Malou Philips
University of Copenhagen
11 Papers
150 Citations
Malou Philips is an academic researcher from University of Copenhagen. The author has contributed to research in topics: Plasminogen activator & Plasminogen activator inhibitor-1. The author has an hindex of 8, co-authored 11 publications.
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Papers
Kinetics of inhibition of tissue-type and urokinase-type plasminogen activator by plasminogen-activator inhibitor type 1 and type 2
TL;DR: The kinetics of inhibition of plasminogen activator suggested that t-PA in blood consists mainly in its single-chain form, suggesting that the C-terminal proteinase part of u-PA (B chain) is responsible for both the primary and the secondary interactions with PAI-1 andPAI-2.
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Immunological relationship between the fast-acting plasminogen activator inhibitors from plasma, blood platelets and endothelial cells demonstrated with a monoclonal antibody against an inhibitor from placenta.
TL;DR: Two plasminogen activator inhibitors (I and II) were demonstrated in human placenta and one antibody (F37), which reacted with both free and complex-bound inhibitor I, indicating that these inhibitors and inhibitor I share a common epitope.
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Plasminogen activator inhibitor-1 is the primary inhibitor of tissue-type plasminogen activator in pregnancy plasma.
TL;DR: It was demonstrated that a monoclonal antibody against PAI-1 almost completely quenched inhibition of single-chain t-PA and most of the inhibition of two- Chain plasminogen activator (t-PA) in plasma during the third trimester of pregnancy.
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A specific immunologic assay for functional plasminogen activator inhibitor 1 in plasma--standardized measurements of the inhibitor and related parameters in patients with venous thromboembolic disease.
TL;DR: It was found that the patients had a decreased fibrinolytic capacity and this could be ascribed to high plasma levels of PAI-1, and no significant difference could be demonstrated between the patients with a thrombotic tendency and the normal subjects.
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Characterization and structural impact of five novel PROS1 mutations in eleven protein S-deficient families.
Bente Damm Andersen,Marie Luise Bisgaard,Bent Lind,Malou Philips,Bruno O. Villoutreix,Sixtus Thorsen +5 more
TL;DR: The mutations reported here are most likely the cause of the protein S deficiency and are compatible with defective protein folding/unstable molecules, impaired secretion and intracellular degradation of mutated protein, which appear to be the major molecular disease mechanisms for missense mutations and certain other mutations found in genetic disorders.
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