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Q27312503-18A0F638-58FD-45F1-848D-F822E5E917D2
Q27312503-18A0F638-58FD-45F1-848D-F822E5E917D2
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http://www.wikidata.org/entity/statement/Q27312503-18A0F638-58FD-45F1-848D-F822E5E917D2
Structural Mechanisms of Mutant Huntingtin Aggregation Suppression by the Synthetic Chaperonin-like CCT5 Complex Explained by Cryoelectron Tomography.
P2860
Q27312503-18A0F638-58FD-45F1-848D-F822E5E917D2
BestRank
Statement
http://www.wikidata.org/entity/statement/Q27312503-18A0F638-58FD-45F1-848D-F822E5E917D2
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wasDerivedFrom
7447e0fb56ac9034c0a57ae5d5d289fcf51cb4ab
P2860
Comparative study of naturally occurring huntingtin fragments in Drosophila points to exon 1 as the most pathogenic species in Huntington's disease