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Q36535089-1D23F8B5-633A-4C99-BA39-8B630F95CC0B
Q36535089-1D23F8B5-633A-4C99-BA39-8B630F95CC0B
BestRank
Statement
http://www.wikidata.org/entity/statement/Q36535089-1D23F8B5-633A-4C99-BA39-8B630F95CC0B
Aliphatic peptides show similar self-assembly to amyloid core sequences, challenging the importance of aromatic interactions in amyloidosis
P2860
Q36535089-1D23F8B5-633A-4C99-BA39-8B630F95CC0B
BestRank
Statement
http://www.wikidata.org/entity/statement/Q36535089-1D23F8B5-633A-4C99-BA39-8B630F95CC0B
rank
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type
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wasDerivedFrom
bd090ff03681cd521e1e495439d84cd8c04d4e9e
P2860
Synchrotron X-ray studies suggest that the core of the transthyretin amyloid fibril is a continuous β-sheet helix