Davie, E.W. and Ratnoff, O.D.

Waterfall sequence for intrinsic blood clotting.
Science 1964 Sept. 18; 145: 1310-1312.
PubMed citation number: 14173416.

Macfarlane, R.G.

An enzyme cascade in the blood clotting mechanism, and its function as a biochemical amplifier.
Nature 1964 May 2; 202: 498-499.
PubMed citation number: 14167839.
Description: The above investigators independently uncovered the fundamental basis of the coagulation cascade, and while several minor points have changed, their models hold true 40 years later.

Østerud, B. and Rapaport, S.

Activation of factor IX by the reaction product of tissue factor and factor VII. Proceedings of the National Academy of Sciences of the United States of America 1977 Dec; 74, 5260-5264.
Description: This was one of the the first demonstrations that factor IX is activated by the extrinsic pathway complex, tissue factor and factor VII. This mode of Factor IX activation proved to be clinically relevant and helps explain the bleeding diathesis of patients with Hemophilia A and B.
PubMed citation number: 271951.

Gailani, D. and Broze, G.J.

Factor XI activation in a revised model of blood coagulation.
Science 1991 Aug 23; 253(5022): 909-912.
Description: This was one of the first studies to show that factor XI can be activated by thrombin more efficiently than by factor XII, partly explaining why patients with Factor XII deficiencies do not have a propensity to bleed.
PubMed citation number: 1652157.

Hoffman, M., Monroe, D.M., Oliver, J.A., and Roberts, H.R.

Factors IXa and Xa play distinct roles in tissue factor-dependent initiation of coagulation. Blood 1995 Sep 1; 86(5): 1794-1801.
Description: The above study implements a physiologically-relevant in vitro model of coagulation to demonstrate the importance of the platelet surface in coagulation and to dissect the distinct roles that Factor IX and X play in the generation of the thrombin burst.
PubMed citation number: 7655009.

Bennett, J.S. and Vilaire, G.

Exposure of platelet fibrinogen receptors by ADP and epinephrine.
J Clin Invest. 1979 Nov; 64(5): 1393-1401.
Description: This was one of the first studies to demonstrate that platelet agonists mediate platelet aggregation largely through the activation or exposure of fibrinogen receptors on the surface of platelets.
PubMed citation number: 574143.

Bennett, J.S., Hoxie, J.A., Leitman, S.F., Leitman, S.F., Vilaire, G., and Cines, D.B.

Inhibition of fibrinogen binding to stimulated human platelets by a monoclonal antibody. Proc Natl Acad Sci USA. 1983 May; 80(9): 2417-2421.
Description: Employing a monoclonal antibody that inhibits platelet aggregation, these investigators demonstrated that the fibrinogen receptor on platelets is the integrin, alpha IIb-IIIa. Their use of a monoclonal antibody that inhibits platelet aggregation by neutralizing platelet IIb-IIIa would later be applied to clinical settings such as percutaneous coronary interventions.
PubMed citation number: 6302680.

Sakariassen, K.S., Bolhuis, P.A., and Sixma, J.J.

Human blood platelet adhesion to artery subendothelium is mediated by factor VIII-Von Willebrand factor bound to the subendothelium.
Nature. 1979 Jun 14; 279(5714): 636-8.
Description: This is one of the earliest studies that demonstrated the important role of von Willebrand factor in mediating platelet adhesion to artery subendothelium.
PubMed citation number: 313016

Savage, B., Saldivar, E., and Ruggeri, Z.M.

Initiation of platelet adhesion by arrest onto fibrinogen or translocation on von Willebrand factor.
Cell. 1996 Jan 26; 84(2):289-97.
Description: These investigators further characterized the kinetics of platelet IIb-IIIa binding to immobilized fibrinogen and glycoprotein Ib binding to von Willebrand factor under physiologically-relevant flow conditions, thus better dissecting the relative roles of the above interactions in mediating arterial thrombosis.
PubMed citation number: 8565074

Dong, J.F., Moake, J.L., Nolasco, L., Bernardo, A., Arceneaux, W., Shrimpton, C.N., Schade, A.J., McIntire, L.V., Fujikawa, K., and Lopez, J.A.

ADAMTS-13 rapidly cleaves newly secreted ultralarge von Willebrand factor multimers on the endothelial surface under flowing conditions.
Blood. 2002 Dec 1; 100(12): 4033-9.
Description: This study provided direct evidence that the protease, ADAMTS-13, is responsible for the rapid cleavage of ultralarge von Willebrand factor multimers on the endothelial surface under flow conditions, which in part explains the clinical phenotypes of familial and acquired TTP, diseases characterized by an inherited deficiency of or acquired inhibitor to ADAMTS-13.
PubMed citation number: 12393397

Weiss, H.J., Sussman, I.I., and Hoyer, L.W.

Stabilization of factor VIII in plasma by the von Willebrand factor. Studies on posttransfusion and dissociated factor VIII and in patients with von Willebrand's disease. J Clin Invest. 1977 Aug; 60(2): 390-404.
Description: This was the first evidence in humans that von Willebrand factor stabilizes Factor VIII in plasma, thus explaining the low levels of Factor VIII seen in von Willebrand’s disease.
PubMed citation number: 17621

Select review articles

Ruggeri, Z.M.

Von Willebrand factor, platelets and endothelial cell interactions.
J Thromb Haemost. 2003 Jul;1(7):1335-42.
PubMed citation number: 12871266.

Davie EW.

A brief historical review of the waterfall/cascade of blood coagulation.
J Biol Chem. 2003 Dec 19;278(51):50819-32.
Epub 2003 Oct 21.
PubMed citation number: 14570883.

Edelberg JM, Christie PD, Rosenberg RD.

Regulation of vascular bed-specific prothrombotic potential.
Circ Res. 2001 Jul 20;89(2):117-24.
PubMed citation number: 11463717.

Dahlback B.

The protein C anticoagulant system: inherited defects as basis for venous thrombosis.
Thromb Res. 1995 Jan 1;77(1):1-43.
PubMed citation number: 7701473.

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