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pubmed-article:7744865 | lifeskim:mentions | umls-concept:C0035820 | lld:lifeskim |
pubmed-article:7744865 | lifeskim:mentions | umls-concept:C0033684 | lld:lifeskim |
pubmed-article:7744865 | lifeskim:mentions | umls-concept:C0038323 | lld:lifeskim |
pubmed-article:7744865 | lifeskim:mentions | umls-concept:C0021920 | lld:lifeskim |
pubmed-article:7744865 | lifeskim:mentions | umls-concept:C0031437 | lld:lifeskim |
pubmed-article:7744865 | lifeskim:mentions | umls-concept:C0015219 | lld:lifeskim |
pubmed-article:7744865 | lifeskim:mentions | umls-concept:C0034987 | lld:lifeskim |
pubmed-article:7744865 | lifeskim:mentions | umls-concept:C1167622 | lld:lifeskim |
pubmed-article:7744865 | lifeskim:mentions | umls-concept:C1511695 | lld:lifeskim |
pubmed-article:7744865 | lifeskim:mentions | umls-concept:C0205171 | lld:lifeskim |
pubmed-article:7744865 | pubmed:issue | 20 | lld:pubmed |
pubmed-article:7744865 | pubmed:dateCreated | 1995-6-12 | lld:pubmed |
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pubmed-article:7744865 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:7744865 | pubmed:abstractText | The cholesterol analogue 25-hydroxycholesterol kills animal cells by blocking the proteolytic activation of two sterol-regulated transcription factors designated sterol regulatory element binding protein-1 and -2 (SREBP-1 and SREBP-2). These proteins, each approximately 1150 amino acids in length, are embedded in the membranes of the nucleus and endoplasmic reticulum by virtue of hydrophobic COOH-terminal segments. In cholesterol-depleted cells the proteins are cleaved to release soluble NH2-terminal fragments of approximately 480 amino acids that enter the nucleus and activate genes encoding the low density lipoprotein receptor and enzymes of cholesterol synthesis. 25-Hydroxycholesterol blocks this cleavage, and cells die of cholesterol deprivation. We previously described a mutant 25-hydroxycholesterol-resistant hamster cell line (SRD-1 cells) in which the SREBP-2 gene had undergone a recombination between the intron following codon 460 and an intron in an unrelated gene. The SREBP-2 sequence terminated at residue 460, eliminating the membrane attachment domain and producing a constitutively active factor that no longer required proteolysis and thus was not inhibited by 25-hydroxycholesterol. Here, we report that two additional sterol-resistant cell lines (SRD-2 and SRD-3) have also undergone genomic rearrangements in the intron following codon 460 of the SREBP-2 gene. Although the molecular rearrangements differ in the three mutant lines, each leads to the production of a constitutively active transcription factor whose SREBP-2 sequence terminates at residue 460. These findings provide a dramatic illustration of the advantage that introns provide in allowing proteins to gain new functions in response to new environmental challenges. | lld:pubmed |
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pubmed-article:7744865 | pubmed:language | eng | lld:pubmed |
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pubmed-article:7744865 | pubmed:citationSubset | IM | lld:pubmed |
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pubmed-article:7744865 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:7744865 | pubmed:month | May | lld:pubmed |
pubmed-article:7744865 | pubmed:issn | 0021-9258 | lld:pubmed |
pubmed-article:7744865 | pubmed:author | pubmed-author:BrownM SMS | lld:pubmed |
pubmed-article:7744865 | pubmed:author | pubmed-author:GoldsteinJ... | lld:pubmed |
pubmed-article:7744865 | pubmed:author | pubmed-author:HoY KYK | lld:pubmed |
pubmed-article:7744865 | pubmed:author | pubmed-author:YangJJ | lld:pubmed |
pubmed-article:7744865 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:7744865 | pubmed:day | 19 | lld:pubmed |
pubmed-article:7744865 | pubmed:volume | 270 | lld:pubmed |
pubmed-article:7744865 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:7744865 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:7744865 | pubmed:pagination | 12152-61 | lld:pubmed |
pubmed-article:7744865 | pubmed:dateRevised | 2008-11-21 | lld:pubmed |
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pubmed-article:7744865 | pubmed:year | 1995 | lld:pubmed |
pubmed-article:7744865 | pubmed:articleTitle | Three different rearrangements in a single intron truncate sterol regulatory element binding protein-2 and produce sterol-resistant phenotype in three cell lines. Role of introns in protein evolution. | lld:pubmed |
pubmed-article:7744865 | pubmed:affiliation | Department of Molecular Genetics, University of Texas Southwestern Medical Center, Dallas 75235, USA. | lld:pubmed |
pubmed-article:7744865 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:7744865 | pubmed:publicationType | Comparative Study | lld:pubmed |
pubmed-article:7744865 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
pubmed-article:7744865 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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