2025
Cutts E. E., Saravanan S., Fisher G. L. M, Rueda D. S., Aragon L. (2025) Substrate accessibility regulation of human TopIIa decatenation by cohesin, Nature Comms, https://doi.org/10.1038/s41467-025-62505-3
Borsellini A*, Conti D*, Cutts EE*^, Harris RJ*, Walstein K, Graziadei A, Cecatiello V, Aarts TF, Xie R, Mazouzi A, Sen S, Hoencamp C, Pleuger R, Ghetti S, Oberste-Lehn L, Pan D, Bange T, Haarhuis JHI, Perrakis A, Brummelkamp TR, Rowland BD^, Musacchio A^, Vannini A^. (2025) Condensin II activation by M18BP1. Mol Cell. http://doi.org/10.1016/j.molcel.2025.06.014
*Equal contribution, ^corresponding
2024
Cutts E. E.^, Tetiker D., Kim E., Aragon L.^, (2025) Molecular Mechanism of Condensin I Activation by KIF4A, EMBO J, https://doi.org/10.1038/s44318-024-00340-w
^corresponding
2021
Houlard M.*, Cutts E. E.*, Shamim M. S., Godwin J., Weisz D., Aiden A. P., Aiden E. L., Schermelleh L., Vannini A., Nasmyth K. (2021) MCPH1 inhibits condensin II during interphase by regulating its SMC2-kleisin interface. eLife, 10:e73348 DOI:10.7554/eLife.73348 *equal contribution
Cutts E.E.*, Taylor G. C.* , Pardo M. Yu L., Wills J. C., Choudhary J. S., Vannini A., Wood A. J. (2021) A commercial antibody to the human condensin II subunit NCAPH2 cross-reacts with a SWI/SNF complex component. Wellcome Open Res, 6:3, doi: https://doi.org/10.12688/wellcomeopenres.16482.1 *equal contribution
2020
Cutts E.E.^, Vannini A. Condensin complexes: understanding loop extrusion one conformational change at a time. (2020) Biochem Soc Trans. 30;48(5):2089-2100. doi: 10.1042/BST20200241.
^corresponding
Kong, M.*, Cutts, E. E.*, Pan D., Beuron, F., Kaliyappan, T. Xue, C., Morris, E., Musacchio A., Vannini A., and Greene E. C. (2020) Human condensin I and II drive extensive ATP–dependent compaction of nucleosome–bound DNA. Molecular Cell, 79(1), 99-114. doi: 10.1016/j.molcel.2020.04.026.
*equal contribution
Cutts, E. E, Egan, J. B., Dodd I. and Shearwin K. (2020) A quantitative binding model for the Apl protein, the dual-purpose recombination-directionality factor and lysis-lysogeny regulator of bacteriophage 186. Nucleic Acids Research. Volume 48, Issue 16, Pages 8914–8926, doi: https://doi.org/10.1093/nar/gkaa655
Pre-2020
Cutts, E. E., Laasch, N., Reiter, D. M., Trenker, R., Slater, L. M., Stansfeld, P. J., & Vakonakis, I. (2017). Structural analysis of P. falciparum KAHRP and PfEMP1 complexes with host erythrocyte spectrin suggests a model for cytoadherent knob protrusions. PLoS Pathogens, 13(8), e1006552. doi:10.1371/journal.ppat.1006552
Cutts, E. E., Inglis, A., Stansfeld, P. J., Vakonakis, I., & Hatzopoulos, G. N. (2015). The centriolar protein CPAP G-box: an amyloid fibril in a single domain. Biochem Soc Trans, 43(5), 838–843. doi:10.1042/BST20150082
Contributing Publications:
Anita F. Meier, Jan Vuckovic, Paul Girvan, Erin Cutts, Theodora Brophy, BenjaminAmbrose, David S. Rueda (2024) Herpes simplex virus type 1 origin binding protein UL9 tethers and loops origin- and non-origin-DNA intra- and intermolecularly bioRxiv, doi: https://doi.org/10.1101/2024.10.30.621104
Martínez‐García, B., Dyson, S. , Segura, J., Ayats, A., Cutts, E. E., Gutierrez‐Escribano, P., Aragón, L. & Roca, J. (2022) Condensin pinches a short negatively supercoiled DNA loop during each round of ATP usage. The EMBO Journal, e111913 doi: 10.15252/embj.2022111913
Choppakatla P., Dekker B., Cutts E. E., Vannini A., Dekker J., Funabiki H., (2021) Linker histone H1.8 inhibits chromatin-binding of condensins and DNA topoisomerase II to tune chromosome length and individualization. eLife 10:e68918 doi: 10.7554/eLife.68918
Ferrari R., de Llobet Cucalon L.I., Di Vona C., Le Dilly F., Vidal E., Lioutas A., Oliete J.Q., Jochem L., Cutts E,Dieci G., Vannini A., Teichmann M., de la Luna S., Beato M. (2019) TFIIIC Binding to Alu Elements Controls Gene Expression via Chromatin Looping and Histone Acetylation. Molecular Cell, 77(3), 475-487
Oberli, A., Zurbrugg, L., Rusch, S., Brand, F., Butler, M. E., Day, J. L., Cutts E. E., Lavstsen T, Vakonakis I, Beck HP. (2016). Plasmodium falciparum Plasmodium helical interspersed subtelomeric proteins contribute to cytoadherence and anchor P. falciparum erythrocyte membrane protein 1 to the host cell cytoskeleton. Cellular Microbiology, 18(10), 1415–1428. doi:10.1111/cmi.12583
Watermeyer, J. M., Hale, V. L., Hackett, F., Clare, D. K., Cutts, E. E., Vakonakis, I., et al. (2016). A spiral scaffold underlies cytoadherent knobs in Plasmodium falciparum-infected erythrocytes. Blood, 127(3), 343–351. doi:10.1182/blood-2015-10-674002
Wojdyla, J. A., Cutts, E., Kaminska, R., Papadakos, G., Hopper, J. T. S., Stansfeld, P. J., Staunton, D., Robinson, C. V., Kleanthous, C. (2015). Structure and function of the Escherichia coli Tol-Pal stator protein TolR. Journal of Biological Chemistry. https://doi.org/10.1074/jbc.M115.671586
Hao, N., Krishna, S., Ahlgren-Berg, A., Cutts, E. E., Shearwin, K. E., & Dodd, I. B. (2014). Road rules for traffic on DNA-systematic analysis of transcriptional roadblocking in vivo. Nucleic Acids Research, 42(14), 8861–8872. doi:10.1093/nar/gku627
Oberli, A.*, Slater, L. M.*, Cutts, E., Brand, F., Mundwiler-Pachlatko, E., Rusch, S., et al. (2014). A Plasmodium falciparum PHIST protein binds the virulence factor PfEMP1 and comigrates to knobs on the host cell surface. FASEB Journal : Official Publication of the Federation of American Societies for Experimental Biology, 28(10), 4420–4433. doi:10.1096/fj.14-256057. *equal contribution
Hatzopoulos, G. N., Erat, M. C., Cutts, E., Rogala, K. B., Slater, L. M., Stansfeld, P. J., & Vakonakis, I. (2013). Structural analysis of the G-box domain of the microcephaly protein CPAP suggests a role in centriole architecture. Structure (London, England : 1993), 21(11), 2069–2077. doi:10.1016/j.str.2013.08.019
Cutts Lab 