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Predicate | Object |
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rdf:type | |
lifeskim:mentions |
umls-concept:C0004358,
umls-concept:C0004364,
umls-concept:C0024141,
umls-concept:C0026809,
umls-concept:C0035687,
umls-concept:C0035820,
umls-concept:C0205224,
umls-concept:C0439851,
umls-concept:C0521447,
umls-concept:C0684076,
umls-concept:C1441547,
umls-concept:C1517004,
umls-concept:C1521761,
umls-concept:C1552596,
umls-concept:C1947931
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pubmed:issue |
8
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pubmed:dateCreated |
1995-1-3
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pubmed:abstractText |
We have previously shown that nuclear transcripts of several pre-mRNAs can be released from nuclei of mammalian cells in a form of large nuclear ribonucleoprotein (InRNP) particles. These particles, which invariably sediment at the 200S region in sucrose gradient, contain all U small nuclear RNPs required for pre-mRNA splicing and a multitude of heterogeneous nuclear RNP proteins. From a panel of mAbs raised against the InRNP particles, a specific mAb (53/4) identified a nuclear protein of 88 kDa as an essential splicing factor (SF53/4). In a parallel independent study, mAbs were established in mice with experimental systemic lupus erythematosus (SLE), that had been induced by immunization with a murine mAb against a human anti-DNA mAb bearing the common 16/6 idiotype. One of the produced mAbs (2C5/3) recognized an 88 kDa RNP protein. In the present study we have used the following criteria to demonstrate that mAb 2C5/3 and mAb 53/4 recognize the same protein. First, mAb 2C5/3 inhibited splicing by direct addition. Second, the 88 kDa polypeptide that had been immunodepleted from HeLa cells nuclear extract by mAb 2C5/3 was recognized by mAb 53/4 in protein blots. Third, the HeLa nuclear extract depleted by mAb 2C5/3 was devoid of splicing activity and could not assemble into splicing complexes with exogenous pre-mRNA; however, splicing and spliceosome assembly activities were restored to such a defective extract by adding back the 88 kDa protein that had been purified by immunoaffinity binding to immobilized mAb 53/4.(ABSTRACT TRUNCATED AT 250 WORDS)
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:month |
Aug
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pubmed:issn |
0953-8178
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
6
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1097-105
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:7981139-Animals,
pubmed-meshheading:7981139-Antibodies, Monoclonal,
pubmed-meshheading:7981139-Autoantibodies,
pubmed-meshheading:7981139-Chromatography, Affinity,
pubmed-meshheading:7981139-Fluorescent Antibody Technique,
pubmed-meshheading:7981139-HeLa Cells,
pubmed-meshheading:7981139-Humans,
pubmed-meshheading:7981139-Immunoblotting,
pubmed-meshheading:7981139-Lupus Erythematosus, Systemic,
pubmed-meshheading:7981139-Mice,
pubmed-meshheading:7981139-Mice, Inbred Strains,
pubmed-meshheading:7981139-RNA Splicing,
pubmed-meshheading:7981139-Radioimmunoassay,
pubmed-meshheading:7981139-Ribonucleoproteins
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pubmed:year |
1994
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pubmed:articleTitle |
An autoantibody derived from mice with experimental systemic lupus erythematosus is directed against the essential splicing factor SF53/4--a possible role for large nuclear ribonucleoprotein particles in autoimmune disorders.
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pubmed:affiliation |
Department of Organic Chemistry, Weizmann Institute of Science, Rehovot, Israel.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, Non-P.H.S.,
Research Support, Non-U.S. Gov't
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