PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
3947091-1	1986	The FAD binding site of rabbit liver glutathione reductase has been explored by reconstitution of the apoprotein with several FAD analogs modified in the isoalloxazine ring.	isoalloxazine	154-167	glutathione-disulfide reductase	Homo sapiens	37-58	
9393673-7	1997	Absorption spectra of inhibited GR showed that the charge-transfer interaction between the isoalloxazine moiety of the prosthetic group flavin adenine dinucleotide (FAD) and the active site thiol Cys63 is disturbed by the modification.	isoalloxazine	91-104	glutathione-disulfide reductase	Homo sapiens	32-34	
1899018-10	1991	This suggests that the isoalloxazine rings of mercuric reductase and glutathione reductase are mutually tilted in slightly different ways.	isoalloxazine	23-36	glutathione-disulfide reductase	Homo sapiens	69-90