1. Carius, AB., Rogne, P., Duchoslav, M. Wolf-Watz, M, Samuelsson G, & Shutova, T.. (2019). Dynamic pH-induced conformational changes of the PsbO protein in the fluctuating acidity of the thylakoid lumen. Physiol Plant, epub ahead of print.


  1. Gupta, A., Reinartz, I., Karunanithy, G., Spilotros, A., Jonna, V.R., Hofer, A., Svergun, D., Baldwin, A., Schug, A.,  & Wolf-Watz, M. (2018).  Formation of a secretion competent protein complex by a dynamic wrap-around binding mechanism. Journal of Molecular Biology, 430, 3157-3169


  1. Rogne, P., Rosselin, M., Grundström, C., Sauer, U.H., & Wolf-Watz, M. (2018).  Molecular Mechanism of ATP versus GTP Selectivity of Adenylate Kinase PNAS, 115, 3012-3017


  1. Kovermann, M., Grundström, C., Sauer-Eriksson. E., Sauer, U.H., & Wolf-Watz, M. (2017).  Structural basis for ligand binding to an enzyme by a conformational selection pathway. PNAS, 114, 6298-6303


  1. Ho, O., Rogne, P., Edgren, T., Wolf-Watz, H., Login, F. H., & Wolf-Watz, M. (2017).  Characterization of the Ruler Protein Interaction Interface on the Substrate Specificity Switch Protein in the Yersinia Type III Secretion System. Journal of Biological Chemistry, 292, 3299-3311


  1. Rogne, P., & Wolf-Watz, M. (2016).  Urea-dependent adenylate kinase activation following redistribution of structural states Biophysical Journal, 11, 1385-1395


  1. Tükenmez, H., Magnussen, H., Kovermann, M.K., Byström, A., & Wolf-Watz, M. (2016).  Linkage between fitness of yeast cells and adenylate kinase catalysis Plos One,


  1. Kovermann, M., Rogne, P.,  & Wolf-Watz, M. (2016).  Protein dynamics and function from solution state NMR spectroscopy. Quarterly Reviews of Biophysics, 49, e6. Invited Review.


  1. Rogne, P., Sparrman, T., Anugwom, I., Mikkola, J-P., & Wolf-Watz, M. (2015).  Real-time 31P NMR investigation on the catalytic behavior of the enzyme Adenylate kinase in the matrix of a switchable ionic liquid. ChemSusChem, 8, 3654-3768


  1. Kovermann, M., Ådèn. J., Grundström, C., Sauer-Eriksson, E., Sauer, U.H., & Wolf-Watz, M. (2015). Structural basis for catalytically restrictive dynamics of a high-energy enzyme state. Nature Communications.


  1. Pedersen, M.N., Foderà, V., Horvath, I., van Maarschalkerweerd, A., Nørgaard Toft, K., Weise, C., Almqvist, F., Wolf-Watz, M., Wittung-Stafshede, P., & Vestergaard, B. (2015). Direct Correlation Between Ligand-Induced α-Synuclein Oligomers and Amyloid-like Fibril Growth. Scientific Reports, 5:10422, doi: 10.1038.



  1. Weise C. F., Login F. H., Ho O., Gröbner G., Wolf-Watz H. & Wolf-Watz M. (2014). Negatively charged lipid membranes promote a disorder-order transition in the Yersinia YscU protein. Biophysical Journal, 107, 1950-1961


  1. Esteban- Martin, S., Fenwick, R. B., Ådén, J., Cossins, B., Bertoncini, C. W., Guallar, V., Wolf-Watz, M. & Salvatella, X. (2014). Correlated Inter-domain communication in adenylate kinase. Plos Computational Biology.


  1. Ådén, J., Weise, C. Brännström, K., Olofsson, A., & Wolf-Watz, M. (2013). Structural topology and activation of an initial adenylate kinase-substrate complex. Biochemistry. 52, 1055-1061.
  1. Österberg, S., Åberg, A., Herrera Seitz, K., Wolf-Watz, M. & Shingler, V. (2013). Genetic dissection of a motility-associated c-di-GMP signalling protein of Pseudomonas putida. Environmental Microbiology Reports. Aug;5(4), 556-565.


  1. Frost, H., Ho, O., Login, F. H., Weise, C. F., Wolf-Watz, H. & Wolf-Watz, M. (2012). Autoproteolysis and intramolecular dissociation of Yersinia YscU precedes secretion of its C-terminal polypeptide YscUCC.  PLOS ONE.
  1. Ådén, J., Verma, A., Schug, A., &  Wolf-Watz, M. (2012). Modulation of a pre-existing conformational equilibrium tunes adenylate kinase activity.  Journal of the American Chemical Society, 134, 16562-16570.
  1. Horvath, I., Weise, C., Andersson, E., Chorell, E., Sellstedt, M., Bengtsson, C., Olofsson, A., Hultgren, S.J., Chapman, M., Wolf-Watz, M., Almqvist, F. & Wittung-Stafshede, P. (2012). Mechanisms of protein oligomerisation. Inhibitor of functional amyloids templates α-synuclein fibrillation.  Journal of the American Chemical Society, 134, 3439-3444.


  1. Dossena, S., Gandini, R., Tamma, G., Vezzoli, V., Nofziger, C., Tamplenizza, M., Salvoni, E., Bernardinelli, E., Meyer, G., Valentin, G., Wolf-Watz, M., Fürst, J. & Paulmichl, M. (2011). The molecular and functional interaction between ICln and HSPC038 modulates the regulation of cell volume.  Journal of Biological Chemistry, 286, 40659-40670


  1. Ådén, J., Wallgren, M., Storm, P., Christiansen, A., Schröder, W., Funk, C., & Wolf-Watz M,  (2011). Extraordinary µs-ms backbone dynamics in  Arabidopsis thaliana Peroxiredoxin, Q.  BBA proteins and proteomics. 1814, 1880-1890.


  1. Palm, M., Weise, C., Lundin, C., Wingsle, G., Nygren, Y., Björn, E., Naeredi, P., Wolf-Watz M & Wittung-Stafshede, P. (2011). Cisplatin binds human copper chaperone Atox1 and promotes unfolding in vitro. PNAS. 108, 6951-6965.


  1. Aguilar, X., Weise, C.F., Sparrman T., Wolf-Watz, M. & Wittung-Stafshede, P. (2011). Macromolecular crowding extended to a heptameric system: the co-chaperonin protein 10. Biochemistry, 50, 3034-3044.
  1. Olsson U. & Wolf-Watz, M. (2010).Overlap between folding and functional energy landscapes for adenylate kinase conformational change. Nature Communications, doi:10.1038/ncomms1106
  1. Bosco, D.A., Eisenmesser, E. Z., Clarkson, M.W., Wolf-Watz, M., Labeikovsky, W., Millet, O., & Kern, K. (2010). Dissecting the microscopic steps of the cyclophilin A enzymatic cycle on the biological HIV-1 capsid substrate by NMR. Journal of Molecular Biology, 403, 723-738.


  1. Gardino, A. K, Vialli, J., Kivensson, A., Lei, M., Liu, C. T., Steindel, P., Eisenmesser, E. Z., Labeikovsky, W., Wolf-Watz, M., Clarkson, M. W. & Kern, K. (2009). Transient non-native hydrogen bonds promote activation of a signaling protein. Cell, 139, 1109-1118.
  1. Malisauskas, M., Weise, C., Yanamandra, K., Wolf-Watz, M. & Morozova-Roche, L. (2009). Lability landscape and protease resistance of human insulin amyloid: A new insight into its molecular properties. Journal of Molecular Biology, 379, 845-858.


  1. Rundqvist, L., Ådén.J., Sparrman, T., Wallgren, M., Olsson, U. & Wolf-Watz M. (2009). Non-cooperative folding of subdomains in adenylate kinase. Biochemistry, 48, 1911-1927.
  1. Wallgren, M., Ådén, J., Pylypenko, O., Mikaelsson, M., Johansson, L., Rak, A., & Wolf-Watz. M. (2008) Extreme temperature tolerance of a hyperthermophilic protein coupled to residual structure in the unfolded state. Journal of Molecular Biology,379, 845-858.
  1. Ådén J. & Wolf-Watz M. (2007). NMR identification of transient complexes critical to adenylate kinase catalysis, Journal of the American Chemical Society, 129, 14003-140012.
  1. Wildman-Henzler K., Thai V., Lei K., Wunderlich M., Wolf-Watz M., Fenn T., Pozharski E., Wilson M. A. , Petsko G. A., Karplus M., Hübner C. &  Kern D. (2007) Intrinsic motions along an enzymatic reaction trajectory, Nature, 450, 838-844.


  1. Eisenmesser, E. Z., Millet, O.,  Labeikovsky, W.,  Korzhnev, D.M., Wolf-Watz, M.,  Bosco, D. A., Skalicky, J.J., Kay, L.E. & Kern, D. (2005). Intrinsic dynamics of an enzyme underlies catalysis. Nature. 438, 117-121.
  1. Kern, D., Eisenmesser E.Z., & Wolf-Watz, M (2005), Enzyme Dynamics during catalysis measured with NMR spectroscopy. Methods in Enzymology, 394, 507-524. Review
  1. Wolf-Watz, M., Thai, V., Henzler-Wildman, K. Hadjipavlou, G., Eisenmesser, E. Z.,  & Kern, D. (2004). Linkage between dynamics and catalysis in a thermophilic – mesophilic enzyme pair. Nature Structural and Molecular Biology. 11, 945-949.
  1. Liu, H., Holm, M., Xie, X.-Q., Wolf-Watz, M., & Grundström, T. (2004) AML1/Runx1 recruits calcineurin to regulate granulocyte macrophage colony-stimulating Factor by Ets1 activation. Journal of Biological Chemistry. 28, 29398-29408.
  1. Bäckström, S., Wolf-Watz, M., Grundström, C., Härd, T., Grundström, T. & Sauer, U. (2002) The RUNX1 Runt domain at 1.25A resolution: a structural switch and specifically bound chloride ions modulate DNA bindingJournal of Molecular Biology, 322, 259-272.
  1. Wolf-Watz, M., Grundström T. & Härd, T. (2001) Structure and backbone dynamics of apo-CBFβ in solution Biochemistry, 40, 11423-11432.

4.  Wolf-Watz, M., Bäckström S., Grundström T., Sauer, U., & Härd, T (2001).Chloride binding by the AML1/Runx1 transcription factor studied by NMR FEBS Letters, 488, 81-84.

  1. Bäckström, S., Huang, S.-H., Wolf-Watz, M., Xie, X.-Q., Härd, T., Grundström, T. & Sauer, U. (2001) Crystallization and preliminary studies of the DNA-binding runt domain of AML1. Acta Crystallographica Section D, 57, 269-271.
  2. Wolf-Watz, M., Xie, X-Q., Holm, M., Grundström T. & Härd, T.(1999)
    Solution properties of the free and DNA-bound runt domain of AML1
    European Journal of Biochemistry, 261, 251-260.

1.  Berglund, H., Wolf-Watz, M., Lundbäck, T., van den Berg, S. & Härd, T. (1997) Structure and Dynamics of the Glucocorticoid Receptor DNA-binding Domain: Comparison of Wild Type and a Mutant with Altered Specificity. Biochemistry, 36, 11188-11197