Mehmood, S., Thirup, S. S., Ahmed, S., Bashir, N., Saeed, A., Rafiq, M., Saeed, Q., Najam-ul-Haq, M., Khaliq, B., Ibrahim, M., Alonazi, W. B. & Akrem, A. (2024). Crystal structure of Kunitz-type trypsin inhibitor: Entomotoxic effect of native and encapsulated protein targeting gut trypsin of Tribolium castaneum Herbst. Computational and Structural Biotechnology Journal, 23, 3132-3142. https://doi.org/10.1016/j.csbj.2024.07.023

Kjærgaard, M., Rasmussen, L. S., Vinther, J. N., Andersen, K. R., Andersen, E. S., Lorentzen, E., Thirup, S. S., Otzen, D. & Brodersen, D. E. (2022). A Semester-Long Learning Path Teaching Computational Skills via Molecular Graphics in PyMOL. The Biophysicist, 3(2), 106–114. https://doi.org/10.35459/tbp.2022.000219

Jankowski, V., Saritas, T., Kjolby, M., Hermann, J., Speer, T., Himmelsbach, A., Mahr, K., Heuschkel, M. A., Schunk, S. J., Thirup, S., Winther, S., Bottcher, M., Nyegard, M., Nykjaer, A., Kramann, R., Kaesler, N., Jankowski, J., Floege, J., Marx, N. & Goettsch, C. (2022). Carbamylated sortilin associates with cardiovascular calcification in patients with chronic kidney disease. Kidney International, 101(3), 574-584. https://doi.org/10.1016/j.kint.2021.10.018

Vilstrup, J., Simonsen, A., Birkefeldt, T., Strandbygård, D., Lyngsø, J., Pedersen, J. S. & Thirup, S. (2020). Crystal and solution structures of fragments of the human leucocyte common antigen-related protein. Acta crystallographica Section D: Structural biology , 76, 406-417. https://doi.org/10.1107/S2059798320003885

Pallesen, L. T., Gustafsen, C., Cramer, J., Petersen, S. V., Thirup, S. S., Madsen, P. & Petersen, C. M. (2020). PAK kinases targets sortilin and modulates its sorting. Molecular and Cellular Biology, 40(3), Article e00411-19. https://doi.org/10.1128/MCB.00411-19

Wong, J. E. M. M., Nadzieja, M., Madsen, L. H., Bücherl, C. A., Dam, S., Sandal, N. N., Couto, D., Derbyshire, P., Uldum-Berentsen, M., Schroeder, S., Schwämmle, V., Nogueira, F. C. S., Asmussen, M. H., Thirup, S., Radutoiu, S., Blaise, M., Andersen, K. R., Menke, F. L. H., Zipfel, C. & Stougaard, J. (2019). A Lotus japonicus cytoplasmic kinase connects Nod factor perception by the NFR5 LysM receptor to nodulation. Proceedings of the National Academy of Sciences (PNAS), 116(28), 14339-14348. https://doi.org/10.1073/pnas.1815425116

Johansen, J. S., Kavaliauskas, D., Pfeil, S., Blaise , M., Cooperman, B., Goldman, Y., Thirup, S. S. & Knudsen, C. R. (2018). E. coli elongation factor Tu bound to a GTP analogue displays an open conformation equivalent to the GDP-bound form. Nucleic Acids Research, 46(16), 8641-8650. https://doi.org/10.1093/nar/gky697

Januliene, D., Andersen, J. L., Nielsen, J. A., Quistgaard, E. M., Hansen, M., Strandbygaard, D., Moeller, A., Petersen, C. M., Madsen, P. & Thirup, S. S. (2017). Acidic Environment Induces Dimerization and Ligand Binding Site Collapse in the Vps10p Domain of Sortilin. Structure, 25(12), 1809-1819.e3. Article 12. https://doi.org/10.1016/j.str.2017.09.015

Gustafsen, C., Olsen, D., Vilstrup, J., Lund, S., Reinhardt, A., Wellner, N., Larsen, T., Andersen, C. B. F., Weyer, K., Li, J.-P., Seeberger, P. H., Thirup, S., Madsen, P. & Glerup, S. (2017). Heparan sulfate proteoglycans present PCSK9 to the LDL receptor. Nature Communications, 8(1), 503. Article 503. https://doi.org/10.1038/s41467-017-00568-7

Januliene, D., Manavalan, A., Ovesen, P. L., Pedersen, K. M., Thirup, S., Nykjær, A. & Moeller, A. (2017). Hidden Twins: SorCS Neuroreceptors Form Stable Dimers. Journal of Molecular Biology, 429(19), 2907-2917. https://doi.org/10.1016/j.jmb.2017.08.006

Andersen, J. L., Lindberg, S., Langgård, M., Maltas, P. J., Rønn, L. C. B., Bundgaard, C., Strandbygaard, D., Thirup, S. & Watson, S. P. (2017). The identification of novel acid isostere based inhibitors of the VPS10P family sorting receptor Sortilin. Bioorganic & Medicinal Chemistry Letters, 27(11), 2629-2633. https://doi.org/10.1016/j.bmcl.2017.02.028

Wong, J. E. M. M., Midtgaard, S. R., Gysel, K., Thygesen, M. B., Sørensen, K. K., Jensen, K. J., Stougaard, J., Thirup, S. & Blaise, M. (2015). An intermolecular binding mechanism involving multiple LysM domains mediates carbohydrate recognition by an endopeptidase. Acta crystallographica Section D: Structural biology , 71(Pt 3), 592-605. https://doi.org/10.1107/S139900471402793X

Kawaharada, Y., Kelly, S., Nielsen, M. W., Hjuler, C. T., Gysel, K., Muszyński, A., Carlson, R. W., Thygesen, M. B., Sandal, N., Asmussen, M. H., Vinther, M., Andersen, S. U., Krusell, L., Thirup, S., Jensen, K. J., Ronson, C. W., Blaise, M., Radutoiu, S. & Stougaard, J. (2015). Receptor-mediated exopolysaccharide perception controls bacterial infection. Nature, 523, 308-312. https://doi.org/10.1038/nature14611

Thirup, S. S., Van, L. B., Nielsen, T. K. & Knudsen, C. R. (2015). Structural outline of the detailed mechanism for elongation factor Ts-mediated guanine nucleotide exchange on elongation factor Tu. Journal of Structural Biology, 191(1), 10-21. https://doi.org/10.1016/j.jsb.2015.06.011

Wong, J. E. M. M., Alsarraf, H. M. A. B., Kaspersen, J. D., Pedersen, J. S., Stougaard, J., Thirup, S. S. & Blaise, M. (2014). Cooperative binding of LysM domains determines the carbohydrate affinity of a bacterial endopeptidase protein. FEBS journal, 281(4), 1196-1208. https://doi.org/10.1111/febs.12698

Andersen, J. L., Schrøder, T. J., Christensen, S., Strandbygård, D. J., Pallesen, L. T., Garcia Alai, M. M., Lindberg, S., Langgård, M., Eskildsen, J. C., David, L., Tagmose, L., Simonsen, K. B., Maltas, P. J., Rønn, L. C. B., de Jong, I. E. M., Malik, I. J., Egebjerg, J., Karlsson, J. J., Uppalanchi, S. ... Thirup, S. (2014). Identification of the first small-molecule ligand of the neuronal receptor sortilin and structure determination of the receptor-ligand complex. Acta Crystallographica. Section D: Biological Crystallography, 70(Part 2), 451-460. https://doi.org/10.1107/S1399004713030149

Quistgaard, E. M., Grøftehauge, M. K., Madsen, P., Pallesen, L. T., Christensen, B. S., Sørensen, E. S., Nissen, P., Petersen, C. M. & Thirup, S. S. (2014). Revisiting the structure of the Vps10 domain of human sortilin and its interaction with neurotensin. Protein Science, 23(9), 1291-1300. https://doi.org/10.1002/pro.2512

Schrøder, T. J., Christensen, S., Lindberg, S., Langgård, M., David, L., Maltas, P. J., Eskildsen, J., Jacobsen, J., Tagmose, L., Simonsen, K. B., Biilmann Rønn, L. C., de Jong, I. E. M., Malik, I. J., Karlsson, J.-J., Bundgaard, C., Egebjerg, J., Stavenhagen, J. B., Strandbygård, D., Thirup, S. S. ... Watson, S. P. (2014). The identification of AF38469: An orally bioavailable inhibitor of the VPS10P family sorting receptor Sortilin: An orally bioavailable inhibitor of the VPS10P family sorting receptor Sortilin. Bioorganic & Medicinal Chemistry Letters, 24(1), 177-180. https://doi.org/10.1016/j.bmcl.2013.11.046

Blaise, M., Alsarraf, H. M. A. B., Wong, J., Roi Midtgaard, S., Laroche, F. J. F., Schack, L., Spaink, H., Stougaard, J. & Thirup, S. S. (2012). Crystal structure of the TLDc domain of oxidation resistance protein 2 from zebrafish. Proteins: Structure, Function, and Bioinformatics, 80(6), 1694-1698. https://doi.org/10.1002/prot.24050

Broghammer, A., Krusell, L., Blaise, M., Sauer, J., Sullivan, J. T., Maolanon, N. N., Vinther, M., Lorentzen, A. M., Madsen, E. B., Jensen, K. J., Roepstorff, P., Thirup, S. S., Ronson, C. W., Thygesen, M. B. & Stougaard, J. (2012). Legume receptors perceive the rhizobial lipochitin oligosaccharide signal molecules by direct binding. Proceedings of the National Academy of Sciences (PNAS), 109(34), 13859-13864. https://doi.org/10.1073/pnas.1205171109

Blaise, M. & Thirup, S. S. (2011). Crystallization of Escherichia coli maltoporin in the trigonal space group R3. Acta Crystallographica. Section F: Structural Biology and Crystallization Communications Online, 67.

Alsarraf, H. M. A. B., Laroche, F. J. F., Spaink, H., Thirup, S. S. & Blaise, M. (2011). Purification, crystallization and preliminary crystallographic studies of the TLDc domain of oxidation resistance protein 2 from zebrafish. Acta Crystallographica. Section F: Structural Biology and Crystallization Communications Online, 67(10).

Blaise, M., Bailly, M., Frechin, M., Behrens, M. A., Fischer, F., Oliveira, C. L. P., Becker, H. D., Pedersen, J. S., Thirup, S. & Kern, D. (2010). Crystal structure of a transfer-ribonucleoprotein particle that promotes asparagine formation. The EMBO Journal, 29(18), 3118-29. https://doi.org/10.1038/emboj.2010.192

Lohmann, G. V., Shimoda, Y., Nielsen, M. W., Jørgensen, F. G., Grossmann, C., Sandal, N., Sørensen, K., Thirup, S., Madsen, L. H., Tabata, S., Sato, S., Stougaard, J. & Radutoiu, S. (2010). Evolution and regulation of the Lotus japonicus LysM receptor gene family. Molecular plant-microbe interactions, 23(4), 510-21. https://doi.org/10.1094/MPMI-23-4-0510

Cramer, J. F., Gustafsen, C., Behrens, M. A., Oliveira, C. L. P., Pedersen, J. S., Madsen, P., Petersen, C. M. & Thirup, S. S. (2010). GGA autoinhibition revisited. Traffic, 11(2), 259-73. https://doi.org/10.1111/j.1600-0854.2009.01017.x

Bek, A. S., Sauer, J., Thygesen, M. B., Duus, J. Ø., Petersen, B. O., Thirup, S., James, E., Jensen, K. J., Stougaard, J. & Radutoiu, S. (2010). Improved Characterization of Nod Factors and Genetically Based Variation in LysM Receptor Domains Identify Amino Acids Expendable for Nod Factor Recognition in Lotus spp. Molecular plant-microbe interactions, 23(1), 58-66. https://doi.org/10.1094/MPMI-23-1-0058

Bailly, M., Blaise, M., Lorber, B., Thirup, S. S. & Kern, D. (2009). Isolation, crystallization and preliminary X-ray analysis of the transamidosome, a ribonucleoprotein involved in asparagine formation. Acta Crystallographica. Section F: Structural Biology and Crystallization Communications Online, 65(Pt 6), 577-81. https://doi.org/10.1107/S1744309109015000

Quistgaard, E. M., Madsen, P., Grøftehauge, M. K., Nissen, P., Petersen, C. M. & Thirup, S. S. (2009). Ligands bind to Sortilin in the tunnel of a ten-bladed beta-propeller domain. Nature Structural and Molecular Biology, 16(1), 96-8. https://doi.org/10.1038/nsmb.1543

Quistgaard, E. M. H. & Thirup, S. S. (2009). Sequence and structural analysis of the Asp-box motif and Asp-box beta-propellers; a widespread propeller-type characteristic of the Vps10 domain family and several glycoside hydrolase families. B M C Structural Biology, 9. https://doi.org/10.1186/1472-6807-9-46

Nielsen, M. J., Petersen, S. V., Jacobsen, C., Thirup, S. S., Enghild, J. J., Graversen, J. H. & Moestrup, S. K. (2007). A unique loop extension in the serine protease domain of haptoglobin is essential for CD163 recognition of the haptoglobin-hemoglobin complex. Journal of Biological Chemistry, 282(2), 1072-1079.

Radutoiu, S., Madsen, L. H., Madsen, E. B., Jurkiewicz, A., Fukai, E., Quistgaard, E. M. H., Albrektsen, A. S., James, E. K., Thirup, S. & Stougaard, J. (2007). LysM domains mediate lipochitin-oligosaccharide recognition and Nfr genes extend the symbiotic host range. E M B O Journal, 26(17), 3923-35. https://doi.org/10.1038/sj.emboj.7601826

Karring, H., Björnsson, A., Thirup, S., Clark, B. F. C. & Knudsen, C. R. (2003). Functional effects of deleting the coiled-coil motif in Escherichia coli elongation factor Ts. FEBS journal, 270, 4294-4305.

Karring, H., Andersen, G. R., Thirup, S. S., Nyborg, J., Spremulli, L. L. & Clark, B. F. C. (2002). Isolation, crystallisation, and preliminary X-ray analysis of the bovine mitochondrial EF-Tu:GDP and EF-Tu:EF-Ts complexes. Biochim. Biophys. Acta., 1601(2), 172-177.

Andersen, G. R., Thirup, S., Spremulli, L. L. & Nyborg, J. (2000). High resolution crystal structure of bovine mitochondrial EF-Tu in complex with GDP. J. Mol. Biol., 297, 421-436.

Clark, B. F. C., Thirup, S., Kjeldgaard, M. & Nyborg, J. (1999). Structural information for explaining the molecular mechanism of protein biosynthesis (minireview). FEBS Letters, 452, 41-46.

Nissen, P., Thirup, S., Kjeldgaard, M. & Nyborg, J. (1999). The crystal structure of Cys-tRNA^Cys--EF-Tu--GDPNP reveals general and specific features in the ternary complex and in tRNA. Structure, 7, 143-156.

Discipio, R. G., Jenner, L., Thirup, S., Sottrup-Jensen, L., Nyborg, J. & Stura, E. (1998). Crystallization of human complement component C5. Acta Crystallographica. Section D: Biological Crystallography, 54(Pt 4), 643-6.

Jenner, L., Husted, L., Thirup, S., Sottrup-Jensen, L. & Nyborg, J. (1998). Crystal structure of the receptor-binding domain of alpha 2-macroglobulin. Structure, 6(5), 595-604.

Nolsø, S., Thirup, S. S., Etzerodt, M., Thøgersen, H. C. & Nyborg, J. (1997). Crystallisation and preliminary X-ray diffraction studies of psoriasin. Acta crystallographica Section D: Structural biology, 53(1), 119-121.

Nolsøe, S., Thirup, S., Etzerodt, M., Thøgersen, H. C. & Nyborg, J. (1997). Crystallization and preliminary X-ray diffraction studies of psoriasin. Acta Crystallographica Section D: Biological Crystallography, 53(1), 119-121. https://doi.org/10.1107/S0907444996008955

Nyborg, J., Nissen, P., Kjeldgaard, M., Thirup, S., Polekhina, G., Clark, B. F. & Reshetnikova, L. (1997). Macromolecular mimicry in protein biosynthesis. Structure, 2(3), S7-11.

Polekhina, G., Thirup, S., Kjeldgaard, M., Nissen, P., Lippmann, C. & Nyborg, J. (1996). Helix unwinding in the effector region of elongation factor EF-Tu-GDP. Structure, 4(10), 1141-51.

Kristensen, O., Reshetnikova, L., Nissen, P., Siboska, G., Thirup, S. & Nyborg, J. (1996). Isolation, crystallization and X-ray analysis of the quaternary complex of Phe-tRNA(Phe), EF-Tu, a GTP analog and kirromycin. FEBS Letters, 399(1-2), 59-62.

Nyborg, J., Nissen, P., Kjeldgaard, M., Thirup, S., Polekhina, G. & Clark, B. F. (1996). Structure of the ternary complex of EF-Tu: macromolecular mimicry in translation. Trends in Biochemical Sciences, 21(3), 81-2.

Nissen, P., Kjeldgaard, M., Thirup, S., Clark, B. F. & Nyborg, J. (1996). The ternary complex of aminoacylated tRNA and EF-Tu-GTP. Recognition of a bond and a fold. Biochimie, 78(11-12), 921-33.