| pubmed-article:9368759 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:9368759 | lifeskim:mentions | umls-concept:C0086282 | lld:lifeskim |
| pubmed-article:9368759 | lifeskim:mentions | umls-concept:C0598988 | lld:lifeskim |
| pubmed-article:9368759 | lifeskim:mentions | umls-concept:C0299508 | lld:lifeskim |
| pubmed-article:9368759 | lifeskim:mentions | umls-concept:C1704675 | lld:lifeskim |
| pubmed-article:9368759 | lifeskim:mentions | umls-concept:C0887840 | lld:lifeskim |
| pubmed-article:9368759 | lifeskim:mentions | umls-concept:C0221821 | lld:lifeskim |
| pubmed-article:9368759 | pubmed:issue | 10 | lld:pubmed |
| pubmed-article:9368759 | pubmed:dateCreated | 1998-2-10 | lld:pubmed |
| pubmed-article:9368759 | pubmed:abstractText | The human immunodeficiency virus (HIV-1) uses the viral protein Rev to regulate gene expression by promoting the export of unspliced and partially spliced viral transcripts. Rev has been shown to function in a variety of organisms, including Saccharomyces cerevisiae. The export activity of Rev depends on a nuclear export signal (NES), which is believed to interact either directly or indirectly with the nuclear pore complex to carry out its export function. Crm1p is a member of the importin-beta protein family, other members of which are known to be directly involved in nuclear import. Crm1p has recently been shown to contribute to nuclear export in vertebrate systems. Here, we have studied this mechanism of nuclear to cytoplasmic transport. | lld:pubmed |
| pubmed-article:9368759 | pubmed:language | eng | lld:pubmed |
| pubmed-article:9368759 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9368759 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:9368759 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:9368759 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:9368759 | pubmed:month | Oct | lld:pubmed |
| pubmed-article:9368759 | pubmed:issn | 0960-9822 | lld:pubmed |
| pubmed-article:9368759 | pubmed:author | pubmed-author:RosbashMM | lld:pubmed |
| pubmed-article:9368759 | pubmed:author | pubmed-author:LeeLL | lld:pubmed |
| pubmed-article:9368759 | pubmed:author | pubmed-author:NevilleMM | lld:pubmed |
| pubmed-article:9368759 | pubmed:author | pubmed-author:DavisL ILI | lld:pubmed |
| pubmed-article:9368759 | pubmed:author | pubmed-author:StutzFF | lld:pubmed |
| pubmed-article:9368759 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:9368759 | pubmed:day | 1 | lld:pubmed |
| pubmed-article:9368759 | pubmed:volume | 7 | lld:pubmed |
| pubmed-article:9368759 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:9368759 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:9368759 | pubmed:pagination | 767-75 | lld:pubmed |
| pubmed-article:9368759 | pubmed:dateRevised | 2009-7-15 | lld:pubmed |
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| pubmed-article:9368759 | pubmed:year | 1997 | lld:pubmed |
| pubmed-article:9368759 | pubmed:articleTitle | The importin-beta family member Crm1p bridges the interaction between Rev and the nuclear pore complex during nuclear export. | lld:pubmed |
| pubmed-article:9368759 | pubmed:affiliation | Howard Hughes Medical Institute, Brandeis University, Waltham, Massachusetts 02254, USA. | lld:pubmed |
| pubmed-article:9368759 | pubmed:publicationType | Journal Article | lld:pubmed |
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