PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
24411479-2	2014	Defining its Cys-Gly binding site is extremely important not only in defining the physiological function of GGT, but also in designing specific and effective inhibitors for pharmaceutical purposes.	cysteinylglycine	13-20	gamma-glutamyltransferase 2, pseudogene	Homo sapiens	108-111	
24411479-10	2014	Ion-spray mass analysis of the inhibited E. coli GGT confirmed the formation of a 1:1 covalent adduct with the catalytic subunit (small subunit) with concomitant loss of phenoxide, leaving the peptidyl moiety that presumably occupies the Cys-Gly binding site.	cysteinylglycine	238-245	gamma-glutamyltransferase 2, pseudogene	Homo sapiens	49-52	
24411479-11	2014	The peptidyl phosphonate inhibitors are highly useful as a ligand for X-ray structural analysis of GGT for defining hitherto unidentified Cys-Gly binding site to design specific inhibitors.	cysteinylglycine	138-145	gamma-glutamyltransferase 2, pseudogene	Homo sapiens	99-102