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Daniel J. D. Johnson
Researcher at University of Cambridge
Publications - 14
Citations - 1338
Daniel J. D. Johnson is an academic researcher from University of Cambridge. The author has contributed to research in topics: Thrombin & Serpin. The author has an hindex of 14, co-authored 14 publications receiving 1257 citations.
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Structure of the antithrombin–thrombin–heparin ternary complex reveals the antithrombotic mechanism of heparin
TL;DR: A notably close contact interface, comprised of extensive active site and exosite interactions, explains, in molecular detail, the basis of the antithrombotic properties of therapeutic heparin.
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Crystal structure of a stable dimer reveals the molecular basis of serpin polymerization
TL;DR: The crystallographic structure of a stable serpin dimer is reported which reveals a domain swap of more than 50 residues, including two long antiparallel β-strands inserting in the centre of the principal β-sheet of the neighbouring monomer.
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Antithrombin–S195A factor Xa-heparin structure reveals the allosteric mechanism of antithrombin activation
TL;DR: The crystallographic structure of the recognition (Michaelis) complex between heparin‐activated AT and S195A fXa is presented, revealing the extensive exosite contacts that confer specificity and explains the molecular basis of protease recognition by AT and the mechanism of action of the important therapeutic low‐molecular‐weight heparins.
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NMR resonance assignments of thrombin reveal the conformational and dynamic effects of ligation
TL;DR: Investigation of the conformational and dynamic effects of thrombin ligation at the active site, exosite I and the Na+-binding site in solution, using modern multidimensional NMR techniques reveal that apo throm bin exists in a highly dynamic zymogen-like state, and relies on ligation to achieve a fully active conformation.
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Molecular basis of factor IXa recognition by heparin-activated antithrombin revealed by a 1.7-Å structure of the ternary complex
TL;DR: The structure reveals why the heparin-induced conformational change in AT is required to permit simultaneous active-site and exosite interactions with fIXa and the nature of these interactions.