Rate My Professor Paul Pace

Dr. Paul Pace is a Senior Research Fellow at the Mātai Hāora – Centre for Redox Biology and Medicine in the Department of Pathology and Biomedical Science, University of Otago, Christchurch, within the Faculty of Medicine, Health Sciences Division. He obtained his BSc (Hons) from the University of London, UK, and his PhD from the University of Cambridge, UK, at the Laboratory of Molecular Biology, where he investigated DNA repair mechanisms. Prior to his current role, Pace worked at Imperial College of Science and Technology in London. His career at Otago encompasses advanced research in redox biology, contributing to the understanding of oxidative stress in disease processes.

Pace's expertise includes molecular biology techniques such as cloning, mutagenesis, and CRISPR applications; protein biochemistry encompassing expression and purification, antibody generation and purification, immunocytochemistry, immunoprecipitation, and analytical methods; and cell biology involving cell culture, transfection, and lentiviral expression. His current research focuses on the biochemistry of peroxiredoxins and their roles in cell signalling, particularly the redox regulation of phosphorylation-dependent cell migration and transformation in cancer. He teaches components of the BBiomedSc(Hons) programme, has supervised two summer students, and co-supervises two PhD students. Key publications include 'Peroxidasin is associated with a mesenchymal-like transcriptional phenotype and promotes invasion in metastatic melanoma' (Free Radical Biology & Medicine, 2025), 'Redox proteomic analysis of H2O2-treated Jurkat cells and effects of bicarbonate and knockout of peroxiredoxins 1 and 2' (Free Radical Biology & Medicine, 2025), 'Effect of peroxiredoxin 1 or peroxiredoxin 2 knockout on the thiol proteome of Jurkat cells' (Free Radical Biology & Medicine, 2024), 'Hypothiocyanous acid reductase is critical for host colonization and infection by Streptococcus pneumoniae' (Journal of Biological Chemistry, 2024), and 'Hyperoxidized peroxiredoxin 2 interacts with the protein disulfide isomerase ERp57' (Biochemical Journal, 2013).