| pubmed-article:7679672 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:7679672 | lifeskim:mentions | umls-concept:C0028584 | lld:lifeskim |
| pubmed-article:7679672 | lifeskim:mentions | umls-concept:C0083188 | lld:lifeskim |
| pubmed-article:7679672 | lifeskim:mentions | umls-concept:C1514562 | lld:lifeskim |
| pubmed-article:7679672 | lifeskim:mentions | umls-concept:C1883221 | lld:lifeskim |
| pubmed-article:7679672 | lifeskim:mentions | umls-concept:C1710082 | lld:lifeskim |
| pubmed-article:7679672 | lifeskim:mentions | umls-concept:C0599894 | lld:lifeskim |
| pubmed-article:7679672 | lifeskim:mentions | umls-concept:C1883204 | lld:lifeskim |
| pubmed-article:7679672 | lifeskim:mentions | umls-concept:C1880389 | lld:lifeskim |
| pubmed-article:7679672 | pubmed:issue | 5 | lld:pubmed |
| pubmed-article:7679672 | pubmed:dateCreated | 1993-3-23 | lld:pubmed |
| pubmed-article:7679672 | pubmed:abstractText | The lamin B receptor (LBR) is a polytopic protein of the inner nuclear membrane. It is synthesized without a cleavable amino-terminal signal sequence and composed of a nucleoplasmic amino-terminal domain of 204 amino acids followed by a hydrophobic domain with eight putative transmembrane segments. To identify a nuclear envelope targeting signal, we have examined the cellular localization by immunofluorescence microscopy of chicken LBR, its amino-terminal domain and chimeric proteins transiently expressed in transfected COS-7. Full-length LBR was targeted to the nuclear envelope. The amino-terminal domain, without any transmembrane segments, was transported to the nucleus but excluded from the nucleolus. When the amino-terminal domain of LBR was fused to the amino-terminal side of a transmembrane segment of a type II integral membrane protein of the ER/plasma membrane, the chimeric protein was targeted to the nuclear envelope, likely the inner nuclear membrane. When the amino-terminal domain was deleted from LBR and replaced by alpha-globin, the chimeric protein was retained in the ER. These findings demonstrate that the amino-terminal domain of LBR is targeted to the nucleus after synthesis in the cytoplasm and that this polypeptide can function as a nuclear envelope targeting signal when located at the amino terminus of a type II integral membrane protein synthesized on the ER. | lld:pubmed |
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| pubmed-article:7679672 | pubmed:language | eng | lld:pubmed |
| pubmed-article:7679672 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7679672 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:7679672 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:7679672 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:7679672 | pubmed:month | Mar | lld:pubmed |
| pubmed-article:7679672 | pubmed:issn | 0021-9525 | lld:pubmed |
| pubmed-article:7679672 | pubmed:author | pubmed-author:WormanH JHJ | lld:pubmed |
| pubmed-article:7679672 | pubmed:author | pubmed-author:SoullamBB | lld:pubmed |
| pubmed-article:7679672 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:7679672 | pubmed:volume | 120 | lld:pubmed |
| pubmed-article:7679672 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:7679672 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:7679672 | pubmed:pagination | 1093-100 | lld:pubmed |
| pubmed-article:7679672 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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| pubmed-article:7679672 | pubmed:meshHeading | pubmed-meshheading:7679672-... | lld:pubmed |
| pubmed-article:7679672 | pubmed:year | 1993 | lld:pubmed |
| pubmed-article:7679672 | pubmed:articleTitle | The amino-terminal domain of the lamin B receptor is a nuclear envelope targeting signal. | lld:pubmed |
| pubmed-article:7679672 | pubmed:affiliation | Department of Medicine, Mount Sinai School of Medicine, New York 10029. | lld:pubmed |
| pubmed-article:7679672 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:7679672 | pubmed:publicationType | In Vitro | lld:pubmed |
| pubmed-article:7679672 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
