| pubmed-article:8663171 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:8663171 | lifeskim:mentions | umls-concept:C0033684 | lld:lifeskim |
| pubmed-article:8663171 | lifeskim:mentions | umls-concept:C0085177 | lld:lifeskim |
| pubmed-article:8663171 | lifeskim:mentions | umls-concept:C0041217 | lld:lifeskim |
| pubmed-article:8663171 | lifeskim:mentions | umls-concept:C0205164 | lld:lifeskim |
| pubmed-article:8663171 | pubmed:issue | 26 | lld:pubmed |
| pubmed-article:8663171 | pubmed:dateCreated | 1996-8-20 | lld:pubmed |
| pubmed-article:8663171 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8663171 | pubmed:abstractText | We have previously identified a set of tyrosine-phosphorylated proteins with apparent molecular masses of 44-46 kDa as some of the major tyrosine phosphorylated species in the protozoan parasite Trypanosoma brucei. We now show that these molecules, herein named Nopp44/46, are localized in the nucleolus. Using monoclonal antibodies, we have isolated Nopp44/46 cDNA clones from expression libraries. Sequence analysis reveals that the predicted amino acid sequence of the molecule is composed of an N-terminal unique region, an internal acidic region, and C-terminal repeat region. Analysis of the cDNA clones and genomic Southern analysis indicated that Nopp44/46 belongs to a multigene family in which different gene copies are very similar but vary in the number of repeats. Interestingly, the repetitive amino acid sequence motif contains multiple RGG (Arg-Gly-Gly) boxes characteristic of RNA-binding proteins. In vitro binding experiments demonstrated that Nopp44/46 is indeed capable of binding nucleic acids. Competition experiments with different RNA homopolymers demonstrated that Nopp44/46 preferentially binds to poly(U). These studies suggest that Nopp44/46 may play a role in RNA metabolism in trypanosomes and raise the possibility that tyrosine phosphorylation may regulate the process. | lld:pubmed |
| pubmed-article:8663171 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8663171 | pubmed:language | eng | lld:pubmed |
| pubmed-article:8663171 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8663171 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:8663171 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:8663171 | pubmed:month | Jun | lld:pubmed |
| pubmed-article:8663171 | pubmed:issn | 0021-9258 | lld:pubmed |
| pubmed-article:8663171 | pubmed:author | pubmed-author:DasAA | lld:pubmed |
| pubmed-article:8663171 | pubmed:author | pubmed-author:ParsonsMM | lld:pubmed |
| pubmed-article:8663171 | pubmed:author | pubmed-author:PetersonG CGC | lld:pubmed |
| pubmed-article:8663171 | pubmed:author | pubmed-author:KannerS BSB | lld:pubmed |
| pubmed-article:8663171 | pubmed:author | pubmed-author:FrevertUU | lld:pubmed |
| pubmed-article:8663171 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:8663171 | pubmed:day | 28 | lld:pubmed |
| pubmed-article:8663171 | pubmed:volume | 271 | lld:pubmed |
| pubmed-article:8663171 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:8663171 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:8663171 | pubmed:pagination | 15675-81 | lld:pubmed |
| pubmed-article:8663171 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
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| pubmed-article:8663171 | pubmed:meshHeading | pubmed-meshheading:8663171-... | lld:pubmed |
| pubmed-article:8663171 | pubmed:year | 1996 | lld:pubmed |
| pubmed-article:8663171 | pubmed:articleTitle | A major tyrosine-phosphorylated protein of Trypanosoma brucei is a nucleolar RNA-binding protein. | lld:pubmed |
| pubmed-article:8663171 | pubmed:affiliation | Seattle Biomedical Research Institute, Seattle, Washington 98109, USA. | lld:pubmed |
| pubmed-article:8663171 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:8663171 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
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