| pubmed-article:1730637 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:1730637 | lifeskim:mentions | umls-concept:C0031727 | lld:lifeskim |
| pubmed-article:1730637 | lifeskim:mentions | umls-concept:C0139030 | lld:lifeskim |
| pubmed-article:1730637 | lifeskim:mentions | umls-concept:C0600388 | lld:lifeskim |
| pubmed-article:1730637 | lifeskim:mentions | umls-concept:C0332120 | lld:lifeskim |
| pubmed-article:1730637 | pubmed:issue | 2 | lld:pubmed |
| pubmed-article:1730637 | pubmed:dateCreated | 1992-2-14 | lld:pubmed |
| pubmed-article:1730637 | pubmed:abstractText | The Raf-1 proto-oncogene protein kinase can be phosphorylated and activated after stimulation of cells with insulin and a variety of other growth factors and mitogens. We recently presented evidence that insulin and certain other growth factors activated one or more Raf-1 kinase kinase activities (Lee, R.M., Rapp, U. R., and Blackshear, P.J. (1991) J. Biol. Chem. 266, 10351-10357). In the present study, four peaks of Raf-1 kinase kinase activity were identified after anion-exchange chromatography of cell lysates, and two of these were activated by insulin. Further chromatographic characterization of these two peaks of insulin-activated kinase activity indicated that they contained three apparently distinct kinase activities. Two of these activities comigrated with immunoreactive extracellular signal-regulated kinases (ERK) 1 and 2 (mitogen-activated protein kinase) through three different chromatographic separations. Both ERK1 and ERK2 phosphorylated Raf-1 with reasonably high affinity (Km for ERK1 = 90 nM; Km for ERK2 = 120 nM), and produced similar, complex phosphopeptide maps; both kinases also phosphorylated myelin basic protein. The third kinase activity also phosphorylated Raf-1 and myelin basic protein but did not comigrate exactly with either immunoreactive ERK1 or ERK2. We conclude that two and possibly three insulin-activated Raf-1 kinase kinases are members of the ERK family. | lld:pubmed |
| pubmed-article:1730637 | pubmed:language | eng | lld:pubmed |
| pubmed-article:1730637 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1730637 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:1730637 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:1730637 | pubmed:month | Jan | lld:pubmed |
| pubmed-article:1730637 | pubmed:issn | 0021-9258 | lld:pubmed |
| pubmed-article:1730637 | pubmed:author | pubmed-author:BlackshearP... | lld:pubmed |
| pubmed-article:1730637 | pubmed:author | pubmed-author:FORDBB | lld:pubmed |
| pubmed-article:1730637 | pubmed:author | pubmed-author:LeeR MRM | lld:pubmed |
| pubmed-article:1730637 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:1730637 | pubmed:day | 15 | lld:pubmed |
| pubmed-article:1730637 | pubmed:volume | 267 | lld:pubmed |
| pubmed-article:1730637 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:1730637 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:1730637 | pubmed:pagination | 1088-92 | lld:pubmed |
| pubmed-article:1730637 | pubmed:dateRevised | 2011-11-17 | lld:pubmed |
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| pubmed-article:1730637 | pubmed:meshHeading | pubmed-meshheading:1730637-... | lld:pubmed |
| pubmed-article:1730637 | pubmed:year | 1992 | lld:pubmed |
| pubmed-article:1730637 | pubmed:articleTitle | Evidence that extracellular signal-regulated kinases are the insulin-activated Raf-1 kinase kinases. | lld:pubmed |
| pubmed-article:1730637 | pubmed:affiliation | Howard Hughes Medical Institute Laboratories, Duke University Medical Center, Durham, North Carolina 27710. | lld:pubmed |
| pubmed-article:1730637 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:1730637 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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