World's Best Scientists 2026 revealed!

D-Index & Metrics

Chemistry

D-Index
68
Citations
13777
World Ranking
6680
National Ranking
86

Biology and Biochemistry

D-Index
68
Citations
13479
World Ranking
7947
National Ranking
104

Overview

Ingemar Björk is affiliated with the Swedish University of Agricultural Sciences in Sweden. The scientist's professional profile is characterized by a focus on agricultural studies and related fields, as indicated by the primary affiliation.

While detailed data on specific publications, co-authors, research topics, and awards are not present, Ingemar Björk's association with an academic institution specializing in agricultural sciences suggests their work contributes to that domain.

The absence of notable recent papers, frequent co-authors, publication venues, or book publications in the data implies either a developing research portfolio or a focus outside of widely indexed outputs. Similarly, no presented information on main or subfields of study and research topics limits detailed insight into specific research areas or thematic concentrations.

There is also no indication of awards or recognition, which may reflect either an early career stage or a profile focused primarily on research activities without public accolades.

Best Publications

  • 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.T. Olson;I Björk;R Sheffer;P.A. Craig

  • Mechanism of the anticoagulant action of heparin

    I. Björk;U. Lindahl

  • Anticoagulant activity of heparin: Separation of high-activity and low-activity heparin species by affinity chromatography on immobilized antithrombin

    Magnus Höök;Ingemar Björk;John Hopwood;Ulf Lindahl

  • Extension and structural variability of the antithrombin-binding sequence in heparin.

    Ulf Lindahl;Lennart Thunberg;Gudrun Backstrom;Johan Riesenfeld

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

    Steven T. Olson;Ingemar Björk;Joseph D. Shore

  • Role of ternary complexes, in which heparin binds both antithrombin and proteinase, in the acceleration of the reactions between antithrombin and thrombin or factor Xa.

    A Danielsson;E Raub;U Lindahl;I Björk

  • Binding of high affinity heparin to antithrombin III. Stopped flow kinetic studies of the binding interaction.

    S.T. Olson;K.R. Srinivasan;I. Björk;J.D. Shore

  • Mechanism of Heparin Activation of Antithrombin ROLE OF INDIVIDUAL RESIDUES OF THE PENTASACCHARIDE ACTIVATING SEQUENCE IN THE RECOGNITION OF NATIVE AND ACTIVATED STATES OF ANTITHROMBIN

    Umesh R. Desai;Maurice Petitou;Ingemar Björk;Steven T. Olson

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

    Unknown

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

    Unknown

  • Some Physicochemical Properties of Protein A from Staphylococcus aureus

    Unknown

  • The size and shape of human and bovine antithrombin III.

    Unknown

  • The binding of low-affinity and high-affinity heparin to antithrombin. Fluorescence studies.

    Birgitta Nordenman;Åke Danielsson;Ingemar Björk

  • Regulation of Thrombin Activity by Antithrombin and Heparin

    Steven T. Olson;Ingemar Björk

  • Binding of low-affinity and high-affinity heparin to antithrombin. Ultraviolet difference spectroscopy and circular dichroism studies.

    Birgitta Nordenman;Ingemar Bjork

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

    Steven T. Olson;Richard Swanson;Elke Raub-Segall;Tina Bedsted

  • The active site of antithrombin. Release of the same proteolytically cleaved form of the inhibitor from complexes with factor IXa, factor Xa, and thrombin.

    I Björk;C M Jackson;H Jörnvall;K K Lavine

  • Regulation of the activity of lysosomal cysteine proteinases by pH-induced inactivation and/or endogenous protein inhibitors, cystatins.

    Boris Turk;Joseph G. Bieth;Ingemar Björk;Iztok Dolenc

  • Evidence for similar conformational changes in α2-macroglobulin on reaction with primary amines or proteolytic enzymes

    Ingemar Björk;Wayne W. Fish

  • Reinvestigation of some physicochemical and chemical properties of human ceruloplasmin (ferroxidase).

    Lars Ryden;Ingemar Bjork

  • 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

  • Heparin and related polysaccharides

    D. A. Lane;Ingemar Björk;Ulf Lindahl

  • A fragment of histidine-rich glycoprotein is a potent inhibitor of tumor vascularization.

    Anna-Karin Olsson;Helena Larsson;Johan Dixelius;Irja Johansson

  • Structure and Antithrombin-Binding Properties of Heparin Isolated From the Clams Anomalocardia Brasiliana and Tivela Mactroides

    Gunnar Pejler;Ake Danielsson;Ingemar Bjork;Ulf Lindahl

Frequent Co-Authors

Boris Turk
Boris Turk Jožef Stefan Institute
Ulf Lindahl
Ulf Lindahl Uppsala University
Johan Stenflo
Johan Stenflo Lund University
Vito Turk
Vito Turk Jožef Stefan Institute
Magnus Abrahamson
Magnus Abrahamson Lund University
Paul E. Bock
Paul E. Bock Vanderbilt University
Hans Jörnvall
Hans Jörnvall Karolinska Institute
Maurice Petitou
Maurice Petitou University of Cambridge
Juan José Cazzulo
Juan José Cazzulo National University of General San Martín
John S. Mort
John S. Mort McGill University

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