Source:http://linkedlifedata.com/resource/pubmed/id/11163132
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
1
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pubmed:dateCreated |
2001-2-22
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pubmed:abstractText |
The microtubule-associated protein tau was originally identified as a protein that co-purified with tubulin in vitro, stimulated assembly of tubulin into microtubules and strongly stabilized microtubules. Recognized now as one of the most abundant axonal microtubule-associated proteins, a convergence of evidence implicates an overlapping in vivo role of tau with other axonal microtubule-associated proteins (e.g. MAP1B) in establishing microtubule stability, axon elongation and axonal structure. Missense and splice-site mutations in the human tau gene are now known to be causes of inherited frontotemporal dementia and parkinsonism linked to chromosome 17, a cognitive disorder of aging. This has provided direct evidence for the hypothesis that aberrant, filamentous assembly of tau, a frequent hallmark of a series of human cognitive diseases, including Alzheimer's disease, can directly provoke neurodegeneration.
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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 |
Feb
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pubmed:issn |
0955-0674
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
13
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
41-8
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pubmed:dateRevised |
2005-11-16
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pubmed:meshHeading | |
pubmed:year |
2001
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pubmed:articleTitle |
Going new places using an old MAP: tau, microtubules and human neurodegenerative disease.
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pubmed:affiliation |
Department of Neuroscience, University of California San Diego, 9500 Gilman Drive, La Jolla, California 92093, USA.
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pubmed:publicationType |
Journal Article,
Review
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