Honors & Awards

  • EMBO Long-Term Fellowship Award, EMBO (2013-2015)

Professional Education

  • Bachelor of Science, University of Manchester (2007)
  • Doctor of Philosophy, University Of Edinburgh (2013)

Stanford Advisors

Research & Scholarship

Lab Affiliations


All Publications

  • Regulating the timing of CENP-A nucleosome assembly by phosphorylation. Developmental cell Miell, M. D., Straight, A. F. 2015; 32 (1): 1-2


    In this issue of Developmental Cell, Yu et al. (2015) demonstrate that CENP-A phosphorylation by CDK1 inhibits its association with the chaperone protein HJURP and that the removal of this modification at mitotic exit is a key regulatory event that controls the timing of new CENP-A nucleosome formation at centromeres.

    View details for DOI 10.1016/j.devcel.2014.12.020

    View details for PubMedID 25584791

  • Reply to "CENP-A octamers do not confer a reduction in nucleosome height by AFM". Nature structural & molecular biology Miell, M. D., Straight, A. F., Allshire, R. C. 2014; 21 (1): 5-8

    View details for DOI 10.1038/nsmb.2744

    View details for PubMedID 24389543

  • CENP-A confers a reduction in height on octameric nucleosomes. Nature structural & molecular biology Miell, M. D., Fuller, C. J., Guse, A., Barysz, H. M., Downes, A., Owen-Hughes, T., Rappsilber, J., Straight, A. F., Allshire, R. C. 2013; 20 (6): 763-765


    Nucleosomes with histone H3 replaced by CENP-A direct kinetochore assembly. CENP-A nucleosomes from human and Drosophila have been reported to have reduced heights as compared to canonical octameric H3 nucleosomes, thus suggesting a unique tetrameric hemisomal composition. We demonstrate that octameric CENP-A nucleosomes assembled in vitro exhibit reduced heights, indicating that they are physically distinct from H3 nucleosomes and negating the need to invoke the presence of hemisomes.

    View details for DOI 10.1038/nsmb.2574

    View details for PubMedID 23644598

  • A novel interaction between the human papillomavirus type 16 E2 and E1 E4 proteins leads to stabilization of E2 VIROLOGY Davy, C., McIntosh, P., Jackson, D. J., Sorathia, R., Miell, M., Wang, Q., Khan, J., Soneji, Y., Doorbar, J. 2009; 394 (2): 266-275


    The E4 (also called E1--E4) and E2 proteins of human papillomavirus type 16 are thought to be expressed within the same cells of a lesion, and their open reading frames overlap, suggesting that they may have a functional relationship. We have examined the effect of co-expression of these two proteins and found that each enhances the level of the other. We also identified the N-terminus of E2 as the first example of a viral protein that directly binds the HPV16 E1--E4 protein. This appears to result in the E2 becoming less soluble and promotes its relocation from the nucleus to the cytoplasm. In addition, the turnover of the E2 protein is decreased in the presence of E1--E4. All this raises the possibility that E1--E4 acts to influence E2 activity by varying the amount of available E2 in the cell.

    View details for DOI 10.1016/j.virol.2009.08.035

    View details for Web of Science ID 000271924500012

    View details for PubMedID 19783272

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