Aarhus Universitets segl

Søren Skou Thirup

Lektor

Søren Skou Thirup

Lektor

  • Institut for Molekylærbiologi og Genetik - Proteinvidenskab
Postaddresse:
Universitetsbyen 81
1872, 416
8000
Aarhus C
Danmark

E-mail: sth@mbg.au.dk

Mobil: +4520585981

Ansættelse

1997 – nu : Lektor ved Institut for Molekylærbiologi og Genetik, Aarhus University.
1993 – 1997: Adjunkt ved Kemisk Institut, Aarhus University.
1986 – 1993: Post doc ved Kemisk Institut, Aarhus University.
1984 – 1986: EMBO long-term fellowship at Dept. of Molecular Biology, Uppsala University

Uddannelse

November 1992: PhD i Biostrukturkemi, Aarhus Universitet
April 1984: cand. scient. i Kemi og Fysik, Aarhus Universitet


Scientific summary

Structure and function of the Sortilins in sorting, endocytosis and signalling.
Methods employed include high-level purification of biological macromolecules and assemblies in defined functional states. Crystallization and X-ray crystallographic structure determination of macromolecules, including protein-protein and protein-ligand complexes. Determination of binding constants using biophysical methods. Bioinformatics analysis of sequences and structures. X-ray techniques: generators, optics and detectors.
63 publications - 4115 citations - h=23 (WoS)2 patents
63 publications - 4115 citations - h=23 (WoS)
2 patents63 publications - 4115 citations - h=23 (WoS)
2 patents63 publications - 4115 citations - h=23 (WoS)
2 patents

Publikationer

A Semester-Long Learning Path Teaching Computational Skills via Molecular Graphics in PyMOL

Kjærgaard, M., Rasmussen, L. S., Vinther, J. N., Andersen, K. R., Andersen, E. S., Lorentzen, E., Thirup, S. S., Otzen, D. & Brodersen, D. E., dec. 2022, I: The Biophysicist. 3, 2, s. 106–114 9 s.

Carbamylated sortilin associates with cardiovascular calcification in patients with chronic kidney disease

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., mar. 2022, I: Kidney International. 101, 3, s. 574-584

SorCS1 binds the insulin receptor to enhance insulin sensitivity

Kjolby, M., Pedersen, K. M., Breining, P., Wellner, N., Sørensen, K. M. J., Vittrup, D. M., Gjesing, A. M. P., Januliene, D., Manavalan, A., Rotman, M., Thotakura, G., Skeldal, S., Madsen, P., Thirup, S., Hermey, G., Vaegter, C. B., Möller, A., Asplund, O., Prasad, R. B., Parlevliet, E. T., Rensen, P. C. N., Füchtbauer, E. M., Madsen, A. N., Holst, B., Andersen, O. M., Hansen, T. & Nykjaer, A., 1 nov. 2020, bioRxiv.

Crystal and solution structures of fragments of the human leucocyte common antigen-related protein

Vilstrup, J., Simonsen, A., Birkefeldt, T., Strandbygård, D., Lyngsø, J., Pedersen, J. S. & Thirup, S., maj 2020, I: Acta crystallographica Section D: Structural biology . 76, s. 406-417 12 s.

PAK kinases targets sortilin and modulates its sorting

Pallesen, L. T., Gustafsen, C., Cramer, J., Petersen, S. V., Thirup, S. S., Madsen, P. & Petersen, C. M., feb. 2020, I: Molecular and Cellular Biology. 40, 3, 16 s., e00411-19.

A Lotus japonicus cytoplasmic kinase connects Nod factor perception by the NFR5 LysM receptor to nodulation

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, I: Proceedings of the National Academy of Sciences of the United States of America. 116, 28, s. 14339-14348 10 s.

E. coli elongation factor Tu bound to a GTP analogue displays an open conformation equivalent to the GDP-bound form

Johansen, J. S., Kavaliauskas, D., Pfeil, S., Blaise, M., Cooperman, B., Goldman, Y., Thirup, S. S. & Knudsen, C. R., 19 sep. 2018, I: Nucleic Acids Research. 46, 16, s. 8641-8650 10 s.

Acidic Environment Induces Dimerization and Ligand Binding Site Collapse in the Vps10p Domain of Sortilin

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., 5 dec. 2017, I: Structure. 25, 12, s. 1809-1819.e3 14 s., 12.

Hidden Twins: SorCS Neuroreceptors Form Stable Dimers

Januliene, D., Manavalan, A., Ovesen, P. L., Pedersen, K. M., Thirup, S., Nykjær, A. & Moeller, A., 15 sep. 2017, I: Journal of Molecular Biology. 429, 19, s. 2907-2917 11 s.

Heparan sulfate proteoglycans present PCSK9 to the LDL receptor

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., 11 sep. 2017, I: Nature Communications. 8, 1, s. 503

The identification of novel acid isostere based inhibitors of the VPS10P family sorting receptor Sortilin

Andersen, J. L., Lindberg, S., Langgård, M., Maltas, P. J., Rønn, L. C. B., Bundgaard, C., Strandbygaard, D., Thirup, S. & Watson, S. P., 1 jun. 2017, I: Bioorganic & Medicinal Chemistry Letters. 27, 11, s. 2629-2633 5 s.

Receptor-mediated exopolysaccharide perception controls bacterial infection

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., 16 jul. 2015, I: Nature. 523, s. 308-312 5 s.

Structural outline of the detailed mechanism for elongation factor Ts-mediated guanine nucleotide exchange on elongation factor Tu

Thirup, S. S., Van, L. B., Nielsen, T. K. & Knudsen, C. R., 11 jun. 2015, I: Journal of Structural Biology. 191, 1, s. 10-21 12 s.

An intermolecular binding mechanism involving multiple LysM domains mediates carbohydrate recognition by an endopeptidase

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., mar. 2015, I: Acta crystallographica Section D: Structural biology . 71, Pt 3, s. 592-605 14 s.

Revisiting the structure of the Vps10 domain of human sortilin and its interaction with neurotensin

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., sep. 2014, I: Protein Science. 23, 9, s. 1291-1300 10 s.

Cooperative binding of LysM domains determines the carbohydrate affinity of a bacterial endopeptidase protein

Wong, J. E. M. M., Alsarraf, H. M. A. B., Kaspersen, J. D., Pedersen, J. S., Stougaard, J., Thirup, S. S. & Blaise, M., feb. 2014, I: F E B S Journal. 281, 4, s. 1196-1208 13 s.

Identification of the first small-molecule ligand of the neuronal receptor sortilin and structure determination of the receptor-ligand complex

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., Sakumudi, D. R., Eradi, P., Watson, S. P. & Thirup, S., feb. 2014, I: Acta Crystallographica. Section D: Biological Crystallography. 70, Part 2, s. 451-460 10 s.

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

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., Andersen, J. L., Uppalanchi, S., Pervaram, S., Kasturi, S. P., Eradi, P., Sakumudi, D. R. & Watson, S. P., 1 jan. 2014, I: Bioorganic & Medicinal Chemistry Letters. 24, 1, s. 177-180 4 s.

Legume receptors perceive the rhizobial lipochitin oligosaccharide signal molecules by direct binding

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., 21 aug. 2012, I: Proceedings of the National Academy of Sciences of the United States of America. 109, 34, s. 13859-13864 6 s.

Crystal structure of the TLDc domain of oxidation resistance protein 2 from zebrafish

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., jun. 2012, I: Proteins: Structure, Function, and Bioinformatics. 80, 6, s. 1694-1698 5 s.

Up, down, and around: Identifying recurrent interactions within and between super-secondary structures in β-propellers

Thirup, S. S., Gupta, V. & Quistgaard, E. M. H., 2012, Protein Supersecondary Structures. Kister, A. E. (red.). Humana Press, s. 35-50 16 s. (Methods in Molecular Biology, Bind 932).

Purification, crystallization and preliminary crystallographic studies of the TLDc domain of oxidation resistance protein 2 from zebrafish

Alsarraf, H. M. A. B., Laroche, F. J. F., Spaink, H., Thirup, S. S. & Blaise, M., okt. 2011, I: Acta Crystallographica. Section F: Structural Biology and Crystallization Communications Online. 67, 10

Crystallization of Escherichia coli maltoporin in the trigonal space group R3.

Blaise, M. & Thirup, S. S., 1 jan. 2011, I: Acta Crystallographica. Section F: Structural Biology and Crystallization Communications Online. 67

Crystal structure of a transfer-ribonucleoprotein particle that promotes asparagine formation

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., 15 sep. 2010, I: The EMBO Journal. 29, 18, s. 3118-29 12 s.

Characterization of LysM-receptors and their ligands involved in development and regulation of legume-rhizobium symbiosis

Broghammer, A., Krusell, L., Blaise, M., Thirup, S. S. & Stougaard, J., sep. 2010. 1 s.

Design and use of Sortilin specific molecular imaging ligands

Thirup, S. S., Grøftehauge, M. K., Madsen, P. S., Petersen, C. M., Nissen, P., Quistgaard, E. M. H., Andersen, J. L. & Cramer, J. F., 2010, Patentnr. PA 2008 00593

Design of specific ligands to Sortilin

Thirup, S. S., Petersen, C. M., Quistgaard, E. M. H., Madsen, P. S., Nissen, P., Grøftehauge, M. K., Cramer, J. F. & Andersen, J. L., 2010, Patentnr. PA 2008 00592

Evolution and regulation of the Lotus japonicus LysM receptor gene family

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, I: Molecular Plant - Microbe Interactions. 23, 4, s. 510-21 11 s.

GGA autoinhibition revisited

Cramer, J. F., Gustafsen, C., Behrens, M. A., Oliveira, C. L. P., Pedersen, J. S., Madsen, P., Petersen, C. M. & Thirup, S. S., 2010, I: Traffic. 11, 2, s. 259-73 14 s.

Improved Characterization of Nod Factors and Genetically Based Variation in LysM Receptor Domains Identify Amino Acids Expendable for Nod Factor Recognition in Lotus spp

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, I: Molecular Plant - Microbe Interactions. 23, 1, s. 58-66 8 s.

Isolation, crystallization and preliminary X-ray analysis of the transamidosome, a ribonucleoprotein involved in asparagine formation

Bailly, M., Blaise, M., Lorber, B., Thirup, S. S. & Kern, D., 2009, I: Acta Crystallographica. Section F: Structural Biology and Crystallization Communications Online. 65, Pt 6, s. 577-81 4 s.

Ligands bind to Sortilin in the tunnel of a ten-bladed beta-propeller domain

Quistgaard, E. M., Madsen, P., Grøftehauge, M. K., Nissen, P., Petersen, C. M. & Thirup, S. S., 2009, I: Nature Structural and Molecular Biology. 16, 1, s. 96-8 3 s.

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

Quistgaard, E. M. H. & Thirup, S. S., 2009, I: B M C Structural Biology. 9

A unique loop extension in the serine protease domain of haptoglobin is essential for CD163 recognition of the haptoglobin-hemoglobin complex

Nielsen, M. J., Petersen, S. V., Jacobsen, C., Thirup, S. S., Enghild, J. J., Graversen, J. H. & Moestrup, S. K., 2007, I: Journal of Biological Chemistry. 282, 2, s. 1072-1079 8 s.

LysM domains mediate lipochitin-oligosaccharide recognition and Nfr genes extend the symbiotic host range.

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, I: E M B O Journal. 26, 17, s. 3923-35 12 s.

Functional effects of deleting the coiled-coil motif in Escherichia coli elongation factor Ts

Karring, H., Björnsson, A., Thirup, S., Clark, B. F. C. & Knudsen, C. R., 2003, I: F E B S Journal. 270, s. 4294-4305 12 s.

Isolation, crystallisation, and preliminary X-ray analysis of the bovine mitochondrial EF-Tu:GDP and EF-Tu:EF-Ts complexes

Karring, H., Andersen, G. R., Thirup, S. S., Nyborg, J., Spremulli, L. L. & Clark, B. F. C., 2002, I: Biochim. Biophys. Acta.. 1601, 2, s. 172-177 6 s.

High resolution crystal structure of bovine mitochondrial EF-Tu in complex with GDP

Andersen, G. R., Thirup, S., Spremulli, L. L. & Nyborg, J., 2000, I: J. Mol. Biol.. 297, s. 421-436 16 s.

Ternary complex of EF-Tu and its action on the ribosome

Andersen, G. R., Stepanov, V. G., Kjeldgaard, M., Thirup, S. S., Nyborg, J., Garrett, R. A. (red.), Douthwaite, S. R. (red.), Liljas, A. (red.), Matheson, A. T. (red.), Moore, P. B. (red.) & Noller, H. F. (red.), 2000, The Ribosome: Structure, Function, Antibiotics, and Cellular Interactions. Washington DC: ASM Press, s. 337-345 9 s.

Structural information for explaining the molecular mechanism of protein biosynthesis (minireview)

Clark, B. F. C., Thirup, S., Kjeldgaard, M. & Nyborg, J., 1999, I: F E B S Letters. 452, s. 41-46 6 s.

The crystal structure of Cys-tRNACys--EF-Tu--GDPNP reveals general and specific features in the ternary complex and in tRNA

Nissen, P., Thirup, S., Kjeldgaard, M. & Nyborg, J., 1999, I: Structure. 7, s. 143-156 14 s.

Crystal structure of the receptor-binding domain of alpha 2-macroglobulin

Jenner, L., Husted, L., Thirup, S., Sottrup-Jensen, L. & Nyborg, J., 1998, I: Structure. 6, 5, s. 595-604 9 s.

Crystallization of human complement component C5

Discipio, R. G., Jenner, L., Thirup, S., Sottrup-Jensen, L., Nyborg, J. & Stura, E., 1998, I: Acta Crystallographica. Section D: Biological Crystallography. 54, Pt 4, s. 643-6 3 s.

Crystallization and preliminary X-ray diffraction studies of psoriasin

Nolsøe, S., Thirup, S., Etzerodt, M., Thøgersen, H. C. & Nyborg, J., 5 apr. 1997, I: Acta Crystallographica Section D: Biological Crystallography. 53, 1, s. 119-121 3 s.

Crystallisation and preliminary X-ray diffraction studies of psoriasin

Nolsø, S., Thirup, S. S., Etzerodt, M., Thøgersen, H. C. & Nyborg, J., 1997, I: Acta Crystallogr. D. Biol. Crystallogr.. 53, 1, s. 119-121

Macromolecular mimicry in protein biosynthesis

Nyborg, J., Nissen, P., Kjeldgaard, M., Thirup, S., Polekhina, G., Clark, B. F. & Reshetnikova, L., 1997, I: Structure. 2, 3, s. S7-11

Helix unwinding in the effector region of elongation factor EF-Tu-GDP

Polekhina, G., Thirup, S., Kjeldgaard, M., Nissen, P., Lippmann, C. & Nyborg, J., 1996, I: Structure. 4, 10, s. 1141-51 10 s.

Isolation, crystallization and X-ray analysis of the quaternary complex of Phe-tRNA(Phe), EF-Tu, a GTP analog and kirromycin

Kristensen, O., Reshetnikova, L., Nissen, P., Siboska, G., Thirup, S. & Nyborg, J., 1996, I: F E B S Letters. 399, 1-2, s. 59-62 3 s.

Structure of the ternary complex of EF-Tu: macromolecular mimicry in translation

Nyborg, J., Nissen, P., Kjeldgaard, M., Thirup, S., Polekhina, G. & Clark, B. F., 1996, I: Trends in Biochemical Sciences. 21, 3, s. 81-2 1 s.

The ternary complex of aminoacylated tRNA and EF-Tu-GTP. Recognition of a bond and a fold

Nissen, P., Kjeldgaard, M., Thirup, S., Clark, B. F. & Nyborg, J., 1996, I: Biochimie. 78, 11-12, s. 921-33 12 s.

Analysis and crystallization of a 25 kDa C-terminal fragment of cloned elongation factor Ts from Escherichia coli

Bøgestrand, S., Wiborg, O., Thirup, S. & Nyborg, J., 1995, I: F E B S Letters. 368, 1, s. 49-54 5 s.

Crystal structure of the ternary complex of Phe-tRNAPhe, EF-Tu, and a GTP analog

Nissen, P., Kjeldgaard, M., Thirup, S., Polekhina, G., Reshetnikova, L., Clark, B. F. & Nyborg, J., 1995, I: Science. 270, 5241, s. 1464-72 8 s.

Crystallisation and preliminary X-ray analysis of the receptor-binding domain of human and bovine alpha 2-macroglobulin

Dolmer, K., Jenner, L. B., Jacobsen, L., Andersen, G. R., Koch, T. J., Thirup, S., Sottrup-Jensen, L. & Nyborg, J., 1995, I: F E B S Letters. 372, 1, s. 93-5 2 s.

Crystallization of human methylamine-treated complement C3 and C3b

Dolmer, K., Thirup, S., Andersen, G. R., Sottrup-Jensen, L. & Nyborg, J., 1 jan. 1994, I: Acta Crystallographica Section D: Biological Crystallography. 50, 5, s. 786-789 4 s.

Low-resolution X-ray diffraction data obtained from hexagonal crystals of methylamine-treated alpha2-macroglobulin

Andersen, G. R., Thirup, S., Nyborg, J., Dolmer, K., Jacobsen, L. & Sottrup-Jensen, L., 1 jan. 1994, I: Acta Crystallographica Section D: Biological Crystallography. 50, 3, s. 298-301 4 s.

Crystallization of proteins of the alpha 2-macroglobulin superfamily

Andersen, G. R., Koch, T., Sørensen, A. H., Thirup, S., Nyborg, J., Dolmer, K., Jacobsen, L. & Sottrup-Jensen, L., 1994, I: New York Academy of Sciences. Annals. 737, s. 444-6 2 s.

Purification and crystallization of the ternary complex of elongation factor Tu:GTP and Phe-tRNA(Phe)

Nissen, P., Reshetnikova, L., Siboska, G., Polekhina, G., Thirup, S., Kjeldgaard, M., Clark, B. F. & Nyborg, J., 1994, I: F E B S Letters. 356, 2-3, s. 165-8 3 s.

The crystal structure of elongation factor EF-Tu from Thermus aquaticus in the GTP conformation

Kjeldgaard, M., Nissen, P., Thirup, S. & Nyborg, J., 1993, I: Structure. 1, 1, s. 35-50 15 s.

Crystallization and preliminary X-ray analysis of methylamine-treated alpha 2-macroglobulin and 3 alpha 2-macroglobulin-proteinase complexes

Andersen, G. R., Jacobsen, L., Thirup, S., Nyborg, J. & Sottrup-Jensen, L., 1991, I: F E B S Letters. 292, 1-2, s. 267-70 3 s.

ALMA, an editor for large sequence alignments

Thirup, S. & Larsen, N. E., 1990, I: Proteins: Structure, Function, and Bioinformatics. 7, 3, s. 291-5 4 s.

Structural determination of the functional sites of E. coli elongation factor Tu

Clark, B. F., Kjeldgaard, M., la Cour, T. F., Thirup, S. & Nyborg, J., 1990, I: BBA General Subjects. 1050, 1-3, s. 203-8 5 s.

Using known substructures in protein model building and crystallography

Jones, T. A. & Thirup, S., 1986, I: E M B O Journal. 5, 4, s. 819-22 3 s.

Structural details of the binding of guanosine diphosphate to elongation factor Tu from E. coli as studied by X-ray crystallography

la Cour, T. F., Nyborg, J., Thirup, S. & Clark, B. F., 1985, I: E M B O Journal. 4, 9, s. 2385-8 3 s.