| pubmed-article:8392180 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:8392180 | lifeskim:mentions | umls-concept:C0037083 | lld:lifeskim |
| pubmed-article:8392180 | lifeskim:mentions | umls-concept:C0752312 | lld:lifeskim |
| pubmed-article:8392180 | lifeskim:mentions | umls-concept:C1419744 | lld:lifeskim |
| pubmed-article:8392180 | lifeskim:mentions | umls-concept:C1419742 | lld:lifeskim |
| pubmed-article:8392180 | lifeskim:mentions | umls-concept:C1419743 | lld:lifeskim |
| pubmed-article:8392180 | pubmed:issue | 13 | lld:pubmed |
| pubmed-article:8392180 | pubmed:dateCreated | 1993-8-6 | lld:pubmed |
| pubmed-article:8392180 | pubmed:abstractText | An explosion of new information linking activation of cell surface signal initiators to changes in gene expression has recently emerged. The focus of much of this information has centered around the agonist-dependent activation of the mitogen-activated protein (MAP) kinases. Although this intracellular signal transduction pathway is extremely complex, conservation of many of its components has been observed in yeast, nematodes, Drosophila, and mammals. Thus, these signaling proteins may participate in the regulation of a variety of cellular processes. | lld:pubmed |
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| pubmed-article:8392180 | pubmed:language | eng | lld:pubmed |
| pubmed-article:8392180 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8392180 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:8392180 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:8392180 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:8392180 | pubmed:month | Jul | lld:pubmed |
| pubmed-article:8392180 | pubmed:issn | 0027-8424 | lld:pubmed |
| pubmed-article:8392180 | pubmed:author | pubmed-author:BlenisJJ | lld:pubmed |
| pubmed-article:8392180 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:8392180 | pubmed:day | 1 | lld:pubmed |
| pubmed-article:8392180 | pubmed:volume | 90 | lld:pubmed |
