Dr Cassandra Terry is a Reader in Biosciences with the School of Human Sciences.
Dr Cassandra Terry is a Reader in Biosciences and has a BSc (Hons) in Biochemistry (The University of Sheffield), an MRes in Structural Proteomics (The University of St Andrews) and a PhD studying Bacillus spore structure (The University of Sheffield).
Her previous research includes working on neurodegenerative diseases (University College London), studying the structure of ATPases (Medical Research Council, Cambridge) and developing anti-cancer treatments (AstraZeneca).
Dr Terry's professional activities include being a professional registration assessor (The Science Council) and an external examiner and lecturer for MSc Neuroscience (King’s College London). She also serves as a scientific committee member and advisor for the British Brain Bee charity.
Her memberships of professional bodies include the Biochemical Society and the Royal Society of Biology (CBiol CSci MRSB). Dr Terry is also a Fellow of Royal Microscopical Society (FRMS).
Dr Terry teaches on the Applied Bioscience, Biomedical Science and Extended Science modules, and is the module leader for Advanced Immunology (MSc) and Human Immunity and Applied Immunology (BSc).
Dr Terry is particularly interested in studying the structure of pathogens that cause disease in particular the body’s own proteins that can misfold resulting in neurodegenerative diseases (such as CJD and Alzheimer’s disease).
Terry C, Harniman RL, Sells J, Wenborn A et al. Structural features distinguishing infectious ex vivo mammalian prions from non-infectious fibrillar assemblies generated in vitro (2018). Submitted.
Terry C. Investigating the structure of prions (2018). The CJD Support Network newsletter
Sarell C, Quarterman E, Yip D, Terry C et al. Soluble AB aggregates can inhibit prion propagation (2017). Open Biol. 7: 170158.
Terry C & Sells J. Experimental Words: a collision of art and science (2018). Network Magazine, MRC.
Sells J & Terry C. FROM BRAIN TO GRAIN: Taking science out of the lab (2017). Roots 14.2
Terry C, Sells J, Sawyer B, Sarell C. Dirty Dopers: cheating or competing? Our Olympics influenced activity addressing doping in sport (2017). The Biochemist.
Terry C, Jiang S, Radford DS, Wan Q, Tzokov S, Moir A, Bullough PA. Molecular tiling on the surface of a bacterial spore- the exosporium of the Bacillus anthracis/cereus/thuringiensis group (2017). Mol Microbiol. doi: 10.1111/mmi.13650. Front cover.
Terry C, Wenborn A, Gros N, Sells J,Joiner S, Hosszu LLP, Tattum MH, et al. Ex vivo mammalian prions are formed of paired double helical prion protein fibrils (2016). Open Biology 6, 160035.
Wenborn A, Terry C, Gros N, Joiner S et al. A novel and rapid method for obtaining high titre intact prion strains from mammalian brain (2015). Sci Rep 5, 10062.
Trevitt CR, Hosszu LL, Batchelor M, Panico S, Terry C, et al. N-terminal Domain of Prion Protein Directs its Oligomeric Association (2014). J Biol Chem. 289, 25497-25508.
Hu NW, Nicoll AJ, Zhang D, Mably AJ, O’Malley T, Purro SA, Terry C, et al. mGlu5 receptors and cellular prion protein mediate amyloid-β-facilitated synaptic long-term depression in vivo (2014). Nat Commun. 4;5:3374 doi: 10.1038/ncomms4374
Nicoll AJ, Panico S, Freir DB, Wright D, Terry C, et al. Amyloid-β nanotubes are associated with prion protein-dependent synaptotoxicity (2013). Nat Commun. 11;4:2416. doi: 10.1038/ncomms3416.
Terry C, Shepherd A, Radford D, Moir A, Bullough PA. YwdL in B. cereus: Its Role in Germination and Exosporium Structure (2011). PLoS One. 6 (8) e23801.
Kailas L, Terry C, Abbott N, Taylor R, et al. Surface Architecture of Bacillus Endospores at the Sub-nanometre Scale (2011). Proc Natl Acad Sci. USA 108 (38) 16014-9.
Mueller DM, Puri N, Kabaleeswaran V, Terry C, Leslie AG, Walker JE. Crystallization and preliminary crystallographic studies of the mitochondrial F1-ATPase from the yeast Saccharomyces cerevisiae (2004). Acta Crystallogr D Biol Crystallogr. 60(Pt 8). 1441-1444.
Mueller DM, Puri N, Kabaleeswaran V, Terry C, Leslie AG, Walker JE. Ni-chelate-affinity purification and crystallization of the yeast mitochondrial F1-ATPase (2004). Protein Expr Purif. 37, 479-485.
Mueller DM, Puri N, Kabaleeswaran V, Terry C, Leslie AGW, and Walker J.E. Structural analysis of the yeast F1- ATPase at a resolution of 2.8Å (2004). Advance Photon Source, Argonne National Laboratories.
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