PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
10493922-0	1999	Intra-A chain disulphide bond forms first during insulin precursor folding.	disulphide	14-24	insulin	Homo sapiens	49-56	
10493922-2	1999	The intra-A chain disulphide bond was found to form early in insulin precursor folding, whereas the corresponding disulphide bond in IGF-I formed late.	disulphide	18-28	insulin	Homo sapiens	61-68	
10493922-7	1999	Time courses of oxidation of reduced insulin A chains, reduced A and B chains, and reduced proinsulins showed that the intra-A chain disulphide bond formed first during insulin precursor folding.	disulphide	133-143	insulin	Homo sapiens	37-44	
10493922-7	1999	Time courses of oxidation of reduced insulin A chains, reduced A and B chains, and reduced proinsulins showed that the intra-A chain disulphide bond formed first during insulin precursor folding.	disulphide	133-143	insulin	Homo sapiens	94-101	
10493922-9	1999	The time course of helix structure formation of insulin A chains also indicated that the intra-A chain disulphide bond formed first, and could stabilize partially folded A chain helix structure.	disulphide	103-113	insulin	Homo sapiens	48-55	
10493922-10	1999	The rate of intra-A chain disulphide bond formation was almost the same as that for both helix structure formation and insulin molecule formation, indicating that the formation of the intra-A chain disulphide bond was the rate limiting step for the folding of insulin precursor.	disulphide	26-36	insulin	Homo sapiens	260-267	
10493922-10	1999	The rate of intra-A chain disulphide bond formation was almost the same as that for both helix structure formation and insulin molecule formation, indicating that the formation of the intra-A chain disulphide bond was the rate limiting step for the folding of insulin precursor.	disulphide	198-208	insulin	Homo sapiens	119-126	
10493922-10	1999	The rate of intra-A chain disulphide bond formation was almost the same as that for both helix structure formation and insulin molecule formation, indicating that the formation of the intra-A chain disulphide bond was the rate limiting step for the folding of insulin precursor.	disulphide	198-208	insulin	Homo sapiens	260-267