Tischer A, Brehm M, Machha V, Moon-Tasson L, Benson L, Nelton K, Leger R, Obser T, Martinez-Vargas M, Whitten S, Chen D, Pruthi R, Bergen H, Cruz M, Schneppenheim R, Auton M. Evidence for the misfolding of the a1 domain within multimeric von willebrand factor in type 2 von willebrand disease. J Mol Biol. 2020;432(2):305–23.

Article  CAS  PubMed  Google Scholar 

T MacArthur, J Goswami, L Moon Tasson, A Tischer, K Bailey, G Spears, J Dong, M Auton, R Kozar, M Park. Quantification of von willebrand factor and adamts-13 after traumatic injury: a pilot study. Trauma Surg Acute Care Open. 2021; 6(1): e000703.

Goodall A, Jarvis J, Chand S, Rawlings E, O’Brien D, McGraw A, Hutton R, Tuddenham E. An immunoradiometric assay for human factor VIII /von willebrand factor (VIII:VWF) using a monoclonal antibody that defines a functional epitope. Br J Haematol. 1985;59(4):565–77.

Article  CAS  PubMed  Google Scholar 

Murdock P, Woodhams B, Matthews K, Pasi K, Goodall A. von willebrand factor activity detected in a monoclonal antibody-based elisa: an alternative to the ristocetin cofactor platelet agglu-tination assay for diagnostic use. Thromb Haemost. 1997;78(4):1272–7.

Article  CAS  PubMed  Google Scholar 

Chand S, McCraw A, Hutton R, Tuddenham E, Goodall A. A two-site, monoclonal antibody-based immunoassay for von willebrand factor–demonstration that vwf function resides in a conforma-tional epitope. Thromb Haemost. 1986;55(3):318–24.

Article  CAS  PubMed  Google Scholar 

Chen D, Tange J, Meyers B, Pruthi R, Nichols W, Heit J. Validation of an automated la-tex particle-enhanced immunoturbidimetric von willebrand factor activity assay. J Thromb Haemost. 2011;9(10):1993–2002.

Article  CAS  PubMed  Google Scholar 

M. Trossa¨ert, C. Ternisien, A. Lefrancois, L. Llopis, J. Goudemand, M. Sigaud, M. Fouassier, C. Caron. Evaluation of an automated von willebrand factor activity assay in von willebrand disease. Clin Appl Thromb Hemost. 2011;17(6):E25–9.

Salem R, Van Cott E. A new automated screening assay for the diagnosis of von willebrand disease. Biochemistry. 2007;127(5):730–5.

Google Scholar 

Spiel A, Mayr F, Ladani N, Wagner P, Schaub R, Gilbert J, Jilma B. The aptamer arc1779 is a potent and specific inhibitor of von willebrand factor mediated ex vivo platelet function in acute myocardial infarction. Platelets. 2009;20(5):334–40.

Article  CAS  PubMed  Google Scholar 

F. Mayr, P. Kno¨bl, B. Jilma, J. Siller-Matula, P. Wagner, R. Schaub, J. Gilbert, and P. Jilma-Stohlawetz. The aptamer arc1779 blocks von willebrand factor-dependent platelet function in patients with throm-botic thrombocytopenic purpura ex vivo. Transfusion. 2010; 50(5): 1079–1087.

P. Jilma-Stohlawetz, J. Gilbert, M. Gorczyca, P. Kn¨obl, and B. Jilma, “A dose ranging phase i/ii trial of the von willebrand factor inhibiting aptamer arc1779 in patients with congenital thrombotic thrombocytopenic purpura. Thromb Haemost. 2011; 106(3): 539–547.

Kovacevic K, Greisenegger S, Langer A, Gelbenegger G, Buchtele N, Pabinger I, Petroczi K, Zhu S, Gilbert J, Jilma B. The aptamer bt200 blocks von willebrand factor and platelet function in blood of stroke patients. Sci Rep. 2021;11(1):3092.

Article  CAS  PubMed  PubMed Central  Google Scholar 

Tischer A, Moon-Tasson L, Auton M. Removal of the vicinal disulfide enhances the platelet capturing function of von willebrand factor. Blood. 2023;141(12):1469–73.

Article  CAS  PubMed  PubMed Central  Google Scholar 

J. Campbell, A. Tischer, V. Machha, L. Moon-Tasson, B. Sankaran, C. Kim, and M. Auton. Data on the purification and crystallization of the loss-of-function von willebrand disease variant (p.gly1324ser) of the von willebrand factor a1 domain. Data Brief. 2016; 7:1700–1706.

A. Tischer, V. Machha, J. R¨osgen, and M. Auton. ““cooperative collapse” of the denatured state revealed through clausius-clapeyron analysis of protein denaturation phase diagrams. Biopolymers. 2018; 109(8): e23106.

M. Auton, K. Sowa, S. Smith, E. Sedl´ak, K. Vijayan, and M. Cruz. Destabilization of the a1 domain in von willebrand factor dissociates the a1a2a3 tri-domain and provokes spontaneous binding to glycopro-tein ibalpha and platelet activation under shear stress. J Biol Chem. 2010; 285(30): 22831–22839.

Fu H, Jiang Y, Yang D, Scheiflinger F, Wong W, Springer T. Flow-induced elongation of von willebrand factor precedes tension-dependent activation. Nat Commun. 2017;8(1):324.

Article  PubMed  PubMed Central  Google Scholar 

Higgins R, Goodwin A. Automated assays for von willebrand factor activity. Am J Hematol. 2019;94(4):496–503.

Article  CAS  PubMed  Google Scholar 

I. Bod´o, J. Eikenboom, R. Montgomery, J. Patzke, R. Schneppenheim, J. Di Paola, W. f. S. o. t. S. von, S. C. of the International Society for Thrombosis, and Haemostasis. Platelet-dependent von willebrand factor activity. nomenclature and methodology: communication from the ssc of the isth. J Thromb Haemost. 2015; 13(7): 1345–1350.

K. Friedman, M. Bo¨hm-Weigert, N. DeSimone, D. Dietzen, C. Eby, C. Flickinger, W. Hoyer, M. Kahl, K. Kottke-Marchant, T. Ortel, J. Patzke, S. Pipe, M. Stuart, A. Timur, and R. Sarode. Evaluation of an automated von willebrand factor glycoprotein ibm activity assay compared with 3 alternative von willebrand factor activity assays. Res Pract Thromb Haemost. 2024; 8(4): 102422.

Giavarina D. Understanding bland altman analysis. Biochem Med (Zagreb). 2015;25(2):141–51.

Article  PubMed  Google Scholar 

M. Pin˜ol, M. Sales, M. Costa, A. Tosetto, M. Canciani, and A. Federici, “Evaluation of a new turbidi-metric assay for von willebrand factor activity useful in the general screening of von willebrand disease.,” Haematologica. 2007; 92(5): 712–713.

Tischer A, Campbell J, Machha V, Moon-Tasson L, Benson L, Sankaran B, Kim C, Auton M. Mutational constraints on local unfolding inhibit the rheological adaptation of von willebrand factor. J Biol Chem. 2016;291(8):3848–59.

Article  CAS  PubMed  Google Scholar 

Tischer A, Moon-Tasson L, Auton M. Structure resolved dynamics of type 2m von willebrand disease. J Thromb Haemost. 2025;S1538-7836(24):00775-X. https://doi.org/10.1016/j.jtha.2024.12.026.

Pace C, Vajdos F, Fee L, Grimsley G, Gray T. How to measure and predict the molar absorption coefficient of a protein. Biochemistry. 1995;4(11):2411–23.

CAS  Google Scholar