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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
4
|
pubmed:dateCreated |
1991-8-27
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pubmed:abstractText |
The structural features necessary for the efficient functioning of the LDL receptor are beginning to emerge from investigation of naturally-occurring and artificially-produced mutations in the gene. Six of the seven repeated sequences in the highly-structured NH2-terminal region are needed for optimal binding of LDL and some of the detailed requirements have been elucidated. The membrane-spanning region is required for insertion of the protein into the plasma membrane, and the cytoplasmic region for internalisation and self-association. Many apparently unrelated mutations affect receptor processing in the Golgi and the role of the carbohydrate chains remains obscure. The main means of regulating LDL-receptor activity is through repression of gene transcription by sterols. This requires a specific element in the promoter region and probably involves more than one transcription factor. Independent effects could be achieved by modulating the activity of these factors.
|
pubmed:language |
eng
|
pubmed:journal | |
pubmed:citationSubset |
IM
|
pubmed:chemical | |
pubmed:status |
MEDLINE
|
pubmed:month |
Oct
|
pubmed:issn |
0007-1420
|
pubmed:author | |
pubmed:issnType |
Print
|
pubmed:volume |
46
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
891-916
|
pubmed:dateRevised |
2005-11-16
|
pubmed:meshHeading | |
pubmed:year |
1990
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pubmed:articleTitle |
Structure and regulation of the LDL-receptor and its gene.
|
pubmed:affiliation |
MRC Lipoprotein Team, Hammersmith Hospital, London, UK.
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pubmed:publicationType |
Journal Article,
Review
|