Maurice Petitou spends much of his time researching Heparin, Stereochemistry, Antithrombin, Biochemistry and Oligosaccharide. He combines subjects such as Anticoagulant, Structure–activity relationship, Pharmacology and Antithrombotic with his study of Heparin. Maurice Petitou has included themes like Iduronic acid, Sulfation and Tetrasaccharide in his Stereochemistry study.
His Antithrombin research is multidisciplinary, relying on both Total synthesis and Binding site. His study in the field of Proteases, Binding domain and Molecular model also crosses realms of Idraparinux. His work carried out in the field of Oligosaccharide brings together such families of science as Residue, Cleavage, Depolymerization and Thrombin.
Maurice Petitou mainly investigates Heparin, Stereochemistry, Antithrombin, Biochemistry and Thrombin. His Heparin research includes elements of Biological activity, Structure–activity relationship, Pharmacology and Antithrombotic. His Stereochemistry research integrates issues from Iduronic acid, Sulfation, Chemical synthesis and Residue.
His research in Antithrombin intersects with topics in Binding domain, Binding site, Anticoagulant, Factor Xa Inhibitor and Conformational change. The various areas that Maurice Petitou examines in his Biochemistry study include Molecule and Bioavailability. His Thrombin study combines topics from a wide range of disciplines, such as Coagulation and Ternary complex.
His primary scientific interests are in Biochemistry, Antithrombin, Heparin, Pharmacology and Oligosaccharide. His Biochemistry research is multidisciplinary, incorporating perspectives in Cancer and Stem cell. As a part of the same scientific family, Maurice Petitou mostly works in the field of Antithrombin, focusing on Factor Xa Inhibitor and, on occasion, Antithrombotic, Anesthesia and Antithrombins.
The Heparin study combines topics in areas such as Plasma protein binding and Anti hiv activity. His study ties his expertise on Stereochemistry together with the subject of Heparan sulfate. His Stereochemistry research includes themes of Glycoprotein and Glucosamine.
His scientific interests lie mostly in Heparin, Antithrombin, Factor Xa Inhibitor, Fondaparinux Sodium and Biochemistry. His Heparan sulfate study in the realm of Heparin interacts with subjects such as Population. The concepts of his Heparan sulfate study are interwoven with issues in Docking, Stereochemistry, Fibroblast growth factor, Random hexamer and Chemical synthesis.
His work deals with themes such as Pharmacokinetics, Virology, Potency, Subcutaneous injection and Biological activity, which intersect with Antithrombin. His Factor Xa Inhibitor research is multidisciplinary, incorporating elements of Discovery and development of direct thrombin inhibitors, Thrombin and Antithrombins. His study in the fields of Plasma protein binding, In vitro, Oligosaccharide and Structure–activity relationship under the domain of Biochemistry overlaps with other disciplines such as Molecular mimicry.
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Structure-activity relationship in heparin : a synthetic pentasaccharide with high affinity for antithrombin III and eliciting high anti-factor Xa activity
J. Choay;M. Petitou;J.C. Lormeau;P. Sinaÿ.
Biochemical and Biophysical Research Communications (1983)
The anticoagulant activation of antithrombin by heparin.
Lei Jin;Jan Pieter Abrahams;Jan Pieter Abrahams;Richard Skinner;Maurice Petitou.
Proceedings of the National Academy of Sciences of the United States of America (1997)
The Unique Antithrombin III Binding Domain of Heparin: A Lead to New Synthetic Antithrombotics
Constant A. A. van Boeckel;Maurice Petitou.
Angewandte Chemie (1993)
The structure of heparin oligosaccharide fragments with high anti-(factor Xa) activity containing the minimal antithrombin III-binding sequence. Chemical and 13C nuclear-magnetic-resonance studies.
B Casu;P Oreste;G Torri;G Zoppetti.
Biochemical Journal (1981)
Synthesis of thrombin-inhibiting heparin mimetics without side effects
Maurice Petitou;Jean-Pascal Hérault;André Bernat;Pierre-Alexandre Driguez.
Conformational flexibility: a new concept for explaining binding and biological properties of iduronic acid-containing glycosaminoglycans
B. Casu;M. Petitou;M. Provasoli;P. Sinaÿ.
Trends in Biochemical Sciences (1988)
Contribution of monosaccharide residues in heparin binding to antithrombin III.
Donald H. Atha;Jean Claude Lormeau;Maurice Petitou;Robert D. Rosenberg.
Total synthesis of a heparin pentasaccharide fragment having high affinity for antithrombin III
Pierre Sinaÿ;Jean-Claude Jacquinet;Maurice Petitou;Philippe Duchaussoy.
Carbohydrate Research (1984)
1976-1983, a critical period in the history of heparin: the discovery of the antithrombin binding site.
Maurice Petitou;Benito Casu;Ulf Lindahl.
Conformer populations of L-iduronic acid residues in glycosaminoglycan sequences.
Dino R. Ferro;Augusto Provasoli;Massimo Ragazzi;Benito Casu.
Carbohydrate Research (1990)
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