Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
1995-5-30
pubmed:abstractText
Recent studies in both vertebrates and invertebrates support an 'hourglass' model for signal transduction from receptor tyrosine kinases: Ras channels signals from diverse receptor tyrosine kinases into a common cytoplasmic kinase cascade, the targets of which are an even more diverse collection of nuclear proteins. What are these nuclear factors, and how do they interact to direct specific cellular responses to a generic signal? The past year has brought considerable progress in our quest to answer these questions in one model genetic system, the Drosophila eye.
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/Drosophila Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Eye Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Membrane Glycoproteins, http://linkedlifedata.com/resource/pubmed/chemical/Nerve Tissue Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Nuclear Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Proto-Oncogene Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Receptor Protein-Tyrosine Kinases, http://linkedlifedata.com/resource/pubmed/chemical/Repressor Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Transcription Factor AP-1, http://linkedlifedata.com/resource/pubmed/chemical/Transcription Factors, http://linkedlifedata.com/resource/pubmed/chemical/Ubiquitin-Protein Ligases, http://linkedlifedata.com/resource/pubmed/chemical/anterior open protein, Drosophila, http://linkedlifedata.com/resource/pubmed/chemical/phyllopod protein, Drosophila, http://linkedlifedata.com/resource/pubmed/chemical/pnt protein, Drosophila, http://linkedlifedata.com/resource/pubmed/chemical/sev protein, Drosophila, http://linkedlifedata.com/resource/pubmed/chemical/seven in absentia proteins
pubmed:status
MEDLINE
pubmed:month
Mar
pubmed:issn
0168-9525
pubmed:author
pubmed:issnType
Print
pubmed:volume
11
pubmed:geneSymbol
Psc, RAG1, Su(z)2, bmi-1, boss, fos, jun, phyl, pnt, raf, ras, sina, yan
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
106-11
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed-meshheading:7732572-Animals, pubmed-meshheading:7732572-Cell Differentiation, pubmed-meshheading:7732572-DNA-Binding Proteins, pubmed-meshheading:7732572-Drosophila Proteins, pubmed-meshheading:7732572-Drosophila melanogaster, pubmed-meshheading:7732572-Eye Proteins, pubmed-meshheading:7732572-Gene Expression Regulation, Developmental, pubmed-meshheading:7732572-Genes, Insect, pubmed-meshheading:7732572-Membrane Glycoproteins, pubmed-meshheading:7732572-Models, Biological, pubmed-meshheading:7732572-Nerve Tissue Proteins, pubmed-meshheading:7732572-Nuclear Proteins, pubmed-meshheading:7732572-Phosphorylation, pubmed-meshheading:7732572-Photoreceptor Cells, Invertebrate, pubmed-meshheading:7732572-Protein Processing, Post-Translational, pubmed-meshheading:7732572-Proto-Oncogene Proteins, pubmed-meshheading:7732572-Receptor Protein-Tyrosine Kinases, pubmed-meshheading:7732572-Repressor Proteins, pubmed-meshheading:7732572-Signal Transduction, pubmed-meshheading:7732572-Transcription Factor AP-1, pubmed-meshheading:7732572-Transcription Factors, pubmed-meshheading:7732572-Ubiquitin-Protein Ligases
pubmed:year
1995
pubmed:articleTitle
Nuclear factors in sevenless signalling.
pubmed:affiliation
Howard Hughes Medical Institute, Department of Molecular and Cell Biology, University of California, Berkeley 94720, USA.
pubmed:publicationType
Journal Article, Review, Research Support, Non-U.S. Gov't