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Q36619982-181D3825-A7A9-4A93-83E6-0231EEF74F65
Q36619982-181D3825-A7A9-4A93-83E6-0231EEF74F65
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http://www.wikidata.org/entity/statement/Q36619982-181D3825-A7A9-4A93-83E6-0231EEF74F65
Electron paramagnetic resonance analysis of the vimentin tail domain reveals points of order in a largely disordered region and conformational adaptation upon filament assembly
P2860
Q36619982-181D3825-A7A9-4A93-83E6-0231EEF74F65
BestRank
Statement
http://www.wikidata.org/entity/statement/Q36619982-181D3825-A7A9-4A93-83E6-0231EEF74F65
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wasDerivedFrom
2f42abfa00abc10d7708f367a210423e897efb2b
P2860
The Alexander disease-causing glial fibrillary acidic protein mutant, R416W, accumulates into Rosenthal fibers by a pathway that involves filament aggregation and the association of alpha B-crystallin and HSP27