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References

  • 1
    Sadler JE. Biochemistry and genetics of von Willebrand factor. Annu Rev Biochem 1998; 67: 395424.
  • 2
    Counts RB, Paskell SL, Elgee SK. Disulfide bonds and the quaternary structure of factor VIII/von Willebrand factor. J Clin Invest 1978; 62: 7029.
  • 3
    Furlan M. Von Willebrand factor: molecular size and functional activity. Ann Hematol 1996; 72: 3418.
  • 4
    Furlan M, Robles R, Lamie B. Partial purification and characterization of a protease from human plasma cleaving von Willebrand factor to fragments produced by in vivo proteolysis. Blood 1996; 87: 422334.
  • 5
    Tsai HM. Physiologic cleavage of von Willebrand factor by a plasma protease is dependent on its conformation and requires calcium ion. Blood 1996; 87: 423544.
  • 6
    Dong JF, Moake JL, Nolasco L, Bernardo A, Arceneaux W, Shrimpton CN, Schade AJ, McIntire LV, Fujikawa K, Lopez JA. ADAMTS-13 rapidly cleaves newly secreted ultralarge von Willebrand factor multimers on the endothelial surface under flowing conditions. Blood 2002; 100: 40339.
  • 7
    Moake JL, Rudy CK, Troll JH, Weinstein MJ, Colannino NM, Azocar J, Seder RH, Hong SL, Deykin D. Unusually large plasma factor VIII:von Willebrand factor multimers in chronic relapsing thrombotic thrombocytopenic purpura. N Engl J Med 1982; 307: 14325.
  • 8
    Levy GG, Nichols WC, Lian EC, Foroud T, McClintick JN, McGee BM, Yang AY, Siemieniak DR, Stark KR, Gruppo R, Sarode R, Shurin SB, Chandrasekaran V, Stabler SP, Sabio H, Bouhassira EE, Upshaw Jr JD, Ginsburg D, Tsai HM. Mutations in a member of the ADAMTS gene family cause thrombotic thrombocytopenic purpura. Nature 2001; 413: 48894.
  • 9
    Furlan M, Robles R, Galbusera M, Remuzzi G, Kyrle PA, Brenner B, Krause M, Scharrer I, Aumann V, Mittler U, Solenthaler M, Lammle B. von Willebrand factor-cleaving protease in thrombotic thrombocytopenic purpura and the hemolytic-uremic syndrome. N Engl J Med 1998; 339: 157884.
  • 10
    Tsai HM, Lian EC. Antibodies to von Willebrand factor-cleaving protease in acute thrombotic thrombocytopenic purpura. N Engl J Med 1998; 339: 158594.
  • 11
    Banno F, Kokame K, Okuda T, Honda S, Miyata S, Kato H, Tomiyama Y, Miyata T. Complete deficiency in ADAMTS13 is prothrombotic, but it alone is not sufficient to cause thrombotic thrombocytopenic purpura. Blood 2006; 107: 31616.
  • 12
    George JN. The role of ADAMTS13 in the pathogenesis of thrombotic thrombocytopenic purpura-hemolytic uremic syndrome. Clin Adv Hematol Oncol 2005; 3: 62732.
  • 13
    Feughelman M. Mechanical Properties and Structure of Alpha-Keratin Fibres. Sydney: UNSW Press, 1997.
  • 14
    Hans-Dietrich W, Rebenfield L, Dansizer C. Kinetics and temperature dependence of the chemical stress relaxation of wool fibres. Text Res J 1966; 36: 53542.
  • 15
    Pimanda JE, Annis DS, Raftery M, Mosher DF, Chesterman CN, Hogg PJ. Willebrand factor-reducing activity of thrombospondin-1 is located in the calcium-binding/C-terminal sequence and requires a free thiol at position 974. Blood 2002; 100: 28328.
  • 16
    Xie L, Chesterman CN, Hogg PJ. Control of von Willebrand factor multimer size by thrombospondin-1. J Exp Med 2001; 193: 13419.
  • 17
    Dong Z, Thoma RS, Crimmins DL, McCourt DW, Tuley EA, Sadler JE. Disulfide bonds required to assemble functional von Willebrand factor multimers. J Biol Chem 1994; 269: 67538.