S. T. Olson

发表

Quantitative characterization of the thrombin-heparin interaction. Discrimination between specific and nonspecific binding models.

H. Halvorson, S. Olson, I. Björk, 1991, The Journal of biological chemistry.

Cathepsin B Controls the Persistence of Memory CD8+ T Lymphocytes

S. Olson, D. Davis, P. Ashton‐Rickardt, 2012, The Journal of Immunology.

Cooperative Interactions of Three Hotspot Heparin Binding Residues Are Critical for Allosteric Activation of Antithrombin by Heparin.

S. Olson, R. Swanson, G. Izaguirre, 2018, Biochemistry.

Identification of Serpin Determinants of Specificity and Selectivity for Furin Inhibition through Studies of α1PDX (α1-Protease Inhibitor Portland)-Serpin B8 and Furin Active-site Loop Chimeras*

G. Izaguirre, S. T. Olson, L. Qi, 2013, The Journal of Biological Chemistry.

Binding of Exosite Ligands to Human Thrombin

S. Olson, P. E. Bock, I. Verhamme, 2002, The Journal of Biological Chemistry.

The COOH-terminal domain of hirudin. An exosite-directed competitive inhibitor of the action of alpha-thrombin on fibrinogen.

J. Shafer, S. Olson, J. Maraganore, 1990, The Journal of biological chemistry.

Apparent Formation of Sodium Dodecyl Sulfate-stable Complexes between Serpins and 3,4-Dichloroisocoumarin-inactivated Proteinases Is Due to Regeneration of Active Proteinase from the Inactivated Enzyme*

S. Olson, P. Patston, I. Björk, 1997, The Journal of Biological Chemistry.

Quantitative evaluation of solution equilibrium binding interactions by affinity partitioning: application to specific and nonspecific protein-heparin interactions.

S. Olson, P. E. Bock, R. Sheffer, 1991, Archives of biochemistry and biophysics.

The role of Arg46 and Arg47 of antithrombin in heparin binding.

I. Björk, V. Arocas, S. C. Bock, 1999, Biochemistry.

Identification of the omega-hydroxylase of Pseudomonas oleovorans as a nonheme iron protein requiring phospholipid for catalytic activity.

M. J. Coon, S. Olson, R. Boyer, 1974, Biochemical and biophysical research communications.

Regulation of Thrombin Activity by Antithrombin and Heparin

S. Olson, I. Björk, S. T. Olson, 1994, Seminars in thrombosis and hemostasis.

Peptide-mediated inactivation of recombinant and platelet plasminogen activator inhibitor-1 in vitro.

D. Lawrence, S. Olson, D. Eitzman, 1995, The Journal of clinical investigation.

Saturation mutagenesis of the plasminogen activator inhibitor-1 reactive center.

D. Lawrence, D. Ginsburg, J. Shore, 1992, The Journal of biological chemistry.

Lysine 114 of Antithrombin Is of Crucial Importance for the Affinity and Kinetics of Heparin Pentasaccharide Binding*

S. Olson, I. Björk, S. Raja, 2001, The Journal of Biological Chemistry.

Antiangiogenic forms of antithrombin specifically bind to the anticoagulant heparin sequence.

S. Olson, B. Richard, Sophia Schedin‐Weiss, 2008, Biochemistry.

Characterization of the Conformational Alterations, Reduced Anticoagulant Activity, and Enhanced Antiangiogenic Activity of Prelatent Antithrombin*

S. Olson, P. Gettins, R. Swanson, 2008, Journal of Biological Chemistry.

Serine Protease Inhibitor 6-Deficient Mice Have Increased Neutrophil Immunity to Pseudomonas aeruginosa1

Sun-Mi Park, M. Peter, S. Olson, 2007, The Journal of Immunology.

Pseudomonas aeruginosa Have Increased Neutrophil Immunity to Serine Protease Inhibitor 6-Deficient Mice Ashton-Rickardt

Sun-Mi Park, M. Peter, S. Olson, 2007 .

Use of fluorescence resonance energy transfer to study serpin-proteinase interactions.

P. Gettins, S. T. Olson, 2004, Methods.

Kinetic Intermediates en Route to the Final Serpin-Protease Complex

P. Gettins, R. Swanson, G. Izaguirre, 2013, The Journal of Biological Chemistry.

Heparin activation of protein Z-dependent protease inhibitor (ZPI) allosterically blocks protein Z activation through an extended heparin-binding site

R. Swanson, Xin Huang, S. T. Olson, 2022, The Journal of biological chemistry.

Antithrombin Regulates Matriptase Activity Involved in Plasmin Generation, Syndecan Shedding, and HGF Activation in Keratinocytes

Michael D. Johnson, S. Olson, Chen-Yong Lin, 2013, PloS one.

The Signature 3-O-Sulfo Group of the Anticoagulant Heparin Sequence Is Critical for Heparin Binding to Antithrombin but Is Not Required for Allosteric Activation*

S. Olson, R. Swanson, B. Richard, 2009, The Journal of Biological Chemistry.

Residues Tyr253 and Glu255 in Strand 3 of β-Sheet C of Antithrombin Are Key Determinants of an Exosite Made Accessible by Heparin Activation to Promote Rapid Inhibition of Factors Xa and IXa*

S. Olson, G. Izaguirre, S. T. Olson, 2006, Journal of Biological Chemistry.

Localization of an Antithrombin Exosite That Promotes Rapid Inhibition of Factors Xa and IXa Dependent on Heparin Activation of the Serpin*

S. Olson, R. Swanson, G. Izaguirre, 2003, Journal of Biological Chemistry.

Mechanism of heparin activation of antithrombin: evidence for an induced-fit model of allosteric activation involving two interaction subsites.

U. Desai, S. Olson, I. Björk, 1998, Biochemistry.

The oligosaccharide side chain on Asn-135 of alpha-antithrombin, absent in beta-antithrombin, decreases the heparin affinity of the inhibitor by affecting the heparin-induced conformational change.

S. Olson, I. Björk, S. C. Bock, 1997, Biochemistry.

Effect of individual carbohydrate chains of recombinant antithrombin on heparin affinity and on the generation of glycoforms differing in heparin affinity.

S. Olson, I. Björk, R. Swanson, 1997, Archives of biochemistry and biophysics.

Serpins: Structure, Function and Biology

S. Olson, P. Gettins, S. T. Olson, 1996 .

Elimination of glycosylation heterogeneity affecting heparin affinity of recombinant human antithrombin III by expression of a beta-like variant in baculovirus-infected insect cells.

I. Björk, E. Ersdal-Badju, A. Lu, 1995, The Biochemical journal.

Decreased affinity of recombinant antithrombin for heparin due to increased glycosylation.

I. Björk, K. Ylinenjärvi, P. Hermentin, 1992, The Biochemical journal.

Predominant contribution of surface approximation to the mechanism of heparin acceleration of the antithrombin-thrombin reaction. Elucidation from salt concentration effects.

S. Olson, I. Björk, S. T. Olson, 1991, The Journal of biological chemistry.

Isolation of human blood coagulation alpha-factor Xa by soybean trypsin inhibitor-sepharose chromatography and its active-site titration with fluorescein mono-p-guanidinobenzoate.

P. Singh, S. Olson, P. Craig, 1989, Archives of biochemistry and biophysics.

Accelerating ability of synthetic oligosaccharides on antithrombin inhibition of proteinases of the clotting and fibrinolytic systems Comparison with heparin and low-molecular-weight heparin

S. Olson, J. Herbert, I. Björk, 2004, Thrombosis and Haemostasis.

Role of Regulatory Exosite I in Binding of Thrombin to Human Factor V, Factor Va, Factor Va Subunits, and Activation Fragments*

S. Olson, P. E. Bock, S. T. Olson, 1999, The Journal of Biological Chemistry.

p-Aminobenzamidine as a fluorescent probe for the active site of serine proteases.

S. Evans, S. Olson, J. Shore, 1982, The Journal of biological chemistry.

Lipid oxidation inactivates the anticoagulant function of protein Z-dependent protease inhibitor (ZPI)

S. Olson, Baoxin Liu, Yidong Wei, 2017, The Journal of Biological Chemistry.

Engineering Functional Antithrombin Exosites in α1-Proteinase Inhibitor That Specifically Promote the Inhibition of Factor Xa and Factor IXa*

S. Olson, G. Izaguirre, A. Rezaie, 2009, Journal of Biological Chemistry.

Specificity and reactive loop length requirements for crmA inhibition of serine proteases

P. Gettins, S. T. Olson, M. P. Raghavendra, 2005, Protein science : a publication of the Protein Society.

Characterization of the Binding of Different Conformational Forms of Plasminogen Activator Inhibitor-1 to Vitronectin

D. Lawrence, S. Olson, S. Stefansson, 1997, The Journal of Biological Chemistry.

Thermodynamic and Kinetic Characterization of the Protein Z-dependent Protease Inhibitor (ZPI)-Protein Z Interaction Reveals an Unexpected Role for ZPI Lys-239*

Aiwu Zhou, S. Olson, Jian S. Zhou, 2015, The Journal of Biological Chemistry.

T HERMODYNAMIC AND K INETIC C HARACTERIZATION OF THE P ROTEIN Z- DEPENDENT P ROTEASE I NHIBITOR (ZPI)-P ROTEIN Z I NTERACTION R EVEALS AN U NEXPECTED R OLE FOR ZPI L YS 239

Aiwu Zhou, S. Olson, Jian S. Zhou, 2015 .

Kinetic Characterization of the Protein Z-dependent Protease Inhibitor Reaction with Blood Coagulation Factor Xa*

S. Olson, G. Broze, R. Swanson, 2008, Journal of Biological Chemistry.

Serine and Cysteine Proteases Are Translocated to Similar Extents upon Formation of Covalent Complexes with Serpins

S. Olson, P. Gettins, R. Swanson, 2007, Journal of Biological Chemistry.

Specificity and selectivity profile of EP217609: a new neutralizable dual-action anticoagulant that targets thrombin and factor Xa.

S. Olson, M. Petitou, R. Swanson, 2012, Blood.

Surface-induced alterations in the kinetic pathway for cleavage of human high molecular weight kininogen by plasma kallikrein.

S. Olson, J. Shore, M. Tayeh, 1994, The Journal of biological chemistry.

Surface-independent acceleration of factor XII activation by zinc ions. II. Direct binding and fluorescence studies.

H. Halvorson, S. Olson, M. Bernardo, 1993, The Journal of biological chemistry.

Surface-independent acceleration of factor XII activation by zinc ions. I. Kinetic characterization of the metal ion rate enhancement.

S. Olson, M. Bernardo, J. Shore, 1993, The Journal of biological chemistry.

Saturation Mutagenesis of the Antithrombin Reactive Center Loop P14 Residue Supports a Three-step Mechanism of Heparin Allosteric Activation Involving Intermediate and Fully Activated States*♦

S. Olson, P. Gettins, R. Swanson, 2015, The Journal of Biological Chemistry.

Importance of lysine 125 for heparin binding and activation of antithrombin.

U. Desai, S. Olson, P. Gettins, 2002, Biochemistry.

The antithrombin P1 residue is important for target proteinase specificity but not for heparin activation of the serpin. Characterization of P1 antithrombin variants with altered proteinase specificity but normal heparin activation.

S. Olson, Y. Chuang, R. Swanson, 2001, Biochemistry.

The region of antithrombin interacting with full-length heparin chains outside the high-affinity pentasaccharide sequence extends to Lys136 but not to Lys139.

I. Björk, V. Arocas, S. C. Bock, 2000, Biochemistry.

Critical Role of the Linker Region between Helix D and Strand 2A in Heparin Activation of Antithrombin*

S. Olson, J. Meagher, P. Gettins, 2000, The Journal of Biological Chemistry.

Antithrombin III Phenylalanines 122 and 121 Contribute to Its High Affinity for Heparin and Its Conformational Activation*

U. Desai, S. Olson, A. Lu, 2003, The Journal of Biological Chemistry.

Deconvolution of the Fluorescence Emission Spectrum of Human Antithrombin and Identification of the Tryptophan Residues That Are Responsive to Heparin Binding*

J. Beechem, S. Olson, J. Meagher, 1998, The Journal of Biological Chemistry.

Binding of high affinity heparin to antithrombin III. Characterization of the protein fluorescence enhancement.

S. Olson, J. Shore, S. T. Olson, 1981, The Journal of biological chemistry.

Conformational Activation of Antithrombin by Heparin Involves an Altered Exosite Interaction with Protease*

S. Olson, P. Gettins, R. Swanson, 2014, The Journal of Biological Chemistry.

Activation of antithrombin as a factor IXa and Xa inhibitor involves mitigation of repression rather than positive enhancement

P. Gettins, S. T. Olson, 2009, FEBS letters.

Quantitative Characterization of the Thrombin-Heparin Interaction

Herbert, S. T. Olson, HalvorsonS, 2001 .

Role of Arginine 129 in Heparin Binding and Activation of Antithrombin*

U. Desai, S. Olson, I. Björk, 2000, The Journal of Biological Chemistry.

Heparin and calcium ions dramatically enhance antithrombin reactivity with factor IXa by generating new interaction exosites.

S. Olson, Y. Chuang, I. Björk, 2003, Biochemistry.

Contribution of Basic Residues of the Autolysis Loop to the Substrate and Inhibitor Specificity of Factor IXa*

S. Olson, A. Rezaie, Likui Yang, 2003, Journal of Biological Chemistry.

Calcium enhances heparin catalysis of the antithrombin-factor Xa reaction by promoting the assembly of an intermediate heparin-antithrombin-factor Xa bridging complex. Demonstration by rapid kinetics studies.

S. Olson, A. Rezaie, S. T. Olson, 2000, Biochemistry.

Specificity of the basic side chains of Lys114, Lys125, and Arg129 of antithrombin in heparin binding.

S. Olson, I. Björk, Sophia Schedin‐Weiss, 2002, Biochemistry.

The Heparin Binding Properties of Heparin Cofactor II Suggest an Antithrombin-like Activation Mechanism*

J. Huntington, S. Olson, T. Baglin, 2004, Journal of Biological Chemistry.

Heparin activates antithrombin anticoagulant function by generating new interaction sites (exosites) for blood clotting proteinases.

S. Olson, Y. Chuang, S. T. Olson, 2002, Trends in cardiovascular medicine.

Matriptase is inhibited by extravascular antithrombin in epithelial cells but not in most carcinoma cells.

Michael D. Johnson, Ming-Shyue Lee, S. Olson, 2011, American journal of physiology. Cell physiology.

Kinetic Characterization of the Proteinase Binding Defect in a Reactive Site Variant of the Serpin, Antithrombin

S. Olson, I. Björk, P. E. Bock, 1995, The Journal of Biological Chemistry.

Deletion of P1 Arginine in a Novel Antithrombin Variant (Antithrombin London) Abolishes Inhibitory Activity but Enhances Heparin Affinity and Is Associated with Early Onset Thrombosis*

S. Olson, M. Laffan, D. Lane, 2003, The Journal of Biological Chemistry.

Engineering plasminogen activator inhibitor 1 mutants with increased functional stability.

D. Lawrence, S. Olson, S. Palaniappan, 1994, Biochemistry.

Analogs of Human Plasminogen That Are Labeled with Fluorescence Probes at the Catalytic Site of the Zymogen

S. Olson, M. Bernardo, P. E. Bock, 1996, The Journal of Biological Chemistry.

Regulation of Thrombin by Antithrombin and Heparin Cofactor II

S. Olson, I. Björk, S. T. Olson, 1992 .

Exosite Determinants of Serpin Specificity*

S. Olson, P. Gettins, S. T. Olson, 2009, The Journal of Biological Chemistry.

Surface-independent Acceleration of Factor XI1 Activation by Zinc Ions

Herbert, Duane, M. Bernardo, 2001 .

Acceleration of surface-dependent autocatalytic activation of blood coagulation factor XII by divalent metal ions.

S. Olson, P. E. Bock, J. Shore, 1987, Biochemistry.

The heparin-binding site of antithrombin is crucial for antiangiogenic activity.

L. Lau, S. Olson, R. Swanson, 2005, Blood.

Transmission of conformational change from the heparin binding site to the reactive center of antithrombin.

I. Turko, P. Gettins, B. Fan, 1993, Biochemistry.

Reactivity of sulfhydryl groups of the flavoenzyme D-lactate dehydrogenase and effect on catalytic activity.

S. Olson, V. Massey, S. T. Olson, 1980, Biochemistry.

The pH Dependence of Serpin-Proteinase Complex Dissociation Reveals a Mechanism of Complex Stabilization Involving Inactive and Active Conformational States of the Proteinase Which Are Perturbable by Calcium*

S. Olson, S. Calugaru, R. Swanson, 2001, The Journal of Biological Chemistry.

Contribution of lysine 60f to S1' specificity of thrombin.

A. Rezaie, S. T. Olson, 1997, Biochemistry.

Purification and properties of the flavoenzyme D-lactate dehydrogenase from Megasphaera elsdenii.

S. Olson, V. Massey, S. T. Olson, 1979, Biochemistry.

Heparin Enhances the Specificity of Antithrombin for Thrombin and Factor Xa Independent of the Reactive Center Loop Sequence

S. Olson, Y. Chuang, R. Swanson, 2001, The Journal of Biological Chemistry.

Structure of the flavin adduct formed in the suicide reaction of alpha-hydroxybutynoate with D-lactate dehydrogenase.

S. Olson, S. Ghisla, V. Massey, 1979, Biochemistry.

Antithrombin. A bloody important serpin.

S. Olson, I. Björk, S. T. Olson, 1997, Advances in experimental medicine and biology.

Kinetic characterization of heparin-catalyzed and uncatalyzed inhibition of blood coagulation proteinases by antithrombin.

S. Olson, I. Björk, J. Shore, 1993, Methods in enzymology.

Mechanism of Heparin Activation of Antithrombin

U. Desai, S. Olson, I. Björk, 1998, The Journal of Biological Chemistry.

Mechanism of Acceleration of Antithrombin-Proteinase Reactions by Low Affinity Heparin

S. Olson, P. Gettins, I. Björk, 1995, The Journal of Biological Chemistry.

Role of the antithrombin-binding pentasaccharide in heparin acceleration of antithrombin-proteinase reactions. Resolution of the antithrombin conformational change contribution to heparin rate enhancement.

S. Olson, P. Craig, I. Björk, 1992, The Journal of biological chemistry.

Demonstration of a two-step reaction mechanism for inhibition of alpha-thrombin by antithrombin III and identification of the step affected by heparin.

S. Olson, J. Shore, S. T. Olson, 1982, The Journal of biological chemistry.

Mechanism of action of heparin and heparin-like antithrombotics

S. Olson, I. Björk, S. T. Olson, 1994 .

Binding of heparin to human high molecular weight kininogen.

S. Olson, I. Björk, J. Shore, 1989, Biochemistry.

Inactivation of Thrombin by Antithrombin Is Accompanied by Inactivation of Regulatory Exosite I*

S. Olson, I. Björk, P. E. Bock, 1997, The Journal of Biological Chemistry.

Structural characterization of new deoxycytidine kinase inhibitors rationalizes the affinity-determining moieties of the molecules.

Jennifer M Murphy, A. Lavie, S. Olson, 2014, Acta crystallographica. Section D, Biological crystallography.

Cytokine Response Modifier A Inhibition of Initiator Caspases Results in Covalent Complex Formation and Dissociation of the Caspase Tetramer*

G. Salvesen, S. Olson, J. Dobó, 2006, Journal of Biological Chemistry.

Inhibitory serpins. New insights into their folding, polymerization, regulation and clearance.

S. Olson, P. Gettins, S. T. Olson, 2016, The Biochemical journal.

Phosphorylation of Serine 256 Suppresses Transactivation by FKHR (FOXO1) by Multiple Mechanisms

Stephen Adam, Haiyun Pan, A. Mesecar, 2002, The Journal of Biological Chemistry.

Antiangiogenic antithrombin induces global changes in the gene expression profile of endothelial cells.

S. Olson, Y. Chuang, L. Leung, 2006, Cancer research.