Gideon Davies

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Gideon Davies
Professor Gideon Davies, FRS, FMedSci.jpg
Gideon Davies in 2010
Born Gideon John Davies
(1964-07-06) 6 July 1964 (age 54)[1]
Great Sutton, Cheshire
Nationality British
Alma mater University of Bristol (BSc, PhD, DSc)
Spouse(s) Valérie Marie-Andrée Ducros[1]
Children Two daughters[1]
Awards
Scientific career
Fields
Institutions
Thesis Phosphoglycerate kinase from Bacillus stearothermophilus (1990)
Doctoral advisor
  • Herman Watson
  • Len Hall[6]
Doctoral students
Website

Gideon John Davies (born 1964) FRS FRSC FMedSci is a Royal Society Ken Murray Research Professor in the York Structural Biology Laboratory (YSBL) at the University of York, in the UK.[4][10][11]

Education[edit]

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.[6][12]

Career[edit]

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 at the Centre national de la recherche scientifique (CNRS) in Grenoble.[13] in 1990, Davies moved to York to work with Dale Wigley and Guy Dodson on DNA gyrase, starting his own group within YSBL in 1996 upon receiving a Royal Society University Research Fellowship[14]. He was appointed Professor at the University of York in 2001[13] and awarded a Royal Society Ken Murray Research Professorship[15] in 2016. He has collaborated with Alywn Jones, Bernard Henrissat,[16][17] Steve Withers and David Vocadlo.[5]

Research[edit]

Davies research investigates the biological chemistry of carbohydrates, from their structure[18][19][20] to their roles in enzymology[21][22], glycobiology[23][24][25][26], use as biofuels[27][28][29] and implications for gut microbiota[30][31]. His research has been funded by the Biotechnology and Biological Sciences Research Council (BBSRC)[32], European Research Council (ERC) and Alzheimer's Research UK[13].

Awards and honours[edit]

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

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

Davies was elected a member of the European Molecular Biology Organization (EMBO) in 2010,[13] 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.[3]

Personal life[edit]

Davies married Valérie Marie-Andrée Ducros[34] in 1999 and has two daughters.[1]

References[edit]

  1. ^ a b c d DAVIES, Prof. Gideon John. ukwhoswho.com. Who's Who. 2014 (online Oxford University Press ed.). A & C Black, an imprint of Bloomsbury Publishing plc.  closed access publication – behind paywall (subscription required)
  2. ^ a b "Professor Gideon John Davies FRS". London: The Royal Society. Archived from the original on 2014-10-25. 
  3. ^ a b Davies, Gideon John (2007). Published work submitted for the degree of D.Sc (DSc thesis). University of Bristol. 
  4. ^ a b Gideon Davies publications indexed by Google Scholar
  5. ^ a b 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. 
  6. ^ a b Professor Gideon Davies, FMedSci, FRS Biography, University of York
  7. ^ 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. PMC 2822703Freely accessible. 
  8. ^ Gloster, Tracey Maureen (2005). Transition state mimicry in glycoside hydrolysis (PhD thesis). University of York. 
  9. ^ He, Yuan (2011). Mechanism and inhibition of a bacterial O-GlcNAcase (PhD thesis). University of York. 
  10. ^ List of publications from Microsoft Academic
  11. ^ Gideon Davies's publications indexed by the Scopus bibliographic database. (subscription required)
  12. ^ Davies, Gideon John (1990). Phosphoglycerate kinase from Bacillus stearothermophilus (PhD thesis). University of Bristol. 
  13. ^ a b c d Professor Gideon Davies, FMedSci, FRS, University of York
  14. ^ "Gideon Davies". royalsociety.org. Retrieved 2017-06-14. 
  15. ^ "Leading scientists awarded Royal Society Research Professorships". royalsociety.org. Retrieved 2017-06-14. 
  16. ^ 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. 
  17. ^ 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. 
  18. ^ Agirre, Jon; Davies, Gideon; Wilson, Keith; Cowtan, Kevin (2015). "Carbohydrate anomalies in the PDB". Nature Chemical Biology. 11 (5): 303–303. doi:10.1038/nchembio.1798. PMID 25885951. 
  19. ^ 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. PMID 26581513. 
  20. ^ Agirre, Jon; Davies, Gideon J; Wilson, Keith S; Cowtan, Kevin D (June 2017). "Carbohydrate structure: the rocky road to automation". Current Opinion in Structural Biology. Carbohydrates: A feast of structural glycobiology • Sequences and topology: Computational studies of protein-protein interactions. 44: 39–47. doi:10.1016/j.sbi.2016.11.011. 
  21. ^ 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. 
  22. ^ 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. 
  23. ^ 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. 
  24. ^ 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. PMID 18587388. 
  25. ^ 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. PMC 5008439Freely accessible. 
  26. ^ Roth, Christian; Chan, Sherry; Offen, Wendy A; Hemsworth, Glyn R; Willems, Lianne I; King, Dustin T; Varghese, Vimal; Britton, Robert; Vocadlo, David J. "Structural and functional insight into human O-GlcNAcase". Nature Chemical Biology. doi:10.1038/nchembio.2358. 
  27. ^ 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. 
  28. ^ 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. 
  29. ^ 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. 12: 298–303. doi:10.1038/nchembio.2029. PMC 4817220Freely accessible. PMID 26928935. 
  30. ^ 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. 
  31. ^ Cuskin, Fiona; Lowe, Elisabeth C.; Temple, Max J.; Zhu, Yanping; Cameron, Elizabeth A.; Pudlo, Nicholas A.; Porter, Nathan T.; Urs, Karthik; Thompson, Andrew J. (2015). "Human gut Bacteroidetes can utilize yeast mannan through a selfish mechanism". Nature. 517 (7533): 165–169. doi:10.1038/nature13995. PMC 4978465Freely accessible. PMID 25567280. 
  32. ^ UK Government research grants awarded to Gideon Davies, via Research Councils UK
  33. ^ "Professor Gideon Davies FRS FMedSci". London: The Academy of Medical Sciences. Archived from the original on 2014-10-25. 
  34. ^ 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.