Mertens K - Search Results

1

Probing activation-driven changes in coagulation factor IX by mass spectrometry.

Freato N, van Alphen FPJ, Boon-Spijker M, van den Biggelaar M, Meijer AB, Mertens K, Ebberink EHTM. Freato N, et al. Among authors: mertens k. J Thromb Haemost. 2021 Jun;19(6):1447-1459. doi: 10.1111/jth.15288. Epub 2021 Apr 5. J Thromb Haemost. 2021. PMID: 33687765 Free PMC article.

2

Factor VIII-driven changes in activated factor IX explored by hydrogen-deuterium exchange mass spectrometry.

Freato N, Ebberink EHTM, van Galen J, Fribourg C, Boon-Spijker M, van Alphen FPJ, Meijer AB, van den Biggelaar M, Mertens K. Freato N, et al. Among authors: mertens k. Blood. 2020 Dec 3;136(23):2703-2714. doi: 10.1182/blood.2020005593. Blood. 2020. PMID: 32678887 Free article.

3

The interface between the EGF2 domain and the protease domain in blood coagulation factor IX contributes to factor VIII binding and factor X activation.

Fribourg C, Meijer AB, Mertens K. Fribourg C, et al. Among authors: mertens k. Biochemistry. 2006 Sep 5;45(35):10777-85. doi: 10.1021/bi060451h. Biochemistry. 2006. PMID: 16939230

4

Mass spectrometry-assisted study reveals that lysine residues 1967 and 1968 have opposite contribution to stability of activated factor VIII.

Bloem E, Meems H, van den Biggelaar M, van der Zwaan C, Mertens K, Meijer AB. Bloem E, et al. Among authors: mertens k. J Biol Chem. 2012 Feb 17;287(8):5775-83. doi: 10.1074/jbc.M111.308627. Epub 2012 Jan 3. J Biol Chem. 2012. PMID: 22215677 Free PMC article.

5

A3 domain region 1803-1818 contributes to the stability of activated factor VIII and includes a binding site for activated factor IX.

Bloem E, Meems H, van den Biggelaar M, Mertens K, Meijer AB. Bloem E, et al. Among authors: mertens k. J Biol Chem. 2013 Sep 6;288(36):26105-26111. doi: 10.1074/jbc.M113.500884. Epub 2013 Jul 24. J Biol Chem. 2013. PMID: 23884417 Free PMC article.

6

Unique surface-exposed hydrophobic residues in the C1 domain of factor VIII contribute to cofactor function and von Willebrand factor binding.

Przeradzka MA, Freato N, Boon-Spijker M, van Galen J, van der Zwaan C, Mertens K, van den Biggelaar M, Meijer AB. Przeradzka MA, et al. Among authors: mertens k. J Thromb Haemost. 2020 Feb;18(2):364-372. doi: 10.1111/jth.14668. Epub 2019 Nov 28. J Thromb Haemost. 2020. PMID: 31675465 Free article.

7

Low density lipoprotein receptor-related protein and factor IXa share structural requirements for binding to the A3 domain of coagulation factor VIII.

Bovenschen N, Boertjes RC, van Stempvoort G, Voorberg J, Lenting PJ, Meijer AB, Mertens K. Bovenschen N, et al. Among authors: mertens k. J Biol Chem. 2003 Mar 14;278(11):9370-7. doi: 10.1074/jbc.M212053200. Epub 2003 Jan 8. J Biol Chem. 2003. PMID: 12522143 Free article.

8

C1 domain residues Lys 2092 and Phe 2093 are of major importance for the endocytic uptake of coagulation factor VIII.

Meems H, van den Biggelaar M, Rondaij M, van der Zwaan C, Mertens K, Meijer AB. Meems H, et al. Among authors: mertens k. Int J Biochem Cell Biol. 2011 Aug;43(8):1114-21. doi: 10.1016/j.biocel.2011.03.014. Epub 2011 Apr 8. Int J Biochem Cell Biol. 2011. PMID: 21497669

9

Distinct roles of Ser-764 and Lys-773 at the N terminus of von Willebrand factor in complex assembly with coagulation factor VIII.

Castro-Núñez L, Bloem E, Boon-Spijker MG, van der Zwaan C, van den Biggelaar M, Mertens K, Meijer AB. Castro-Núñez L, et al. Among authors: mertens k. J Biol Chem. 2013 Jan 4;288(1):393-400. doi: 10.1074/jbc.M112.400572. Epub 2012 Nov 20. J Biol Chem. 2013. PMID: 23168412 Free PMC article.

10

Factor VIII C1 domain spikes 2092-2093 and 2158-2159 comprise regions that modulate cofactor function and cellular uptake.

Bloem E, van den Biggelaar M, Wroblewska A, Voorberg J, Faber JH, Kjalke M, Stennicke HR, Mertens K, Meijer AB. Bloem E, et al. Among authors: mertens k. J Biol Chem. 2013 Oct 11;288(41):29670-9. doi: 10.1074/jbc.M113.473116. Epub 2013 Sep 5. J Biol Chem. 2013. PMID: 24009077 Free PMC article.

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