Rate My Professor Sarah Heath

Heath is first author on the seminal 2024 Nature Communications paper 'Amyloid formation and depolymerization of tumor suppressor p16INK4a are regulated by a thiol-dependent redox mechanism,' showing cancer-associated mutations increase amyloid propensity while stabilizing mutations inhibit it. Additional peer-reviewed publications include co-authorship on 'Characterizing the amyloid core region of the tumor suppressor protein p16INK4a using a limited proteolysis and peptide-based approach' (Journal of Biological Chemistry, 2024), 'Oxidation of caspase-8 by hypothiocyanous acid enables TNF-mediated necroptosis' (2023), 'Molecular basis of a redox switch: molecular dynamics simulations and surface plasmon resonance provide insight into reduced and oxidised angiotensinogen' (2021), and 'Modifying the resolving cysteine affects the structure and hydrogen peroxide reactivity of peroxiredoxin 2' (2021). She has presented her work verbally and via posters at the 32nd Society for Redox Research Australasia Meeting, 34th Queenstown Molecular Biology Meeting, and Queenstown Research Week Biomolecular Interactions Meeting. Funded by the Royal Society Marsden Fund and Health Research Council of New Zealand, her contributions advance understanding of redox biology in cancer, with potential impacts on diagnostics and treatments, as highlighted in University of Otago news.