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Klinger, S. C., Glerup, S., Raarup, M. K., Mari, M. C., Nyegaard, M., Koster, G., Prabakaran, T., Nilsson, B. S., Kjaergaard, M. M., Bakke, O., Nykjær, A., Olivecrona, G., Petersen, C. M. & Nielsen, M. S. (2011). SorLA regulates the activity of lipoprotein lipase by intracellular trafficking. Journal of Cell Science, 124(Pt 7), 1095-105. https://doi.org/10.1242/jcs.072538
Vaegter, C. B., Jansen, P., Fjorback, A. W., Glerup, S., Skeldal, S., Kjølby, M. F., Richner, M., Erdmann, B., Nyengaard, J. R., Tessarollo, L., Lewin, G. R., Willnow, T. E., Chao, M. V. & Nykjaer, A. (2011). Sortilin associates with Trk receptors to enhance anterograde transport and neurotrophin signaling. Nature Neuroscience, 14(1), 54-61. https://doi.org/10.1038/nn.2689
Andersen, O. S., Boisguerin, P., Glerup, S., Skeldal, S., Volkmer, R., Wilnow, T. E., Nykjær, A. & Andersen, O. M. (2010). Identification of a linear epitope in sortilin that partakes in pro-neurotropin binding. Journal of Biological Chemistry, 12210-12222.
Terkelsen, C. J., Oxvig, C., Nørgaard, B. L., Glerup, S., Poulsen, T. S., Lassen, J. F., Møller, H. J., Thuesen, L., Falk, E., Nielsen, T. T. & Andersen, H. R. (2008). Temporal course of pregnancy-associated plasma protein-A in angioplasty-treated ST-elevation myocardial infarction patients and potential significance of concomitant heparin administration. American Journal of Cardiology, 103(1), 29-35. https://doi.org/10.1016/j.amjcard.2008.08.027
Glerup, S., Kløverpris, S., Laursen, L. S., Dagnaes-Hansen, F., Thiel, S., Conover, C. A. & Oxvig, C. (2007). Cell surface detachment of pregnancy-associated plasma protein-A requires the formation of intermolecular proteinase-inhibitor disulfide bonds and glycosaminoglycan covalently bound to the inhibitor. Journal of Biological Chemistry, 282(3), 1769-1778. https://doi.org/10.1074/jbc.M608454200
Glerup, S. (2007). Inhibition of proteolysis and prohormone conversion by proMBP.
Boldt, H. B., Glerup, S., Overgaard, M. T., Sottrup-Jensen, L. & Oxvig, C. (2006). Definition, expression, and characterization of a protein domain in the N-terminus of pregnancy-associated plasma protein-A distantly related to the family of laminin G-like modules. Protein Expr Purif., 48(2), 261-73.
Glerup, S., Kløverpris, S. & Oxvig, C. (2006). Proform of eosinophil major basic protein binds the cell surface through a site distinct from its c-type lectin ligand-binding region. Journal of Biological Chemistry, 281, 31509-31516.
Glerup, S., Kløverpris, S. & Oxvig, C. (2006). The proform of the eosinophil major basic protein binds the cell surface through a site distinct from its C-type lectin ligand-binding region. Journal of Biological Chemistry, 281(42), 31509-31516. https://doi.org/10.1074/jbc.M605824200
Glerup, S., Boldt, H. B., Overgaard, M., Sottrup-Jensen, L., Giudice, L. C. & Oxvig, C. (2005). Proteinase inhibition by proform of eosinophil major basic protein (pro-MBP is a multistep process of intra- and intermolecular disulfide rearrangements). Journal of Biological Chemistry, 280, 9823-9832.
Overgaard, M. T., Glerup, S., Boldt, H. B., Olsen, I. M., Christiansen, M., Sottrup-Jensen, L., Giudice, L. C. & Oxvig, C. (2004). Inhibition of proteolysis by the proform of eosinophil major basic protein (proMBP) requires covalent binding to its target proteinase. FEBS Letters, 560, 147-152.
Overgaard, M. T., Glerup, S., Boldt, H. B., Rodacker, V., Marie Olsen, I., Christiansen, M., Sottrup-Jensen, L., Giudice, L. C. & Oxvig, C. (2004). Inhibition of proteolysis by the proform of eosinophil major basic protein (proMBP) requires covalent binding to its target proteinase. FEBS Letters, 560, 147-152.

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Susanne Schousboe Sjøgaard