PMID-sentid	Pub_year	Sent_text	compound_name	comp_offset	prot_official_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
12534281-3	2003	DPIV substrates include the glucagonlike peptides, neuropeptide Y, and the chemokines CCL3, CCL5, CCL11, CCL22, and CXCL12.	dpiv	0-4	C-C motif chemokine ligand 3	Homo sapiens	86-90
17161345-2	2006	Based on the findings that DPIV and APN inhibitors induce the TGF-beta1 and IL-10 production and a suppression of T helper cell proliferation in parallel, and that particularly APN inhibitors amplify the suppressing activity of regulatory T cells, both peptidases represent a promising target complex for treatment of diseases associated with an imbalanced T cell response, such as inflammatory bowel diseases (IBD).	dpiv	27-31	transforming growth factor, beta 1	Mus musculus	62-71
17161345-2	2006	Based on the findings that DPIV and APN inhibitors induce the TGF-beta1 and IL-10 production and a suppression of T helper cell proliferation in parallel, and that particularly APN inhibitors amplify the suppressing activity of regulatory T cells, both peptidases represent a promising target complex for treatment of diseases associated with an imbalanced T cell response, such as inflammatory bowel diseases (IBD).	dpiv	27-31	interleukin 10	Mus musculus	76-81
17161345-2	2006	Based on the findings that DPIV and APN inhibitors induce the TGF-beta1 and IL-10 production and a suppression of T helper cell proliferation in parallel, and that particularly APN inhibitors amplify the suppressing activity of regulatory T cells, both peptidases represent a promising target complex for treatment of diseases associated with an imbalanced T cell response, such as inflammatory bowel diseases (IBD).	dpiv	27-31	alanyl (membrane) aminopeptidase	Mus musculus	177-180
15584901-7	2005	DPIV has a variety of peptide substrates, the best studied being GLP-1 (glucagon-like peptide-1), NPY (neuropeptide Y) and CXCL12.	dpiv	0-4	glucagon	Homo sapiens	65-70
15584901-7	2005	DPIV has a variety of peptide substrates, the best studied being GLP-1 (glucagon-like peptide-1), NPY (neuropeptide Y) and CXCL12.	dpiv	0-4	glucagon	Homo sapiens	72-95
15584901-7	2005	DPIV has a variety of peptide substrates, the best studied being GLP-1 (glucagon-like peptide-1), NPY (neuropeptide Y) and CXCL12.	dpiv	0-4	neuropeptide Y	Homo sapiens	98-101
15584901-7	2005	DPIV has a variety of peptide substrates, the best studied being GLP-1 (glucagon-like peptide-1), NPY (neuropeptide Y) and CXCL12.	dpiv	0-4	neuropeptide Y	Homo sapiens	103-117
15584901-7	2005	DPIV has a variety of peptide substrates, the best studied being GLP-1 (glucagon-like peptide-1), NPY (neuropeptide Y) and CXCL12.	dpiv	0-4	C-X-C motif chemokine ligand 12	Homo sapiens	123-129
12534281-3	2003	DPIV substrates include the glucagonlike peptides, neuropeptide Y, and the chemokines CCL3, CCL5, CCL11, CCL22, and CXCL12.	dpiv	0-4	C-C motif chemokine ligand 5	Homo sapiens	92-96
12534281-3	2003	DPIV substrates include the glucagonlike peptides, neuropeptide Y, and the chemokines CCL3, CCL5, CCL11, CCL22, and CXCL12.	dpiv	0-4	C-X-C motif chemokine ligand 12	Homo sapiens	116-122
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
20186930-8	2010	Cytoplasmic DP enzyme activity was increased (P < 0.05) in DPIV(-/-) mice at day 6 of DSS, while DP2 activity was increased (P < 0.05) in WT mice with colitis.	dpiv	62-66	angiotensin I converting enzyme (peptidyl-dipeptidase A) 1	Mus musculus	12-14
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
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 9	Homo sapiens	109-112
12675232-3	2003	Similar effects on T cell proliferation and function have been observed in response to inhibition of DPIV, which is strongly suggestive of a functional synergism of APN and DPIV.	dpiv	101-105	alanyl aminopeptidase, membrane	Homo sapiens	165-168
12675232-4	2003	In support of this hypothesis evidence is provided showing that the simultaneous application of inhibitors of DPIV and APN further enhances the anti-inflammatory and immunosuppressive effects provoked by the inhibition of APN or DPIV alone.	dpiv	110-114	alanyl aminopeptidase, membrane	Homo sapiens	222-225
12675232-4	2003	In support of this hypothesis evidence is provided showing that the simultaneous application of inhibitors of DPIV and APN further enhances the anti-inflammatory and immunosuppressive effects provoked by the inhibition of APN or DPIV alone.	dpiv	229-233	alanyl aminopeptidase, membrane	Homo sapiens	119-122
8852605-9	1996	These data strongly suggest that Tat protein is a potent "natural" inhibitor of DP IV/CD26, and they support the hypothesis that DPIV plays a role in Tat"s immunosuppressive activity.	dpiv	129-133	tyrosine aminotransferase	Homo sapiens	33-36
8852605-9	1996	These data strongly suggest that Tat protein is a potent "natural" inhibitor of DP IV/CD26, and they support the hypothesis that DPIV plays a role in Tat"s immunosuppressive activity.	dpiv	129-133	dipeptidyl peptidase 4	Homo sapiens	80-85
8852605-9	1996	These data strongly suggest that Tat protein is a potent "natural" inhibitor of DP IV/CD26, and they support the hypothesis that DPIV plays a role in Tat"s immunosuppressive activity.	dpiv	129-133	tyrosine aminotransferase	Homo sapiens	150-153
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