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| pubmed-article:1517230 | lifeskim:mentions | umls-concept:C0086418 | lld:lifeskim |
| pubmed-article:1517230 | lifeskim:mentions | umls-concept:C0812201 | lld:lifeskim |
| pubmed-article:1517230 | lifeskim:mentions | umls-concept:C0012854 | lld:lifeskim |
| pubmed-article:1517230 | lifeskim:mentions | umls-concept:C0029005 | lld:lifeskim |
| pubmed-article:1517230 | lifeskim:mentions | umls-concept:C0597298 | lld:lifeskim |
| pubmed-article:1517230 | lifeskim:mentions | umls-concept:C1167622 | lld:lifeskim |
| pubmed-article:1517230 | lifeskim:mentions | umls-concept:C0392747 | lld:lifeskim |
| pubmed-article:1517230 | lifeskim:mentions | umls-concept:C1554963 | lld:lifeskim |
| pubmed-article:1517230 | lifeskim:mentions | umls-concept:C1998793 | lld:lifeskim |
| pubmed-article:1517230 | pubmed:issue | 25 | lld:pubmed |
| pubmed-article:1517230 | pubmed:dateCreated | 1992-10-7 | lld:pubmed |
| pubmed-article:1517230 | pubmed:abstractText | The human ETS1 proto-oncogene proteins have been isolated from the T-cell leukemia line, CEM, by immunoaffinity chromatography and their identity confirmed by NH2-terminal amino acid sequencing. Incubation of CEM cells with N alpha-p-tosyl-L-lysine chloromethyl ketone (TLCK) indicates that ETS proteins can be modified in their cellular context and that pretreatment of the cells with N-ethylmaleimide (NEM) protects ETS1 proteins from TLCK modification. These data show that ETS1 proteins can exist in at least two different states, -SH-available and -SH-protected. Renatured human ETS1 has DNA sequence-specific binding to the PEA3 (CAGGAAGT) motif. The ETS1.PEA3 complex can be observed by electrophoretic mobility shift assays (EMSA). Purified ETS1 retards a band which is exactly the same size as a complex that is retarded from nuclear extracts prepared from CEM cells. Reduced ETS1 is required to form the ETS1.PEA3 complex, however; modification of the ETS1 -SH groups by either NEM or by TLCk does not inhibit formation of the complex. The ETS1.PEA3 complex formed with TLCK-modified ETS1 has a slower mobility than the complex formed with unmodified ETS1. Zone sedimentation analysis of purified ETS1 indicates that it is the monomer of ETS1 which binds to the PEA3 oligonucleotide. | lld:pubmed |
| pubmed-article:1517230 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1517230 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:1517230 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:1517230 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:1517230 | pubmed:month | Sep | lld:pubmed |
| pubmed-article:1517230 | pubmed:issn | 0021-9258 | lld:pubmed |
| pubmed-article:1517230 | pubmed:author | pubmed-author:PapasT STS | lld:pubmed |
| pubmed-article:1517230 | pubmed:author | pubmed-author:FisherR JRJ | lld:pubmed |
| pubmed-article:1517230 | pubmed:author | pubmed-author:KoizumiSS | lld:pubmed |
| pubmed-article:1517230 | pubmed:author | pubmed-author:KondohAA | lld:pubmed |
| pubmed-article:1517230 | pubmed:author | pubmed-author:BhatN KNK | lld:pubmed |
| pubmed-article:1517230 | pubmed:author | pubmed-author:Mavrothalassi... | lld:pubmed |
| pubmed-article:1517230 | pubmed:author | pubmed-author:MarianoJ MJM | lld:pubmed |
| pubmed-article:1517230 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:1517230 | pubmed:day | 5 | lld:pubmed |
| pubmed-article:1517230 | pubmed:volume | 267 | lld:pubmed |
| pubmed-article:1517230 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:1517230 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:1517230 | pubmed:pagination | 17957-65 | lld:pubmed |
| pubmed-article:1517230 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
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| pubmed-article:1517230 | pubmed:meshHeading | pubmed-meshheading:1517230-... | lld:pubmed |
| pubmed-article:1517230 | pubmed:year | 1992 | lld:pubmed |
| pubmed-article:1517230 | pubmed:articleTitle | Human ETS1 oncoprotein. Purification, isoforms, -SH modification, and DNA sequence-specific binding. | lld:pubmed |
| pubmed-article:1517230 | pubmed:affiliation | Laboratory of Cellular Biochemistry, Program Resources, Inc./DynCorp, Frederick Cancer Research and Development Center, Maryland. | lld:pubmed |
| pubmed-article:1517230 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:1517230 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
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