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  • Perez-Riba, A., A. R. Lowe, E. R. G. Main, L. S. Itzhaki. Context-Dependent Energetics of Loop Extensions in a Family of Tandem-Repeat Proteins. Biophys. J. 114(11):2552-2562, 2018.
  • Perez-Riba, A.*, M. Synakewicz* and L. S. Itzhaki. Opinion piece: Folding cooperativity and allosteric function in the tandem-repeat protein class.


  • Guttenplan, A. P. M.,  L. J. Young, D. Matak-Vinkovic, C. F. Kaminski, T. P. J. Knowles and L. S. Itzhaki. Nanoscale click-reactive scaffolds from peptide self-assembly. J. Nanobiotechnol. 15:70, 2017.
  • Perez-Riba, A., and L. S. Itzhaki. A method for rapid high-throughput biophysical analysis of proteins. Scientific Reports 7, 9071, 2017
  • Serrano, J. C., J. Sipthorp, W. Xu, L. S. Itzhaki and S. V. Ley. A New Methodology for Incorporating Chiral Linkers into Stapled Peptides. ChemBioChem 18:1066–1071, 2017.
  • Xu, W., Y. Heng Lau, G. Fischer, Y. S. Tan, A. Chattopadhyay, M. de la Roche, M. Hyvönen, C. S. Verma, D. R. Spring, and L. S. Itzhaki. Macrocyclized extended peptide Inhibiting the substrate-recognition domain of tankyrase. J. Am. Chem Soc., 139:2245-2256 139, 2017.
  • Wiedmann, M. M., Y. S. Tan, Y. Wu, S. Aibara, W. Xu, H. F. Sore, C. S. Verma, L. S. Itzhaki, M. Stewart, J. D. Brenton, and D. R. Spring. Development of Cell-Permeable, Non-Helical Constrained Peptides to Target a Key Protein–Protein Interaction in Ovarian Cancer. Angew. Chem. Int. Edit., 56:524 –529, 2017.


  • Chattopadhyay, A., C. J. O'Connor, F. Zhang, C. Galvagnion, W. R. J. D. Galloway, Y. S. Tan, J. E. Stokes, T. Rahman, C. Verma, D. R. Spring, and L. S. Itzhaki. Discovery of a small-molecule binder of the oncoprotein gankyrin that modulates gankyrin activity in the cell. Sci. Rep., 6:23732, 2016.


  • Hutton, R. D., J. Wilkinson, M. Faccin, E. Sivertsson, A. Pelizzola, A. R. Lowe, P. Bruscolini, and L. S. Itzhaki. Mapping the topography of a protein energy landscape. J. Am. Chem. Soc. 137(46):14610–14625, 2015.
  • Gaboriau, D. C., P. J. Rowling, C. G. Morrison, and L. S. Itzhaki. Protein stability versus function: effects of destabilizing missense mutations on BRCA1 DNA repair activity. Biochemical Journal, 466(3):613–624, 2015.
  • Tsytlonok, M., S. M. Ibrahim, P. Rowling, W. Xu, M. J. Ruedas-Rama, A. Orte, D. Klenerman, and L. Itzhaki. Single-molecule FRET reveals hidden complexity in a protein energy landscape. Structure, 23(1):190–198, 2015.
  • Rowling, P. J. E., E. M. Sivertsson, A. Perez-Riba, E. R. G. Main and L. S. Itzhaki. Dissecting and reprogramming the folding and assembly of tandem-repeat proteins.


  • Kelly, S. E., G. Meisl, P. J. E. Rowling, S. H. McLaughlin, T. Knowles, and L. S. Itzhaki. Diffuse transition state structure for the unfolding of a leucine-rich repeat protein. Phys. Chem. Chem. Phys., 16:6448–6459, 2014.
  • Lau, Y. H., P. de Andrade, S.-T. Quah, M. Rossmann, L. Laraia, N. Skold, T. J. Sum, P. J. E. Rowling, T. L. Joseph, C. Verma, M. Hyvonen, L. S. Itzhaki, A. R. Venkitaraman, C. J. Brown, D. P. Lane, and D. R. Spring. Functionalised staple linkages for modulating the cellular activity of stapled peptides. Chem. Sci., 5:1804–1809, 2014.
  • Sivertsson, E. and L. S. Itzhaki. Protein folding: when ribosomes pick the structure. Nature Chemistry, 6:378–379, 2014.
  • Sivertsson, E. and L. Itzhaki. A virus that can take the heat. Structure, 22(11):1549 – 1550, 2014.


  • Javadi, Y. and L. S. Itzhaki. Tandem-repeat proteins: regularity plus modularity equals design-ability. Current Opinion in Structural Biology, 23(4):622 – 631, 2013.
  • Settanni, G., D. Serquera, P. E. Marszalek, E. Paci, and L. S. Itzhaki. Effects of ligand binding on the mechanical properties of ankyrin repeat protein gankyrin. PLoS Comput Biol, 9(1):e1002864, 2013.
  • Tsytlonok, M., P. O. Craig, E. Sivertsson, D. Serquera, S. Perrett, R. B. Best, P. G. Wolynes, and L. S. Itzhaki. Complex energy landscape of a giant repeat protein. Structure, 21(11):1954–1965, 2013.
  • Tsytlonok, M. and L. S. Itzhaki. The how’s and why’s of protein folding intermediates. Archives of Biochemistry and Biophysics, 531(12):14 – 23, 2013. Protein Folding and Stability.
  • Tsytlonok, M., P. Sormanni, P. J. E. Rowling, M. Vendruscolo, and L. S. Itzhaki. Subdomain architecture and stability of a giant repeat protein. The Journal of Physical Chemistry B, 117(42):13029–13037, 2013.
  • Xu, L.-Q., S. Wu, A. K. Buell, S. I. A. Cohen, L.-J. Chen, W.-H. Hu, S. A. Cusack, L. S. Itzhaki, H. Zhang, T. P. J. Knowles, C. M. Dobson, M. E. Welland, G. W. Jones, and S. Perrett. Influence of specific HSP70 domains on fibril formation of the yeast prion protein Ure2. Philosophical Transactions of the Royal Society of London B: Biological Sciences, 368(1617), 2013.


  • Itzhaki, L. S. and G. D. Rose. Folding and binding: lingering questions, emerging answers. Current Opinion in Structural Biology, 22(1):1 – 3, 2012.
  • Itzhaki, L. and A. Lowe. From artificial antibodies to nanosprings. In Matthews, J., editor, Protein Dimerization and Oligomerization in Biology, volume 747 of Advances in Experimental Medicine and Biology, pages 153–166. Springer New York, 2012.
  • Roark, R., L. Itzhaki, and A. Philpott. Complex regulation controls Neurogenin3 proteolysis. Biology Open, 1(12):1264–1272, 2012.
  • Rousseau, F., J. Schymkowitz, and L. Itzhaki. Implications of 3D domain swapping for protein folding, misfolding and function. In Matthews, J., editor, Protein Dimerization and Oligomerization in Biology, volume 747 of Advances in Experimental Medicine and Biology, pages 137–152. Springer New York, 2012.
  • Tsytlonok, M. and L. S. Itzhaki. Using FlAsH to probe conformational changes in a large HEAT repeat protein. ChemBioChem, 13(8):1199–1205, 2012.


  • Itzhaki, L. and P. Wolynes. Nature and nurture in protein folding and binding. Current Opinion in Structural Biology, 20(1):1 – 2, 2010.
  • Murton, B. L., W. L. Chin, C. P. Ponting, and L. S. Itzhaki. Characterising the binding specificities of the subunits associated with the KMT2/Set1 histone lysine methyltransferase. Journal of Molecular Biology, 398(4):481 – 488, 2010.
  • Rowling, P. J. E., R. Cook, and L. S. Itzhaki. Toward classification of BRCA1 missense variants using a biophysical approach. Journal of Biological Chemistry, 285(26):20080–20087, 2010.
  • Serquera, D., W. Lee, G. Settanni, P. E. Marszalek, E. Paci, and L. S. Itzhaki. Mechanical unfolding of an ankyrin repeat protein. Biophysical Journal, 98(7):1294–1301, 2010.


  • Zhang, H., H. M. Loovers, L.-Q. Xu, M. Wang, P. J. E. Rowling, L. S. Itzhaki, W. Gong, J.-M. Zhou, G. W. Jones, and S. Perrett. Alcohol oxidase (AOX1) from Pichia pastoris is a novel inhibitor of prion propagation and a potential ATPase. Molecular Microbiology,
    71(3):702–716, 2009.


  • Itzhaki, L. and P. Wolynes. The quest to understand protein folding. Current Opinion in Structural Biology, 18(1):1 – 3, 2008.
  • Werbeck, N. D., P. J. E. Rowling, V. R. Chellamuthu, and L. S. Itzhaki. Shifting transition states in the unfolding of a large ankyrin repeat protein. Proceedings of the National Academy of Sciences, 105(29):9982–9987, 2008.


  • Lian, H.-Y., H. Zhang, Z.-R. Zhang, H. M. Loovers, G. W. Jones, P. J. E. Rowling, L. S. Itzhaki, J.-M. Zhou, and S. Perrett. Hsp40 interacts directly with the native state of the yeast prion protein Ure2 and inhibits formation of amyloid-like fibrils. Journal of Biological Chemistry, 282(16):11931–11940, 2007.
  • Lowe, A. R. and L. S. Itzhaki. Biophysical characterisation of the small ankyrin repeat protein myotrophin. Journal of Molecular Biology, 365(4):1245 – 1255, 2007. Lowe, A. R. and L. S. Itzhaki. Rational redesign of the folding pathway of a modular protein. Proceedings of the National Academy of Sciences, 104(8):2679–2684, 2007.
  • Moreau, M. J., A. T. McGeoch, A. R. Lowe, L. S. Itzhaki, and S. D. Bell. ATPase site architecture and helicase mechanism of an archaeal MCM. Molecular Cell, 28(2):304 – 314, 2007.
  • Werbeck, N. D. and L. S. Itzhaki. Probing a moving target with a plastic unfolding intermediate of an ankyrin-repeat protein. Proceedings of the National Academy of Sciences, 104(19):7863–7868, 2007.


  • Bader, R., M. A. Seeliger, S. E. Kelly, L. L. Ilag, F. Meersman, A. Limones, B. F. Luisi, C. M. Dobson, and L. S. Itzhaki. Folding and fibril formation of the cell cycle protein Cks1. Journal of Biological Chemistry, 281(27):18816–18824, 2006.
  • Rousseau, F., H. Wilkinson, J. Villanueva, L. Serrano, J. W. Schymkowitz, and L. S. Itzhaki. Domain swapping in p13suc1 results in formation of native-like, cytotoxic aggregates. Journal of Molecular Biology, 363(2):496 – 505, 2006.
  • Yao, Z.-P., M. Zhou, S. E. Kelly, M. A. Seeliger, C. V. Robinson, and L. S. Itzhaki. Activation of ubiquitin ligase SCF(Skp2) by Cks1: Insights from hydrogen exchange mass spectrometry. Journal of Molecular Biology, 363(3):673 – 686, 2006.


  • Chavali, G. B., C. M. Ekblad, B. P. Basu, N. C. Brissett, D. Veprintsev, L. Hughes-Davies, T. Kouzarides, L. S. Itzhaki, and A. J. Doherty. Crystal structure of the ENT domain of human EMSY. Journal of Molecular Biology, 350(5):964 – 973, 2005.
  • Ekblad, C. M. S., G. B. Chavali, B. P. Basu, S. M. V. Freund, D. Veprintsev, L. Hughes-Davies, T. Kouzarides, A. J. Doherty, and L. S. Itzhaki. Binding of emsy to HP1β: implications for recruitment of HP1β and BS69. EMBO reports, 6(7):675–680, 2005.
  • Seeliger, M. A., M. Spichty, S. E. Kelly, M. Bycroft, S. M. V. Freund, M. Karplus, and L. S. Itzhaki. Role of conformational heterogeneity in domain swapping and adapter function of the Cks proteins. Journal of Biological Chemistry, 280(34):30448–30459, 2005.


  • Ekblad, C. M., A. Friedler, D. Veprintsev, R. L. Weinberg, and L. S. Itzhaki. Comparison of BRCT domains of BRCA1 and 53BP1: A biophysical analysis. Protein Science, 13(3):617–625, 2004.
  • Rousseau, F., J. W. H. Schymkowitz, H. R. Wilkinson, and L. S. Itzhaki. Intermediates control domain swapping during folding of p13suc1. Journal of Biological Chemistry, 279(9):8368–8377, 2004.


  • Rousseau, F., J. W. Schymkowitz, and L. S. Itzhaki. The unfolding story of three-dimensional domain swapping. Structure, 11(3):243 – 251, 2003.
  • Seeliger, M., S. Breward, and L. Itzhaki. Weak cooperativity in the core causes a switch in folding mechanism between two proteins of the Cks family. Journal of Molecular Biology, 325(1):189 – 199, 2003.
  • Seeliger, M. A., S. E. Breward, A. Friedler, O. Schon, and L. S. Itzhaki. Cooperative organization in a macromolecular complex. Nature Structural & Molecular Biology, 10:718–724, 2003.


  • Tang, K. S., A. R. Fersht, and L. S. Itzhaki. Sequential unfolding of ankyrin repeats in tumor suppressor p16. Structure, 11(1):67 – 73, 2003.
  • Seeliger, M. A., J. W. H. Schymkowitz, F. Rousseau, H. R. Wilkinson, and L. S. Itzhaki. Folding and association of the human cell cycle regulatory proteins ckshs1 and ckshs2. Biochemistry, 41(4):1202–1210, 2002.
  • Sitry, D., M. A. Seeliger, T. K. Ko, D. Ganoth, S. E. Breward, L. S. Itzhaki, M. Pagano, and A. Hershko. Three different binding sites of Cks1 are required for p27-ubiquitin ligation. Journal of Biological Chemistry, 277(44):42233–42240, 2002.


  • Rousseau, F., J. W. H. Schymkowitz, H. R. Wilkinson, and L. S. Itzhaki. Three-dimensional domain swapping in p13suc1 occurs in the unfolded state and is controlled by conserved proline residues. Proceedings of the National Academy of Sciences, 98(10):5596–5601, 2001.
  • Schymkowitz, J. W., F. Rousseau, H. R. Wilkinson, A. Friedler, and L. S. Itzhaki. Observation of signal transduction in three-dimensional domain swapping. Nature Structural & Molecular Biology, 8:888–892, 2001.


  • Schymkowitz, J., F. Rousseau, L. Irvine, and L. Itzhaki. The folding pathway of the cell-cycle regulatory protein p13suc1: clues for the mechanism of domain swapping. Structure, 8(1):89 – 100, 2000.
  • Schymkowitz, J., F. Rousseau, and L. itzhaki. Sequence conservation provides the best prediction of the role of proline residues in p13suc1. Journal of Molecular Biology, 301(1):199 – 204, 2000.


For a full alphabetical list including publications older than 2000, see here.