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Chemistry

D-Index
53
Citations
10504
World Ranking
13036
National Ranking
3443

Biology and Biochemistry

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53
Citations
10461
World Ranking
16135
National Ranking
6686

Overview

Peter G. W. Gettins is affiliated with the University of Illinois at Chicago in the United States. Their research spans multiple areas within medicine and biochemistry, with a focus on protease and inhibitor mechanisms, calpain protease function and regulation, blood properties and coagulation, research related to leishmaniasis, inflammatory mediators, NSAID effects, as well as blood coagulation and thrombosis mechanisms.

Their recent publication record includes papers in notable venues such as UNC Libraries and Biochemistry. Among these are:

  • The Serpins Are an Expanding Superfamily of Structurally Similar but Functionally Diverse Proteins: EVOLUTION, MECHANISM OF INHIBITION, NOVEL FUNCTIONS, AND A REVISED NOMENCLATURE, 2021, UNC Libraries
  • Paramount Importance of Core Conformational Changes for Heparin Allosteric Activation of Antithrombin, 2021, Biochemistry

Peter G. W. Gettins frequently collaborates with other researchers including Gary A. Silverman, Phillip I. Bird, Robin W. Carrell, Frank Church, and Paul Coughlin. These co-authors have contributed to advancing research in related biochemical and medical fields.

Their publications have appeared in venues such as:

  • UNC Libraries
  • Biochemistry

Primary fields of study for Gettins include Medicine and Biochemistry, Genetics and Molecular Biology. Their subfields cover Cancer Research, Cell Biology, Pulmonary and Respiratory Medicine, Public Health, Environmental and Occupational Health, and Pharmacology.

Core research topics addressed by Gettins comprise:

  • Protease and Inhibitor Mechanisms
  • Calpain Protease Function and Regulation
  • Blood Properties and Coagulation
  • Research on Leishmaniasis Studies
  • Inflammatory Mediators and NSAID Effects
  • Blood Coagulation and Thrombosis Mechanisms

Best Publications

  • The serpins are an expanding superfamily of structurally similar but functionally diverse proteins - Evolution, mechanism of inhibition, novel functions, and a revised nomenclature

    Gary A. Silverman;Phillip I. Bird;Robin W. Carrell;Frank C. Church

  • Serpin Structure, Mechanism, and Function

    Peter G. W. Gettins

  • Formation of the covalent serpin-proteinase complex involves translocation of the proteinase by more than 70 A and full insertion of the reactive center loop into beta-sheet A.

    Efstratios Stratikos;Peter G. W. Gettins

  • Mechanism of serpin action: evidence that C1 inhibitor functions as a suicide substrate.

    Philip A. Patston;Peter Gettins;Joe Beechem;Marc Schapira

  • Molecular mechanisms of antithrombin-heparin regulation of blood clotting proteinases. a paradigm for understanding proteinase regulation by serpin family protein proteinase inhibitors

    Steven T. Olson;Benjamin Richard;Gonzalo Izaguirre;Sophia Schedin-Weiss

  • Alkaline phosphatase, solution structure, and mechanism.

    Joseph E. Coleman;Peter Gettins

  • Crystal structure of human PEDF, a potent anti-angiogenic and neurite growth-promoting factor

    Miljan Simonovic;Peter G W Gettins;Karl W. Volz

  • The ternary complex of antithrombin-anhydrothrombin-heparin reveals the basis of inhibitor specificity.

    Alexey Dementiev;Maurice Petitou;Jean-Marc Herbert;Peter G W Gettins

  • Major proteinase movement upon stable serpin–proteinase complex formation

    Efstratios Stratikos;Peter G. W. Gettins

  • Pathogenic α1-Antitrypsin Polymers are Formed by Reactive Loop-β-Sheet a Linkage

    P Sivasothy;TD Dafforn;Pwg Gettins;DA Lomas

  • Active Site Distortion Is Sufficient for Proteinase Inhibition by Serpins STRUCTURE OF THE COVALENT COMPLEX OF α1-PROTEINASE INHIBITOR WITH PORCINE PANCREATIC ELASTASE

    Alexey Dementiev;József Dobó;Peter G.W. Gettins

  • Mechanism of Heparin Activation of Antithrombin. Evidence for Reactive Center Loop Preinsertion with Expulsion upon Heparin Binding

    James A. Huntington;Steven T. Olson;Bingqi Fan;Peter G. W. Gettins

  • The role of conformational change in serpin structure and function

    Peter Gettins;Philip A. Patston;Marc Schapira

  • .alpha.1-Proteinase Inhibitor Variant T345R. Influence of P14 Residue on Substrate and Inhibitory Pathways

    Darryl B. Hood;James A. Huntington;Peter G. W. Gettins

  • Canonical inhibitor-like interactions explain reactivity of alpha1-proteinase inhibitor Pittsburgh and antithrombin with proteinases

    Alexey Dementiev;Miljan Simonovic;Karl Volz;Peter G.W. Gettins

  • Exosite Determinants of Serpin Specificity

    Peter G. W. Gettins;Steven T. Olson

  • NMR solution structure of complement-like repeat CR8 from the low density lipoprotein receptor-related protein.

    Wen Huang;Klavs Dolmer;Peter G.W. Gettins

  • Mechanism of acceleration of antithrombin-proteinase reactions by low affinity heparin. Role of the antithrombin binding pentasaccharide in heparin rate enhancement.

    Virginia J. Streusand;Ingemar Björk;Peter G.W. Gettins;Maurice Petitou

  • Structure of an antibody combining site by magnetic resonance.

    R A Dwek;S Wain-Hobson;S Dower;P Gettins

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

    Peter G.W. Gettins;Steven T. Olson

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

    Peter G. W. Gettins;Bingqi Fan;Brenda C. Crews;Illarion V. Turko

Frequent Co-Authors

Raymond A. Dwek
Raymond A. Dwek University of Oxford
James A. Huntington
James A. Huntington University of Cambridge
David Givol
David Givol Weizmann Institute of Science
Simon Wain-Hobson
Simon Wain-Hobson Institut Pasteur
Joseph M. Beechem
Joseph M. Beechem NanoString Technologies
Dudley K. Strickland
Dudley K. Strickland American Red Cross
Guy S. Salvesen
Guy S. Salvesen Sanford Burnham Prebys Medical Discovery Institute
Robin W. Carrell
Robin W. Carrell University of Cambridge
Lijun Rong
Lijun Rong University of Illinois at Chicago
Stephen J. Perkins
Stephen J. Perkins University College London

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