pubmed-article:6232502 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:6232502 | lifeskim:mentions | umls-concept:C0229671 | lld:lifeskim |
pubmed-article:6232502 | lifeskim:mentions | umls-concept:C1167298 | lld:lifeskim |
pubmed-article:6232502 | lifeskim:mentions | umls-concept:C0040648 | lld:lifeskim |
pubmed-article:6232502 | lifeskim:mentions | umls-concept:C0443146 | lld:lifeskim |
pubmed-article:6232502 | lifeskim:mentions | umls-concept:C1514668 | lld:lifeskim |
pubmed-article:6232502 | lifeskim:mentions | umls-concept:C1514665 | lld:lifeskim |
pubmed-article:6232502 | lifeskim:mentions | umls-concept:C0004083 | lld:lifeskim |
pubmed-article:6232502 | pubmed:issue | 7 | lld:pubmed |
pubmed-article:6232502 | pubmed:dateCreated | 1984-6-5 | lld:pubmed |
pubmed-article:6232502 | pubmed:abstractText | RNA polymerase III transcription can be inhibited in vitro by two sera from patients with autoimmune diseases. The first serum, designated anti-SS-B (or La), has antibodies directed against a 50,000 dalton polypeptide that is part of a larger ribonucleoprotein complex. The second serum, designated anti-SpNo, recognizes a target antigen polypeptide of greater than 100,000 daltons as well as the SS-B antigen. Both sera selectively remove required transcription factors from the transcription extract, and inhibition can be rescued by the addition of a HeLa S100 extract to the depleted transcription system. The HeLa S100 extract was sequentially fractionated by ion-exchange chromatography on DEAE-cellulose and phosphocellulose. The high salt eluate from the latter column was also able to rescue the anti-SS-B inhibition as was the immunoaffinity-purified SS-B ribonucleoprotein complex isolated from HeLa, Xenopus or rabbit thymus. Immunoblots of the active fractions indicated that all contained the SS-B immunoreactive polypeptide, but probes of replica filters for DNA-binding suggested that the transcription factor is not the SS-B antigen but a 64,000 dalton polypeptide component of the antigen ribonucleoprotein complex. SS-B is itself an RNA-binding protein and could be shown to bind nascent 5S RNA transcripts in vitro. Differential ammonium sulfate precipitation and DNA cellulose chromatography has confirmed that a group of 64-68 K dalton polypeptides are components of the SS-B ribonucleoprotein complex associated with transcription factor activity. | lld:pubmed |
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pubmed-article:6232502 | pubmed:language | eng | lld:pubmed |
pubmed-article:6232502 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:6232502 | pubmed:citationSubset | IM | lld:pubmed |
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pubmed-article:6232502 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:6232502 | pubmed:month | Apr | lld:pubmed |
pubmed-article:6232502 | pubmed:issn | 0305-1048 | lld:pubmed |
pubmed-article:6232502 | pubmed:author | pubmed-author:GottesfeldJ... | lld:pubmed |
pubmed-article:6232502 | pubmed:author | pubmed-author:HochS OSO | lld:pubmed |
pubmed-article:6232502 | pubmed:author | pubmed-author:AndrewsD LDL | lld:pubmed |
pubmed-article:6232502 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:6232502 | pubmed:day | 11 | lld:pubmed |
pubmed-article:6232502 | pubmed:volume | 12 | lld:pubmed |
pubmed-article:6232502 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:6232502 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:6232502 | pubmed:pagination | 3185-200 | lld:pubmed |
pubmed-article:6232502 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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pubmed-article:6232502 | pubmed:year | 1984 | lld:pubmed |
pubmed-article:6232502 | pubmed:articleTitle | Association of an RNA polymerase III transcription factor with a ribonucleoprotein complex recognized by autoimmune sera. | lld:pubmed |
pubmed-article:6232502 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:6232502 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
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