| pubmed-article:11431474 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:11431474 | lifeskim:mentions | umls-concept:C0085828 | lld:lifeskim |
| pubmed-article:11431474 | lifeskim:mentions | umls-concept:C0012854 | lld:lifeskim |
| pubmed-article:11431474 | lifeskim:mentions | umls-concept:C0033684 | lld:lifeskim |
| pubmed-article:11431474 | lifeskim:mentions | umls-concept:C0332281 | lld:lifeskim |
| pubmed-article:11431474 | lifeskim:mentions | umls-concept:C0456387 | lld:lifeskim |
| pubmed-article:11431474 | pubmed:issue | 34 | lld:pubmed |
| pubmed-article:11431474 | pubmed:dateCreated | 2001-8-20 | lld:pubmed |
| pubmed-article:11431474 | pubmed:abstractText | We have identified seven ERK-related proteins ("ERPs"), including ERK2, that are stably associated in vivo with AP-1 dimers composed of diverse Jun and Fos family proteins. These complexes have kinase activity. We designate them as "class I ERPs." We originally hypothesized that these ERPs associate with DNA along with AP-1 proteins. We devised a DNA affinity chromatography-based analytical assay for DNA binding, the "nucleotide affinity preincubation specificity test recognition" (NAPSTER) assay. In this assay, class I ERPs do not associate with AP-1 DNA. However, several new "class II" ERPs do associate with DNA. p41 and p44 are ERK1/2-related ERPs that lack kinase activity and associate along with AP-1 proteins with AP-1 DNA. Class I ERPs and their associated kinase activity thus appear to bind AP-1 dimers when they are not bound to DNA and then disengage and are replaced by class II ERPs to form higher order complexes when AP-1 dimers bind DNA. p97 is a class III ERP, related to ERK3, that associates with AP-1 DNA without AP-1 proteins. With the exception of ERK2, none of the 10 ERPs appear to be known mitogen-activated protein kinase superfamily members. | lld:pubmed |
| pubmed-article:11431474 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11431474 | pubmed:language | eng | lld:pubmed |
| pubmed-article:11431474 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11431474 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:11431474 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:11431474 | pubmed:month | Aug | lld:pubmed |
| pubmed-article:11431474 | pubmed:issn | 0021-9258 | lld:pubmed |
| pubmed-article:11431474 | pubmed:author | pubmed-author:KumarN VNV | lld:pubmed |
| pubmed-article:11431474 | pubmed:author | pubmed-author:BernsteinL... | lld:pubmed |
| pubmed-article:11431474 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:11431474 | pubmed:day | 24 | lld:pubmed |
| pubmed-article:11431474 | pubmed:volume | 276 | lld:pubmed |
| pubmed-article:11431474 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:11431474 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:11431474 | pubmed:pagination | 32362-72 | lld:pubmed |
| pubmed-article:11431474 | pubmed:dateRevised | 2009-11-19 | lld:pubmed |
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| pubmed-article:11431474 | pubmed:meshHeading | pubmed-meshheading:11431474... | lld:pubmed |
| pubmed-article:11431474 | pubmed:year | 2001 | lld:pubmed |
| pubmed-article:11431474 | pubmed:articleTitle | Ten ERK-related proteins in three distinct classes associate with AP-1 proteins and/or AP-1 DNA. | lld:pubmed |
| pubmed-article:11431474 | pubmed:affiliation | Department of Pathology and Laboratory Medicine, Texas A & M University System Health Science Center, College Station, Texas 77843-1114, USA. | lld:pubmed |
| pubmed-article:11431474 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:11431474 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:11431474 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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