| pubmed-article:9701560 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:9701560 | lifeskim:mentions | umls-concept:C0028606 | lld:lifeskim |
| pubmed-article:9701560 | lifeskim:mentions | umls-concept:C1704675 | lld:lifeskim |
| pubmed-article:9701560 | lifeskim:mentions | umls-concept:C1514562 | lld:lifeskim |
| pubmed-article:9701560 | lifeskim:mentions | umls-concept:C1883221 | lld:lifeskim |
| pubmed-article:9701560 | lifeskim:mentions | umls-concept:C0475264 | lld:lifeskim |
| pubmed-article:9701560 | lifeskim:mentions | umls-concept:C1149290 | lld:lifeskim |
| pubmed-article:9701560 | lifeskim:mentions | umls-concept:C0086597 | lld:lifeskim |
| pubmed-article:9701560 | lifeskim:mentions | umls-concept:C1883204 | lld:lifeskim |
| pubmed-article:9701560 | lifeskim:mentions | umls-concept:C1880389 | lld:lifeskim |
| pubmed-article:9701560 | lifeskim:mentions | umls-concept:C0028608 | lld:lifeskim |
| pubmed-article:9701560 | pubmed:dateCreated | 1999-5-25 | lld:pubmed |
| pubmed-article:9701560 | pubmed:abstractText | Nopp44/46 is a phosphoprotein of the protozoan parasite Trypanosoma brucei that is localized to the nucleolus. Based on the primary sequence, Nopp44/46 appears to be a protein composed of distinct domains. This communication describes the relationship of these domains to the known functional interactions of the molecule and suggests that the amino-terminal region defines a novel homology region that functions in nucleolar targeting. We have previously shown that Nopp44/46 is capable of interacting with nucleic acids and associating with a protein kinase. Using in vitro transcription and translation, we now demonstrate that the nucleic acid binding function maps to the carboxy-terminal domain of the molecule, a region rich in arginine-glycine-glycine motifs. Our experiments reveal that a central region containing a high proportion of acidic residues is required for association with the protein kinase. Analysis of transfectants expressing epitope-tagged Nopp44/46 deletion constructs showed that the amino-terminal 96 amino acids allowed nuclear and nucleolar accumulation of the protein. This region of the molecule shows homology to several recently described nucleolar proteins. Deletion of a 27-amino-acid region within this domain abrogated nucleolar, but not nuclear, localization. These studies show that Nopp44/46 is composed of distinct modules, each of which plays a different role in molecular interactions. We suggest that this protein could facilitate interactions between sets of nucleolar molecules. | lld:pubmed |
| pubmed-article:9701560 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9701560 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9701560 | pubmed:language | eng | lld:pubmed |
| pubmed-article:9701560 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9701560 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:9701560 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9701560 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9701560 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9701560 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9701560 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9701560 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9701560 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9701560 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:9701560 | pubmed:month | Sep | lld:pubmed |
| pubmed-article:9701560 | pubmed:issn | 0021-9533 | lld:pubmed |
| pubmed-article:9701560 | pubmed:author | pubmed-author:DasAA | lld:pubmed |
| pubmed-article:9701560 | pubmed:author | pubmed-author:ParkJ HJH | lld:pubmed |
| pubmed-article:9701560 | pubmed:author | pubmed-author:ParsonsMM | lld:pubmed |
| pubmed-article:9701560 | pubmed:author | pubmed-author:HagenC BCB | lld:pubmed |
| pubmed-article:9701560 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:9701560 | pubmed:volume | 111 ( Pt 17) | lld:pubmed |
| pubmed-article:9701560 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:9701560 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:9701560 | pubmed:pagination | 2615-23 | lld:pubmed |
| pubmed-article:9701560 | pubmed:dateRevised | 2009-11-19 | lld:pubmed |
| pubmed-article:9701560 | pubmed:meshHeading | pubmed-meshheading:9701560-... | lld:pubmed |
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| pubmed-article:9701560 | pubmed:meshHeading | pubmed-meshheading:9701560-... | lld:pubmed |
| pubmed-article:9701560 | pubmed:meshHeading | pubmed-meshheading:9701560-... | lld:pubmed |
| pubmed-article:9701560 | pubmed:meshHeading | pubmed-meshheading:9701560-... | lld:pubmed |
| pubmed-article:9701560 | pubmed:meshHeading | pubmed-meshheading:9701560-... | lld:pubmed |
| pubmed-article:9701560 | pubmed:year | 1998 | lld:pubmed |
| pubmed-article:9701560 | pubmed:articleTitle | Distinct domains of a nucleolar protein mediate protein kinase binding, interaction with nucleic acids and nucleolar localization. | lld:pubmed |
| pubmed-article:9701560 | pubmed:affiliation | Seattle Biomedical Research Institute, Seattle, WA 98109, USA. | lld:pubmed |
| pubmed-article:9701560 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:9701560 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
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