PMID-sentid Pub_year Sent_text comp_official_name comp_offset protein_name organism prot_offset 18981290-0 2009 N-Glycans of ADAMTS13 modulate its secretion and von Willebrand factor cleaving activity. n-glycans 0-9 A disintegrin and metalloproteinase with thrombospondin motifs 13 Cricetulus griseus 13-21 18981290-2 2009 ADAMTS13 contains 10 putative N-glycosylation sites in or near its metalloprotease sequence, spacer region, thrombospondin type 1 repeat no. Nitrogen 30-31 A disintegrin and metalloproteinase with thrombospondin motifs 13 Cricetulus griseus 0-8 18981290-7 2009 However, ADAMTS13 with oligomannose N-glycans cleaved its substrate, von Willebrand factor (VWF) multimers, less effectively, with a higher K(m) but similar k(cat) value. oligomannose n-glycans 23-45 A disintegrin and metalloproteinase with thrombospondin motifs 13 Cricetulus griseus 9-17 18981290-5 2009 Tunicamycin treatment markedly decreased the secretion of ADAMTS13 into the culture medium of transfected cells. Tunicamycin 0-11 A disintegrin and metalloproteinase with thrombospondin motifs 13 Cricetulus griseus 58-66 18981290-9 2009 Enzymatic removal of N-glycans from ADAMTS13 did not affect its VWF cleaving activity. n-glycans 21-30 A disintegrin and metalloproteinase with thrombospondin motifs 13 Cricetulus griseus 36-44 18981290-10 2009 Thus, N-glycosylation is necessary for efficient secretion of ADAMTS13, while conversion of the N-glycans from oligomannose to complex type in the Golgi complex enhances the proteolytic activity of the protease toward VWF multimers. Nitrogen 6-7 A disintegrin and metalloproteinase with thrombospondin motifs 13 Cricetulus griseus 62-70