PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 15606553-2 2005 Native or mutant VWF-A1-domains were transiently overexpressed on COS-7 cells as membrane glycosylphosphatidylinositol (GPI)-anchored FLAG-tagged fusion proteins. carbonyl sulfide 66-69 von Willebrand factor Homo sapiens 17-20 19624459-6 2009 The effect of the R924Q substitution on the biosynthesis and intracellular trafficking of VWF was explored by in vitro expression studies in COS-7 and AtT-20 cells. carbonyl sulfide 141-144 von Willebrand factor Homo sapiens 90-93 18637125-5 2008 In vitro mutagenesis and expression in COS-7 cells confirmed the impairment of the mutant in botrocetin- and ristocetin-mediated VWF binding to GPIb. carbonyl sulfide 39-42 von Willebrand factor Homo sapiens 129-132 16676067-8 2006 The mutated recombinant (r)VWF-D2801, the hybrid rVWF-A/D2801 and the mutated C-terminal VWF fragment rSPII-D2801 were expressed in COS-7 cells. carbonyl sulfide 132-135 von Willebrand factor Homo sapiens 27-30 12353070-5 2002 Expression in vitro of the mutation demonstrated that 1156M-VWF is secreted from COS-7 cells in a much reduced amount and lacking large multimers. carbonyl sulfide 81-84 von Willebrand factor Homo sapiens 60-63 15461624-4 2004 Expression studies in Cos-7 cells showed that these abnormalities, which implicate cysteine residues, induced secretion, multimerization and FVIII binding defects of corresponding recombinant VWF. carbonyl sulfide 22-25 von Willebrand factor Homo sapiens 192-195 15219197-3 2004 This substitution, which was not found in 55 unrelated normal individuals, was reproduced by in vitro site directed mutagenesis of a full-length VWF cDNA and was subsequently expressed in COS-7 cells. carbonyl sulfide 188-191 von Willebrand factor Homo sapiens 145-148 15219197-4 2004 The corresponding recombinant mutant VWF protein was partially retained in COS-7 cells yet the full spectrum of multimers was observed, suggesting that the absence of the highest molecular weight multimers results from increased proteolysis. carbonyl sulfide 75-78 von Willebrand factor Homo sapiens 37-40 12588349-4 2003 Using site-directed mutagenesis and transient expression in COS-7 cells, we showed that both mutations, although located in the D3 domain of VWF, outside the tryptic fragment containing the FVIII domain, dramatically decrease the binding of VWF to FVIII. carbonyl sulfide 60-63 von Willebrand factor Homo sapiens 141-144 12588349-4 2003 Using site-directed mutagenesis and transient expression in COS-7 cells, we showed that both mutations, although located in the D3 domain of VWF, outside the tryptic fragment containing the FVIII domain, dramatically decrease the binding of VWF to FVIII. carbonyl sulfide 60-63 von Willebrand factor Homo sapiens 241-244 8639896-3 1996 The structure of recombinant Arg834Gln vWF within transfected COS-7 cells and the secretion of HMW multimers were similar to wild type vWF. carbonyl sulfide 62-65 von Willebrand factor Homo sapiens 39-42 11019957-5 2000 This substitution was reproduced by in vitro site directed mutagenesis of full-length VWF cDNA and transiently expressed in COS-7 cells. carbonyl sulfide 124-127 von Willebrand factor Homo sapiens 86-89 10887119-5 2000 Recombinant VWF having the R273W mutation was expressed in COS-7 cells. carbonyl sulfide 59-62 von Willebrand factor Homo sapiens 12-15 9845532-5 1998 Recombinant vWF (rvWF) containing the candidate (Asn116) missense mutation was expressed in COS-7 cells. carbonyl sulfide 92-95 von Willebrand factor Homo sapiens 12-15 9129031-5 1997 Recombinant vWF (rvWF) containing the candidate mutation was transiently expressed in COS-7 cells. carbonyl sulfide 86-89 von Willebrand factor Homo sapiens 12-15 2251280-6 1990 The functional specificity of PACE for mediating propeptide cleavage at paired basic amino acid residues was demonstrated by the enhancement of propeptide processing of human von Willebrand factor when coexpressed with PACE in COS-1 cells. carbonyl sulfide 227-230 von Willebrand factor Homo sapiens 175-196 8123843-3 1994 We reproduced this mutation in vWF cDNA and expressed the recombinant protein in Cos-7 cells. carbonyl sulfide 81-84 von Willebrand factor Homo sapiens 31-34 8352730-1 1993 Transcriptional regulation of the human von Willebrand factor (vWF) gene was investigated in calf pulmonary artery endothelial (CPAE), HeLa, COS 7 and Hep G2 cells. carbonyl sulfide 141-144 von Willebrand factor Homo sapiens 40-61 8352730-1 1993 Transcriptional regulation of the human von Willebrand factor (vWF) gene was investigated in calf pulmonary artery endothelial (CPAE), HeLa, COS 7 and Hep G2 cells. carbonyl sulfide 141-144 von Willebrand factor Homo sapiens 63-66 1571548-2 1992 By coexpression of vWF and various propeptide processing enzymes in COS-1 cells, we here demonstrate that vWF is preferentially processed by the paired dibasic amino acid-cleaving enzyme PACE (furin). carbonyl sulfide 68-71 von Willebrand factor Homo sapiens 19-22 1571548-2 1992 By coexpression of vWF and various propeptide processing enzymes in COS-1 cells, we here demonstrate that vWF is preferentially processed by the paired dibasic amino acid-cleaving enzyme PACE (furin). carbonyl sulfide 68-71 von Willebrand factor Homo sapiens 106-109 8500791-7 1993 Recombinant vWF containing the observed amino acid substitution was expressed in COS-1 cells. carbonyl sulfide 81-84 von Willebrand factor Homo sapiens 12-15 1557393-5 1992 Recombinant vWF containing the vWF R543W mutation expressed in COS-7 cells also demonstrated increased binding of large vWF multimers. carbonyl sulfide 63-66 von Willebrand factor Homo sapiens 12-15 1557393-5 1992 Recombinant vWF containing the vWF R543W mutation expressed in COS-7 cells also demonstrated increased binding of large vWF multimers. carbonyl sulfide 63-66 von Willebrand factor Homo sapiens 31-34 1557393-5 1992 Recombinant vWF containing the vWF R543W mutation expressed in COS-7 cells also demonstrated increased binding of large vWF multimers. carbonyl sulfide 63-66 von Willebrand factor Homo sapiens 31-34 1537829-4 1992 In COS-7 cells, 3 single amino acid substitutions, Val844----Asp, Ser743----Leu, and Gly742----Arg, impaired the transport of vWF multimers between the endoplasmic reticulum and the Golgi complex, with more profound effects on the secretion of HMW multimers than lower molecular weight forms. carbonyl sulfide 3-6 von Willebrand factor Homo sapiens 126-129 1537829-6 1992 The vWF structure observed within patient platelets correlated closely with the synthesis pattern seen for the corresponding mutants in COS-7 cells. carbonyl sulfide 136-139 von Willebrand factor Homo sapiens 4-7 3131331-3 1988 Evidence is presented showing that proteolytic processing of pro-vWF by COS-1 cells occurs at the peptide bond between arginine and serine in the sequence Lys762-Arg763-Ser764, identical to endothelial cell-associated proteolysis. carbonyl sulfide 72-75 von Willebrand factor Homo sapiens 65-68