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Understanding and Manipulating Intrinsically Disordered Protein-Protein interactions of the Aurora A Kinase

   Faculty of Biological Sciences

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  Dr Takashi Ochi, Prof R.W. Bayliss  Applications accepted all year round  Competition Funded PhD Project (Students Worldwide)

Leeds United Kingdom Biochemistry Biophysics Cell Biology Molecular Biology Organic Chemistry Structural Biology

About the Project

Transient protein-protein interactions (PPIs) control all cellular processes relevant to health and disease. Thus, a major problem in life-sciences research is to understand and manipulate PPIs with molecular and temporal resolution. Addressing this challenge will illuminate our understanding of disease development e.g. cell signalling in cancer and aggregation in amyloid disease and provide starting points for drug-discovery. However, methods to interrogate and manipulate PPIs are not well established. Moreover, intrinsically disordered regions, segments of protein with no fixed structure, that undergo disorder-to-order transitions upon formation of the PPI, compound this challenge. A PhD studentship is available to work on Deciphering the function of intrinsically disordered protein regions in a cellular context using The Aurora A kinase (Aurora A) as a target. This will, focus on chemical biology, structural molecular biology, or cell biology and involve a combination of supervisors from a project team that include: Prof Andy Wilson, Prof Richard Bayliss, Dr Megan Wright, Dr Takashi Ochi, Dr Darren Tomlinson and Professor Sheena Radford and Professor Colin Johnson.

Funding Notes

Please refer to the University of Leeds website for information regarding funding opportunities.


1. J. Miles, F. Hobor, C. Trinh, J. Taylor, C. Tiede, P. Rowell, B. Jackson, F. Nadat, P. Ramsahye, H. Kyle, B. Wicky, J. Clarke, D. Tomlinson, A. Wilson and T. Edwards, ChemBioChem, 2020, n/a, 10.1002/cbic.202000585.
2. C. M. Grison, G. M. Burslem, J. A. Miles, L. K. A. Pilsl, D. J. Yeo, Z. Imani, S. L. Warriner, M. E. Webb and A. J. Wilson, Chemical Science, 2017, 8, 5166-5171.
3. J. A. Miles, D. J. Yeo, P. Rowell, S. Rodriguez-Marin, C. M. Pask, S. L. Warriner, T. A. Edwards and A. J. Wilson, Chemical Science, 2016, 7, 3694-3702.
4. S. G. Burgess, A. Oleksy, T. Cavazza, M. W. Richards, I. Vernos, D. Matthews and R. Bayliss, Open Biology, 2016, 6, 160089.
5. J. E. Horne, M. Walko, A. N. Calabrese, M. A. Levenstein, D. J. Brockwell, N. Kapur, A. J. Wilson and S. E. Radford, Angewandte Chemie International Edition, 2018, 57, 16688-16692.
6. M. H. Wright, C. Fetzer and S. A. Sieber, Journal of the American Chemical Society, 2017, 139, 6152-6159.
7. M. W. Richards, S. G. Burgess, E. Poon, A. Carstensen, M. Eilers, L. Chesler and R. Bayliss, Proceedings of the National Academy of Sciences of the United States of America, 2016, 113, 13726-13731.
8. Y. K. Rennie, P. J. McIntyre, T. Akindele, R. Bayliss and A. G. Jamieson, ACS Chemical Biology, 2016, 11, 3383-3390.
9. S. G. Burgess, M. Mukherjee, S. Sabir, N. Joseph, C. Gutiérrez-Caballero, M. W. Richards, N. Huguenin-Dezot, J. W. Chin, E. J. Kennedy, M. Pfuhl, S. J. Royle, F. Gergely and R. Bayliss, EMBO J., 2018, 37, e97902.
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