Steven T. Olson
University of Illinois at Chicago
97 Papers
1.5K Citations
Steven T. Olson is an academic researcher from University of Illinois at Chicago. The author has contributed to research in topics: Serpin & Antithrombin. The author has an hindex of 39, co-authored 95 publications.
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Papers
Mechanism of Heparin Activation of Antithrombin ROLE OF INDIVIDUAL RESIDUES OF THE PENTASACCHARIDE ACTIVATING SEQUENCE IN THE RECOGNITION OF NATIVE AND ACTIVATED STATES OF ANTITHROMBIN
TL;DR: It is demonstrated that the nonreducing-end residues of the pentasaccharide function both to recognize the native low-heparin-affinity conformation of antithrombin and to induce and stabilize the activated high- heparin -affinity Conformation.
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Molecular mechanisms of antithrombin-heparin regulation of blood clotting proteinases. a paradigm for understanding proteinase regulation by serpin family protein proteinase inhibitors
TL;DR: Antithrombin has thus evolved a sophisticated means of regulating the activity of blood clotting proteinases in a time and location-dependent manner that exploits the multiple conformational states of the serpin and their differential stabilization by glycosaminoglycan cofactors.
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Heparin enhances the specificity of antithrombin for thrombin and factor Xa independent of the reactive center loop sequence. Evidence for an exosite determinant of factor Xa specificity in heparin-activated antithrombin.
TL;DR: The results suggest that the specificity of both native and heparin-activated antithrombin for thrombin and factor Xa is only weakly dependent on the P6–P3′ residues flanking the primary P1–P1′ recognition site in the serpin-reactive center loop.
166
Accelerating ability of synthetic oligosaccharides on antithrombin inhibition of proteinases of the clotting and fibrinolytic systems Comparison with heparin and low-molecular-weight heparin
Steven T. Olson,Richard Swanson,Elke Raub-Segall,Tina Bedsted,Morvardi Sadri,Maurice Petitou,Jean-Pascal Herault,Jean-Marc Herbert,Ingemar Björk +8 more
TL;DR: The proteinase targets of heparin derivatives currently used in or considered for thrombosis therapy are established and new insights are given into the mechanism ofheparin acceleration of antithrombin inhibition of proteinases.
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Partitioning of Serpin-Proteinase Reactions between Stable Inhibition and Substrate Cleavage Is Regulated by the Rate of Serpin Reactive Center Loop Insertion into β-Sheet A
Daniel A. Lawrence,Steven T. Olson,Shabazz Muhammad,Duane E. Day,Jan-Olov Kvassman,David Ginsburg,Joseph D. Shore +6 more
TL;DR: The present study demonstrates that partitioning between inhibitor and substrate modes of reaction can be altered by varying either the rates of RCL insertion or deacylation using a library of serpin RCL mutants substituted in the critical P14 hinge residue and three different proteinases.
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