Source:http://linkedlifedata.com/resource/pubmed/id/11145205
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
1
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pubmed:dateCreated |
2000-12-28
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pubmed:abstractText |
Substantial biological data indicate that the myelin basic protein (MBP) and myelin proteolipid protein (PLP/DM20) genes produce products with functions beyond that of serving as myelin structural proteins. Much of this evidence comes from studies on naturally-occurring and man-made mutations of these genes in mice and other species. This review focuses upon recent evidence showing the existence of other products of these genes that may account for some of these other functions, and recent studies providing evidence for alternative biological functions of PLP/DM20. The MBP and PLP/DM20 genes each encode the classic MBP and PLP isoforms, as well as a second family of proteins that are not involved in myelin structure. The biological roles of these other products of the genes are becoming clarified. The non-classic MBP gene products appear to be components of transcriptional complexes in the nucleus, and they also may be involved in signaling pathways in T-cells and in neural cells. The non-classic PLP/DM20 gene products appear to be components of intracellular transport vesicles in oligodendrocytes. There is evidence for other functions of the classic PLP/DM20 proteins, including a role in neural cell death mechanisms, autocrine and paracrine regulation of oligodendrocytes and neurons, intracellular transport and oligodendrocyte migration.
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pubmed:grant | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:month |
Jan
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pubmed:issn |
1015-6305
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
11
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
74-91
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:11145205-Amino Acid Sequence,
pubmed-meshheading:11145205-Animals,
pubmed-meshheading:11145205-Cell Communication,
pubmed-meshheading:11145205-Gene Expression,
pubmed-meshheading:11145205-Humans,
pubmed-meshheading:11145205-Mutation,
pubmed-meshheading:11145205-Myelin Basic Proteins,
pubmed-meshheading:11145205-Myelin Proteolipid Protein,
pubmed-meshheading:11145205-Myelin Sheath,
pubmed-meshheading:11145205-Oligodendroglia,
pubmed-meshheading:11145205-Protein Conformation
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pubmed:year |
2001
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pubmed:articleTitle |
The pathobiology of myelin mutants reveal novel biological functions of the MBP and PLP genes.
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pubmed:affiliation |
Neuropsychiatric Institute, UCLA School of Medicine, 90024, USA. acampagnoni@mednet.ucla.edu
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Review,
Research Support, Non-U.S. Gov't
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