PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
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	
7925685-3	1994	By measuring the residual activity of ALR2 incubated in different glutathione redox buffers at 25 degrees C, an apparent redox equilibrium constant of 1.4 +/- 0.1 was evaluated.	Glutathione	66-77	lens aldose reductase pseudogene	Bos taurus	38-42	
7925685-4	1994	Thus the rate and the maximal extent of ALR2 inactivation are proportional to the redox ratio of the thiol used as modifying agent (i.e. [GSH]/[GSSG]).	Glutathione	138-141	lens aldose reductase pseudogene	Bos taurus	40-44	
7925685-11	1994	Besides being a general feature of protein reactivity in oxidative conditions, the glutathione-mediated ALR2 modification might be part of a cell strategy to preserve reducing power in conditions of oxidative stress.	Glutathione	83-94	lens aldose reductase pseudogene	Bos taurus	104-108