Source:http://linkedlifedata.com/resource/pubmed/id/16515455
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
3
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pubmed:dateCreated |
2006-3-6
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pubmed:abstractText |
A common mechanism of conformational changes and pathological aggregation of proteins associated with amyloid diseases remains to be proven. High pressure is emerging as a new strategy for studying aspects of amyloid formation. Pressure provides a convenient means to populate and characterize partially folded states, which are thought to have a key role in assembly processes of proteins into amyloid fibrils. High pressure can also be used to dissociate aggregates and amyloid fibrils or on the opposite to generate such species.
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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:issn |
0929-8665
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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 |
271-7
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading | |
pubmed:year |
2006
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pubmed:articleTitle |
High pressure modulates amyloid formation.
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pubmed:affiliation |
INSERM U710, CC 105, Université Montpellier 2, Place Eugène Bataillon, F-34095 Montpellier cédex 5, France.
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pubmed:publicationType |
Journal Article,
Review,
Research Support, Non-U.S. Gov't
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