PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
28655775-0	2017	The iron chaperone poly(rC)-binding protein 2 forms a metabolon with the heme oxygenase 1/cytochrome P450 reductase complex for heme catabolism and iron transfer.	Iron	4-8	poly(rC) binding protein 2	Homo sapiens	19-45	
28655775-3	2017	Recently, we demonstrated that the iron chaperone poly(rC)-binding protein 2 (PCBP2) can directly receive ferrous iron from DMT1 or transfer iron to the iron exporter, ferroportin 1.	Iron	35-39	poly(rC) binding protein 2	Homo sapiens	50-76	
28655775-3	2017	Recently, we demonstrated that the iron chaperone poly(rC)-binding protein 2 (PCBP2) can directly receive ferrous iron from DMT1 or transfer iron to the iron exporter, ferroportin 1.	Iron	35-39	poly(rC) binding protein 2	Homo sapiens	78-83	
28655775-3	2017	Recently, we demonstrated that the iron chaperone poly(rC)-binding protein 2 (PCBP2) can directly receive ferrous iron from DMT1 or transfer iron to the iron exporter, ferroportin 1.	Iron	114-118	poly(rC) binding protein 2	Homo sapiens	50-76	
28655775-3	2017	Recently, we demonstrated that the iron chaperone poly(rC)-binding protein 2 (PCBP2) can directly receive ferrous iron from DMT1 or transfer iron to the iron exporter, ferroportin 1.	Iron	114-118	poly(rC) binding protein 2	Homo sapiens	78-83	
28655775-3	2017	Recently, we demonstrated that the iron chaperone poly(rC)-binding protein 2 (PCBP2) can directly receive ferrous iron from DMT1 or transfer iron to the iron exporter, ferroportin 1.	Iron	114-118	poly(rC) binding protein 2	Homo sapiens	50-76	
28655775-3	2017	Recently, we demonstrated that the iron chaperone poly(rC)-binding protein 2 (PCBP2) can directly receive ferrous iron from DMT1 or transfer iron to the iron exporter, ferroportin 1.	Iron	114-118	poly(rC) binding protein 2	Homo sapiens	78-83	
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.	Iron	178-190	poly(rC) binding protein 2	Homo sapiens	167-172	
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.	Iron	178-190	poly(rC) binding protein 2	Homo sapiens	167-172	
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.	Iron	36-40	poly(rC) binding protein 2	Homo sapiens	76-81	
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.	Iron	140-144	poly(rC) binding protein 2	Homo sapiens	76-81