P. Bock

发表

Phosphofructokinase. I. Mechanism of the pH-dependent inactivation and reactivation of the rabbit muscle enzyme.

Carl Frieden, P. E. Bock, P. Bock, 1976, The Journal of biological chemistry.

Phosphofructokinase. II. Role of ligands in pH-dependent structural changes of the rabbit muscle enzyme.

Carl Frieden, P. E. Bock, P. Bock, 1976, The Journal of biological chemistry.

A Novel Allosteric Pathway of Thrombin Inhibition

U. Desai, P. E. Bock, Brian L. Henry, 2007, 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.

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

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

Protein-protein interactions in contact activation of blood coagulation. Binding of high molecular weight kininogen and the 5-(iodoacetamido) fluorescein-labeled kininogen light chain to prekallikrein, kallikrein, and the separated kallikrein heavy and light chains.

J. Griffin, P. E. Bock, J. Shore, 1985, The Journal of biological chemistry.

Protein-protein interactions in contact activation of blood coagulation. Characterization of fluorescein-labeled human high molecular weight kininogen-light chain as a probe.

J. Shore, P. Bock, 1983, The Journal of biological chemistry.

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.

Protein Z-dependent protease inhibitor (ZPI) is a physiologically significant inhibitor of prothrombinase function

R. Swanson, Xin Huang, H. Kroh, 2019, The Journal of Biological Chemistry.

Signal Recognition Particle Binds to Ribosome-bound Signal Sequences with Fluorescence-detected Subnanomolar Affinity That Does Not Diminish as the Nascent Chain Lengthens*

J. Flanagan, Jialing Lin, P. E. Bock, 2003, 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.

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.

The Preferred Pathway of Glycosaminoglycan-accelerated Inactivation of Thrombin by Heparin Cofactor II*

P. E. Bock, I. Verhamme, C. Jackson, 2004, Journal of Biological Chemistry.

Complete genome of Staphylococcus aureus Tager 104 provides evidence of its relation to modern systemic hospital-acquired strains

D. Mead, M. Nahrendorf, M. Liles, 2016, BMC Genomics.

The staphylocoagulase family of zymogen activator and adhesion proteins

W. Bode, P. Panizzi, P. Fuentes-Prior, 2004, Cellular and Molecular Life Sciences CMLS.

Active site selective labeling of serine proteases with spectroscopic probes using thioester peptide chloromethyl ketones: demonstration of thrombin labeling using N alpha-[(acetylthio)acetyl]-D-Phe-Pro-Arg-CH2Cl.

P. E. Bock, P. Bock, 1988, Biochemistry.

Development of Coagulation Factor Probes for the Identification of Procoagulant Circulating Tumor Cells

Flor A. Cianchetti, O. McCarty, P. E. Bock, 2012, Front. Oncol..

Spatial Distribution of Factor Xa, Thrombin, and Fibrin(ogen) on Thrombi at Venous Shear

O. McCarty, S. Watson, P. Panizzi, 2010, PloS one.

Exosites in the substrate specificity of blood coagulation reactions

P. Panizzi, P. E. Bock, I. Verhamme, 2007, Journal of thrombosis and haemostasis : JTH.

Von Willebrand factor-binding protein is a hysteretic conformational activator of prothrombin

P. Panizzi, P. E. Bock, H. Kroh, 2009, Proceedings of the National Academy of Sciences.

Platelet heterogeneity in activation-induced glycoprotein shedding: functional effects.

Renhao Li, J. Heemskerk, P. Collins, 2018, Blood advances.

In vivo detection of Staphylococcus aureus endocarditis by targeting pathogen-specific prothrombin activation

R. Weissleder, Jose-Luiz Figueiredo, M. Pittet, 2011, Nature Medicine.

Fibrinogen Substrate Recognition by Staphylocoagulase·(Pro)thrombin Complexes*

W. Bode, P. Panizzi, K. Richter, 2006, Journal of Biological Chemistry.

Novel Fluorescent Prothrombin Analogs as Probes of Staphylocoagulase-Prothrombin Interactions*

W. Bode, P. Panizzi, P. Fuentes-Prior, 2006, Journal of Biological Chemistry.

Staphylocoagulase is a prototype for the mechanism of cofactor-induced zymogen activation

R. Huber, W. Bode, S. Kawabata, 2003, Nature.

Rapid Binding of Plasminogen to Streptokinase in a Catalytic Complex Reveals a Three-step Mechanism*

P. E. Bock, I. Verhamme, P. Bock, 2014, The Journal of Biological Chemistry.

Full Time Course Kinetics of the Streptokinase-Plasminogen Activation Pathway*

P. E. Bock, M. Nolan, S. Bouldin, 2013, The Journal of Biological Chemistry.

Plasminogen Substrate Recognition by the Streptokinase-Plasminogen Catalytic Complex Is Facilitated by Arg253, Lys256, and Lys257 in the Streptokinase β-Domain and Kringle 5 of the Substrate*

P. Panizzi, P. Fuentes-Prior, P. E. Bock, 2009, The Journal of Biological Chemistry.

Rapid-reaction Kinetic Characterization of the Pathway of Streptokinase-Plasmin Catalytic Complex Formation*

P. E. Bock, I. Verhamme, P. Bock, 2008, Journal of Biological Chemistry.

Coupling of Conformational and Proteolytic Activation in the Kinetic Mechanism of Plasminogen Activation by Streptokinase*

P. E. Bock, P. D. Boxrud, P. Bock, 2004, Journal of Biological Chemistry.

Resolution of Conformational Activation in the Kinetic Mechanism of Plasminogen Activation by Streptokinase*

P. E. Bock, I. Verhamme, P. D. Boxrud, 2004, Journal of Biological Chemistry.

Streptokinase Binds to Human Plasmin with High Affinity, Perturbs the Plasmin Active Site, and Induces Expression of a Substrate Recognition Exosite for Plasminogen*

W. Fay, P. E. Bock, P. D. Boxrud, 2000, The Journal of Biological Chemistry.

Pathogen activators of plasminogen

P. Panizzi, P. E. Bock, I. Verhamme, 2015, Journal of thrombosis and haemostasis : JTH.

Active Site-labeled Prothrombin Inhibits Prothrombinase in Vitro and Thrombosis in Vivo*

B. Furie, J. Rosing, P. Panizzi, 2011, The Journal of Biological Chemistry.

Restricted Active Site Docking by Enzyme-bound Substrate Enforces the Ordered Cleavage of Prothrombin by Prothrombinase*

P. Panizzi, R. Camire, S. Krishnaswamy, 2007, Journal of Biological Chemistry.

Expression of Allosteric Linkage between the Sodium Ion Binding Site and Exosite I of Thrombin during Prothrombin Activation*

G. Nicolaes, J. Rosing, P. E. Bock, 2007, Journal of Biological Chemistry.

Exosite-mediated Substrate Recognition of Factor IX by Factor XIa

I. Verhamme, D. Gailani, T. Ogawa, 2005, Journal of Biological Chemistry.

Role of Prothrombin Fragment 1 in the Pathway of Regulatory Exosite I Formation during Conversion of Human Prothrombin to Thrombin*

P. E. Bock, P. Anderson, P. Bock, 2003, Journal of Biological Chemistry.

Role of Proexosite I in Factor Va-dependent Substrate Interactions of Prothrombin Activation*

P. E. Bock, P. Anderson, A. Nesset, 2000, The Journal of Biological Chemistry.

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.

Skizzle Is a Novel Plasminogen- and Plasmin-binding Protein from Streptococcus agalactiae That Targets Proteins of Human Fibrinolysis to Promote Plasmin Generation*

P. Panizzi, P. E. Bock, H. Kroh, 2010, The Journal of Biological Chemistry.

Active-site-selective labeling of blood coagulation proteinases with fluorescence probes by the use of thioester peptide chloromethyl ketones. II. Properties of thrombin derivatives as reporters of prothrombin fragment 2 binding and specificity of the labeling approach for other proteinases.

P. Bock, 1992, The Journal of biological chemistry.

Thioester peptide chloromethyl ketones: reagents for active site-selective labeling of serine proteinases with spectroscopic probes.

P. E. Bock, P. Bock, 1993, Methods in enzymology.

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.

Promotion of experimental thrombus formation by the procoagulant activity of breast cancer cells

M. Berny-Lang, O. McCarty, A. Gruber, 2011, Physical biology.

Streptokinase Triggers Conformational Activation of Plasminogen through Specific Interactions of the Amino-terminal Sequence and Stabilizes the Active Zymogen Conformation*

W. Fay, P. E. Bock, I. Verhamme, 2001, The Journal of Biological Chemistry.

Role of the Catalytic Serine in the Interactions of Serine Proteinases with Protein Inhibitors of the Serpin Family

D. Lawrence, S. Olson, I. Björk, 1995, 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.

junction B domain - sequence is critical for processing at the heavy chain 672 -Glu 666 Structural basis of thrombin-mediated factor V activation: the Glu

R. Gutiérrez-Gallego, M. Corral-Rodríguez, P. Fuentes-Prior, 2013 .

Effect of Zymogen Domains and Active Site Occupation on Activation of Prothrombin by von Willebrand Factor-binding Protein*

H. Kroh, P. Bock, 2012, The Journal of Biological Chemistry.

Notecarin D Binds Human Factor V and Factor Va with High Affinity in the Absence of Membranes*

J. I. Creamer, Hong Xu, G. Tans, 2011, The Journal of Biological Chemistry.

Engineering streptokinase for generation of active site-labeled plasminogen analogs.

M. Nahrendorf, P. Panizzi, P. E. Bock, 2011, Analytical biochemistry.

Structural basis of thrombin-mediated factor V activation: the Glu666-Glu672 sequence is critical for processing at the heavy chain-B domain junction.

R. Gutiérrez-Gallego, M. Corral-Rodríguez, P. Fuentes-Prior, 2011, Blood.

Segregation of Platelet Aggregatory and Procoagulant Microdomains in Thrombus Formation: Regulation by Transient Integrin Activation

M. V. van Zandvoort, S. Watson, J. Rosing, 2007, Arteriosclerosis, thrombosis, and vascular biology.

Role of the Streptokinase α-Domain in the Interactions of Streptokinase with Plasminogen and Plasmin*

P. E. Bock, I. Verhamme, Ronald R. Bean, 2005, Journal of Biological Chemistry.

Effects of Activation Peptide Bond Cleavage and Fragment 2 Interactions on the Pathway of Exosite I Expression during Activation of Human Prethrombin 1 to Thrombin*

P. Anderson, A. Nesset, P. Bock, 2003, Journal of Biological Chemistry.

Biotin derivatives of D-Phe-Pro-Arg-CH2Cl for active-site-specific labeling of thrombin and other serine proteinases.

P. Anderson, P. Bock, Patricia J. Anderson, 2001, Analytical biochemistry.

Characterization of bothrojaracin interaction with human prothrombin

R. Zingali, P. E. Bock, R. Monteiro, 2001, Protein science : a publication of the Protein Society.

Modulation of Thrombin and Heparin Activities by Fibrin

P. Hogg, P. E. Bock, P. Bock, 1997, Thrombosis and Haemostasis.

Binding of Fibrin Monomer and Heparin to Thrombin in a Ternary Complex Alters the Environment of the Thrombin Catalytic Site, Reduces Affinity for Hirudin, and Inhibits Cleavage of Fibrinogen*

P. Hogg, P. E. Bock, J. Labanowski, 1996, The Journal of Biological Chemistry.

Thrombin–thrombomodulin activation of protein C facilitates the activation of progelatinase A

P. E. Bock, R. Hoover, S. R. Pekovich, 2001, FEBS letters.

Characterization of Proexosite I on Prothrombin*

P. E. Bock, P. Anderson, A. Nesset, 2000, The Journal of Biological Chemistry.

Demonstration of exosite I-dependent interactions of thrombin with human factor V and factor Va involving the factor Va heavy chain: analysis by affinity chromatography employing a novel method for active-site-selective immobilization of serine proteinases.

K. R. Dharmawardana, P. Bock, 1998, Biochemistry.

In Vivo Tracking of Streptococcal Infections of Subcutaneous Origin in a Murine Model

M. Nahrendorf, Heather Eggleston, P. Panizzi, 2015, Molecular Imaging and Biology.

The multiple complexes formed by the interaction of platelet factor 4 with heparin.

J. Holbrook, P. E. Bock, D. Pepper, 1980, The Biochemical journal.

Inhibition of Thrombin Formation by Active Site Mutated (S360A) Activated Protein C*

B. Dahlbäck, G. Nicolaes, J. Rosing, 2010, The Journal of Biological Chemistry.

Characterization of Novel Forms of Coagulation Factor XIa

P. E. Bock, I. Verhamme, D. Gailani, 2008, Journal of Biological Chemistry.

Structural Basis for Reduced Staphylocoagulase-mediated Bovine Prothrombin Activation*

W. Bode, S. Kawabata, P. Panizzi, 2006, Journal of Biological Chemistry.

Independence of Factor XIa Subunits in Factor IX Activation.

D. Gailani, Mao-fu Sun, Stephen B. Smith, 2006 .

Another look at the cold lability of enzymes

Carl Frieden, P. Bock, 1978 .

pH-induced cold lability of rabbit skeletal muscle phosphofructokinase.

Carl Frieden, P. E. Bock, P. Bock, 1974, Biochemistry.

Binding of Exosite Ligands to Human Thrombin RE-EVALUATION OF ALLOSTERIC LINKAGE BETWEEN THROMBIN EXOSITES I AND II*

S. Olson, I. Verhamme, D. Tollefsen, 2002 .

Ratcheting of the substrate from the zymogen to proteinase conformations directs the sequential cleavage of prothrombin by prothrombinase.

P. Panizzi, E. Bianchini, P. E. Bock, 2005, Proceedings of the National Academy of Sciences of the United States of America.

Structure, function, and regulation of free and membrane-bound ribosomes: the view from their substrates and products.

J. Flanagan, P. E. Bock, A. Johnson, 2001, Cold Spring Harbor symposia on quantitative biology.

Phosphofructokinase. III. Correlation of the regulatory kinetic and molecular properties of the rabbit muscle enzyme.

Carl Frieden, H. Gilbert, P. E. Bock, 1976, The Journal of biological chemistry.

Analysis of the cold lability behavior of rabbit muscle phosphofructokinase.

Carl Frieden, H. Gilbert, P. E. Bock, 1975, Biochemical and biophysical research communications.

Activation of intrinsic blood coagulation by ellagic acid: insoluble ellagic acid-metal ion complexes are the activating species.

P. E. Bock, J. Shore, K. Srinivasan, 1981, Biochemistry.

The Role of Thrombin Exosites I and II in the Activation of Human Coagulation Factor V*

B. Dahlbäck, G. Nicolaes, J. Rosing, 2007, 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.

Multimodal imaging of bacterial-host interface in mice and piglets with Staphylococcus aureus endocarditis

G. Wojtkiewicz, Y. Iwamoto, C. Calcagno, 2020, Science Translational Medicine.

Allosteric effects of a monoclonal antibody against thrombin exosite II.

C. Gibbs, P. E. Bock, D. Tollefsen, 1998, Biochemistry.

Active-site-selective labeling of blood coagulation proteinases with fluorescence probes by the use of thioester peptide chloromethyl ketones. I. Specificity of thrombin labeling.

P. Bock, 1992, The Journal of biological chemistry.

Specificity and affinity of the N-terminal residues in staphylocoagulase in binding to prothrombin

J. Meiler, P. Panizzi, I. Verhamme, 2020, The Journal of Biological Chemistry.

Binding of the COOH-terminal Lysine Residue of Streptokinase to Plasmin(ogen) Kringles Enhances Formation of the Streptokinase·Plasmin(ogen) Catalytic Complexes*

P. Panizzi, P. E. Bock, I. Verhamme, 2006, Journal of Biological Chemistry.

Conversion of antithrombin from an inhibitor of thrombin to a substrate with reduced heparin affinity and enhanced conformational stability by binding of a tetradecapeptide corresponding to the P1 to P14 region of the putative reactive bond loop of the inhibitor.

S. Olson, I. Björk, K. Ylinenjärvi, 1992, The Journal of biological chemistry.

Molecular weight of human high-molecular-weight kininogen light chain by equilibrium sedimentation in an air-driven ultracentrifuge.

H. Halvorson, P. Bock, 1983, Analytical biochemistry.

Platelet heterogeneity in activation-induced glycoprotein shedding: functional effects.

Renhao Li, J. Heemskerk, P. Collins, 2018, Blood advances.

Pathogen activators of plasminogen

I. Verhamme, P. Bock, Peter R. Panizzi, 2015, Journal of thrombosis and haemostasis : JTH.