PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
19954880-0	2010	Mechanism of suppression of dithiothreitol-induced aggregation of bovine alpha-lactalbumin by alpha-crystallin.	Dithiothreitol	28-42	lactalbumin alpha	Bos taurus	73-90	
25445690-3	2015	To characterize chaperone-like activity of alpha-crystallin damaged by UV irradiation, a test system based on dithiothreitol-induced aggregation of holo-alpha-lactalbumin from bovine milk was used.	Dithiothreitol	110-124	lactalbumin alpha	Bos taurus	153-170	
19954758-2	2010	The potential of small peptides derived from precursor food proteins, to bind to partly unfolded stressed proteins to prevent their irreversible aggregation and inactivation has been demonstrated in various in vitro test systems: dithiothreitol-induced aggregation of alpha-lactalbumin (LA), heat-induced aggregation of alcohol dehydrogenase (ADH), and aggregation and inactivation of bovine erythrocyte carbonic anhydrase (CA) in the process of its refolding after removal of stress conditions.	Dithiothreitol	230-244	lactalbumin alpha	Bos taurus	268-285	
19954880-1	2010	The kinetics of dithiothreitol (DTT)-induced aggregation of alpha-lactalbumin from bovine milk has been studied using dynamic light-scattering technique.	Dithiothreitol	16-30	lactalbumin alpha	Bos taurus	60-77	
19954880-1	2010	The kinetics of dithiothreitol (DTT)-induced aggregation of alpha-lactalbumin from bovine milk has been studied using dynamic light-scattering technique.	Dithiothreitol	32-35	lactalbumin alpha	Bos taurus	60-77	
19954880-2	2010	Analysis of the distribution of the particles formed in the solution of alpha-lactalbumin after the addition of DTT by size showed that the initial stage of the aggregation process was the stage of formation of the start aggregates with the hydrodynamic radius (R(h)) of 80-100nm.	Dithiothreitol	112-115	lactalbumin alpha	Bos taurus	72-89	
12054825-1	2002	The unfolding of the apo and holo forms of bovine alpha-lactalbumin (alpha-LA) upon reduction by dithiothreitol (DTT) in the presence of the small heat-shock protein alpha-crystallin, a molecular chaperone, has been monitored by visible and UV absorption spectroscopy, mass spectrometry and (1)H NMR spectroscopy.	Dithiothreitol	97-111	lactalbumin alpha	Bos taurus	50-67	
12054825-1	2002	The unfolding of the apo and holo forms of bovine alpha-lactalbumin (alpha-LA) upon reduction by dithiothreitol (DTT) in the presence of the small heat-shock protein alpha-crystallin, a molecular chaperone, has been monitored by visible and UV absorption spectroscopy, mass spectrometry and (1)H NMR spectroscopy.	Dithiothreitol	97-111	lactalbumin alpha	Bos taurus	69-77	
12054825-1	2002	The unfolding of the apo and holo forms of bovine alpha-lactalbumin (alpha-LA) upon reduction by dithiothreitol (DTT) in the presence of the small heat-shock protein alpha-crystallin, a molecular chaperone, has been monitored by visible and UV absorption spectroscopy, mass spectrometry and (1)H NMR spectroscopy.	Dithiothreitol	113-116	lactalbumin alpha	Bos taurus	50-67	
12054825-1	2002	The unfolding of the apo and holo forms of bovine alpha-lactalbumin (alpha-LA) upon reduction by dithiothreitol (DTT) in the presence of the small heat-shock protein alpha-crystallin, a molecular chaperone, has been monitored by visible and UV absorption spectroscopy, mass spectrometry and (1)H NMR spectroscopy.	Dithiothreitol	113-116	lactalbumin alpha	Bos taurus	69-77	
12054825-8	2002	In holo alpha-LA, the disulphide bonds are less accessible to DTT, because of the stabilisation of the protein by the bound calcium ion, and reduction occurs much more slowly.	Dithiothreitol	62-65	lactalbumin alpha	Bos taurus	8-16	
10425180-0	1999	The mode of chaperoning of dithiothreitol-denatured alpha-lactalbumin by alpha-crystallin.	Dithiothreitol	27-41	lactalbumin alpha	Bos taurus	52-69	
9346914-5	1997	The complex is formed following reduction of alpha-lactalbumin by dithiothreitol in the presence of alpha-crystallin, and this interaction has been monitored in real time by 1H NMR spectroscopy.	Dithiothreitol	66-80	lactalbumin alpha	Bos taurus	45-62	
35111980-0	2022	Sensitive and resistant of the homologous disulfide-bridged proteins alpha-lactalbumin and lysozyme to attack of hydrogen-atoms, dithiothreitol and trifluoroacetic acid, examined by matrix-assisted laser desorption/ionization mass spectrometry.	Dithiothreitol	129-143	lactalbumin alpha	Bos taurus	69-86