Structure, 1878-4186

Journal

  1. 2020
  2. 2019
  3. 2018
  4. Baker, L. A., Sinnige, T., Schellenberger, P., de Keyzer, J., Siebert, C. A., Driessen, A. J. M., Baldus, M., & Grünewald, K. (2018). Combined 1H-Detected Solid-State NMR Spectroscopy and Electron Cryotomography to Study Membrane Proteins across Resolutions in Native Environments. Structure, 26(1), 161-170. [j.str.2017.11.011]. https://doi.org/10.1016/j.str.2017.11.011
  5. 2017
  6. Sardis, M. F., Tsirigotaki, A., Chatzi, K. E., Portaliou, A. G., Gouridis, G., Karamanou, S., & Economou, A. (2017). Preprotein Conformational Dynamics Drive Bivalent Translocase Docking and Secretion. Structure, 25(7), 1056-+. https://doi.org/10.1016/j.str.2017.05.012
  7. 2015
  8. Zak, K. M., Kitel, R., Przetocka, S., Golik, P., Guzik, K., Musielak, B., Dömling, A., Dubin, G., & Holak, T. A. (2015). Structure of the Complex of Human Programmed Death 1, PD-1, and Its Ligand PD-L1. Structure, 23(12), 2341-2348. https://doi.org/10.1016/j.str.2015.09.010
  9. Lokareddy, R. K., Hapsari, R. A., van Rheenen, M., Pumroy, R. A., Bhardwaj, A., Steen, A., Veenhoff, L. M., & Cingolani, G. (2015). Distinctive Properties of the Nuclear Localization Signals of Inner Nuclear Membrane Proteins Heh1 and Heh2. Structure, 23(7), 1305-1316. https://doi.org/10.1016/j.str.2015.04.017
  10. 2014
  11. 2013
  12. Bista, M., Wolf, S., Khoury, K., Kowalska, K., Huang, Y., Wrona, E., Arciniega, M., Popowicz, G. M., Holak, T. A., & Dömling, A. (2013). Transient protein states in designing inhibitors of the MDM2-p53 interaction. Structure, 21(12), 2143-2151. https://doi.org/10.1016/j.str.2013.09.006
  13. 2012
  14. 2011
  15. Rose, R. J., Labrijn, A. F., van den Bremer, E. T. J., Loverix, S., Lasters, I., van Berkel, P. H. C., van de Winkel, J. G. J., Schuurman, J., Parren, P. W. H. I., & Heck, A. J. R. (2011). Quantitative Analysis of the Interaction Strength and Dynamics of Human IgG4 Half Molecules by Native Mass Spectrometry. Structure, 19(9), 1274-1282. https://doi.org/10.1016/j.str.2011.06.016
  16. 2010
  17. 2009
  18. 2008
  19. 2006
  20. 2002
  21. Fusetti, F., Schröter, K. H., Steiner, R. A., Noort, P. I. V., Pijning, T., Rozeboom, H. J., Kalk, K. H., Egmond, M. R., & Dijkstra, B. W. (2002). Crystal structure of the copper-containing quercetin 2,3-dioxygenase from Aspergillus japonicus. Structure, 10(2), 259-268. https://doi.org/10.1016/S0969-2126(02)00704-9
  22. 1999
  23. Asselt, E. J. V., Dijkstra, A. J., Kalk, K. H., Takacs, B., Keck, W., & Dijkstra, B. W. (1999). Crystal structure of Escherichia coli lytic transglycosylase Slt35 reveals a lysozyme-like catalytic domain with an EF-hand. Structure, 7(10), 1167-1180. https://doi.org/10.1016/S0969-2126(00)80051-9
  24. 1998
  25. van Montfort, R. L. M., Pijning, T., Kalk, K. H., Hanqyi, I., Kouwijzer, M. L. C. E., Robillard, G. T., & Dijkstra, B. W. (1998). The structure of the Escherichia phosphotransferase IIAmannitol reveals a novel fold with two conformations of the active site. Structure, 3, 377 - 388.
  26. 1997
  27. van Montfort, R. L. M., Pijning, T., Kalk, K. H., Reizer, J., Saier Jr., M. H., Thunnissen, M. M. G. M., Robillard, G. T., & Dijkstra, B. W. (1997). The structure of an energy-coupling protein from bacteria, IIBcellobiose, reveals similarity to eukaryotic protein tyrosine phosphatases. Structure, 5(2), 217-225. https://doi.org/10.1016/S0969-2126(97)00180-9
  28. 1996
  29. Groves, M. R., Taylor, M. A., Scott, M., Cummings, N. J., Pickersgill, R. W., & Jenkins, J. A. (1996). The prosequence of procaricain forms an alpha-helical domain that prevents access to the substrate-binding cleft. Structure, 4(10), 1193-203.
  30. 1994
  31. VANSCHELTINGA, ACT., KALK, KH., BEINTEMA, JJ., & DIJKSTRA, BW. (1994). CRYSTAL-STRUCTURES OF HEVAMINE, A PLANT DEFENSE PROTEIN WITH CHITINASE AND LYSOZYME ACTIVITY, AND ITS COMPLEX WITH AN INHIBITOR. Structure, 2(12), 1181-1189.

ID: 765134