PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
11023791-0	2000	Dissecting the hydrogen exchange properties of insulin under amyloid fibril forming conditions: a site-specific investigation by mass spectrometry.	Hydrogen	15-23	insulin	Bos taurus	47-54	
11934523-6	2002	When normalized against bovine GAPDH as an internal control, 0.5 or 1h treatment with 10 ng/mL insulin gave 39+/-4 and 64+/-2-fold increase in leptin mRNA compared with 0 h control.	Hydrogen	68-70	insulin	Bos taurus	95-102	
11023791-1	2000	We have examined the hydrogen exchange properties of bovine insulin under solution conditions that cause it to aggregate and eventually form amyloid fibrils.	Hydrogen	21-29	insulin	Bos taurus	60-67	
1372979-9	1992	The predictions from this method are compared to known hydrogen positions for bovine pancreatic trypsin inhibitor, insulin, RNase-A, and trypsin for which the neutron diffraction structures have been determined.	Hydrogen	55-63	insulin	Bos taurus	115-122	
7811688-0	1994	A 1H-NMR determination of the solution structure of the A-chain of insulin: comparison with the crystal structure and an examination of the role of solvent.	Hydrogen	2-4	insulin	Bos taurus	67-74	
7811688-1	1994	The 1H-NMR chemical shift assignments for the oxidized A-chain of bovine insulin have been determined in aqueous and 30% trifluoroethanol/water solutions.	Hydrogen	4-6	insulin	Bos taurus	73-80	
8567187-0	1995	Solution structure of the B-chain of insulin as determined by 1H NMR spectroscopy.	Hydrogen	62-64	insulin	Bos taurus	37-44	
8567187-2	1995	The solution structure of the isolated B-chain of bovine insulin has been determined by 1H NMR spectroscopy combined with simulated annealing calculations.	Hydrogen	88-90	insulin	Bos taurus	57-64	
34699915-6	2022	The functional groups from the amino acids, like CO, N-H and aromatic functional groups, are anticipated to further stabilize the insulin conformation by forming hydrogen bond and van der Waals interactions with the key amyloidogenic sequences of insulin, A13-A20 from A-chain and B9-B20 from B-chain.	Hydrogen	162-170	insulin	Bos taurus	130-137	
34699915-6	2022	The functional groups from the amino acids, like CO, N-H and aromatic functional groups, are anticipated to further stabilize the insulin conformation by forming hydrogen bond and van der Waals interactions with the key amyloidogenic sequences of insulin, A13-A20 from A-chain and B9-B20 from B-chain.	Hydrogen	162-170	insulin	Bos taurus	247-254	
2896788-0	1988	The discrimination between human, porcine and bovine insulin with 1H NMR spectroscopy.	Hydrogen	66-68	insulin	Bos taurus	53-60	
2896788-1	1988	The 1H- and 1H-1H correlation (COSY) NMR spectra of human, porcine and bovine insulin have been recorded.	Hydrogen	4-6	insulin	Bos taurus	78-85	
2896788-1	1988	The 1H- and 1H-1H correlation (COSY) NMR spectra of human, porcine and bovine insulin have been recorded.	Hydrogen	12-14	insulin	Bos taurus	78-85	
2896788-1	1988	The 1H- and 1H-1H correlation (COSY) NMR spectra of human, porcine and bovine insulin have been recorded.	Hydrogen	12-14	insulin	Bos taurus	78-85	
25459908-9	2014	Feeding LS versus HS resulted in an increase in the ratio of bovine somatotropin to insulin.	Hydrogen	18-20	insulin	Bos taurus	84-91	
3885857-8	1985	This may suggest that the formation of the insulin dimer is not driven by hydrophobic bonding but, rather, is driven by the formation between subunits of four hydrogen bonds in an apolar environment.	Hydrogen	159-167	insulin	Bos taurus	43-50	
24796962-5	2014	The fast evolution of some hydrogen bonds of bovine insulin in the presence of the 1.0 V/nm electric field shows that different microwaves could either speed up protein folding or destroy the secondary structure of globular proteins deponding on the intensity of the external electric field.	Hydrogen	27-35	insulin	Bos taurus	52-59