Christopher J. Schofield

Christopher J. Schofield
Born
Christopher Joseph Schofield

(1960-06-17) 17 June 1960 (age 64)
United Kingdom
NationalityBritish
Other namesChris Schofield, CJS
Alma materUniversity of Manchester (BSc) University of Oxford (DPhil)
AwardsFellow of the Royal Society
Scientific career
FieldsHypoxic Response, Epigenetic, Oxygenases, Antibiotic Resistance
InstitutionsChemistry Research Laboratory, University of Oxford
Websitehttp://schofield.chem.ox.ac.uk/home http://research.chem.ox.ac.uk/christopher-schofield.aspx

Christopher Joseph Schofield (also known as Chris Schofield) is a Professor of Chemistry at the University of Oxford[1] and a Fellow of the Royal Society. Chris Schofield is a professor of organic chemistry at the University of Oxford, Department of Chemistry[2] and a Fellow of Hertford College.[3] Schofield studied functional, structural and mechanistic understanding of enzymes that employ oxygen and 2-oxoglutarate as a co-substrate.[4] His work has opened up new possibilities in antibiotic research,[5] oxygen sensing,[6] and gene regulation.[7]

After work on plant and microbial oxygenases,[4] he studied uncharacterised human oxygenases.[8] His research has identified unanticipated roles for oxygenases[9] in regulating gene expression, importantly in the cellular hypoxic response,[10] and has revealed new post-translational modifications to chromatin and RNA splicing proteins.[11] The work has identified new opportunities for medicinal intervention.[12]

  1. ^ "Christopher Schofield". University of Oxford. Retrieved 24 July 2023.
  2. ^ "Home – Schofield Group". University of Oxford. Retrieved 8 August 2016.
  3. ^ "Professor Chris Schofield FRS | Hertford College". University of Oxford. Retrieved 8 August 2016.
  4. ^ a b Chowdhury, Rasheduzzaman; Sekirnik, Rok; Brissett, Nigel C.; Krojer, Tobias; Ho, Chia-hua; Ng, Stanley S.; Clifton, Ian J.; Ge, Wei; Kershaw, Nadia J. (19 June 2014). "Ribosomal oxygenases are structurally conserved from prokaryotes to humans". Nature. 510 (7505): 422–426. Bibcode:2014Natur.510..422C. doi:10.1038/nature13263. ISSN 0028-0836. PMC 4066111. PMID 24814345.
  5. ^ Hamed, Refaat B.; Gomez-Castellanos, J. Ruben; Henry, Luc; Ducho, Christian; McDonough, Michael A.; Schofield, Christopher J. (10 December 2012). "The enzymes of β-lactam biosynthesis". Natural Product Reports. 30 (1): 21–107. doi:10.1039/C2NP20065A. ISSN 1460-4752. PMID 23135477.
  6. ^ Schofield, Christopher J.; Ratcliffe, Peter J. (1 May 2004). "Oxygen sensing by HIF hydroxylases". Nature Reviews Molecular Cell Biology. 5 (5): 343–354. doi:10.1038/nrm1366. ISSN 1471-0072. PMID 15122348. S2CID 6586977.
  7. ^ Thinnes, Cyrille C.; England, Katherine S.; Kawamura, Akane; Chowdhury, Rasheduzzaman; Schofield, Christopher J.; Hopkinson, Richard J. (1 December 2014). "Targeting histone lysine demethylases – Progress, challenges, and the future". Biochimica et Biophysica Acta (BBA) - Gene Regulatory Mechanisms. Methylation: A Multifaceted Modification – looking at transcription and beyond. 1839 (12): 1416–1432. doi:10.1016/j.bbagrm.2014.05.009. PMC 4316176. PMID 24859458.
  8. ^ Horita, Shoichiro; Scotti, John S.; Thinnes, Cyrille; Mottaghi-Taromsari, Yousef S.; Thalhammer, Armin; Ge, Wei; Aik, WeiShen; Loenarz, Christoph; Schofield, Christopher J. (7 April 2015). "Structure of the Ribosomal Oxygenase OGFOD1 Provides Insights into the Regio- and Stereoselectivity of Prolyl Hydroxylases". Structure. 23 (4): 639–652. doi:10.1016/j.str.2015.01.014. PMC 4396695. PMID 25728928.
  9. ^ Chowdhury, R; McDonough, MA; Mecinović, J; Loenarz, C; Flashman, E; Hewitson, KS; Domene, C; Schofield, CJ (July 2009). "Structural Basis for Binding of Hypoxia-Inducible Factor to the Oxygen-Sensing Prolyl Hydroxylases". Structure. 17 (7): 981–989. doi:10.1016/j.str.2009.06.002. PMID 19604478.
  10. ^ Hon, Wai-Ching; Wilson, Michael I.; Harlos, Karl; Claridge, Timothy D. W.; Schofield, Christopher J.; Pugh, Christopher W.; Maxwell, Patrick H.; Ratcliffe, Peter J.; Stuart, David I. (27 June 2002). "Structural basis for the recognition of hydroxyproline in HIF-1α by pVHL". Nature. 417 (6892): 975–978. Bibcode:2002Natur.417..975H. doi:10.1038/nature00767. ISSN 0028-0836. PMID 12050673. S2CID 4388644.
  11. ^ Webby, Celia J.; Wolf, Alexander; Gromak, Natalia; Dreger, Mathias; Kramer, Holger; Kessler, Benedikt; Nielsen, Michael L.; Schmitz, Corinna; Butler, Danica S. (3 July 2009). "Jmjd6 Catalyses Lysyl-Hydroxylation of U2AF65, a Protein Associated with RNA Splicing". Science. 325 (5936): 90–93. Bibcode:2009Sci...325...90W. doi:10.1126/science.1175865. hdl:10033/78493. ISSN 0036-8075. PMID 19574390. S2CID 38938528.
  12. ^ "ReOx Ltd - Oxford Spin-out to Develop New Drug Therapies". Retrieved 8 August 2016.