PMID-sentid	Pub_year	Sent_text	comp_official_name	comp_offset	protein_name	organism	prot_offset
17764451-6	2008	Two antibodies recognizing CCP2 and CCP3 were capable of blocking C3b and C4b CFA and heparan sulphate binding, but only one could inhibit DAA.	Heparitin Sulfate	86-102	AGBL carboxypeptidase 3	Homo sapiens	36-40
23022338-6	2012	Of the 9 CCP3+/CCP2- patients, 6 (66.7%) had RA, one patient had ankylosing spondylitis, one osteoarthritis and one psoriatic arthritis.	Radium	45-47	AGBL carboxypeptidase 3	Homo sapiens	9-13
23022338-7	2012	The CCP3-/CCP2+ patient had juvenile RA.	Radium	37-39	AGBL carboxypeptidase 3	Homo sapiens	4-8
19403955-6	2009	The relative change in 3-MH (CCP -4.7% +/- 70.2%, CP -0.4% +/- 81.4%, P 20.3% +/- 75.2%) was less in the groups receiving creatine (p < .05), with the difference for NTx also close to significance (p = .055; CCP -3.4% +/- 66.6%, CP -3.9% +/- 64.9%, P 26.0% +/- 63.8%).	Creatine	122-130	AGBL carboxypeptidase 3	Homo sapiens	211-217
25103237-5	2014	Here we complete the functional characterization of this protein family by demonstrating that CCP2 and CCP3 are deglutamylases, with CCP3 being able to hydrolyze aspartic acids with similar efficiency.	Aspartic Acid	162-176	AGBL carboxypeptidase 3	Homo sapiens	103-107
25103237-5	2014	Here we complete the functional characterization of this protein family by demonstrating that CCP2 and CCP3 are deglutamylases, with CCP3 being able to hydrolyze aspartic acids with similar efficiency.	Aspartic Acid	162-176	AGBL carboxypeptidase 3	Homo sapiens	133-137
11369776-8	2001	The spatial arrangements of the first CCPs were found to be important, as introduction of alanine residues between CCPs 1 and 2, CCPs 2 and 3, and CCPs 3 and 4 resulted in functional impairment.	Alanine	90-97	AGBL carboxypeptidase 3	Homo sapiens	147-159
15066178-4	2004	Based on site-directed mutagenesis, we here delineate the PAPP-A GAG-binding site in the C-terminal modules CCP3 and CCP4.	Glycosaminoglycans	65-68	AGBL carboxypeptidase 3	Homo sapiens	108-112
15066178-5	2004	Using heparin affinity chromatography, commonly employed in such studies, we define three clusters of arginines and lysines of CCP3, which are important for the interaction of PAPP-A with heparin.	Heparin	6-13	AGBL carboxypeptidase 3	Homo sapiens	127-131
15066178-5	2004	Using heparin affinity chromatography, commonly employed in such studies, we define three clusters of arginines and lysines of CCP3, which are important for the interaction of PAPP-A with heparin.	Arginine	102-111	AGBL carboxypeptidase 3	Homo sapiens	127-131
15066178-5	2004	Using heparin affinity chromatography, commonly employed in such studies, we define three clusters of arginines and lysines of CCP3, which are important for the interaction of PAPP-A with heparin.	Lysine	116-123	AGBL carboxypeptidase 3	Homo sapiens	127-131
15066178-5	2004	Using heparin affinity chromatography, commonly employed in such studies, we define three clusters of arginines and lysines of CCP3, which are important for the interaction of PAPP-A with heparin.	Heparin	188-195	AGBL carboxypeptidase 3	Homo sapiens	127-131
15066178-11	2004	Furthermore, when acidic residues of the homologous proteinase PAPP-A2 (Asp1547, Glu1555 and Glu1567) were introduced into the corresponding positions in the sequence of PAPP-A, located in each of the three basic clusters of CCP3, binding to heparin was strongly impaired and cell surface binding was abrogated.	Heparin	242-249	AGBL carboxypeptidase 3	Homo sapiens	225-229