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Q58731093-00776B0C-F0BA-422D-8A36-A195B0ACEE4E
Q58731093-00776B0C-F0BA-422D-8A36-A195B0ACEE4E
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http://www.wikidata.org/entity/statement/Q58731093-00776B0C-F0BA-422D-8A36-A195B0ACEE4E
A FTIR microspectroscopy study of the structural and biochemical perturbations induced by natively folded and aggregated transthyretin in HL-1 cardiomyocytes
P2860
Q58731093-00776B0C-F0BA-422D-8A36-A195B0ACEE4E
BestRank
Statement
http://www.wikidata.org/entity/statement/Q58731093-00776B0C-F0BA-422D-8A36-A195B0ACEE4E
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7f222952146edcaf0aa73124839c63809fe6cf21
P2860
Potentially amyloidogenic conformational intermediates populate the unfolding landscape of transthyretin: insights from molecular dynamics simulations.