Heparin-binding motif mutations of human diamine oxidase allow the development of a first-in-class histamine-degrading biopharmaceutical

  1. Elisabeth Gludovacz
  2. Kornelia Schuetzenberger
  3. Marlene Resch
  4. Katharina Tillmann
  5. Karin Petroczi
  6. Markus Schosserer
  7. Sigrid Vondra
  8. Serhii Vakal
  9. Gerald Klanert
  10. Jürgen Pollheimer
  11. Tiina A Salminen
  12. Bernd Jilma
  13. Nicole Borth
  14. Thomas Boehm  Is a corresponding author
  1. Department of Biotechnology, University of Natural Resources and Life Sciences, Vienna, Austria
  2. Center for Medical Physics and Biomedical Engineering, Medical University of Vienna, Austria
  3. Department of Clinical Pharmacology, Medical University of Vienna, Austria
  4. Center for Biomedical Research, Medical University of Vienna, Austria
  5. University of Natural Resources and Life Sciences, Vienna, Austria
  6. Department of Obstetrics and Gynecology, Medical University of Vienna, Austria
  7. Structural Bioinformatics Laboratory, Biochemistry, Faculty of Science and Engineering, Åbo Akademi University, Finland
  8. Medical University of Vienna, Austria
  9. Department of Biotechnology, University of Natural Resources and Life Sciences, Austria
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  1. Elisabeth Gludovacz
  2. Kornelia Schuetzenberger
  3. Marlene Resch
  4. Katharina Tillmann
  5. Karin Petroczi
  6. Markus Schosserer
  7. Sigrid Vondra
  8. Serhii Vakal
  9. Gerald Klanert
  10. Jürgen Pollheimer
  11. Tiina A Salminen
  12. Bernd Jilma
  13. Nicole Borth
  14. Thomas Boehm
(2021)
Heparin-binding motif mutations of human diamine oxidase allow the development of a first-in-class histamine-degrading biopharmaceutical
eLife 10:e68542.
https://doi.org/10.7554/eLife.68542