PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 9013976-0 1997 Secreted chondroitin sulfate proteoglycan of human B cell lines binds to the complement protein C1q and inhibits complex formation of C1. Chondroitin Sulfates 9-28 complement C1q A chain Homo sapiens 96-99 9013976-6 1997 Binding of C1q to CSPG was competitively inhibited by free glycosaminoglycans (GAG) in the order dextran sulfate > heparin > heparan sulfate > chondroitin-6-sulfate (CS-C) > dermatan sulfate (CS-B) > chondroitin-4-sulfate (CS-A). Chondroitin Sulfates 152-173 complement C1q A chain Homo sapiens 11-14 9013976-6 1997 Binding of C1q to CSPG was competitively inhibited by free glycosaminoglycans (GAG) in the order dextran sulfate > heparin > heparan sulfate > chondroitin-6-sulfate (CS-C) > dermatan sulfate (CS-B) > chondroitin-4-sulfate (CS-A). Chondroitin Sulfates 215-236 complement C1q A chain Homo sapiens 11-14 9013976-6 1997 Binding of C1q to CSPG was competitively inhibited by free glycosaminoglycans (GAG) in the order dextran sulfate > heparin > heparan sulfate > chondroitin-6-sulfate (CS-C) > dermatan sulfate (CS-B) > chondroitin-4-sulfate (CS-A). Chondroitin Sulfates 238-242 complement C1q A chain Homo sapiens 11-14 6800936-2 1981 The binding of the alkaline phosphatase conjugated fibronectin to C1q was dose dependent and inhibited by fibronectin and by the sulfated polymers heparin and chondroitin sulfate. Chondroitin Sulfates 159-178 complement C1q A chain Homo sapiens 66-69 8172566-5 1993 At the N-terminal end of the C1q A-chain is a leader peptide sequence that anchors the intact C1q molecule firmly in the membrane of macrophages, the C1q molecule can thus be classified as a type II membrane protein, functioning as an additional receptor for molecules known to react with C1q in fluid phase such as the Fc region of IgG, LPS and polyanionic molecules (e.g. chondroitin sulphate, heparin, dextran sulphate etc.). Chondroitin Sulfates 374-394 complement C1q A chain Homo sapiens 29-32 8172566-5 1993 At the N-terminal end of the C1q A-chain is a leader peptide sequence that anchors the intact C1q molecule firmly in the membrane of macrophages, the C1q molecule can thus be classified as a type II membrane protein, functioning as an additional receptor for molecules known to react with C1q in fluid phase such as the Fc region of IgG, LPS and polyanionic molecules (e.g. chondroitin sulphate, heparin, dextran sulphate etc.). Chondroitin Sulfates 374-394 complement C1q A chain Homo sapiens 94-97 8172566-5 1993 At the N-terminal end of the C1q A-chain is a leader peptide sequence that anchors the intact C1q molecule firmly in the membrane of macrophages, the C1q molecule can thus be classified as a type II membrane protein, functioning as an additional receptor for molecules known to react with C1q in fluid phase such as the Fc region of IgG, LPS and polyanionic molecules (e.g. chondroitin sulphate, heparin, dextran sulphate etc.). Chondroitin Sulfates 374-394 complement C1q A chain Homo sapiens 94-97 8172566-5 1993 At the N-terminal end of the C1q A-chain is a leader peptide sequence that anchors the intact C1q molecule firmly in the membrane of macrophages, the C1q molecule can thus be classified as a type II membrane protein, functioning as an additional receptor for molecules known to react with C1q in fluid phase such as the Fc region of IgG, LPS and polyanionic molecules (e.g. chondroitin sulphate, heparin, dextran sulphate etc.). Chondroitin Sulfates 374-394 complement C1q A chain Homo sapiens 94-97 3492025-2 1986 Several lines of evidence suggest that this factor is distinct from the documented C1q inhibitor which is a chondroitin sulphate. Chondroitin Sulfates 108-128 complement C1q A chain Homo sapiens 83-86 6788768-0 1981 The C1q inhibitor in serum is a chondroitin 4-sulfate proteoglycan. Chondroitin Sulfates 32-53 complement C1q A chain Homo sapiens 4-7 6788768-5 1981 Additional evidence for the noncartilaginous origin of C1q inhibitor is that its glycosaminoglycan chains totally lack chondroitin 6-sulfate isomers. Chondroitin Sulfates 119-140 complement C1q A chain Homo sapiens 55-58 21268013-6 2011 Interactions between SG and C1q as well as MBL are diminished in the presence of chondroitin sulfate type E. In addition, we localized the SG-binding site to the collagen-like stalk of C1q. Chondroitin Sulfates 81-100 complement C1q A chain Homo sapiens 28-31 18503629-7 2008 C1q was identified as the recognition molecule, as it bound directly to CS, and CS-triggered complement activation could be restored in C1q-depleted serum by adding purified C1q. Chondroitin Sulfates 72-74 complement C1q A chain Homo sapiens 0-3 18503629-7 2008 C1q was identified as the recognition molecule, as it bound directly to CS, and CS-triggered complement activation could be restored in C1q-depleted serum by adding purified C1q. Chondroitin Sulfates 80-82 complement C1q A chain Homo sapiens 0-3 18503629-7 2008 C1q was identified as the recognition molecule, as it bound directly to CS, and CS-triggered complement activation could be restored in C1q-depleted serum by adding purified C1q. Chondroitin Sulfates 80-82 complement C1q A chain Homo sapiens 136-139 18503629-7 2008 C1q was identified as the recognition molecule, as it bound directly to CS, and CS-triggered complement activation could be restored in C1q-depleted serum by adding purified C1q. Chondroitin Sulfates 80-82 complement C1q A chain Homo sapiens 136-139