R Egelund

Summary

Affiliation: University of Aarhus
Country: Denmark

Publications

  1. ncbi request reprint Type-1 plasminogen-activator inhibitor -- conformational differences between latent, active, reactive-centre-cleaved and plasminogen-activator-complexed forms, as probed by proteolytic susceptibility
    R Egelund
    Department of Molecular and Structural Biology, University of Aarhus, Denmark
    Eur J Biochem 248:775-85. 1997
  2. ncbi request reprint A serpin-induced extensive proteolytic susceptibility of urokinase-type plasminogen activator implicates distortion of the proteinase substrate-binding pocket and oxyanion hole in the serpin inhibitory mechanism
    R Egelund
    The Laboratory of Cellular Protein Science, Department of Molecular and Structural Biology, Aarhus University, Denmark
    Eur J Biochem 268:673-85. 2001
  3. ncbi request reprint Solvent effects on activity and conformation of plasminogen activator inhibitor-1
    P A Andreasen
    Department of Molecular and Structural Biology, Aarhus University, Denmark
    Thromb Haemost 81:407-14. 1999
  4. ncbi request reprint A regulatory hydrophobic area in the flexible joint region of plasminogen activator inhibitor-1, defined with fluorescent activity-neutralizing ligands. Ligand-induced serpin polymerization
    R Egelund
    Laboratory of Cellular Protein Science, Department of Molecular and Structural Biology, Aarhus University, 8000 Aarhus C, Denmark
    J Biol Chem 276:13077-86. 2001
  5. ncbi request reprint The plasminogen activation system in tumor growth, invasion, and metastasis
    P A Andreasen
    Department of Molecular and Structural Biology, Aarhus University, Denmark
    Cell Mol Life Sci 57:25-40. 2000

Collaborators

  • J Deinum
  • P A Andreasen
  • H H Petersen
  • S Jensen
  • K W Rodenburg

Detail Information

Publications5

  1. ncbi request reprint Type-1 plasminogen-activator inhibitor -- conformational differences between latent, active, reactive-centre-cleaved and plasminogen-activator-complexed forms, as probed by proteolytic susceptibility
    R Egelund
    Department of Molecular and Structural Biology, University of Aarhus, Denmark
    Eur J Biochem 248:775-85. 1997
    ....
  2. ncbi request reprint A serpin-induced extensive proteolytic susceptibility of urokinase-type plasminogen activator implicates distortion of the proteinase substrate-binding pocket and oxyanion hole in the serpin inhibitory mechanism
    R Egelund
    The Laboratory of Cellular Protein Science, Department of Molecular and Structural Biology, Aarhus University, Denmark
    Eur J Biochem 268:673-85. 2001
    ..The distorted region includes the so-called activation domain, also known to change conformation on zymogen activation...
  3. ncbi request reprint Solvent effects on activity and conformation of plasminogen activator inhibitor-1
    P A Andreasen
    Department of Molecular and Structural Biology, Aarhus University, Denmark
    Thromb Haemost 81:407-14. 1999
    ..These results provide new information about the structural basis for serpin substrate behaviour...
  4. ncbi request reprint A regulatory hydrophobic area in the flexible joint region of plasminogen activator inhibitor-1, defined with fluorescent activity-neutralizing ligands. Ligand-induced serpin polymerization
    R Egelund
    Laboratory of Cellular Protein Science, Department of Molecular and Structural Biology, Aarhus University, 8000 Aarhus C, Denmark
    J Biol Chem 276:13077-86. 2001
    ..The defined binding area may be a target for development of compounds for neutralizing PAI-1 in cancer and cardiovascular diseases...
  5. ncbi request reprint The plasminogen activation system in tumor growth, invasion, and metastasis
    P A Andreasen
    Department of Molecular and Structural Biology, Aarhus University, Denmark
    Cell Mol Life Sci 57:25-40. 2000
    ..The increased knowledge about the plasminogen activation system may allow utilization of its components as targets for anti-invasive therapy...