PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
34339840-6	2021	Specifically, the aggregation of phosphorylated full-length TDP-43 protein (pS410) was monitored by transmission electron microscopy (TEM), turbidity absorbance, and thioflavin (ThT).	thioflavin T	166-176	TAR DNA binding protein	Homo sapiens	60-66	
23124365-8	2013	The demonstration that pathological TDP-43 can be amyloidogenic in situ suggests the following conclusions: (1) the conformational changes associated with TDP-43 aggregation are more complex than previously thought; (2) Thioflavin-S positive SLI may be composed primarily of filamentous ultrastructures.	thioflavin T	220-232	TAR DNA binding protein	Homo sapiens	36-42	
28754988-7	2017	These structures are thioflavin-T-positive allowing to hypothesize the direct implication of zinc ions in pathological aggregation of TDP-43.	thioflavin T	21-33	TAR DNA binding protein	Homo sapiens	134-140