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Chemistry

D-Index
44
Citations
5452
World Ranking
17028
National Ranking
4192

Overview

Paul E. Bock is affiliated with Vanderbilt University in the United States and focuses on research primarily within the field of Medicine. Their work encompasses several subfields, including Infectious Diseases, Epidemiology, Public Health, Environmental and Occupational Health, Surgery, and Molecular Biology.

Their research topics highlight specialized areas such as Antimicrobial Resistance in Staphylococcus, Infective Endocarditis Diagnosis and Management, Streptococcal Infections and Treatments, Orthopedic Infections and Treatments, Biochemical and Structural Characterization, Peptidase Inhibition and Analysis, and Venomous Animal Envenomation and Studies.

Frequent coauthors in their publications include:

  • Ingrid M. Verhamme
  • Peter Panizzi
  • Jens Meiler
  • Ashoka A. Maddur
  • Heather K. Kroh

Major publication venues where Paul E. Bock has contributed include:

  • Journal of Biological Chemistry
  • Science Translational Medicine
  • bioRxiv (Cold Spring Harbor Laboratory)
  • UNC Libraries

Notable recent papers authored or coauthored by Paul E. Bock are:

  • Multimodal imaging of bacterial-host interface in mice and piglets with Staphylococcus aureus endocarditis, 2020, Science Translational Medicine
  • Specificity and affinity of the N-terminal residues in staphylocoagulase in binding to prothrombin, 2020, Journal of Biological Chemistry
  • Mapping of the fibrinogen-binding site on the staphylocoagulase C-terminal repeat region, 2021, Journal of Biological Chemistry
  • Mapping of the fibrinogen-binding site on the staphylocoagulase C-terminal repeat region, 2021, bioRxiv (Cold Spring Harbor Laboratory)
  • Author Index, 2020, Journal of Biological Chemistry

Best Publications

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

    Rainer Friedrich;Peter Panizzi;Pablo Fuentes-Prior;Klaus Richter

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

    Imke C.A. Munnix;Marijke J.E. Kuijpers;Jocelyn Auger;Christella M.L.G.D. Thomassen

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

    Peter Panizzi;Matthias Nahrendorf;Jose-Luiz Figueiredo;Jennifer Panizzi

  • Exosites in the substrate specificity of blood coagulation reactions

    P. E. Bock;P. Panizzi;I. M. A. Verhamme

  • Signal recognition particle binds to ribosome-bound signal sequences with fluorescence-detected subnanomolar affinity that does not diminish as the nascent chain lengthens

    John J. Flanagan;Jui Chang Chen;Yiwei Miao;Yuanlong Shao

  • 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.

    I Björk;K Ylinenjärvi;S T Olson;P E Bock

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

    P E Bock;M Luscombe;S E Marshall;D S Pepper

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

    P E Bock;C Frieden

  • Isolation of human blood coagulation α-factor Xa by soybean trypsin inhibitor-Sepharose chromatography and its active-site titration with fluorescein mono-p-guanidinobenzoate☆

    Paul E. Bock;Paul A. Craig;Steven T. Olson;Pratap Singh

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

    Heather K. Kroh;Peter Panizzi;Paul E. Bock

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

    Paul E. Bock;K. R. Srinivasan;Joseph D. Shore

  • Role of the Catalytic Serine in the Interactions of Serine Proteinases with Protein Inhibitors of the Serpin Family CONTRIBUTION OF A COVALENT INTERACTION TO THE BINDING ENERGY OF SERPIN-PROTEINASE COMPLEXES

    Steven T. Olson;Paul E. Bock;Jan Kvassman;Joseph D. Shore

  • 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

    Paul E. Bock

  • 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 E Bock

  • Streptokinase binds to human plasmin with high affinity, perturbs the plasmin active site, and induces expression of a substrate recognition exosite for plasminogen.

    Paul D. Boxrud;William P. Fay;Paul E. Bock

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

    Patricia J. Anderson;Anna Nesset;Kumudini R. Dharmawardana;Paul E. Bock

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

    Ingrid M. Verhamme;Steven T. Olson;Douglas M. Tollefsen;Paul E. Bock

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

    P E Bock;C Frieden

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

    C Frieden;H R Gilbert;P E Bock

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

    Paul E. Bock;Steven T. Olson;Ingemar Björk

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

    Tina Bedsted;Richard Swanson;Yung-Jen Chuang;Paul E. Bock

Frequent Co-Authors

Carl Frieden
Carl Frieden Washington University in St. Louis
Guido Tans
Guido Tans Maastricht University
Rainer W. Friedrich
Rainer W. Friedrich Friedrich Miescher Institute
Sriram Krishnaswamy
Sriram Krishnaswamy Children's Hospital of Philadelphia
Wolfram Bode
Wolfram Bode Max Planck Society
Ingemar Björk
Ingemar Björk Swedish University of Agricultural Sciences
Owen J. T. McCarty
Owen J. T. McCarty Oregon Health & Science University
J. John Holbrook
J. John Holbrook University of Bristol
Jan Rosing
Jan Rosing Maastricht University
Philip J. Hogg
Philip J. Hogg Centenary Institute of Cancer Medicine and Cell Biology

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