PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
34369377-4	2021	Here, we describe the effects of ATP-independent Hsp40 chaperones, DNAJA2 and DNAJB1, on tau amyloid-fiber formation, and compare these to the small heat-shock protein HSPB1.	Adenosine Triphosphate	33-36	DnaJ heat shock protein family (Hsp40) member A2	Homo sapiens	67-73	
29414793-5	2018	As a model system, we chose heat shock protein 70 (Hsp70), which is an ATP-dependent molecular chaperone that interacts with co-chaperones, including DnaJA2 and BAG2.	Adenosine Triphosphate	71-74	DnaJ heat shock protein family (Hsp40) member A2	Homo sapiens	150-156	
15047721-8	2004	bag-1 further stimulates ATP hydrolysis and protein refolding by Hsp70 plus DjA2 but not by Hsp70 plus DjA4.	Adenosine Triphosphate	25-28	DnaJ heat shock protein family (Hsp40) member A2	Homo sapiens	76-80	
12021775-5	2002	The APIase activity shows both regio and stereo selectivity and is stimulated two-fold in the presence of the complete DnaK/GrpE/DnaJ/ATP refolding system.	Adenosine Triphosphate	134-137	DnaJ heat shock protein family (Hsp40) member A2	Homo sapiens	129-133