PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
17068111-6	2006	Most highly conserved between EMR2 and CD97 is the fourth EGF domain, which mediates binding to chondroitin sulfate, a ligand specificity shared by both receptors.	Chondroitin Sulfates	96-115	adhesion G protein-coupled receptor E2	Homo sapiens	30-34	
15693006-2	2005	Chondroitin sulfates (CS) have recently been identified as ligands for EMR2 and CD97.	Chondroitin Sulfates	0-20	adhesion G protein-coupled receptor E2	Homo sapiens	71-75	
15693006-2	2005	Chondroitin sulfates (CS) have recently been identified as ligands for EMR2 and CD97.	Chondroitin Sulfates	22-24	adhesion G protein-coupled receptor E2	Homo sapiens	71-75	
15498814-0	2005	Expression of the largest CD97 and EMR2 isoforms on leukocytes facilitates a specific interaction with chondroitin sulfate on B cells.	Chondroitin Sulfates	103-122	adhesion G protein-coupled receptor E2	Homo sapiens	35-39	
15498814-3	2005	The first two EGF domains of CD97 (but not EMR2) bind CD55 (decay-accelerating factor), while the fourth EGF domain of both CD97 and EMR2 interacts with the glycosaminoglycan chondroitin sulfate (CS).	Chondroitin Sulfates	175-194	adhesion G protein-coupled receptor E2	Homo sapiens	133-137	
15498814-4	2005	Using fluorescent beads coated with soluble recombinant CD97 and EMR2 protein, and isoform-specific monoclonal antibodies, we have determined the cellular and molecular characteristics of the interaction with CS.	Chondroitin Sulfates	209-211	adhesion G protein-coupled receptor E2	Homo sapiens	65-69	
15498814-6	2005	The interaction between CD97/EMR2 and CS may therefore play a role in the interaction of activated T cells, dendritic cells, and macrophages with B cells.	Chondroitin Sulfates	38-40	adhesion G protein-coupled receptor E2	Homo sapiens	29-33	
12829604-6	2003	Through the use of mutant Chinese hamster ovary (CHO) cell lines defective in glycosaminoglycans (GAGs) biosynthesis as well as the enzymatic removal of specific cell surface GAGs, the molecular identity of the EMR2 ligand was identified as chondroitin sulfate (CS).	Chondroitin Sulfates	241-260	adhesion G protein-coupled receptor E2	Homo sapiens	211-215	
12829604-6	2003	Through the use of mutant Chinese hamster ovary (CHO) cell lines defective in glycosaminoglycans (GAGs) biosynthesis as well as the enzymatic removal of specific cell surface GAGs, the molecular identity of the EMR2 ligand was identified as chondroitin sulfate (CS).	Chondroitin Sulfates	262-264	adhesion G protein-coupled receptor E2	Homo sapiens	211-215	
12829604-7	2003	Thus, exogenous CS GAGs blocked the EMR2-ligand interaction in a dose-dependent manner.	Chondroitin Sulfates	16-18	adhesion G protein-coupled receptor E2	Homo sapiens	36-40	
12829604-8	2003	EMR2-CS interaction is Ca2+- and sulphation-dependent and results in cell attachment.	Chondroitin Sulfates	5-7	adhesion G protein-coupled receptor E2	Homo sapiens	0-4