H
H. Pannekoek
Researcher at University of Amsterdam
Publications - 12
Citations - 336
H. Pannekoek is an academic researcher from University of Amsterdam. The author has contributed to research in topics: Plasminogen activator inhibitor-1 & Plasminogen activator. The author has an hindex of 7, co-authored 12 publications receiving 334 citations. Previous affiliations of H. Pannekoek include Queen's University.
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Journal Article
Novel low-molecular-weight inhibitor of PAI-1 (XR5118) promotes endogenous fibrinolysis and reduces postthrombolysis thrombus growth in rabbits
Philip W. Friederich,M.M. Levi,B. J. Biemond,P. Charlton,D. Templeton,A.J. van Zonneveld,P. Bevan,H. Pannekoek,J W ten Cate +8 more
TL;DR: In this article, a non-antibody, non-peptide, diketopiperazine-based inhibitor of PAI-1, XR5118, was tested in an experimental thrombosis model in rabbits.
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A Steady-state Template Model That Describes the Kinetics of Fibrin-stimulated [Glu1]- and [Lys78]Plasminogen Activation by Native tissue-type Plasminogen Activator and Variants That Lack Either the Finger or Kringle-2 Domain
TL;DR: The model indicates that catalytic efficiency is determined by the stability of the ternary activator-fibrin-plasminogen complex rather than the binding of the activator or plasminogens to fibrin, which implies that efforts to improve the enzymatic properties of t-PA might be more fruitfully directed at enhancing the Stability of the Ternary Complex rather than fibrIn binding.
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The Suicide Substrate Reaction Between Plasminogen Activator Inhibitor 1 and Thrombin Is Regulated by the Cofactors Vitronectin and Heparin
M van Meijer,A.E. Smilde,A.E. Smilde,G. Tans,G. Tans,Michael E. Nesheim,Michael E. Nesheim,H. Pannekoek,H. Pannekoek,Anton J. G. Horrevoets,Anton J. G. Horrevoets +10 more
TL;DR: Results show that physiological cofactors are able to switch a protease-serpin inhibition reaction to a substrate reaction, depending on the local concentrations of each of the components.
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Identification of functional interaction sites on proteins using bacteriophage-displayed random epitope libraries.
TL;DR: A phage-display-based method to identify epitopes or interaction sites on proteins, such as viral genomes or complete cDNA libraries, which may also be applied to more complex systems than single-protein genes.
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Thrombin-variable region 1 (VR1). Evidence for the dominant contribution of VR1 of serine proteases to their interaction with plasminogen activator inhibitor 1.
TL;DR: The results demonstrate the importance and specificity of the protease domain VR1 region for the interaction of PAI-1 with its target proteases.