Mertens K - Search Results

1

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.

2

Residues Phe342-Asn346 of activated coagulation factor IX contribute to the interaction with low density lipoprotein receptor-related protein.

Rohlena J, Kolkman JA, Boertjes RC, Mertens K, Lenting PJ. Rohlena J, et al. Among authors: mertens k. J Biol Chem. 2003 Mar 14;278(11):9394-401. doi: 10.1074/jbc.M209097200. Epub 2003 Jan 9. J Biol Chem. 2003. PMID: 12522212 Free article.

3

Clearance of coagulation factor VIII in very low-density lipoprotein receptor knockout mice.

Bovenschen N, van Dijk KW, Havekes LM, Mertens K, van Vlijmen BJ. Bovenschen N, et al. Among authors: mertens k. Br J Haematol. 2004 Sep;126(5):722-5. doi: 10.1111/j.1365-2141.2004.05093.x. Br J Haematol. 2004. PMID: 15327526 Free article.

4

LDL receptor cooperates with LDL receptor-related protein in regulating plasma levels of coagulation factor VIII in vivo.

Bovenschen N, Mertens K, Hu L, Havekes LM, van Vlijmen BJ. Bovenschen N, et al. Among authors: mertens k. Blood. 2005 Aug 1;106(3):906-12. doi: 10.1182/blood-2004-11-4230. Epub 2005 Apr 19. Blood. 2005. PMID: 15840700 Free article.

5

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

6

Functional duplication of ligand-binding domains within low-density lipoprotein receptor-related protein for interaction with receptor associated protein, alpha2-macroglobulin, factor IXa and factor VIII.

Meijer AB, Rohlena J, van der Zwaan C, van Zonneveld AJ, Boertjes RC, Lenting PJ, Mertens K. Meijer AB, et al. Among authors: mertens k. Biochim Biophys Acta. 2007 Jun;1774(6):714-22. doi: 10.1016/j.bbapap.2007.04.003. Epub 2007 Apr 14. Biochim Biophys Acta. 2007. PMID: 17512806

7

Factor VIII C1 domain residues Lys 2092 and Phe 2093 contribute to membrane binding and cofactor activity.

Meems H, Meijer AB, Cullinan DB, Mertens K, Gilbert GE. Meems H, et al. Among authors: mertens k. Blood. 2009 Oct 29;114(18):3938-46. doi: 10.1182/blood-2009-01-197707. Epub 2009 Aug 17. Blood. 2009. PMID: 19687511 Free article.

8

A single lysine of the two-lysine recognition motif of the D3 domain of receptor-associated protein is sufficient to mediate endocytosis by low-density lipoprotein receptor-related protein.

van den Biggelaar M, Sellink E, Klein Gebbinck JW, Mertens K, Meijer AB. van den Biggelaar M, et al. Among authors: mertens k. Int J Biochem Cell Biol. 2011 Mar;43(3):431-40. doi: 10.1016/j.biocel.2010.11.017. Epub 2010 Dec 7. Int J Biochem Cell Biol. 2011. PMID: 21144910

9

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

10

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.

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