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Q35679065-18647EA9-E200-44FB-9154-0B3226CAF5BA
Q35679065-18647EA9-E200-44FB-9154-0B3226CAF5BA
BestRank
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http://www.wikidata.org/entity/statement/Q35679065-18647EA9-E200-44FB-9154-0B3226CAF5BA
Investigating how peptide length and a pathogenic mutation modify the structural ensemble of amyloid beta monomer.
P2860
Q35679065-18647EA9-E200-44FB-9154-0B3226CAF5BA
BestRank
Statement
http://www.wikidata.org/entity/statement/Q35679065-18647EA9-E200-44FB-9154-0B3226CAF5BA
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wasDerivedFrom
370700ce1f533e8441e8e6cfc193696cfe4811e0
P2860
Charge states rather than propensity for beta-structure determine enhanced fibrillogenesis in wild-type Alzheimer's beta-amyloid peptide compared to E22Q Dutch mutant.