PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
33610557-3	2021	Here we test the effects of Brazilin on both seeded and unseeded alpha-syn fibril formation and show that the natural polyphenol inhibits fibrillogenesis of alpha-syn by a unique mechanism that alters conformational equilibria in two separate points of the assembly mechanism: Brazilin preserves the natively unfolded state of alpha-syn by specifically binding to the compact conformation of the alpha-syn monomer.	Polyphenols	118-128	synuclein alpha	Homo sapiens	157-166	
33610557-3	2021	Here we test the effects of Brazilin on both seeded and unseeded alpha-syn fibril formation and show that the natural polyphenol inhibits fibrillogenesis of alpha-syn by a unique mechanism that alters conformational equilibria in two separate points of the assembly mechanism: Brazilin preserves the natively unfolded state of alpha-syn by specifically binding to the compact conformation of the alpha-syn monomer.	Polyphenols	118-128	synuclein alpha	Homo sapiens	157-166	
33610557-3	2021	Here we test the effects of Brazilin on both seeded and unseeded alpha-syn fibril formation and show that the natural polyphenol inhibits fibrillogenesis of alpha-syn by a unique mechanism that alters conformational equilibria in two separate points of the assembly mechanism: Brazilin preserves the natively unfolded state of alpha-syn by specifically binding to the compact conformation of the alpha-syn monomer.	Polyphenols	118-128	synuclein alpha	Homo sapiens	157-166