New insights into the regulation of the blood clotting cascade derived from the X-ray crystal structure of bovine meizothrombin des F1 in complex with PPACK (Q27748810)

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English	New insights into the regulation of the blood clotting cascade derived from the X-ray crystal structure of bovine meizothrombin des F1 in complex with PPACK	scientific article

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scholarly article

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New insights into the regulation of the blood clotting cascade derived from the X-ray crystal structure of bovine meizothrombin des F1 in complex with PPACK (English)

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crystal structure

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X-ray crystallography

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author name string

P D Martin

1

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M G Malkowski

2

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J Box

3

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C T Esmon

4

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B F Edwards

5

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publication date

15 December 1997

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5

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1681-93

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12

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Characterization of the complementary deoxyribonucleic acid and gene coding for human prothrombin

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The coagulation cascade: initiation, maintenance, and regulation

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The role of factor V in the assembly of the prothrombinase complex

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Changes in membrane phospholipid distribution during platelet activation

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Structural comparisons of meizothrombin and its precursor prothrombin in the presence or absence of procoagulant membranes

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Meizothrombin: active intermediate formed during prothrombinase-catalyzed activation of prothrombin

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Functional characterization of recombinant human meizothrombin and Meizothrombin(desF1). Thrombomodulin-dependent activation of protein C and thrombin-activatable fibrinolysis inhibitor (TAFI), platelet aggregation, antithrombin-III inhibition

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Comparison of the active-site conformations of bovine alpha-thrombin and meizothrombin(desF1) by electron spin resonance

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Evolution of the proteases of blood coagulation and fibrinolysis by assembly from modules

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Structures of the noncovalent complexes of human and bovine prothrombin fragment 2 with human PPACK-thrombin

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Crystallographic evidence that the F2 kringle catalytic domain linker of prothrombin does not cover the fibrinogen recognition exosite.

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Three-dimensional structure of the kringle sequence: structure of prothrombin fragment 1.

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Phosphatidylserine-containing membranes alter the thermal stability of prothrombin's catalytic domain: a differential scanning calorimetric study.

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Soluble Phospholipids Enhance Factor Xa-Catalyzed Prothrombin Activation in Solution†

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Refined structure of the hirudin-thrombin complex

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Crystallographic structures of thrombin complexed with thrombin receptor peptides: existence of expected and novel binding modes

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10.1016/S0969-2126(97)00314-6

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