| pubmed-article:1833773 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:1833773 | lifeskim:mentions | umls-concept:C1179435 | lld:lifeskim |
| pubmed-article:1833773 | lifeskim:mentions | umls-concept:C0142661 | lld:lifeskim |
| pubmed-article:1833773 | lifeskim:mentions | umls-concept:C0041217 | lld:lifeskim |
| pubmed-article:1833773 | lifeskim:mentions | umls-concept:C0205369 | lld:lifeskim |
| pubmed-article:1833773 | lifeskim:mentions | umls-concept:C0008551 | lld:lifeskim |
| pubmed-article:1833773 | lifeskim:mentions | umls-concept:C0205214 | lld:lifeskim |
| pubmed-article:1833773 | pubmed:issue | 20 | lld:pubmed |
| pubmed-article:1833773 | pubmed:dateCreated | 1991-11-15 | lld:pubmed |
| pubmed-article:1833773 | pubmed:abstractText | We have developed a procedure for the affinity purification of small nuclear ribonucleoproteins (snRNPs) of Trypanosoma brucei (U2 and U4/U6 snRNPs), which are essential for trans splicing. Each of these snRNPs can be specifically and efficiently selected from T. brucei extracts through biotinylated antisense 2'-O-methylated RNA oligonucleotides immobilized on streptavidin-agarose. Protein analysis revealed a set of five low molecular weight polypeptides common to the U2 and U4/U6 snRNPs and the spliced leader RNP. In addition, several U2 and U4/U6 snRNP-specific protein components were identified. Using monoclonal antibodies against human snRNP proteins, we could not detect any significant cross-reaction with the trypanosomal U2 snRNP proteins. Thus, the trypanosomal snRNPs exhibit principal differences from the higher eukaryotic snRNPs not only in their RNA but also in their protein components. | lld:pubmed |
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| pubmed-article:1833773 | pubmed:language | eng | lld:pubmed |
| pubmed-article:1833773 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1833773 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:1833773 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:1833773 | pubmed:month | Oct | lld:pubmed |
| pubmed-article:1833773 | pubmed:issn | 0027-8424 | lld:pubmed |
| pubmed-article:1833773 | pubmed:author | pubmed-author:CrossMM | lld:pubmed |
| pubmed-article:1833773 | pubmed:author | pubmed-author:LanzoDD | lld:pubmed |
| pubmed-article:1833773 | pubmed:author | pubmed-author:BindereifAA | lld:pubmed |
| pubmed-article:1833773 | pubmed:author | pubmed-author:PaleyKK | lld:pubmed |
| pubmed-article:1833773 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:1833773 | pubmed:day | 15 | lld:pubmed |
| pubmed-article:1833773 | pubmed:volume | 88 | lld:pubmed |
| pubmed-article:1833773 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:1833773 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:1833773 | pubmed:pagination | 9097-101 | lld:pubmed |
| pubmed-article:1833773 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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| pubmed-article:1833773 | pubmed:year | 1991 | lld:pubmed |
| pubmed-article:1833773 | pubmed:articleTitle | Affinity purification of Trypanosoma brucei small nuclear ribonucleoproteins reveals common and specific protein components. | lld:pubmed |
| pubmed-article:1833773 | pubmed:affiliation | Max-Planck-Institut für Molekulare Genetik, Otto-Warburg-Laboratorium, Federal Republic of Germany. | lld:pubmed |
| pubmed-article:1833773 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:1833773 | pubmed:publicationType | Comparative Study | lld:pubmed |
| pubmed-article:1833773 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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