Structural basis for the anticoagulant activity of the thrombin-thrombomodulin complex (Q27622194)

2

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R Huber

3

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R Pagila

4

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G Rumennik

5

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M Seto

6

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J Morser

7

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D R Light

8

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W Bode

The coagulation cascade: initiation, maintenance, and regulation

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language of work or name

English

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publication date

30 March 2000

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published in

Nature

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volume

404

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issue

6777

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page(s)

518-25

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cites work

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TAFI, or plasma procarboxypeptidase B, couples the coagulation and fibrinolytic cascades through the thrombin-thrombomodulin complex

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Conversion of thrombin into an anticoagulant by protein engineering

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Evidence for multiple conformational changes in the active center of thrombin induced by complex formation with thrombomodulin: an analysis employing nitroxide spin-labels

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Energetics of thrombin-thrombomodulin interaction.

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Molecular mechanisms of thrombin function

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Structure of a nonadecapeptide of the fifth EGF domain of thrombomodulin complexed with thrombin

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Thrombin interacts with thrombomodulin, protein C, and thrombin-activatable fibrinolysis inhibitor via specific and distinct domains

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Structure of the thrombin complex with triabin, a lipocalin-like exosite-binding inhibitor derived from a triatomine bug

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Solution structure of a pair of calcium-binding epidermal growth factor-like domains: implications for the Marfan syndrome and other genetic disorders

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Oxidation of a specific methionine in thrombomodulin by activated neutrophil products blocks cofactor activity. A potential rapid mechanism for modulation of coagulation

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The interaction of thrombomodulin with Ca2+

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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

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The ternary microplasmin-staphylokinase-microplasmin complex is a proteinase-cofactor-substrate complex in action

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Synthesis, activity, and preliminary structure of the fourth EGF-like domain of thrombomodulin

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The shape of thrombomodulin and interactions with thrombin as determined by electron microscopy.

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Identification of a region in protein C involved in thrombomodulin-stimulated activation by thrombin: potential repulsion at anion-binding site I in thrombin

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Epidermal growth factor-like modules

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Thrombomodulin as a model of molecular mechanisms that modulate protease specificity and function at the vessel surface

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7 January 2021

The 2.8 A crystal structure of Gla-domainless activated protein C

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7 January 2021

Mutation of protease domain residues Lys37-39 in human protein C inhibits activation by the thrombomodulin-thrombin complex without affecting activation by free thrombin

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7 January 2021

Amino acids 225-235** of the protein C serine-protease domain are important for the interaction with the thrombin-thrombomodulin complex

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7 January 2021