| pubmed-article:10347184 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:10347184 | lifeskim:mentions | umls-concept:C0205103 | lld:lifeskim |
| pubmed-article:10347184 | lifeskim:mentions | umls-concept:C0443286 | lld:lifeskim |
| pubmed-article:10347184 | lifeskim:mentions | umls-concept:C1514545 | lld:lifeskim |
| pubmed-article:10347184 | lifeskim:mentions | umls-concept:C0949374 | lld:lifeskim |
| pubmed-article:10347184 | pubmed:issue | 23 | lld:pubmed |
| pubmed-article:10347184 | pubmed:dateCreated | 1999-7-1 | lld:pubmed |
| pubmed-article:10347184 | pubmed:abstractText | We discovered several novel interactions between proteins involved in Crm1-mediated nuclear export of the nuclear export signal containing human immunodeficiency virus type 1 protein Rev. First, a Rev/Crm1/RanGTP complex (where Ran is Ras-related nuclear protein) reacts with some nucleoporins (Nup42 and Nup159) but not others (NSP1, Nup116, and Nup1), forming a Nup/Crm1/RanGTP complex and concomitantly releasing Rev. Second, RanBP1 (or homologous proteins) can displace Nup and form a ternary RanBP1/RanGTP/Crm1 complex that can be disassembled by RanGAP via GTP hydrolysis. Third, and most surprisingly, RanBP1/RanGTP/Crm1 can be disassembled without GTP hydrolysis by the nucleotide exchange factor RanGEF. Recycling of a Ran/RanGEF complex by GTP and Mg2+ is stimulated by both Crm1 and Rev, allowing reformation of a Rev/Crm1/RanGTP complex. Based on these reactions we propose a model for Crm1-mediated export. | lld:pubmed |
| pubmed-article:10347184 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:10347184 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:10347184 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:10347184 | pubmed:month | Jun | lld:pubmed |
| pubmed-article:10347184 | pubmed:issn | 0021-9258 | lld:pubmed |
| pubmed-article:10347184 | pubmed:author | pubmed-author:BlobelGG | lld:pubmed |
| pubmed-article:10347184 | pubmed:author | pubmed-author:FloerMM | lld:pubmed |
| pubmed-article:10347184 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:10347184 | pubmed:day | 4 | lld:pubmed |
| pubmed-article:10347184 | pubmed:volume | 274 | lld:pubmed |
| pubmed-article:10347184 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:10347184 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:10347184 | pubmed:pagination | 16279-86 | lld:pubmed |
| pubmed-article:10347184 | pubmed:dateRevised | 2010-9-20 | lld:pubmed |
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| pubmed-article:10347184 | pubmed:year | 1999 | lld:pubmed |
| pubmed-article:10347184 | pubmed:articleTitle | Putative reaction intermediates in Crm1-mediated nuclear protein export. | lld:pubmed |
| pubmed-article:10347184 | pubmed:affiliation | Laboratory of Cell Biology, Howard Hughes Medical Institute, The Rockefeller University, New York, New York 10021, USA. | lld:pubmed |
| pubmed-article:10347184 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:10347184 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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