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.
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
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
Andersen, G. R., Stepanov, V. G., Kjeldgaard, M.
, Thirup, S. S., Nyborg, J., Garrett, R. A. (Ed.), Douthwaite, S. R. (Ed.), Liljas, A. (Ed.), Matheson, A. T. (Ed.), Moore, P. B. (Ed.) & Noller, H. F. (Ed.) (2000).
Ternary complex of EF-Tu and its action on the ribosome. In
The Ribosome: Structure, Function, Antibiotics, and Cellular Interactions (pp. 337-345). ASM Press.
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.
Clark, B. F., Kjeldgaard, M., la Cour, T. F.
, Thirup, S. & Nyborg, J. (1990).
Structural determination of the functional sites of E. coli elongation factor Tu.
BBA General Subjects,
1050(1-3), 203-8.
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.
... Nykjaer, A. (2020).
SorCS1 binds the insulin receptor to enhance insulin sensitivity. bioRxiv.
https://doi.org/10.1101/2020.11.10.376178
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
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
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).
Nissen, P., Reshetnikova, L., Siboska, G., Polekhina, G.
, Thirup, S., Kjeldgaard, M., Clark, B. F. & Nyborg, J. (1994).
Purification and crystallization of the ternary complex of elongation factor Tu:GTP and Phe-tRNA(Phe).
F E B S Letters,
356(2-3), 165-8.
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
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.
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
Andersen, G. R., Thirup, S., Nyborg, J., Dolmer, K., Jacobsen, L. & Sottrup-Jensen, L. (1994).
Low-resolution X-ray diffraction data obtained from hexagonal crystals of methylamine-treated alpha2-macroglobulin.
Acta Crystallographica Section D: Biological Crystallography,
50(3), 298-301.
https://doi.org/10.1107/S0907444993013125
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
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,
109(34), 13859-13864.
https://doi.org/10.1073/pnas.1205171109
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.
F E B S Letters,
399(1-2), 59-62.
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
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.
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
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
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
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
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.
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
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.
F E B S Journal,
270, 4294-4305.
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
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
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).
Design of specific ligands to Sortilin. (Patent No.
PA 2008 00592).
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).
Design and use of Sortilin specific molecular imaging ligands. (Patent No.
PA 2008 00593).
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
Nissen, P., Kjeldgaard, M.
, Thirup, S., Polekhina, G., Reshetnikova, L., Clark, B. F. & Nyborg, J. (1995).
Crystal structure of the ternary complex of Phe-tRNAPhe, EF-Tu, and a GTP analog.
Science,
270(5241), 1464-72.
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.
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
Andersen, G. R., Koch, T., Sørensen, A. H.
, Thirup, S., Nyborg, J., Dolmer, K., Jacobsen, L. & Sottrup-Jensen, L. (1994).
Crystallization of proteins of the alpha 2-macroglobulin superfamily.
New York Academy of Sciences. Annals,
737, 444-6.
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.
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
Andersen, G. R., Jacobsen, L.
, Thirup, S., Nyborg, J. & Sottrup-Jensen, L. (1991).
Crystallization and preliminary X-ray analysis of methylamine-treated alpha 2-macroglobulin and 3 alpha 2-macroglobulin-proteinase complexes.
F E B S Letters,
292(1-2), 267-70.
Nolsø, S.
, Thirup, S. S., Etzerodt, M., Thøgersen, H. C. & Nyborg, J. (1997).
Crystallisation and preliminary X-ray diffraction studies of psoriasin.
Acta Crystallogr. D. Biol. Crystallogr.,
53(1), 119-121.
Dolmer, K., Jenner, L. B., Jacobsen, L.
, Andersen, G. R., Koch, T. J.
, Thirup, S., Sottrup-Jensen, L. & Nyborg, J. (1995).
Crystallisation and preliminary X-ray analysis of the receptor-binding domain of human and bovine alpha 2-macroglobulin.
F E B S Letters,
372(1), 93-5.