The Revd Professor Robert Gilbert

Background

After a BSc in Molecular Biology and Biochemistry at the University of Durham, Robert Gilbert researched for a PhD at Leicester University in the Departments of Biochemistry and Microbiology and Immunology. He came to Oxford as a post-doc in the Division of Structural Biology and in 2002 became Fellow and Tutor in Biochemistry at Magdalen. He was later a Royal Society University Research Fellow (2004-2012) and Professor of Biophysics and Director of Graduate Studies in the Nuffield Department of Medicine (2015-2026). He is now the Team Rector of the Cherwell Valley Benefice in Oxford Diocese.

His book “Science and the Truthfulness of Beauty” is published by Routledge.

Research Interests

Structural and biophysical methods applied to biomedically-important cellular processes, including miRNA maturation and degradation in the cell, of relevance to a broad range of cancers, metabolism, inflammation and innate viral immunity; membrane pore formation by proteins of the membrane attack complex/perforin and cholesterol-dependent cytolysin family involved in infection, immunity and development; and the regulation of membrane adhesion to other cells at the extracellular matrix.

Selected Publications

• Yi G, Mamalis D, Ye M, Carrique L, Fairhead M, Li H, Duerr KL, Zhang P, Sauer DB, von Delft F, Davis BG, Gilbert RJC (2026) Covalently constrained ‘Di-Gembodies’ enable parallel structure solutions by cryo-EM. Nat. Chem. Biol. 22, 69-76. 
• Bano F, Banerji S, Ni T, Green DE, Cook KR, Manfield IW, DeAngelis PL, Paci E, Lepšík M, Gilbert RJC, Richter RP, Jackson DG (2025) Structure and unusual binding mechanism of the hyaluronan receptor LYVE-1 mediating leucocyte entry to lymphatics. Nat. Commun. 16, 2754.
• Yi, G, Ye, M, Carrique, L, El-Sagheer, A, Brown, T, Norbury, CJ, Zhang, P and Gilbert, RJC (2024) Structural basis for activity switching in polymerases determining the fate of let-7 pre-miRNAs. Nat. Struct. Mol. Biol. 31, 1426-1438.
• Yu, X, Ni, T, Munson, G, Zhang, P and Gilbert, RJC (2022) Cryo‐EM structures of perforin‐2 in isolation and assembled on a membrane suggest a mechanism for pore formation. EMBO J. 41, e111857.