibitor.
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pubmed:affiliation |
Department of Molecular Genetics, The Ohio State University, Columbus, Ohio 43210 USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, Non-P.H.S.,
Research Support, Non-U.S. Gov't
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