Source:http://linkedlifedata.com/resource/pubmed/id/19061244
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
1
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pubmed:dateCreated |
2008-12-16
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pubmed:abstractText |
The mechanisms responsible for amyloid deposition at different times and in different organs, even in individuals with the same amyloidogenic mutation, are not known. The demonstration, in hereditary systemic transthyretin Val30Met amyloidosis, that such differences are consistently associated with amyloid fibrils composed of different length transthyretin fragments sheds new light on this question and will open the way to further informative studies.
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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 |
Jan
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pubmed:issn |
1096-9896
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pubmed:author | |
pubmed:issnType |
Electronic
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pubmed:volume |
217
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1-3
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pubmed:meshHeading | |
pubmed:year |
2009
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pubmed:articleTitle |
A molecular correlate of clinicopathology in transthyretin amyloidosis.
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pubmed:affiliation |
Centre for Amyloidosis and Acute Phase Proteins, Division of Medicine, Royal Free Campus, University College London Medical School, London, UK. m.pepys@medsch.ucl.ac.uk
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pubmed:publicationType |
Journal Article,
Review
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