The Centenary Award will be presented to Professor Sheena Radford OBE in 2025. Sheena obtained her BSc in Biochemistry from the University of Birmingham in 1984 and PhD from the University of Cambridge in 1987, before moving to the University of Oxford, where she was first a postdoc and then Royal Society University Research Fellow in the Oxford Centre for Molecular Sciences. In 1995, she moved to the University of Leeds as Lecturer in Biochemistry and was a founder member of the Astbury Centre for Structural Molecular Biology. She was made a full Professor of the University of Leeds in 2000 and was Director of the Astbury Centre from 2012-2021. She currently holds the position of Royal Society Research Professor and is the Astbury Professor of Biophysics. Her research spans the disciplines, focussing on the question of how proteins fold, how gram-negative bacteria fold proteins into the outer membrane to create their cell wall, and how proteins misfold and form amyloid in disease. She has received several awards in recognition of her work, including the Biochemical Society’s Colworth Medal, Membership of EMBO and of the Academia Europaea, Fellowships of the Royal Society, Academy of Medical Sciences, Society of Biology and Royal Society of Chemistry and was made member of the Order of the British Empire (OBE) in 2020 for her services to molecular biology.

Sheena said: "I am delighted and humbled to receive this award. I have been a member of the Biochemical Society since I was an undergraduate, which makes the award even more special for me. I have been lucky to have worked with a fantastic group of talented early career scientists and collaborators both in the Astbury Centre at Leeds and across the globe. I thank them all. The very best of science is performed in collaborative and supportive teams. If I have helped to promote that working ethos, and to help others, then I have done my job! The field of protein folding has never been more exciting and I hope that this award will inspire others to join our community and help to tackle the dire consequences caused when protein folding goes wrong.”

The Centenary Award will be presented to Professor Gideon Davies in 2024. Gideon obtained his PhD from the University of Bristol in 1990 before moving to the EMBL Hamburg. He moved to York, with visits to Grenoble and Uppsala before taking up a Royal Society University Research Fellowship (URF) in 1996. In 2000, he was the inaugural “Peter Wall Catalytic Visitor” at the University of British Columbia before being made a full Professor of the University of York in 2001. In 2016, he received the Royal Society "Ken Murray" Research Professorship. His research work spans chemistry and biology with a focus on the enzymes that synthesise and degrade carbohydrates and glycans. He is well known for his work on enzyme mechanism, following the unusual contortions of sugars in enzyme active sites, and building on this to develop inhibitors and more recently activity-based probes. Recent impact includes the development of inhibitor classes that underpinned the development of compounds in clinical trial for neurodegeneration, studies of the human heparanase enzyme and development of new anti-cancer compounds as well as applying activity probes and new chemistries in the field of industrial biomass conversion.

On winning the Centenary Award for 2024, Gideon said “It is especially important to me that this award, beyond research impact, also reflects a commitment to nurture talent within the scientific community. I am so proud of the wonderful, diverse, group of young and early-career scientists I have worked with throughout my career and to see them thriving in academia, industry, education and child support is the true highlight of my career. I hope the award will inspire other young scientists, from all backgrounds, to dive into the exciting world of the glycosciences.”

The 2023 Centenary Award was presented to Professor Matthias Hentze. Matthias is the Director of the European Molecular Biology Laboratory (EMBL) and Co-Director of the Molecular Medicine Partnership Unit (MMPU). Following medical training in Germany and the UK, he codiscovered “iron-responsive elements” as the first mammalian regulatory elements in mature mRNAs during his postdoctoral research at NIH. After two decades of elucidating mechanisms of RNA regulation by RNA binding proteins, the Hentze group recently uncovered hundreds of new RNA-binding proteins, including many metabolic enzymes. Their current work focuses on riboregulation in metabolism and cell biology.

Matthias is a co-founder of the MMPU, an interdisciplinary and translational research unit between EMBL and Heidelberg University. His work has been widely recognized, including Germany’s most prestigious Gottfried Wilhelm Leibniz Prize and the Lifetime Achievement Award of the RNA Society. He is an elected member of the European Molecular Biology Organisation, the German Academy of Sciences Leopoldina, the Academia Europaea, the Australian Academy of Science, and the American Academy of Arts and Sciences. Matthias serves on numerous scientific advisory and editorial boards, and in 2020 initiated the Environmental Research Initiative and Fund.

Matthias says: “I feel deeply honoured to receive this prestigious award which I want to share with the many outstanding team members whom I had the pleasure to mentor. RNA science holds so many more exciting secrets and I hope that the award helps to draw attention to this.” 

Matthias presented his Award lecture at RNA Granules on 10 October 2023.

The 2020 Centenary Award was presented to Professor Dame Kay E Davies of the University of Oxford, UK.

Kay completed her D.Phil studies at the Department of Biochemistry, University of Oxford. After a Royal Society Fellowship in France she moved back to St Mary’s Hospital Medical School to study Duchenne muscular dystrophy (DMD), a progressive muscle wasting disease. In 1984, as a MRC Senior Fellow, she moved back to Oxford to work on the molecular analysis of neurological disorders. She was appointed Professor of Genetics and then Dr Lee’s Professor of Anatomy and set up the MRC Functional Genomics Unit to apply genomics to genetic disease analysis. Her own group focuses on the development of therapeutic strategies for DMD. Kay’s earlier work paved the way for the use of mini dystrophin gene delivery using AAV and contributed to the exon skipping approach to therapy. She also discovered the dystrophin related protein, utrophin, and demonstrated that increased levels of utrophin can compensate for the lack of dystrophin in the mdx mouse model of the disease. This has led to the identification of small molecules which increase utrophin in adult mdx muscle and prevent pathology. Kay co-founded Summit Therapeutics to translate her work into the clinic. She is a founding fellow of the UK Academy of Medical Sciences and was elected a Fellow of the Royal Society in 2003. She was a Governor of the Wellcome Trust from 2008-17 and Deputy Chairman from 2013-2017. Kay was made Dame Commander of the British Empire for services to science in 2008.

Kay said: “I am very honoured and delighted to have my work recognised in this way by the Biochemical Society. I am also very grateful to all the talented researchers I have had the privilege to work with over the years.”

Kay presented her Award lecture on Wednesday 29 July 2020 as part of the Biochemistry Focus webinar series. View the recording.

The 2019 Centenary Award was presented to R. John Ellis from the University of Warwick, UK. John has made fundamental discoveries through the study of the mechanism of protein folding essential for light harvesting and photosynthesis. His work focused on the pathway by which the key enzyme of photosynthesis (RUBISCO) – the most abundant protein on earth – is made and assembled in plant cells. From this specific case, John developed key concepts which have revolutionized thinking about how proteins assemble and fold in all cells. John termed these other proteins that assist in protein folding and assembly ‘molecular chaperones’ and his key insight showed that these chaperones are not restricted to the protein assembly pathway that he studied, but exist universally in all cells.

The 2018 Centenary Award was presented to Professor Frank McCormick from the University of California San Francisco Helen Diller Family Comprehensive Cancer Center. Frank has been a leader in the field of RAS oncogene function and regulation for over 30 years, having made a large number of seminal discoveries about the signalling pathway regulated by the RAS protein. His identification of RAS GAP marked the start of the rush to understand the regulation of RAS proteins and their normal role within the cell. With the identification of the NF1 protein as a member of the GAP family this led to fundamental understanding of Neurofibromatosis type I. Frank has also contributed very important observations about the downstream pathways regulated by RAS, including the RAF/MAPK pathway and PI3K signaling. Frank has also been hugely influential outside of his own lab, he founded ONYX Pharmaceuticals, a company dedicated to developing new cancer therapies. In addition to all this, Frank has also been President of the AACR and made many other contributions to the cancer research community at the highest level. 

Of winning the Centenary Award, Frank said “I am absolutely thrilled to receive this award.  It means a great deal to me to be recognized by my peers, especially as I was trained as a biochemist in the UK and attended many outstanding Biochemical Society meetings in which I made connections and gained new insights that have affected my entire career.”

Read his review article 'Progress in targeting RAS with small molecule drugs' published in the Biochemical Journal. 

The 2016 Centenary Award was presented to Patrick Cramer from Max Planck Institute for Biophysical Chemistry, Germany.  The award is made in recognition of Patrick’s successful systems biology approach to uncovering the importance of and mechanisms in transcriptome surveillance and RNA degradation in the balanced production of mRNAs.  Furthermore, two important crystal structures were published in 2013.

Patrick Cramer received his award at the 80th Harden Conference: Machines on Genes IV – Mechanisms of Actions of Large Macromolecular Machines on Genes Across Biological Scales at Shrigley Hall Hotel, Macclesfield, UK, 31 July—4 August 2016.

Read his review article published in Biochemical Society Transactions here: Structure determination of transient transcription complexes. 

The 2013 Centenary Award was presented to G. Marius Clore. 

Read his article 'Seeing the invisible by paramagnetic and diamagnetic NMR' published in Biochemical Society Transactions here. 

The 2012 Centenary Award was presented to David Baker.

Read his article 'Protein folding, structure prediction and design' published in Biochemical Society Transactions here.

The 2011 Centenary Award was presented to Nahum Sonenberg.

Read his review article 'Signalling to eIF4E in cancer' published in Biochemical Society Transactions here.