PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
11580274-0	2001	Thiol/disulfide interconversion in bovine lens aldose reductase induced by intermediates of glutathione turnover.	Sulfhydryl Compounds	0-5	aldose reductase	Bos taurus	47-63	
11580274-0	2001	Thiol/disulfide interconversion in bovine lens aldose reductase induced by intermediates of glutathione turnover.	Disulfides	6-15	aldose reductase	Bos taurus	47-63	
11580274-0	2001	Thiol/disulfide interconversion in bovine lens aldose reductase induced by intermediates of glutathione turnover.	Glutathione	92-103	aldose reductase	Bos taurus	47-63	
11580274-2	2001	Disulfides of both thiol compounds appear to be very effective as ALR2 thiolating agents.	Disulfides	0-10	lens aldose reductase pseudogene	Bos taurus	66-70	
11580274-2	2001	Disulfides of both thiol compounds appear to be very effective as ALR2 thiolating agents.	Sulfhydryl Compounds	19-24	lens aldose reductase pseudogene	Bos taurus	66-70	
11580274-3	2001	Cysteine- and CysGly-modified ALR2 forms (Cys-ALR2 and CysGly-ALR2, respectively) are characterized by the presence of a mixed disulfide bond involving Cys298, as demonstrated by a combined electrospray mass spectrometry and Edman degradation approach.	Cysteine	0-8	lens aldose reductase pseudogene	Bos taurus	30-34	
11580274-3	2001	Cysteine- and CysGly-modified ALR2 forms (Cys-ALR2 and CysGly-ALR2, respectively) are characterized by the presence of a mixed disulfide bond involving Cys298, as demonstrated by a combined electrospray mass spectrometry and Edman degradation approach.	Cysteine	0-8	lens aldose reductase pseudogene	Bos taurus	46-50	
11580274-3	2001	Cysteine- and CysGly-modified ALR2 forms (Cys-ALR2 and CysGly-ALR2, respectively) are characterized by the presence of a mixed disulfide bond involving Cys298, as demonstrated by a combined electrospray mass spectrometry and Edman degradation approach.	Cysteine	0-8	lens aldose reductase pseudogene	Bos taurus	46-50	
11580274-3	2001	Cysteine- and CysGly-modified ALR2 forms (Cys-ALR2 and CysGly-ALR2, respectively) are characterized by the presence of a mixed disulfide bond involving Cys298, as demonstrated by a combined electrospray mass spectrometry and Edman degradation approach.	Cysteine	0-3	lens aldose reductase pseudogene	Bos taurus	30-34	
11580274-3	2001	Cysteine- and CysGly-modified ALR2 forms (Cys-ALR2 and CysGly-ALR2, respectively) are characterized by the presence of a mixed disulfide bond involving Cys298, as demonstrated by a combined electrospray mass spectrometry and Edman degradation approach.	Cysteine	0-3	lens aldose reductase pseudogene	Bos taurus	46-50	
11580274-3	2001	Cysteine- and CysGly-modified ALR2 forms (Cys-ALR2 and CysGly-ALR2, respectively) are characterized by the presence of a mixed disulfide bond involving Cys298, as demonstrated by a combined electrospray mass spectrometry and Edman degradation approach.	Cysteine	0-3	lens aldose reductase pseudogene	Bos taurus	46-50	
11580274-3	2001	Cysteine- and CysGly-modified ALR2 forms (Cys-ALR2 and CysGly-ALR2, respectively) are characterized by the presence of a mixed disulfide bond involving Cys298, as demonstrated by a combined electrospray mass spectrometry and Edman degradation approach.	Disulfides	127-136	lens aldose reductase pseudogene	Bos taurus	30-34	
11580274-3	2001	Cysteine- and CysGly-modified ALR2 forms (Cys-ALR2 and CysGly-ALR2, respectively) are characterized by the presence of a mixed disulfide bond involving Cys298, as demonstrated by a combined electrospray mass spectrometry and Edman degradation approach.	Disulfides	127-136	lens aldose reductase pseudogene	Bos taurus	46-50	
11580274-3	2001	Cysteine- and CysGly-modified ALR2 forms (Cys-ALR2 and CysGly-ALR2, respectively) are characterized by the presence of a mixed disulfide bond involving Cys298, as demonstrated by a combined electrospray mass spectrometry and Edman degradation approach.	Disulfides	127-136	lens aldose reductase pseudogene	Bos taurus	46-50	
11580274-4	2001	Both Cys-ALR2 and CysGly-ALR2 essentially retain the ability to reduce glyceraldehyde but lose the susceptibility to inhibition by Sorbinil and other ALR2 inhibitors.	Glyceraldehyde	71-85	lens aldose reductase pseudogene	Bos taurus	9-13	
11580274-4	2001	Both Cys-ALR2 and CysGly-ALR2 essentially retain the ability to reduce glyceraldehyde but lose the susceptibility to inhibition by Sorbinil and other ALR2 inhibitors.	Glyceraldehyde	71-85	lens aldose reductase pseudogene	Bos taurus	25-29	
11580274-4	2001	Both Cys-ALR2 and CysGly-ALR2 essentially retain the ability to reduce glyceraldehyde but lose the susceptibility to inhibition by Sorbinil and other ALR2 inhibitors.	Glyceraldehyde	71-85	lens aldose reductase pseudogene	Bos taurus	25-29	
11580274-4	2001	Both Cys-ALR2 and CysGly-ALR2 essentially retain the ability to reduce glyceraldehyde but lose the susceptibility to inhibition by Sorbinil and other ALR2 inhibitors.	sorbinil	131-139	lens aldose reductase pseudogene	Bos taurus	9-13	
11580274-4	2001	Both Cys-ALR2 and CysGly-ALR2 essentially retain the ability to reduce glyceraldehyde but lose the susceptibility to inhibition by Sorbinil and other ALR2 inhibitors.	sorbinil	131-139	lens aldose reductase pseudogene	Bos taurus	25-29	
11580274-4	2001	Both Cys-ALR2 and CysGly-ALR2 essentially retain the ability to reduce glyceraldehyde but lose the susceptibility to inhibition by Sorbinil and other ALR2 inhibitors.	sorbinil	131-139	lens aldose reductase pseudogene	Bos taurus	25-29	
11580274-5	2001	Cys-ALR2 and CysGly-ALR2 are easily reduced back to the native enzyme form by dithiothreitol and GSH treatment; on the contrary, Cys and 2-mercaptoethanol appear to act as protein trans-thiolating agents, rather than reducing agents.	Dithiothreitol	78-92	lens aldose reductase pseudogene	Bos taurus	4-8	
11580274-5	2001	Cys-ALR2 and CysGly-ALR2 are easily reduced back to the native enzyme form by dithiothreitol and GSH treatment; on the contrary, Cys and 2-mercaptoethanol appear to act as protein trans-thiolating agents, rather than reducing agents.	Dithiothreitol	78-92	lens aldose reductase pseudogene	Bos taurus	20-24	
11580274-5	2001	Cys-ALR2 and CysGly-ALR2 are easily reduced back to the native enzyme form by dithiothreitol and GSH treatment; on the contrary, Cys and 2-mercaptoethanol appear to act as protein trans-thiolating agents, rather than reducing agents.	Glutathione	97-100	lens aldose reductase pseudogene	Bos taurus	4-8	
11580274-5	2001	Cys-ALR2 and CysGly-ALR2 are easily reduced back to the native enzyme form by dithiothreitol and GSH treatment; on the contrary, Cys and 2-mercaptoethanol appear to act as protein trans-thiolating agents, rather than reducing agents.	Glutathione	97-100	lens aldose reductase pseudogene	Bos taurus	20-24	
11580274-5	2001	Cys-ALR2 and CysGly-ALR2 are easily reduced back to the native enzyme form by dithiothreitol and GSH treatment; on the contrary, Cys and 2-mercaptoethanol appear to act as protein trans-thiolating agents, rather than reducing agents.	Cysteine	0-3	lens aldose reductase pseudogene	Bos taurus	4-8	
11580274-5	2001	Cys-ALR2 and CysGly-ALR2 are easily reduced back to the native enzyme form by dithiothreitol and GSH treatment; on the contrary, Cys and 2-mercaptoethanol appear to act as protein trans-thiolating agents, rather than reducing agents.	Mercaptoethanol	137-154	lens aldose reductase pseudogene	Bos taurus	4-8	
11580274-5	2001	Cys-ALR2 and CysGly-ALR2 are easily reduced back to the native enzyme form by dithiothreitol and GSH treatment; on the contrary, Cys and 2-mercaptoethanol appear to act as protein trans-thiolating agents, rather than reducing agents.	Mercaptoethanol	137-154	lens aldose reductase pseudogene	Bos taurus	20-24	
11580274-6	2001	The treatment at 37 degrees C of both Cys-ALR2 and CysGly-ALR2, unlikely what observed for glutathionyl-modified ALR2 (GS-ALR2), promotes the generation of an intramolecular disulfide bond between Cys298 and Cys303 residues.	Cysteine	38-41	lens aldose reductase pseudogene	Bos taurus	42-46	
11580274-6	2001	The treatment at 37 degrees C of both Cys-ALR2 and CysGly-ALR2, unlikely what observed for glutathionyl-modified ALR2 (GS-ALR2), promotes the generation of an intramolecular disulfide bond between Cys298 and Cys303 residues.	Cysteine	38-41	lens aldose reductase pseudogene	Bos taurus	119-126	
11580274-6	2001	The treatment at 37 degrees C of both Cys-ALR2 and CysGly-ALR2, unlikely what observed for glutathionyl-modified ALR2 (GS-ALR2), promotes the generation of an intramolecular disulfide bond between Cys298 and Cys303 residues.	glutathionyl	91-103	lens aldose reductase pseudogene	Bos taurus	42-46	
11580274-6	2001	The treatment at 37 degrees C of both Cys-ALR2 and CysGly-ALR2, unlikely what observed for glutathionyl-modified ALR2 (GS-ALR2), promotes the generation of an intramolecular disulfide bond between Cys298 and Cys303 residues.	glutathionyl	91-103	lens aldose reductase pseudogene	Bos taurus	58-62	
11580274-6	2001	The treatment at 37 degrees C of both Cys-ALR2 and CysGly-ALR2, unlikely what observed for glutathionyl-modified ALR2 (GS-ALR2), promotes the generation of an intramolecular disulfide bond between Cys298 and Cys303 residues.	glutathionyl	91-103	lens aldose reductase pseudogene	Bos taurus	58-62	
11580274-6	2001	The treatment at 37 degrees C of both Cys-ALR2 and CysGly-ALR2, unlikely what observed for glutathionyl-modified ALR2 (GS-ALR2), promotes the generation of an intramolecular disulfide bond between Cys298 and Cys303 residues.	glutathionyl	91-103	lens aldose reductase pseudogene	Bos taurus	119-126	
11580274-6	2001	The treatment at 37 degrees C of both Cys-ALR2 and CysGly-ALR2, unlikely what observed for glutathionyl-modified ALR2 (GS-ALR2), promotes the generation of an intramolecular disulfide bond between Cys298 and Cys303 residues.	Disulfides	174-183	lens aldose reductase pseudogene	Bos taurus	42-46	
11580274-6	2001	The treatment at 37 degrees C of both Cys-ALR2 and CysGly-ALR2, unlikely what observed for glutathionyl-modified ALR2 (GS-ALR2), promotes the generation of an intramolecular disulfide bond between Cys298 and Cys303 residues.	Disulfides	174-183	lens aldose reductase pseudogene	Bos taurus	58-62	
11580274-6	2001	The treatment at 37 degrees C of both Cys-ALR2 and CysGly-ALR2, unlikely what observed for glutathionyl-modified ALR2 (GS-ALR2), promotes the generation of an intramolecular disulfide bond between Cys298 and Cys303 residues.	Disulfides	174-183	lens aldose reductase pseudogene	Bos taurus	58-62	
11580274-6	2001	The treatment at 37 degrees C of both Cys-ALR2 and CysGly-ALR2, unlikely what observed for glutathionyl-modified ALR2 (GS-ALR2), promotes the generation of an intramolecular disulfide bond between Cys298 and Cys303 residues.	Disulfides	174-183	lens aldose reductase pseudogene	Bos taurus	119-126	
11580274-7	2001	A rationale for the special susceptibility of Cys-ALR2 and CysGly-ALR2, as compared to GS-ALR2, to the thermally induced intramolecular rearrangement is given on the basis of a molecular dynamic and energy minimization approach.	Cysteine	46-49	lens aldose reductase pseudogene	Bos taurus	50-54	
11580274-8	2001	A pathway of thiol/disulfide interconversion for bovine lens ALR2 induced, in oxidative conditions, by physiological thiol compounds is proposed.	Sulfhydryl Compounds	13-18	lens aldose reductase pseudogene	Bos taurus	61-65	
11580274-8	2001	A pathway of thiol/disulfide interconversion for bovine lens ALR2 induced, in oxidative conditions, by physiological thiol compounds is proposed.	Disulfides	19-28	lens aldose reductase pseudogene	Bos taurus	61-65	
11580274-8	2001	A pathway of thiol/disulfide interconversion for bovine lens ALR2 induced, in oxidative conditions, by physiological thiol compounds is proposed.	Sulfhydryl Compounds	117-122	lens aldose reductase pseudogene	Bos taurus	61-65