PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
18275857-3	2008	Since DPIV is known to process chemokines we surveyed 27 chemokines for cleavage by DP8.	dpiv	6-10	dipeptidyl peptidase 8	Homo sapiens	84-87	
20536396-8	2010	Homology modelling of DP8 using DPIV and FAP crystal structures suggested that DP8(D772), DP8(H434) and DP8(D435) were located at the edge of the S2 catalytic pocket, contributing to the junction between the alpha-beta hydrolase and beta-propeller domains.	dpiv	32-36	dipeptidyl peptidase 8	Homo sapiens	22-25	
20536396-9	2010	This study provides insights into how the DP8 substrate pocket and dimer interface differ from DPIV and FAP which could be utilised for designing more selective DP8 inhibitors.	dpiv	95-99	dipeptidyl peptidase 8	Homo sapiens	161-164	
12675227-4	2003	The similarities between DP8, DP9 and DPIV in tissue expression pattern suggest a potential role for DP8 and DP9 in liver disease, T cell activation and immune function.	dpiv	38-42	dipeptidyl peptidase 8	Homo sapiens	101-104