Gideon Davies

Gideon Davies

Gideon Davies in 2010
Born Gideon John Davies
(1964-07-06) 6 July 1964[1]
Great Sutton, Cheshire
Nationality British
Fields
Institutions
Alma mater University of Bristol (BSc, PhD, DSc)
Thesis Phosphoglycerate kinase from Bacillus stearothermophilus (1990)
Doctoral advisor
  • Herman Watson
  • Len Hall[4]
Doctoral students
Notable awards
Spouse Valérie Marie-Andrée Ducros[1]
Children Two daughters[1]

Website

Gideon John Davies (born 1964) FRS FRSC FMedSci is a Professor of Chemistry in the York Structural Biology Laboratory (YSBL) at the University of York, in the UK.[2][10][11][12]

Education

Davies was educated at the University of Bristol where he was awarded a Bachelor of Science degree in Biochemistry and a PhD in 1990 for research on the enzyme phosphoglycerate kinase isolated from the bacterium Bacillus stearothermophilus, and supervised by Herman Watson and Len Hall.[4][13]

Career

Following his PhD, Davies did postdoctoral research at the European Molecular Biology Laboratory (EMBL) outstation in Hamburg working with Keith S. Wilson on the use of synchrotron radiation in protein crystallography and also and the Centre national de la recherche scientifique (CNRS) in Grenoble.[14] in 1990 Davies moved to York to work with Dale Wigley and Guy Dodson on DNA gyrase. He was appointed Professor at the University of York in 2001.[14] He has collaborated with Alywn Jones, Bernard Henrissat,[15][16] Steve Withers and David Vocadlo.[3]

Research

Davies research investigates the biological chemistry of carbohydrates, from their structure[17][18] to their roles in enzymology,[19][20] glycobiology,[21][22][23] use as biofuels[24][25][26] and implications for microbiota.[27][28] His research has been funded by the Biotechnology and Biological Sciences Research Council (BBSRC),[29] European Research Council (ERC) and Alzheimer's Research UK.[14]

Awards and honours

Davies was elected a Fellow of the Royal Society (FRS) in 2010. His nomination reads:

“ Professor Gideon Davies' research is focused on "structural enzymology". In this he addresses the enzymes, and their accessory domains, that are involved in the synthesis, modification and breakdown of carbohydrates. His chemical and structural insight into protein-carbohydrate interactions and his brilliant exploitation of advanced crystallographic methods provide the basis for understanding how the chemical and structural factors in the stereochemical pathway of the enzyme:substrate complex govern specificity and catalysis. His research is having an immense impact on carbohydrate chemistry and biology and biological catalysis generally.[8] ”

Davies was elected a Fellow of the Academy of Medical Sciences (FMedSci) in 2014, his nomination reads

“ Gideon Davies, who is Professor of Biological Chemistry at University of York, has made world-leading contributions to Biochemistry. He has made fundamental additions to our understanding of enzyme mechanism and carbohydrate biochemistry. As a direct result of his work into the conformation of sugars during turnover, he described the rational design of highly potent inhibitors of O-linked glucosamine modifying enzymes. These compounds are showing potential as treatments for Alzheimer's disease. Recently he has turned to study the human microbiota, which are now recognised to be an essential component of human health, and their carbohydrate metabolism is implicated in several disease states.[30] ”

Davies was elected a member of the European Molecular Biology Organization (EMBO) in 2010,[14] is a Fellow of the Royal Society of Chemistry (FRSC) and was awarded a Doctor of Science (DSc) degree from the University of Bristol in 2007.[9]

Personal life

Davies married Valérie Marie-Andrée Ducros[31] in 1999 and has two daughters.[1]

References

  1. 1 2 3 4 DAVIES, Prof. Gideon John. Who's Who. 2014 (online Oxford University Press ed.). A & C Black, an imprint of Bloomsbury Publishing plc. (subscription required)
  2. 1 2 Gideon Davies's publications indexed by Google Scholar
  3. 1 2 Vocadlo, D. J.; Davies, G. J.; Laine, R; Withers, S. G. (2001). "Catalysis by hen egg-white lysozyme proceeds via a covalent intermediate". Nature. 412 (6849): 835–8. doi:10.1038/35090602. PMID 11518970.
  4. 1 2 Professor Gideon Davies, FMedSci, FRS Biography, University of York
  5. ↑ Gloster, T. M.; Davies, G. J. (2010). "Glycosidase inhibition: Assessing mimicry of the transition state". Organic & Biomolecular Chemistry. 8 (2): 305–320. doi:10.1039/B915870G.
  6. ↑ Gloster, Tracey Maureen (2005). Transition state mimicry in glycoside hydrolysis (PhD thesis). University of York.
  7. ↑ He, Yuan (2011). Mechanism and inhibition of a bacterial O-GlcNAcase (PhD thesis). University of York.
  8. 1 2 "Professor Gideon John Davies FRS". London: The Royal Society. Archived from the original on 2014-10-17.
  9. 1 2 Davies, Gideon John (2007). Published work submitted for the degree of D.Sc. (DSc thesis). University of Bristol.
  10. ↑ List of publications from Microsoft Academic Search
  11. ↑ Gideon Davies's publications indexed by the Scopus bibliographic database, a service provided by Elsevier. (subscription required)
  12. ↑ Gideon Davies on Twitter
  13. ↑ Davies, Gideon John (1990). Phosphoglycerate kinase from Bacillus stearothermophilus (PhD thesis). University of Bristol.
  14. 1 2 3 4 Professor Gideon Davies, FMedSci, FRS, University of York
  15. ↑ Henrissat, B.; Davies, G. (1997). "Structural and sequence-based classification of glycoside hydrolases". Current Opinion in Structural Biology. 7 (5): 637–44. doi:10.1016/S0959-440X(97)80072-3. PMID 9345621.
  16. ↑ Davies, G.; Henrissat, B. (1995). "Structures and mechanisms of glycosyl hydrolases". Structure. 3 (9): 853–9. doi:10.1016/S0969-2126(01)00220-9. PMID 8535779.
  17. ↑ Agirre, Jon; Davies, Gideon; Wilson, Keith; Cowtan, Kevin. "Carbohydrate anomalies in the PDB". Nature Chemical Biology. 11 (5): 303–303. doi:10.1038/nchembio.1798.
  18. ↑ Agirre, Jon; Iglesias-Fernández, Javier; Rovira, Carme; Davies, Gideon J; Wilson, Keith S; Cowtan, Kevin D. "Privateer: software for the conformational validation of carbohydrate structures". Nature Structural & Molecular Biology. 22 (11): 833–834. doi:10.1038/nsmb.3115.
  19. ↑ Vocadlo, D. J.; Davies, G. J.; Laine, R.; Withers, S. G. (2001-08-23). "Catalysis by hen egg-white lysozyme proceeds via a covalent intermediate". Nature. 412 (6849): 835–838. doi:10.1038/35090602. ISSN 0028-0836. PMID 11518970.
  20. ↑ Ducros, Valérie M.-A.; Zechel, David L.; Murshudov, Garib N.; Gilbert, Harry J.; Szabó, Lóránd; Stoll, Dominik; Withers, Stephen G.; Davies, Gideon J. (2002-08-02). "Substrate distortion by a beta-mannanase: snapshots of the Michaelis and covalent-intermediate complexes suggest a B(2,5) conformation for the transition state". Angewandte Chemie International Edition in English. 41 (15): 2824–2827. doi:10.1002/1521-3773(20020802)41:15<2824::AID-ANIE2824>3.0.CO;2-G. ISSN 1433-7851. PMID 12203498.
  21. ↑ Coutinho, Pedro M.; Deleury, Emeline; Davies, Gideon J.; Henrissat, Bernard (2003-04-25). "An evolving hierarchical family classification for glycosyltransferases". Journal of Molecular Biology. 328 (2): 307–317. doi:10.1016/s0022-2836(03)00307-3. ISSN 0022-2836. PMID 12691742.
  22. ↑ Yuzwa, Scott A; Macauley, Matthew S; Heinonen, Julia E; Shan, Xiaoyang; Dennis, Rebecca J; He, Yuan; Whitworth, Garrett E; Stubbs, Keith A; McEachern, Ernest J. "A potent mechanism-inspired O-GlcNAcase inhibitor that blocks phosphorylation of tau in vivo". Nature Chemical Biology. 4 (8): 483–490. doi:10.1038/nchembio.96.
  23. ↑ Wu, Liang; Viola, Cristina M; Brzozowski, Andrzej M; Davies, Gideon J. "Structural characterization of human heparanase reveals insights into substrate recognition". Nature Structural & Molecular Biology. 22 (12): 1016–1022. doi:10.1038/nsmb.3136.
  24. ↑ Yin, DeLu (Tyler); Urresti, Saioa; Lafond, Mickael; Johnston, Esther M.; Derikvand, Fatemeh; Ciano, Luisa; Berrin, Jean-Guy; Henrissat, Bernard; Walton, Paul H. (2015-12-18). "Structure-function characterization reveals new catalytic diversity in the galactose oxidase and glyoxal oxidase family". Nature Communications. 6: 10197. doi:10.1038/ncomms10197. PMC 4703870Freely accessible. PMID 26680532.
  25. ↑ Quinlan, R. Jason; Sweeney, Matt D.; Leggio, Leila Lo; Otten, Harm; Poulsen, Jens-Christian N.; Johansen, Katja Salomon; Krogh, Kristian B. R. M.; Jørgensen, Christian Isak; Tovborg, Morten (2011-09-13). "Insights into the oxidative degradation of cellulose by a copper metalloenzyme that exploits biomass components". Proceedings of the National Academy of Sciences. 108 (37): 15079–15084. doi:10.1073/pnas.1105776108. ISSN 0027-8424. PMC 3174640Freely accessible. PMID 21876164.
  26. ↑ Frandsen, Kristian E H; Simmons, Thomas J; Dupree, Paul; Poulsen, Jens-Christian N; Hemsworth, Glyn R; Ciano, Luisa; Johnston, Esther M; Tovborg, Morten; Johansen, Katja S. "The molecular basis of polysaccharide cleavage by lytic polysaccharide monooxygenases". Nature Chemical Biology. doi:10.1038/nchembio.2029.
  27. ↑ Larsbrink, Johan; Rogers, Theresa E.; Hemsworth, Glyn R.; McKee, Lauren S.; Tauzin, Alexandra S.; Spadiut, Oliver; Klinter, Stefan; Pudlo, Nicholas A.; Urs, Karthik. "A discrete genetic locus confers xyloglucan metabolism in select human gut Bacteroidetes". Nature. 506 (7489): 498–502. doi:10.1038/nature12907. PMC 4282169Freely accessible. PMID 24463512.
  28. ↑ Cuskin, Fiona; Lowe, Elisabeth C.; Temple, Max J.; Zhu, Yanping; Cameron, Elizabeth A.; Pudlo, Nicholas A.; Porter, Nathan T.; Urs, Karthik; Thompson, Andrew J. "Human gut Bacteroidetes can utilize yeast mannan through a selfish mechanism". Nature. 517 (7533): 165–169. doi:10.1038/nature13995.
  29. ↑ UK Government research grants awarded to Gideon Davies, via Research Councils UK
  30. ↑ "Professor Gideon Davies FRS FMedSci". London: The Academy of Medical Sciences. Archived from the original on 2014-10-25.
  31. ↑ Ducros, V. R.; Brzozowski, A. M.; Wilson, K. S.; Brown, S. H.; Østergaard, P.; Schneider, P.; Yaver, D. S.; Pedersen, A. H.; Davies, G. J. (1998). "Crystal structure of the type-2 Cu depleted laccase from Coprinus dnereus at 2.2 Å resolution". Nature Structural Biology. 5 (4): 310–316. doi:10.1038/nsb0498-310.
This article is issued from Wikipedia - version of the 11/8/2016. The text is available under the Creative Commons Attribution/Share Alike but additional terms may apply for the media files.