PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
7947925-1	1994	It has been proposed that the function of serum amyloid P component (SAP) may closely relate with its binding to polysaccharides, especially glycosaminoglycans.	Polysaccharides	113-128	amyloid P component, serum	Homo sapiens	42-67	
18626489-4	2008	From numerous studies over the past 15 years it is clear that glycans can influence T cell responses either by contribution to the structure of the epitope or by influencing the profile of peptide epitopes presented by APCs.	Polysaccharides	62-69	amyloid P component, serum	Homo sapiens	219-223	
18626489-6	2008	Here we discuss the potential impact of glycans on the profile of self-epitopes presented by APCs and the consequence of changes in glycosylation to generate neo self-epitopes resulting in the loss of tolerance and the development of autoimmune diseases.	Polysaccharides	40-47	amyloid P component, serum	Homo sapiens	93-97	
18056364-0	2007	Introduction of zwitterionic motifs into bacterial polysaccharides generates TLR2 agonists able to activate APCs.	Polysaccharides	51-66	amyloid P component, serum	Homo sapiens	108-112	
18056364-1	2007	It was shown previously that bacterial polysaccharides (PS), which naturally contain both positive and negative charges, are able to activate T cells and APCs.	Polysaccharides	39-54	amyloid P component, serum	Homo sapiens	154-158	
18056364-1	2007	It was shown previously that bacterial polysaccharides (PS), which naturally contain both positive and negative charges, are able to activate T cells and APCs.	Polysaccharides	56-58	amyloid P component, serum	Homo sapiens	154-158	
7947925-1	1994	It has been proposed that the function of serum amyloid P component (SAP) may closely relate with its binding to polysaccharides, especially glycosaminoglycans.	Polysaccharides	113-128	amyloid P component, serum	Homo sapiens	69-72	
2071579-13	1991	Dissociation of the SAP.C4BP complex by sulfated polysaccharides such as heparin may be a physiological response that could be important during tissue damage or complement activation.	Polysaccharides	49-64	amyloid P component, serum	Homo sapiens	20-23	
2478195-3	1989	It was shown for the first time that the calcium-dependent polymerization of SAP was inhibited by some sulfated polysaccharides.	Polysaccharides	112-127	amyloid P component, serum	Homo sapiens	77-80	
3211159-0	1988	Evidence that serum amyloid P component binds to mannose-terminated sequences of polysaccharides and glycoproteins.	Polysaccharides	81-96	amyloid P component, serum	Homo sapiens	14-39	
3211159-10	1988	These findings indicate that mannose-terminated oligosaccharides of polysaccharides and glycoproteins represent a new class of ligands for SAP and suggest that SAP may function as a mannose-binding protein.	Polysaccharides	68-83	amyloid P component, serum	Homo sapiens	139-142	
3211159-10	1988	These findings indicate that mannose-terminated oligosaccharides of polysaccharides and glycoproteins represent a new class of ligands for SAP and suggest that SAP may function as a mannose-binding protein.	Polysaccharides	68-83	amyloid P component, serum	Homo sapiens	160-163	
3211159-2	1988	In the presence of calcium, SAP binds to certain complex polysaccharides, including agarose and zymosan.	Polysaccharides	57-72	amyloid P component, serum	Homo sapiens	28-31