PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
7559469-8	1995	These data suggest that only the position 99 glycosylation site (Asn99-X-Thr101) in tHON is important in the reduction of binding of osteonectin to collagen V. Consistent with the binding data is the observation that both the N71Q and T73A mutant proteins migrate on SDS-polyacrylamide gel electrophoresis gels identically to wild-type tHON, suggesting that there is little or no N-glycosylation of residue 71 in wild-type osteonectin.	Nitrogen	87-88	secreted protein acidic and cysteine rich	Bos taurus	133-144	
7559469-8	1995	These data suggest that only the position 99 glycosylation site (Asn99-X-Thr101) in tHON is important in the reduction of binding of osteonectin to collagen V. Consistent with the binding data is the observation that both the N71Q and T73A mutant proteins migrate on SDS-polyacrylamide gel electrophoresis gels identically to wild-type tHON, suggesting that there is little or no N-glycosylation of residue 71 in wild-type osteonectin.	Nitrogen	87-88	secreted protein acidic and cysteine rich	Bos taurus	423-434	
7559469-0	1995	Role of N-linked glycosylation in human osteonectin.	Nitrogen	8-9	secreted protein acidic and cysteine rich	Bos taurus	40-51