Amalie Carnbring Bonde
Research Subjects
Amalie Carnbring Bonde has a total of 13 co-authors. Here are the top co-authors by number of shared publications:
Eva Johansson
Research & Early Development Novo Nordisk A/S Måløv Denmark
1 shared publicationHelle Heibroch Petersen
Research and Development, LEO Pharma, 2750 Ballerup, Denmark
1 shared publicationJacob Lund
Global Research, Novo Nordisk A/S, 2760 Måløv, Denmark
1 shared publication- Jacob Lund
Novo Nordisk A/S, Måløv, Denmark
1 shared publication Jais Rose Bjelke
Research & Early Development Novo Nordisk A/S Måløv Denmark
1 shared publication- Jais Rose Bjelke
Global Research, Novo Nordisk A/S, 2760 Måløv, Denmark
1 shared publication
Latest Publications
- Open Access
- 18 February 2022
- Published by Wiley in FEBS Letters
- Vol. 596 (12) , 1567-1575
Site‐specific functional roles of the Factor X activation peptide in the intrinsic tenase‐mediated Factor X activation
The conversion of zymogen Factor X (FX) to an active protease involves the removal of a 52‐residue long activation peptide (AP). Through site‐directed mutagenesis, we investigate the role of the AP and demonstrate that the high abundance of proline residues is important for efficient proteolysis of FX. Moreover, we identify an essential interaction site for Factor IXa (FIXa) between residues 22 and 30 (AP numbering) and find that the residues between 31 and 41 may provide an important interaction site for the intrinsic tenase complex, composed of Factor IXa (FIXa) and Factor VIIIa (FVIIIa). Finally, we suggest that the carbohydrate chain at Asn‐39 restricts the activator specificity, as elimination of this glycosylation site increases the activation rate for activation by FIXa and FXa.
- 18 February 2022
- Published by Wiley in FEBS Letters
- Vol. 596 (12) , 1567-1575
Open AccessSite‐specific functional roles of the Factor X activation peptide in the intrinsic tenase‐mediated Factor X activation
The conversion of zymogen Factor X (FX) to an active protease involves the removal of a 52‐residue long activation peptide (AP). Through site‐directed mutagenesis, we investigate the role of the AP and demonstrate that the high abundance of proline residues is important for efficient proteolysis of FX. Moreover, we identify an essential interaction site for Factor IXa (FIXa) between residues 22 and 30 (AP numbering) and find that the residues between 31 and 41 may provide an important interaction site for the intrinsic tenase complex, composed of Factor IXa (FIXa) and Factor VIIIa (FVIIIa). Finally, we suggest that the carbohydrate chain at Asn‐39 restricts the activator specificity, as elimination of this glycosylation site increases the activation rate for activation by FIXa and FXa.
- 20 December 2021
- Published by Elsevier in Journal of Thrombosis and Haemostasis
- Vol. 20 (3) , 589-599
The functional role of the autolysis loop in the regulation of factor X upon hemostatic response
- 20 December 2021
- Published by Elsevier in Journal of Thrombosis and Haemostasis
- Vol. 20 (3) , 589-599
The functional role of the autolysis loop in the regulation of factor X upon hemostatic response