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Department of Biochemistry

Dee Scadden PI

Teaching in Biochemistry, Technology Enabled Learning

Over the past 6 years, I have had the opportunity to primarily focus my efforts on teaching, teaching development, and the expansion of digital learning in Biochemistry and the School of the Biological Sciences (SBS). The importance of engagement in these aspects of teaching came to the fore as we recently negotiated the impact of the Covid-19 pandemic. As the landscape of teaching continues to develop and change, innovation in key areas of teaching means we are well positioned to respond to unexpected challenges and requirements in teaching, alongside having the capacity to initiate transformative changes within our teaching portfolio. Importantly, in all aspects of teaching development, decisions are underpinned by an overarching desire to ensure our teaching is pedagogically sound and accessible to every student.


Key areas of innovation in teaching

  • Development of resources to support online delivery of teaching, including delivery of interactive online practical sessions 
  • Production of animated films to facilitate student engagement and deliver outreach activities
  • Production of films to explain fundamental biochemical or molecular biology concepts
  • Development of resources to support inclusive approaches to teaching and learning (Universal Design for Learning)
  • Implementatioin of an online exam platform (Inspera Assessment; the pilot in SBS commenced in the 2021–22 academic year). Link to the Inspera Moodle site (self-enrolment) HERE.


Recognition for teaching innovation

  • Pilkington Teaching Prize (University of Cambridge) (2021)
  • Technology Enabled Learning Prize in STEM (Cambridge University Press, Cambridge Centre for Teaching and Learning) (2019)
  • Biochemical Society Teaching Excellence Award (2017)


Research Interests – RNA Editing and Stress Responses

Double stranded RNA in mammalian cells may be edited by 'Adenosine deaminases that act on RNA' (ADARs), which convert adenosine (A) residues to inosine (I). Editing may be very selective, sometimes resulting in a single amino acid change in the encoded protein, but it may alternatively be widespread. In this case, 'hyper-editing' of dsRNA can result in up to 50% of A residues being converted to I, which has a significant impact on both the sequence and structure of the dsRNA. Wholesale editing thus gives rise to distinct molecules that are readily recognizable in mammalian cells. The role(s) of these hyper-edited dsRNAs in cells are poorly understood. However, deletion of ADAR1, which is likely to play a substantial role in hyper-editing of long dsRNAs, results in embryonic lethality in mice – thereby demonstrating the importance of hyper-edited dsRNA. Our research focussed on the role of hyper-edited dsRNA in mammalian cells.


 Key publications:

  1. Ng, S.K., Weissbach, R., Ronson, G. and Scadden, A.D.J. (2013).  Proteins that contain a functional Z-DNA binding domain localize to cytoplasmic stress granules.  Nucleic Acids Research, first published online August 27, 2013 doi:10.1093/nar/gkt750
  2. Vitali, P. and Scadden, A.D.J. (2010). Double-stranded RNAs containing multiple IU pairs are sufficient to suppress interferon induction and apoptosis.  Nature Structural & Molecular Biology, 17, 1043–1050.
  3. Scadden, A.D.J. (2007).  Inosine-containing dsRNA binds a stress-granule-like complex and downregulates gene expression in trans. Molecular Cell, 28, 491–500.
  4. Scadden, A.D.J. (2005). The RISC subunit Tudor-SN binds to hyper-edited double-stranded RNA and promotes its cleavage. Nature Structural & Molecular Biology, 12, 489–496.