pubmed-article:7828890 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:7828890 | lifeskim:mentions | umls-concept:C0086418 | lld:lifeskim |
pubmed-article:7828890 | lifeskim:mentions | umls-concept:C0006104 | lld:lifeskim |
pubmed-article:7828890 | lifeskim:mentions | umls-concept:C0009015 | lld:lifeskim |
pubmed-article:7828890 | lifeskim:mentions | umls-concept:C0006556 | lld:lifeskim |
pubmed-article:7828890 | lifeskim:mentions | umls-concept:C0120465 | lld:lifeskim |
pubmed-article:7828890 | lifeskim:mentions | umls-concept:C0542341 | lld:lifeskim |
pubmed-article:7828890 | lifeskim:mentions | umls-concept:C0679058 | lld:lifeskim |
pubmed-article:7828890 | lifeskim:mentions | umls-concept:C0851285 | lld:lifeskim |
pubmed-article:7828890 | lifeskim:mentions | umls-concept:C0936012 | lld:lifeskim |
pubmed-article:7828890 | lifeskim:mentions | umls-concept:C1547699 | lld:lifeskim |
pubmed-article:7828890 | lifeskim:mentions | umls-concept:C2700640 | lld:lifeskim |
pubmed-article:7828890 | pubmed:issue | 1-2 | lld:pubmed |
pubmed-article:7828890 | pubmed:dateCreated | 1995-2-22 | lld:pubmed |
pubmed-article:7828890 | pubmed:abstractText | Ras proteins bound to GDP are biologically inactive while those bound to GTP are active. Ras-specific guanine nucleotide-exchange factors (GEFs) have been shown to activate Ras proteins. We used oligodeoxyribonucleotide primers with sequences similar to the cDNAs of rat and mouse cdc25 (encoding a Ras-GEF) to amplify, by the PCR, sequences with the potential to encode a 1275-amino-acid protein homologous to the rodent Cdc25GEF proteins. Northern blot analysis detected a brain-specific 5-kb transcript. We provide evidence for a novel alternately spliced transcript of cdc25 and show that these alternately spliced transcripts are differentially expressed in various regions of the adult nervous system. Antibodies raised against the C terminus of the protein recognize a 140-kDa protein in brain extracts of human, rat, guinea pig and cow; the 140-kDa protein is associated predominantly, if not exclusively, with a crude membrane fraction of brain. The C terminus of human Cdc25GEF can complement the loss of CDC25 function in Saccharomyces cerevisiae. A glutathione S-transferase fusion protein containing the C terminus of the cdc25 product can stimulate guanine nucleotide exchange on H-Ras in vitro. Further, the Cdc25-fusion protein binds tightly to the nucleotide-free form of H-Ras in vitro, and this binding is reversed by the addition of GTP. | lld:pubmed |
pubmed-article:7828890 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:7828890 | pubmed:language | eng | lld:pubmed |
pubmed-article:7828890 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:7828890 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:7828890 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:7828890 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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pubmed-article:7828890 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:7828890 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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pubmed-article:7828890 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:7828890 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:7828890 | pubmed:month | Dec | lld:pubmed |
pubmed-article:7828890 | pubmed:issn | 0378-1119 | lld:pubmed |
pubmed-article:7828890 | pubmed:author | pubmed-author:DayHH | lld:pubmed |
pubmed-article:7828890 | pubmed:author | pubmed-author:WeiWW | lld:pubmed |
pubmed-article:7828890 | pubmed:author | pubmed-author:ParkWW | lld:pubmed |
pubmed-article:7828890 | pubmed:author | pubmed-author:BroekDD | lld:pubmed |
pubmed-article:7828890 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:7828890 | pubmed:day | 30 | lld:pubmed |
pubmed-article:7828890 | pubmed:volume | 151 | lld:pubmed |
pubmed-article:7828890 | pubmed:geneSymbol | cdc25 | lld:pubmed |
pubmed-article:7828890 | pubmed:geneSymbol | cdc25<up>GEF</up> | lld:pubmed |
pubmed-article:7828890 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:7828890 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:7828890 | pubmed:pagination | 279-84 | lld:pubmed |
pubmed-article:7828890 | pubmed:dateRevised | 2007-11-15 | lld:pubmed |
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pubmed-article:7828890 | pubmed:year | 1994 | lld:pubmed |
pubmed-article:7828890 | pubmed:articleTitle | Cloning and analysis of human cDNAs encoding a 140-kDa brain guanine nucleotide-exchange factor, Cdc25GEF, which regulates the function of Ras. | lld:pubmed |
pubmed-article:7828890 | pubmed:affiliation | Department of Biochemistry and Molecular Biology, USC/Norris Comprehensive Cancer Center, University of Southern California School of Medicine, Los Angeles 90033. | lld:pubmed |
pubmed-article:7828890 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:7828890 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
pubmed-article:7828890 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
entrez-gene:5923 | entrezgene:pubmed | pubmed-article:7828890 | lld:entrezgene |
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