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Crystal structures of the FXIa catalytic domain in complex with ecotin mutants reveal substrate-like interactionsMolecular cloning and expression of mouse and human cDNAs encoding heparan sulfate D-glucosaminyl 3-O-sulfotransferaseStructural and mutational analyses of the molecular interactions between the catalytic domain of factor XIa and the Kunitz protease inhibitor domain of protease nexin 2Purification of heparan sulfate D-glucosaminyl 3-O-sulfotransferaseA peptide found by phage display discriminates a specific structure of a trisaccharide in heparin.Identification of factor Xa residues critical for interaction with protein Z-dependent protease inhibitor: both active site and exosite interactions are required for inhibition.Acquired antithrombin deficiency in sepsis.Continuing education course #2: current understanding of hemostasis.High-resolution probing heparan sulfate-antithrombin interaction on a single endothelial cell surface: single-molecule AFM studies.Heparin binding preference and structures in the fibroblast growth factor family parallel their evolutionary diversification.Fast-degrading elastomer enables rapid remodeling of a cell-free synthetic graft into a neoartery.P1 and P2' site mutations convert protease nexin-2 from a factor XIa inhibitor to a plasmin inhibitorAntithrombin is protective against myocardial ischemia and reperfusion injury.Apixaban for the prevention of stroke in atrial fibrillation.Micelle-like nanoassemblies based on polymer-drug conjugates as an emerging platform for drug delivery.Properties of bovine factor IX (Christmas factor).Improved blood compatibility by sustained release of heparin-deoxycholic acid conjugates in a PCL-PEG multiblock copolymer matrix.Physicochemical aspects of heparin cofactor II.Anticoagulant activities of heparin and fragments.Role of endothelial cell surface heparin-like polysaccharides.A simple two-step isolation procedure for human and bovine antithrombin II/III (heparin cofactor): a comparison of two methods.Statistical analysis of low molecular mass heparin nanoencapsulation.Relationship between anticoagulant activity of heparin and susceptibility to periodate oxidation.Partial activation of antithrombin without heparin through deletion of a unique sequence on the reactive site loop of the serpin.SERPIN regulation of factor XIa. The novel observation that protease nexin 1 in the presence of heparin is a more potent inhibitor of factor XIa than C1 inhibitor.Overexpression of recombinant human antithrombin III in Chinese hamster ovary cells results in malformation and decreased secretion of recombinant protein.The production of an inactive form of antithrombin through limited proteolysis by thrombin.Anticoagulant activity of heparin: separation of high-activity and low-activity heparin species by affinity chromatography on immobilized antithrombin.In vitro analysis of polyurethane foam as a topical hemostatic agent.Anticoagulant activity of immobilized heparin on the polypropylene nonwoven fabric surface depending upon the pH of processing environment.Thrombin-Responsive Transcutaneous Patch for Auto-Anticoagulant Regulation.Establishing the dose-dependent daily variations of a low molecular weight heparin (Fraxiparine) through a population approach analysis in the rat.Calcium enhances heparin catalysis of the antithrombin-factor Xa reaction by a template mechanism. Evidence that calcium alleviates Gla domain antagonism of heparin binding to factor Xa.A luminescent and colorimetric probe based on the functionalization of gold nanoparticles by ruthenium(ii) complexes for heparin detection.Expression and functional characterization of two natural heparin-binding site variants of antithrombin.Location of two of the introns in the antithrombin-III gene.Protein adsorption and platelet adhesion onto ion-containing polyurethanes.Purification and characterization of guinea pig antithrombin III.
P2860
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P2860
description
article publié dans la revue scientifique Nature
@fr
scientific article published in Nature
@en
wetenschappelijk artikel
@nl
наукова стаття, опублікована в Nature в грудні 1973
@uk
name
Anticoagulant Action of Heparin
@en
Anticoagulant Action of Heparin
@nl
type
label
Anticoagulant Action of Heparin
@en
Anticoagulant Action of Heparin
@nl
prefLabel
Anticoagulant Action of Heparin
@en
Anticoagulant Action of Heparin
@nl
P2093
P356
P1433
P1476
Anticoagulant action of heparin
@en
P2093
P2888
P304
P356
10.1038/246355A0
P407
P577
1973-12-01T00:00:00Z
P6179
1041572042