Ben G. Davis

Ben Davis

Ben Davis at the Royal Society admissions day in London, July 2015
Born Benjamin Guy Davis
(1970-08-08) 8 August 1970[1][2][3]
Fields
Institutions
Alma mater University of Oxford (BA, DPhil)
Thesis Synthesis of inhibitors of sugar processing enzymes (1996)
Doctoral advisor George Fleet[6]
Other academic advisors J. Bryan Jones[7]
Doctoral students
Notable awards
Website
users.ox.ac.uk/~dplb0149

Benjamin Guy Davis FRS[20] (born 8 August 1970) is a Professor of Chemistry in the Department of Chemistry at the University of Oxford.[22][23][24][25][26]

Education

Davis was educated at the University of Oxford where he was awarded Bachelor of Arts degree in 1993 followed by a Doctor of Philosophy in chemistry in 1996 as a postgraduate student of Keble College, Oxford.[27][6]

Research and career

After his PhD, Davis spent two years as a postdoctoral research fellow in the laboratory of J. Bryan Jones at the University of Toronto, exploring protein chemistry and biocatalysis.[21]In 1998 he returned to the United Kingdom to take up a lectureship at Durham University. In the autumn of 2001 he moved to the Dyson Perrins Laboratory and received a fellowship at Pembroke College, Oxford. He was promoted to Professor in 2005.[21]

His group's research centres on the chemical understanding and exploitation of biomolecular function (Synthetic Biology, Chemical Biology and Medicinal chemistry), with an emphasis on carbohydrates and proteins. In particular, the group's interests encompass synthesis and methodology; target biomolecule synthesis; inhibitor/probe/substrate design; biocatalysis; enzyme & biomolecule mechanism; biosynthetic pathway determination; protein engineering; drug delivery; molecular biology; structural biology; cell biology; glycobiology; molecular imaging and in vivo biology.[21]

Research in the Davis laboratory has been funded by the Engineering and Physical Sciences Research Council (EPSRC), the Biotechnology and Biological Sciences Research Council (BBSRC), the Medical Research Council, UCB-Celltech, AstraZeneca, the European Union, GlaxoSmithKline, Cancer Research UK, the Wellcome Trust and the Royal Society.[6]

Awards and honours

Davis was elected a Fellow of the Royal Society (FRS) in 2015.[21] His certificate of election reads:

Professor Davis is noted for his chemical interrogation and manipulation of biological systems, particularly those that hinge on carbohydrates and proteins. He has developed selective and benign bond forming strategies that have been applied to biology, allowing the construction of synthetic biomolecules and bioconjugates; the creation of synthetic cells and viruses; and in vivo chemistry. These have enabled associated mechanistic details of protein and sugar biology to be elucidated and exploited for biotechnological applications.[20]


References

  1. DAVIS, Prof. Benjamin Guy. ukwhoswho.com. Who's Who. 2016 (online Oxford University Press ed.). A & C Black, an imprint of Bloomsbury Publishing plc. (subscription required)
  2. Anon (2009). "Benjamin G. Davis". Angewandte Chemie. 48 (22): 3900. doi:10.1002/anie.200901068.
  3. Davis, B. (2010). "Future Visions of Chemistry: Ben Davis". ChemistryViews. doi:10.1002/chemv.201000012.
  4. Davis, B. G. (2002). "Synthesis of glycoproteins". Chemical Reviews. 102 (2): 579–602. PMID 11841255. doi:10.1021/cr0004310.
  5. Gamblin, David P.; Scanlan, Eoin M.; Davis, Benjamin G. (2009). "Glycoprotein Synthesis: An Update". Chemical Reviews. 109 (1): 131–163. ISSN 0009-2665. PMID 19093879. doi:10.1021/cr078291i.
  6. 1 2 3 4 "The Davis Group". University of Oxford. Archived from the original on 15 June 2013.
  7. Ambrosi, M; Cameron, N. R.; Davis, B. G. (2005). "Lectins: Tools for the molecular understanding of the glycocode". Organic and Biomolecular Chemistry. 3 (9): 1593–608. PMID 15858635. doi:10.1039/b414350g.
  8. Bhushan, Bhaskar (2014). Unnatural amino acids as metal-mediated probes of biological function (DPhil thesis). University of Oxford.
  9. Lercher, Lukas A. (2014). Chemical tools for the study of epigenetic mechanisms (DPhil thesis). University of Oxford. OCLC 897880623.
  10. Lercher, L; McGouran, J. F.; Kessler, B. M.; Schofield, C. J.; Davis, B. G. (2013). "DNA modification under mild conditions by Suzuki-Miyaura cross-coupling for the generation of functional probes". Angewandte Chemie International Edition. 52 (40): 10553–8. PMC 3823066Freely accessible. PMID 23943570. doi:10.1002/anie.201304038.
  11. Lin, Yuya Angel (2013). Olefin metathesis for site-selective protein modification (DPhil thesis). University of Oxford. OCLC 868073622.
  12. Patel, Mitul Kiran (2011). Unravelling the biological roles of charged carbohydrates (DPhil thesis). University of Oxford. OCLC 941069418.
  13. Patel, M. K.; Davis, B. G. (2010). "Flow chemistry kinetic studies reveal reaction conditions for ready access to unsymmetrical trehalose analogues". Organic & Biomolecular Chemistry. 8 (19): 4232–5. PMID 20668770. doi:10.1039/c0ob00226g.
  14. Saliba, Régis C. (2014). Design and synthesis of nanoparticles functionalised with Lewis oligosaccharides for selective targeting of DC-SIGN (DPhil thesis). University of Oxford.
  15. Shanley, Samantha Jane (2009). A glycopore for bacterial sensing (DPhil thesis). University of Oxford. OCLC 757099623.
  16. Wyszynski, Filip Jan (2010). Dissecting tunicamycin biosynthesis : a potent carbohydrate processing enzyme inhibitor (DPhil thesis). University of Oxford. OCLC 757140035.
  17. Wyszynski, F. J.; Lee, S. S.; Yabe, T; Wang, H; Gomez-Escribano, J. P.; Bibb, M. J.; Lee, S. J.; Davies, G. J.; Davis, B. G. (2012). "Biosynthesis of the tunicamycin antibiotics proceeds via unique exo-glycal intermediates". Nature Chemistry. 4 (7): 539–46. PMID 22717438. doi:10.1038/nchem.1351.
  18. Yamamoto, Keisuke (2013). Modification and application of glycosidases to create homogeneous glycoconjugates (DPhil thesis). University of Oxford.
  19. Yamamoto, K; Davis, B. G. (2012). "Creation of an α-mannosynthase from a broad glycosidase scaffold". Angewandte Chemie International Edition. 51 (30): 7449–53. PMID 22696205. doi:10.1002/anie.201201081.
  20. 1 2 3 "Professor Benjamin Davis FRS". London: The Royal Society. Archived from the original on 2 May 2015.
  21. 1 2 3 4 5 Anon (2015). "Professor Benjamin Davis FRS". London: Royal Society. Archived from the original on 17 November 2015. One or more of the preceding sentences incorporates text from the royalsociety.org website where:
    “All text published under the heading 'Biography' on Fellow profile pages is available under Creative Commons Attribution 4.0 International License.” --"Royal Society Terms, conditions and policies". Archived from the original on 25 September 2015. Retrieved 9 March 2016.
  22. Ben G. Davis's publications indexed by the Scopus bibliographic database, a service provided by Elsevier. (subscription required)
  23. Dixon, D. P.; Davis, B. G.; Edwards, R (2002). "Functional divergence in the glutathione transferase superfamily in plants. Identification of two classes with putative functions in redox homeostasis in Arabidopsis thaliana". Journal of Biological Chemistry. 277 (34): 30859–69. PMID 12077129. doi:10.1074/jbc.M202919200.
  24. Van Kasteren, S. I.; Kramer, H. B.; Jensen, H. H.; Campbell, S. J.; Kirkpatrick, J.; Oldham, N. J.; Anthony, D. C.; Davis, B. G. (2007). "Expanding the diversity of chemical protein modification allows post-translational mimicry". Nature. 446 (7139): 1105–9. PMID 17460675. doi:10.1038/nature05757.
  25. Anon (2007). "Interview with Ben Davis: Sugar Solutions". Royal Society of Chemistry. Archived from the original on 2 June 2008.
  26. Robinson, M. A.; Charlton, S. T.; Garnier, P; Wang, X. T.; Davis, S. S.; Perkins, A. C.; Frier, M; Duncan, R; Savage, T. J.; Wyatt, D. A.; Watson, S. A.; Davis, B. G. (2004). "LEAPT: Lectin-directed enzyme-activated prodrug therapy". Proceedings of the National Academy of Sciences. 101 (40): 14527–32. PMC 521935Freely accessible. PMID 15448212. doi:10.1073/pnas.0303574101.
  27. Davis, Benjamin Guy (1996). Synthesis of inhibitors of sugar processing enzymes (DPhil thesis). University of Oxford.
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