PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
20028124-5	2010	Thioflavin-T fluorescence-monitored kinetic experiments, transmission electron microscopy, and circular dichroism showed that rat IAPP lengthened the lag phase for amyloid formation by human IAPP, slowed the growth rate, reduced the amount of amyloid fibrils produced in a dose-dependent manner, and altered the morphology of the fibrils.	thioflavin T	0-12	islet amyloid polypeptide	Rattus norvegicus	130-134	
20707388-7	2010	Fluorescence-detected thioflavin-T binding assays and transmission electron microscopy confirm that the compound inhibits unseeded amyloid fibril formation as well as disaggregates IAPP amyloid.	thioflavin T	22-34	islet amyloid polypeptide	Rattus norvegicus	181-185	
32027132-6	2020	We test the influence of Cu2+ on the aggregation properties of these amylin analogues with thioflavin T assays.	thioflavin T	91-103	islet amyloid polypeptide	Rattus norvegicus	69-75	
25347820-2	2014	Suppression of islet amyloid polypeptide (IAPP) fibril formation by compound 1 was demonstrated by thioflavin T fluorescence and atomic force microscopy.	thioflavin T	99-111	islet amyloid polypeptide	Rattus norvegicus	42-46	
23339420-5	2013	Equal molar ratios of PGG to IAPP substantially reduced the ability of IAPP to bind thioflavin T.	thioflavin T	84-96	islet amyloid polypeptide	Rattus norvegicus	29-33	
23339420-5	2013	Equal molar ratios of PGG to IAPP substantially reduced the ability of IAPP to bind thioflavin T.	thioflavin T	84-96	islet amyloid polypeptide	Rattus norvegicus	71-75