In 2011, the Biochemical Society introduced the Centenary Award to replace the Jubilee Lecture.
The Jubilee Lecture was established to commemorate the Society’s 50th anniversary in 1961. It was awarded to a biochemist of distinction from any part of the world and the awardee was asked to lecture on their chosen field of research. The award was changed to the Centenary Award, first awarded in 2011 to celebrate the Society’s 100th anniversary.
Congratulations to Professor Matthew Freeman from the University of Oxford!
Find out more about Matthew below
Sheena Radford will present her Award Lecture at Protein Evolution, Design and Bioinformatics Edinburgh between 13-15 May 2026.
Register now!For further information please get in touch with the Awards department.
The Centenary Award will be presented to Professor Matthew Freeman in 2027. Matthew is the Head of the Dunn School of Pathology at the University of Oxford. After a PhD from Imperial College, London, he did a postdoctoral fellowship at the University of California, Berkeley. He returned to the UK to establish his own group at the MRC Laboratory of Molecular Biology in Cambridge, where he became Head of the Division of Cell Biology, before moving in 2013 to Oxford to lead the Dunn School.
His group originally worked on developmental genetics in Drosophila, but the long-term focus on cell signalling mechanisms steered the lab towards the cell biology, genetics, biochemistry and structural biology of membrane proteins, with a specific focus on the rhomboid-like superfamily of proteases and pseudoproteases, which they discovered. Although primarily driven by fundamental discovery science, his group’s work has the goal of revealing principles relevant to human disease. Recently, this has included insights into inflammation, immunity and cancer.
Matthew Freeman has chaired the British Society of Developmental Biology, the Company of Biologists, and EMBO Council. He is a member of EMBO, and a Fellow of the Royal Society and the Academy of Medical Sciences.
Matthew said: "It’s a huge honour to receive the Centenary Award, especially when I look through the illustrious list of previous recipients.
We do not do science for awards but, honestly, recognition by peers and colleagues is lovely! Of course, the real credit for the research that my lab has done belongs to the many really outstanding past and current students and postdocs with whom I have had the privilege to work.
I started my scientific life as a biochemistry student and have since moved between genetics, developmental biology and cell biology. More recently, I have increasingly returned to biochemistry, so it's a particular pleasure to receive an award from the Biochemical Society."
The Centenary Award will be presented to Professor Kevan Shokat in 2026. Kevan is currently an Investigator of the Howard Hughes Medical Institute, Professor in the Department of Cellular and Molecular Pharmacology at UCSF and a Professor of Chemistry at UC Berkeley. Kevan received his undergraduate degree at Reed College, his PhD at UC Berkeley and did post-doctoral training at Stanford. He was inducted into the National Academy of Sciences (2010), the National Academy of Medicine (2011), and the American Academy of Arts and Sciences (2011). His lab is most well-known for drugging the "undruggable" oncogene K-Ras (G12C) in 2013. K-Ras was the first human oncogene to be discovered in 1982 and remained undrugged until work from the Shokat lab at UCSF. In May of 2021 the drug sotorasib which binds to the pocket identified by Shokat on K-Ras (G12C) was approved for the treatment of lung cancer patients with this mutation. The field of K-Ras drug discovery is expanding quickly to hunt for drugs to target the other K-Ras mutants such as those which drive colon and pancreatic cancers which collectively represent almost 20% of all cancer patients world-wide.
Kevan said: "I would like to thank the Biochemical Society for this recognition of our lab’s efforts to develop tool molecules and drugs which target key drivers of cancer including protein and lipid kinases and the GTPase K-Ras.”
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.”
Gideon presented his Award lecture at Advances and New Horizons in Glycobiology on 5 December 2024.
Read Gideon's review article published in the Biochemical Journal - Activity-based probes for dynamic characterisation of polysaccharide-degrading enzymes
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 2022 Centenary Award was presented to Professor Jeremy Thorner. Professor Thorner is a biochemist recognized for his contributions to our understanding of biological signal transduction mechanisms. Born, raised, and educated in the public schools in Quincy, Massachusetts, USA, he received his A.B. magna cum laude (Biochemical Sciences) from Harvard College (1967) and his PhD (Biochemistry) under Henry Paulus from Harvard University (1972). He was a Jane Coffin Childs Postdoctoral Fellow (1972-74) under I. Robert Lehman in the Biochemistry Department at Stanford University School of Medicine. Appointed to the faculty at the University of California, Berkeley, in 1974, he held the William V. Power Chair in Biology for 20 years (1991-2011). He is (since 2020) Professor Emeritus of Biochemistry, Biophysics and Structural Biology in the Department of Molecular and Cell Biology at UC Berkeley. Other honors he has received for his research and teaching include a 10-year MERIT Award (1989-1998) from the National Institute for General Medical Sciences, the Dean’s Award for Distinguished Research Mentoring of Undergraduates in the College of Letters and Science at Berkeley (2004), election to the American Academy of Arts and Sciences (2007) and US National Academy of Sciences (2015), and the Herbert Tabor Research Award of the American Society for Biochemistry and Molecular Biology (2019).
Jeremy said: "When I examine the list of previous recipients of the honor of The Centenary Award, and its predecessor the Jubilee Lectureship, I am truly humbled to be placed in the same company. Moreover, I freely acknowledge that, through me, this high accolade is actually bestowed on each of the many outstanding scientists who worked with me over the past 47 years and were directly responsible for our mutual success".
Jeremy presented his Award lecture at the 5th European Workshop on AMPK and AMPK-related kinases on 27 September 2022.
Read Jeremy's article published in the Biochemical Journal - TOR complex 2 is a master regulator of plasma membrane homeostasis
The 2021 Centenary Award will be presented to Professor Kim Nasmyth at the University of Oxford, UK. Kim currently holds the Whitley Chair at the Department of Biochemistry, University of Oxford and is a fellow of Trinity College. After completing his PhD in the late 1970s, he has been a Robertson Research Fellow at Cold Spring Harbor, and a member of staff at the MRC laboratory for molecular biology in Cambridge. Kim later moved to the Research Institute of Molecular Pathology in Vienna, where he was a Senior Scientist from 1988–1997 and Director from 1997–2006. His scientific work has addressed the mechanisms by which genes are turned on and off during development, how DNA replication is controlled, and how chromosomes are segregated during mitosis and meiosis.
On winning the Centenary Award, Kim said: “I must confess that I never trained as a biochemist. I had planned to read chemistry but changed to biology shortly after arriving at university and eventually became a molecular geneticist. Ever since, I have always strived to explain biological phenomena in terms as simple as possible. Partly by chance and partly by inclination, I have spent much of my research career attempting to understand the propagation of chromosomes during cell division, a biochemical process unique to living systems. This required molecular genetics to identify the key players, such as cohesin, but now requires biochemistry and biophysics to understand its mode of action. There are times now when I regret abandoning chemistry so early in my career, but if I had not, I would never have discovered cohesin or had the privilege to be one of the first people to study its remarkable enzymology. As a molecular geneticist, I am therefore especially honoured to have been recognized by the Biochemical Society’s Centenary Award as an honorary biochemist.”
Kim presented his Award Lecture at Genome organisation by SMC complexes on 29 September 2022.
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 2017 Centenary Award was awarded to Salvador Moncada from the University of Manchester. Salvador has been successively at the forefront of three areas of research in his career to date. Earlier in his career he pioneered prostaglandin pharmacology, he was then a central figure in nitric oxide biology and he has since led the way in understanding how energy metabolism can be regulated and adapted by various signalling pathways. In all of these areas, his work has been ground-breaking and widely recognised by the scientific community.
Another major aspect of Salvador’s career has been his leadership roles, first in the Wellcome Research Laboratories, then at UCL and more recently at the CNIC in Spain and in Manchester. In all these projects Salvador has built a reputation in building research institutions and in developing the careers of others. He has also driven the translation of much of this work into new products and start-up companies. In all of these his ability to straddle the two worlds of basic and applied science was a huge advantage that enabled him to drive basic breakthroughs in ways that led on to improvements in human health.
Salvador presented his award lecture at the Biochemical Society conference entitled ‘ROS and Mitochondria in Nervous System Function and Disease‘, 27—29 March 2017, at Charles Darwin House, London, UK.
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 2014 Centenary Award was presented to Professor Susan Taylor from the Howard Hughes Medical Institute, University of California San Diego, USA. Susan has made fundamental and pioneering contributions to understanding the structure and function of protein kinases. Susan received her undergraduate degree at the University of Wisconsin and her PhD in Physiological Chemistry from the Johns Hopkins University. She did her postdoctoral work at the MRC Laboratory of Molecular
Biology in Cambridge with Brian Hartley and then went to the newly founded University of San Diego, first as a postdoctoral fellow with Nathan Kaplan and then rising through the ranks to the level of Distinguished Professor of Chemistry and Biochemistry and of Pharmacology. She is also a Howard Hughes Medical Institute Investigator.
Her research on the structure and function of cAMP-dependent protein kinase (PKA) led to her solving the crystal structure of the first protein kinase in 1991. The PKA catalytic subunit has served as the prototype for the entire protein kinase superfamily that regulates so many biological processes. Her subsequent structures of the PKA regulatory subunits and most recently of full-length tetrameric holoenzymes show how a large macromolecular signalling complex is assembled at specific sites in the cell.
Susan presented her Award Lecture 'PKA: Dynamic Assembly of Alloseteric Macromolecular Signaling Complexes' at The University of Dundee's College of Life Sciences on 14 July 2014.
Read Susan's article published in Biochemical Society Transactions - Pseudokinases from a structural perspective.
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.
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