PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
2480779-10	1989	When solubilized placental receptors were pretreated with dithiothreitol (DTT) under conditions reported to reduce intramolecular (class I) disulphide bonds, the immunoreactivity of IGF-I receptors was abolished although total IGF-I binding was little affected.	disulphide	140-150	insulin like growth factor 1	Homo sapiens	182-187	
2479583-1	1989	Reversed-phase chromatography (RPC) was used to resolve two variants of recombinant amino terminal methionyl residue (N-Met) insulin-like growth factor-I (IGF-I) with the same amino acid constitution but different disulphide linkages.	disulphide	214-224	insulin like growth factor 1	Homo sapiens	155-160	
2479583-7	1989	In this system the N-Met IGF-I peak 1 peptide proved 15-fold less potent than the peak 2 peptide with correct disulphide linkages.	disulphide	110-120	insulin like growth factor 1	Homo sapiens	25-30	
3019315-0	1986	Disulphide reduction alters the immunoreactivity and increases the affinity of insulin-like growth-factor-I receptors in human placenta.	disulphide	0-10	insulin like growth factor 1	Homo sapiens	79-107	
15642270-4	2005	Key features of the structures include (1) a disulphide bond ladder that binds to IGF and partially masks the IGF residues responsible for type 1 IGF receptor (IGF-IR) binding, (2) the high-affinity IGF-I interaction site formed by residues 39-82 in a globular fold, and (3) CBP-4 interactions.	disulphide	45-55	insulin like growth factor 1	Homo sapiens	160-165	
11287679-1	2001	The structure and biological activities of two disulphide isomers of a C-region deletion mutant of insulin-like growth factor-I (IGF-I) which has an Asn--Gly link engineered at the junction of the A- and B-regions were studied before and after chemical cleavage.	disulphide	47-57	insulin like growth factor 1	Homo sapiens	99-127	
11287679-1	2001	The structure and biological activities of two disulphide isomers of a C-region deletion mutant of insulin-like growth factor-I (IGF-I) which has an Asn--Gly link engineered at the junction of the A- and B-regions were studied before and after chemical cleavage.	disulphide	47-57	insulin like growth factor 1	Homo sapiens	129-134	
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	114-124	insulin like growth factor 1	Homo sapiens	133-138	
7986379-1	1994	Recombinant human insulin-like growth factor I (IGF-I), a 70-amino-acid peptide containing three disulphide bonds, produces two monomeric and several multimeric species during refolding.	disulphide	97-107	insulin like growth factor 1	Homo sapiens	18-46	
8948444-1	1995	The oxidative folding of human insulin-like growth factor (IGF)-I yields two major disulphide folding isomers.	disulphide	83-93	insulin like growth factor 1	Homo sapiens	31-65	
10325399-1	1999	Insulin-like growth factor-1 (IGF-1) is a serum protein which unexpectedly folds to yield two stable tertiary structures with different disulphide connectivities; native IGF-1 [18-61,6-48,47-52] and IGF-1 swap [18-61,6-47, 48-52].	disulphide	136-146	insulin like growth factor 1	Homo sapiens	30-35	
10325399-0	1999	Modelling of the disulphide-swapped isomer of human insulin-like growth factor-1: implications for receptor binding.	disulphide	17-27	insulin like growth factor 1	Homo sapiens	52-80	
10325399-1	1999	Insulin-like growth factor-1 (IGF-1) is a serum protein which unexpectedly folds to yield two stable tertiary structures with different disulphide connectivities; native IGF-1 [18-61,6-48,47-52] and IGF-1 swap [18-61,6-47, 48-52].	disulphide	136-146	insulin like growth factor 1	Homo sapiens	0-28	
7986379-1	1994	Recombinant human insulin-like growth factor I (IGF-I), a 70-amino-acid peptide containing three disulphide bonds, produces two monomeric and several multimeric species during refolding.	disulphide	97-107	insulin like growth factor 1	Homo sapiens	48-53	
2173560-4	1990	The closely related impurities were identified to be a misfolded form of IGF-I, having mismatched disulphide bonds, a form with the single methionine residue in IGF-I oxidized to methionine sulphoxide and a variant in which the methionine residue was substituted by a norleucine residue during protein synthesis.	disulphide	98-108	insulin like growth factor 1	Homo sapiens	73-78