PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
2868714-3	1986	The properties of the technique are illustrated by an investigation of cleavage reactions of the disulfide bonds in bovine insulin, cyclic somatostatin, and conotoxin G1 utilizing the reducing agent dithiothreitol.	Disulfides	97-106	insulin	Bos taurus	123-169	
3180835-0	1988	The occurrence of glutathione-insulin transhydrogenase (protein-disulfide interchange enzyme) in the lens.	Disulfides	64-73	insulin	Bos taurus	30-37	
3899711-0	1985	Nonspecific reaction of a thiol: protein disulfide oxidoreductase with the disulfide bonds of insulin.	Disulfides	41-50	insulin	Bos taurus	94-101	
681081-1	1978	An insulin fragment containing residues A 18-21 and B 19-26 linked by the disulfide bond between residues A 20 and B 19 was synthesized.	Disulfides	74-83	insulin	Bos taurus	3-10	
28194735-6	2017	Since disulfide bond can be selectively cleaved and modified upon methoxy addition, subsequent MS2 CID of the methoxy addition product provides enhanced sequence coverage as demonstrated by the analysis of bovine insulin.	Disulfides	6-15	insulin	Bos taurus	213-220	
29142703-0	2015	Mechanisms and energetics of free radical initiated disulfide bond cleavage in model peptides and insulin by mass spectrometry.	Disulfides	52-61	insulin	Bos taurus	98-105	
29997815-2	2016	The site-selective functionalization of (a) the peptide hormone somatostatin, (b) the interchain disulfide of bovine insulin and (c) functionalization of the proteins GFP and lysozyme with allyl sulfones proceeds in aqueous solution.	Disulfides	97-106	insulin	Bos taurus	117-124	
29142703-3	2015	We show that even multiple disulfide bonds in intact bovine insulin are fragmented in the MS2 stage, releasing the A- and B-chains with a high yield, which has been challenging to achieve by other ion activation methods.	Disulfides	27-36	insulin	Bos taurus	60-67	
9314099-0	1997	Fluoresceinthiocarbamyl-insulin: a potential analytical tool for the assay of disulfide bond reduction.	Disulfides	78-87	insulin	Bos taurus	24-31	
25510931-8	2015	Insulin ions show dramatically reduced HDX levels and exchange rates, which can be attributed to decreased conformational flexibility resulting from the disulfide bonds.	Disulfides	153-162	insulin	Bos taurus	0-7	
22125416-0	2011	Cleavage of Multiple Disulfide Bonds in Insulin via Gold Cationization and Collision-induced Dissociation.	Disulfides	21-30	insulin	Bos taurus	40-47	
22125416-5	2011	However, the incorporation of two gold cations, regardless of oxidation state, resulted in efficient cleavage of the disulfide bonds connecting the two chains of insulin.	Disulfides	117-126	insulin	Bos taurus	162-169	
20835491-0	2010	The application of negative ion electrospray mass spectrometry for the sequencing of underivatized disulfide-containing proteins: insulin and lysozyme.	Disulfides	99-108	insulin	Bos taurus	130-137	
20027620-3	2010	The experimental results show that there are two anodic peaks for the oxidative damage of bovine insulin, which arise from the oxidation of the exposed disulfide bond S--S(CYS7A,CYS7B), forming sulfenic acid RSOH (1.20 V, vs. SCE), sulfinic acid RSO(2)H and sulfonic acid RSO(3)H (1.35 V, vs. SCE).	Disulfides	152-161	insulin	Bos taurus	97-104	
20196567-6	2010	These findings were demonstrated in 14 peptides containing disulfide bonds and further by bovine insulin, which has three disulfide bonds.	Disulfides	122-131	insulin	Bos taurus	97-104	
19383476-0	2009	Bovine insulin filaments induced by reducing disulfide bonds show a different morphology, secondary structure, and cell toxicity from intact insulin amyloid fibrils.	Disulfides	45-54	insulin	Bos taurus	7-14	
19383476-2	2009	Insulin is a 51-residue polypeptide hormone, with its two polypeptide chains linked by one intrachain and two interchain disulfide bonds, and has long been known to self-assemble in vitro into amyloid fibrils.	Disulfides	121-130	insulin	Bos taurus	0-7	
16774767-2	2006	Insulin is a small, predominantly alpha-helical protein consisting of 51 residues in two disulfide-linked polypeptide chains that readily assembles into amyloid fibrils under conditions of low pH and elevated temperature.	Disulfides	89-98	insulin	Bos taurus	0-7	
15739495-2	1997	Insulin contains 51 amino acids and two intrachain disulfide bridges.	Disulfides	51-60	insulin	Bos taurus	0-7	
15739495-4	1997	The results show that the conformation of insulin has changed before cleavage of the disulfide bonds to A and B chains.	Disulfides	85-94	insulin	Bos taurus	42-49	
9314099-6	1997	On this basis, di-fluoresceinthiocarbamyl-insulin constitutes an analytical tool to test the capacity of biochemical preparations in the reduction of disulfide bonds.	Disulfides	150-159	insulin	Bos taurus	42-49	
1570358-9	1992	Insulin proteolysis was inhibited by specific insulin protease inhibitors and stimulated by disulfide reducing agents.	Disulfides	92-101	insulin	Bos taurus	0-7	
8274532-2	1993	The turbidimetric assay of thioredoxin with insulin as the disulfide substrate was optimized; by incorporation of the lag time (tau) into the calculations, linearity was maintained for a wider range of thioredoxin concentrations, and a distinction could be made between reduced and non-reduced forms.	Disulfides	59-68	insulin	Bos taurus	44-51	
2201313-1	1990	We report the synthesis and biological evaluation of a two-chain, disulfide-linked, insulin-like compound consisting of the B-chain of bovine insulin and an A-chain corresponding to the A- and D- domains of human insulin-like growth factor-I (IGF-I) in which the A-domain amino-acid residues -Phe49-Arg50-Ser51-found in IGF-I have been replaced by -Ala-Gly-Val-, the homologous region of sheep insulin.	Disulfides	66-75	insulin	Bos taurus	142-149