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

Biochemical journal, 2016-08, Vol.473 (15), p.2273-2293

2016

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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

Biochimie, 2010-11, Vol.92 (11), p.1587-1596

2010

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On 'The polymerization of proteins: the action of thrombin on fibrinogen' by Koloman Laki

Archives of biochemistry and biophysics, 2022-09, Vol.726, p.109176-109176, Article 109176

Olson, Steven T.

2022

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Exosite Determinants of Serpin Specificity

The Journal of biological chemistry, 2009-07, Vol.284 (31), p.20441-20445

2009

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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

The Journal of biological chemistry, 2009-10, Vol.284 (40), p.27054-27064

2009

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

The Journal of biological chemistry, 2015-04, Vol.290 (15), p.9906-9918

2015

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

The Journal of biological chemistry, 2022-06, Vol.298 (6), p.102022, Article 102022

2022

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Heparin Is a Major Activator of the Anticoagulant Serpin, Protein Z-dependent Protease Inhibitor

The Journal of biological chemistry, 2011-03, Vol.286 (11), p.8740-8751

2011

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Basis for the Specificity and Activation of the Serpin Protein Z-dependent Proteinase Inhibitor (ZPI) as an Inhibitor of Membrane-associated Factor Xa

The Journal of biological chemistry, 2010-06, Vol.285 (26), p.20399-20409

2010

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

The Journal of biological chemistry, 2008-10, Vol.283 (44), p.29770-29783

2008

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Characterization of the Heparin-Binding Site of the Protein Z‑Dependent Protease Inhibitor

Biochemistry (Easton), 2012-05, Vol.51 (19), p.4078-4085

2012

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

Thrombosis and haemostasis, 2004-11, Vol.92 (5), p.929-939

2004

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Structural basis for catalytic activation of protein Z–dependent protease inhibitor (ZPI) by protein Z

Blood, 2012-08, Vol.120 (8), p.1726-1733

2012

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Mechanism by Which Exosites Promote the Inhibition of Blood Coagulation Proteases by Heparin-activated Antithrombin

The Journal of biological chemistry, 2007-11, Vol.282 (46), p.33609-33622

2007

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Paul E. Bock, PhD (21 October, 1949–11 October, 2019)

Journal of thrombosis and haemostasis, 2020-01, Vol.18 (1), p.262-263

2020

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

Biochemistry (Easton), 2018-04, Vol.57 (15), p.2211-2226

2018

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Paramount Importance of Core Conformational Changes for Heparin Allosteric Activation of Antithrombin

Biochemistry (Easton), 2021-04, Vol.60 (15), p.1201-1213

2021

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

The Journal of biological chemistry, 2017-09, Vol.292 (35), p.14625-14635

2017

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

Cancer research (Chicago, Ill.), 2006-05, Vol.66 (10), p.5047-5055

2006

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

Blood, 2012-03, Vol.119 (10), p.2187-2195

2012

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

The Journal of biological chemistry, 2004-11, Vol.279 (48), p.50267-50273

2004

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Disease-causing mutations in the serpin antithrombin reveal a key domain critical for inhibiting protease activities

The Journal of biological chemistry, 2017-10, Vol.292 (40), p.16513-16520

2017

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

The Journal of biological chemistry, 2003-12, Vol.278 (51), p.51433-51440

2003

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

The Journal of biological chemistry, 2006-12, Vol.281 (50), p.38781-38790

2006

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

Blood, 2005-09, Vol.106 (5), p.1621-1628

2005

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

Molecular mechanisms of antithrombin–heparin regulation of blood clotting proteinases. A paradigm for understanding proteinase regulation by serpin family protein proteinase inhibitors

On 'The polymerization of proteins: the action of thrombin on fibrinogen' by Koloman Laki

Exosite Determinants of Serpin Specificity

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

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

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

Heparin Is a Major Activator of the Anticoagulant Serpin, Protein Z-dependent Protease Inhibitor

Basis for the Specificity and Activation of the Serpin Protein Z-dependent Proteinase Inhibitor (ZPI) as an Inhibitor of Membrane-associated Factor Xa

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

Characterization of the Heparin-Binding Site of the Protein Z‑Dependent Protease Inhibitor

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

Structural basis for catalytic activation of protein Z–dependent protease inhibitor (ZPI) by protein Z

Mechanism by Which Exosites Promote the Inhibition of Blood Coagulation Proteases by Heparin-activated Antithrombin

Paul E. Bock, PhD (21 October, 1949–11 October, 2019)

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

Paramount Importance of Core Conformational Changes for Heparin Allosteric Activation of Antithrombin

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

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

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

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

Disease-causing mutations in the serpin antithrombin reveal a key domain critical for inhibiting protease activities

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

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

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

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