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Department of Pharmacology

 

 

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       2022  

 

  • Synakewicz M., R. S. Eapen, A. Perez-Riba, P. J. E. Rowling, D. Bauer, A. Weißl, G. Fischer, M. Hyvönen, M. Rief, L. S. Itzhaki, and J. Stigler. Unraveling the mechanics of a repeat-protein nanospring: from folding of individual repeats to fluctuations of the superhelix. ACS Nano, 16(3): 3895-3905, 2022.

 

       2021  

 

  • Burbidge O., M. W. Pastok, S. L. Hodder, G. Zenkevičiūtė, M. E. M. Noble, J. A. Endicott, and L. S. Itzhaki. Nanobodies restore stability to cancer-associated mutants of tumor suppressor protein p16INK4a. Pre-print.  
  • Synakewicz M., R. S. Eapen, A. Perez-Riba, D. Bauer, A. Weißl, G. Fischer, M. Hyvönen, M. Rief, L. S. Itzhaki, and J. Stigler. Consensus tetratricopeptide repeat proteins are complex superhelical nanosprings. Pre-print.  
  • Ripka J. F., A. Perez-Riba, P. K. Chaturbedy, and L. S. Itzhaki. Testing the length limit of loop grafting in a helical repeat protein. Curr. Res. Struct. Biol., 3(1): 30-40, 2021   
  • Smith B. M., P. J. E. Rowling, C. M. Dobson, and L. S. Itzhaki. Parallel and sequential pathways of molecular recognition of a tandem-repeat protein and its intrinsically disordered binding partner. Biomolecules, 11(6):827, 2021.   
  • Diamante, A., P. Chaturbedy, P. Rowling, J. Kumita, R. S. Eapen, S. H. McLaughlin, M. de la Roche, A. Perez-Riba, and L. S. Itzhaki. Engineering mono- and multi-valent inhibitors on a modular scaffold. Chem. Sci., 12(3):880-895, 2021.  

    2020  

 

  • Du Z., S. Chakrabarti, Y. Kulaberoglu, E. S. J. Smith, C. M. Dobson, L. S. Itzhaki, and J. R. Kumita. Probing the unfolded protein response in long-lived naked mole-rats. Biochem. Biophys. Res. Commun., 529(4):1151-1157, 2020.   
  • Madden S. K., and L. S. Itzhaki. Structural and mechanistic insights into the Keap1-Nrf2 system as a route to drug discovery. Biochim. Biophys. Acta Proteins Proteom., 1868(7):140405, 2020.   
  • Sharma K., A. V. Strizhak, E. Fowler, W. Xu, B. Chappell, H. F. Sore, W. R. J. D. Galloway, M. N. Grayson, Y. H. Lau, L. S. Itzhaki, and D. R. Spring. Functionalized double strain-promoted stapled peptides for inhibiting the p53-MDM2 interaction. ACS Omega., 5(2):1157-1169, 2020.   
  • Strizhak A. V., O. Babii, S. Afonin, I. Bakanovich, T. Pantelejevs, W. Xu, E. Fowler, R. Eapen, K. Sharma, M. O. Platonov, V. V. Hurmach, L. S. Itzhaki, M. Hyvönen, A. S. Ulrich, D. R. Spring, and I. V. Komarov. Diarylethene moiety as an enthalpy-entropy switch: photoisomerizable stapled peptides for modulating p53/MDM2 interaction. Org. Biomol. Chem., 18(28):5359-5369, 2020. 
  • Bergkvist, L., Z. Du, G. Elovsson, H. Appelqvist, L. S. Itzhaki, J. R. Kumita, K. Kågedal, and A. C. Brorsson. Mapping pathogenic processes contributing to neurodegeneration in Drosophila models of Alzheimer's disease. FEBS Open Bio., 10(3):338-350, 2020.

    2019  

 

  • Lowe A. R., and L. S. Itzhaki. Editorial Overview: Biophysical and computational methods. Curr. Opin. Struct. Biol., 58(1):7-9, 2019.   
  • Sharma K., A. V. Strizhak, E. Fowler, X. Wang, W. Xu, C. H. Jensen, Y. Wu, H. F. Sore, Y. H. Lau, M. Hyvönen, L. S. Itzhaki, and D. R. Spring. Water-soluble, stable and azide-reactive strained dialkynes for biocompatible double strain-promoted click chemistry. Org. Biomol. Chem., 17(34):8014-8018, 2019.   
  • Perez-Riba, A., E. Komives, E. R. G. Main and L. S. Itzhaki. Decoupling a tandem-repeat protein: Impact of multiple loop insertions on a modular scaffold. Sci. Rep., 9:15439, 2019. 
  • Synakewicz, M., D. Bauer, M. Rief, and L. S. Itzhaki. Bioorthogonal protein-DNA conjugation methods for force spectroscopy. Sci. Rep., 9:13820, 2019.  
  • Wright, J. N., W. L. Wong, J. A. Harvey, J. A. Garnett, L. S. Itzhaki, and E. R. G. Main. Scalable geometrically designed protein cages assembled via genetically encoded split inteins. Structure, 27(5):776-784, 2019.  
  • Sivertsson, E. M., S. E. Jackson, and L. S. Itzhaki. The AAA+ protease ClpXP can easily degrade a 31 and a 52-knotted protein. Sci Rep., 9:2421, 2019.  
  • Madden, S. K., A. Perez-Riba, and L. S. Itzhaki. Exploring new strategies for grafting binding peptides onto protein loops using a consensus-designed tetratricopeptide repeat scaffold. Protein Sci., 28(4):738-745, 2019.  
  • Perez-Riba, A., and L. S. Itzhaki. The tetratricopeptide-repeat motif is a versatile platform that enables diverse modes of molecular recognition. Curr Opin Struct Biol., 54(1):43-49, 2019.  
  • Wu, Y., A. Kaur, E. Fowler, M. M. Wiedmann, R. Young, W. R. J. D. Galloway, L. Olsen, H. F. Sore, A. Chattopadhyay, T. T. Kwan, W. Xu, S. J. Walsh, P. de Andrade, M. Janecek, S. Arumugam, L. S. Itzhaki, Y. H. Lau, and D. R. Spring. Toolbox of diverse linkers for navigating the cellular efficacy landscape of stapled peptides. ACS Chem. Biol., 14(3):526-533, 2019.  
  • Yadahalli, S., J. L. Neira, C. M. Johnson, Y. S. Tan, P. J. E. Rowling, A. Chattopadhyay, C. S. Verma, and L. S. Itzhaki. Kinetic and thermodynamic effects of phosphorylation on p53 binding to MDM2. Sci. Rep., 9:693, 2019. 

    2018  

 

  • Perez-Riba, A., A. R. Lowe, E. R. G. Main, and 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. Phil. Trans. R. Soc. B, 373:20170188, 2018.  
  • Harvey, J. A., L. S. Itzhaki, and E. R. G. Main. Programmed protein self-assembly driven by genetically encoded intein-mediated native chemical ligation. ACS Synth. Biol., 7(4):1067-1074, 2018.  
  • Lowe A. R., A. Perez-Riba, L. S. Itzhaki, and E. R. G. Main. PyFolding: An open-source software package for graphing, analysis and simulation of thermodynamic and kinetic models of protein folding. Biophys. J., 114(3):511-521, 2018. 

    2017  

 

  • 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(1):70, 2017.  
  • Perez-Riba, A., and L. S. Itzhaki. A method for rapid high-throughput biophysical analysis of proteins. Sci. Rep., 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(1):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(1):2245-2256, 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(1):524 –529, 2017. 

    2016  

 

  • 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. 

    2015  

 

  • 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. Biochem. J., 466(3):613–624, 2015.  
  • Tsytlonok, M., S. M. Ibrahim, P. Rowling, W. Xu, M. J. Ruedas-Rama, A. Orte, D. Klenerman, and L. S. 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. Biochem. Soc. T., 43(5):881-888, 2015. 

    2014  

 

  • 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(1):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(1):1804–1809, 2014.  
  • Sivertsson, E. and L. S. Itzhaki. Protein folding: when ribosomes pick the structure. Nat. Chem., 6:378–379, 2014.  
  • Sivertsson, E. and L. S. Itzhaki. A virus that can take the heat. Structure, 22(11):1549 – 1550, 2014. 

    2013  

 

  • Javadi, Y., and L. S. Itzhaki. Tandem-repeat proteins: regularity plus modularity equals design-ability. Curr. Opin. Struct. Biol., 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. Arch. Biochem. Biophys., 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. J. Phys. Chem., 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. Philos. Trans. R. Soc. Lond., B, Biol. Sci., 368(1617), 2013. 

    2012  

 

  • Itzhaki, L. S., and G. D. Rose. Folding and binding: lingering questions, emerging answers. Curr. Opin. Struct. Biol., 22(1):1–3, 2012.  
  • Itzhaki, L. S., 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. S. Itzhaki, and A. Philpott. Complex regulation controls Neurogenin3 proteolysis. Biol. 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. 

    2010  

 

  • Itzhaki, L. S., and P. Wolynes. Nature and nurture in protein folding and binding. Curr. Opin. Struct. Biol., 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. J. Mol. Biol., 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. J. Biol. Chem., 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. Biophys. J., 98(7):1294–1301, 2010. 

    2009  

 

  • 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. Mol. Microbiol.,
    71(3):702–716, 2009. 

    2008  

 

  • Itzhaki, L. S., and P. Wolynes. The quest to understand protein folding. Curr. Opin. Struct. Biol., 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. Proc. Natl. Acad. Sci., 105(29):9982–9987, 2008. 

    2007  

 

  • 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. J. Biol. Chem., 282(16):11931–11940, 2007.  
  • Lowe, A. R., and L. S. Itzhaki. Biophysical characterisation of the small ankyrin repeat protein myotrophin. J. Mol. Bio., 365(4):1245 – 1255, 2007.   
  • Lowe, A. R., and L. S. Itzhaki. Rational redesign of the folding pathway of a modular protein. Proc. Natl. Acad. Sci., 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. Mol. 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. Proc. Natl. Acad. Sci., 104(19):7863–7868, 2007. 

 

 

 

A full list including publications older than 2007 can be found on PubMed.