PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
8900411-0	1996	Role of dehydroascorbate in rabbit erythrocyte hexokinase inactivation induced by ascorbic acid/Fe(II).	Dehydroascorbic Acid	8-24	hexokinase-2	Oryctolagus cuniculus	47-57	
9705206-0	1998	Substrates of hexokinase, glucose-6-phosphate dehydrogenase, and glyceraldehyde-3-phosphate dehydrogenase prevent the inhibitory response induced by ascorbic acid/iron and dehydroascorbic acid in rabbit erythrocytes.	Dehydroascorbic Acid	172-192	hexokinase-2	Oryctolagus cuniculus	14-24	
9186478-0	1997	Hexokinase inactivation induced by ascorbic acid/Fe(II) in rabbit erythrocytes is independent of glutathione-reductive processes and appears to be mediated by dehydroascorbic acid.	Dehydroascorbic Acid	159-179	hexokinase-2	Oryctolagus cuniculus	0-10	
9186478-8	1997	Our results demonstrate superimposable kinetics of hexokinase decay promoted by either ascorbic acid/Fe(II) or dehydroascorbic acid in erythrocyte lysates in which the reduced glutathione (GSH) levels were variously manipulated.	Dehydroascorbic Acid	111-131	hexokinase-2	Oryctolagus cuniculus	51-61	
9186478-11	1997	As a consequence, dehydroascorbic acid appears to be the species which directly inhibits hexokinase.	Dehydroascorbic Acid	18-38	hexokinase-2	Oryctolagus cuniculus	89-99	
8900411-3	1996	The H202 formed during this process accelerates the formation of dehydroascorbic acid, which appears to be necessary and sufficient to induce hexokinase inactivation.	Dehydroascorbic Acid	65-85	hexokinase-2	Oryctolagus cuniculus	142-152	
8900411-5	1996	Taken together, these results demonstrate that the process of hexokinase inactivation induced by ascorbic acid/Fe(II) is mediated by dehydroascorbate and that iron and H202 have the sole function of accelerating its formation.	Dehydroascorbic Acid	133-149	hexokinase-2	Oryctolagus cuniculus	62-72