PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
28655775-8	2017	In heme-loaded cells, heme prompted HO1-CPR complex formation and decreased the HO1/PCBP2 interaction.	Heme	3-7	poly(rC) binding protein 2	Homo sapiens	84-89	
28655775-8	2017	In heme-loaded cells, heme prompted HO1-CPR complex formation and decreased the HO1/PCBP2 interaction.	Heme	22-26	poly(rC) binding protein 2	Homo sapiens	84-89	
28655775-9	2017	Furthermore, in vitro reconstitution experiments with purified recombinant proteins indicated that HO1 could bind to PCBP2 in the presence of heme, whereas loading of PCBP2 with ferrous iron caused PCBP2 to lose its affinity for HO1.	Heme	142-146	poly(rC) binding protein 2	Homo sapiens	117-122	
28655775-10	2017	These results indicate that ferrous iron released from heme can be bound by PCBP2 and suggest a model for an integrated heme catabolism and iron transport metabolon.	Heme	55-59	poly(rC) binding protein 2	Homo sapiens	76-81