PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
16735468-8	2006	Although it now seems reasonable that Sco1, which is characterized by a thioredoxin fold, has evolved to bind a metal atom via the di-Cys motif to act as a copper chaperone, the oxidized form of the nickel-bound protein suggests that it may also maintain the thioredoxin function.	Nickel	199-205	thioredoxin	Homo sapiens	72-83	
16735468-8	2006	Although it now seems reasonable that Sco1, which is characterized by a thioredoxin fold, has evolved to bind a metal atom via the di-Cys motif to act as a copper chaperone, the oxidized form of the nickel-bound protein suggests that it may also maintain the thioredoxin function.	Nickel	199-205	thioredoxin	Homo sapiens	259-270	
32129160-3	2020	The fusion protein, trx-hAS, was initially released by osmotic shock treatment from the host cells and subsequently purified using a nickel affinity chromatography.	Nickel	133-139	thioredoxin	Homo sapiens	20-23	
8617783-3	1996	The combined effect of two histidine mutants, E30H and Q62H, gave thioredoxin the capacity to bind to nickel ions immobilized on iminodiacetic acid- and nitrilotriacetic acid-Sepharose resins.	Nickel	102-108	thioredoxin	Homo sapiens	66-77	
32895213-5	2020	The fusion protein Trx-MVF-HER3 I was purified using nickel ion affinity chromatography, and the purified protein was digested by enterokinase to remove Trx tag.	Nickel	53-59	thioredoxin	Homo sapiens	19-22