Colworth Medal

Colworth Medal
Awarded for outstanding research by a young biochemist of any nationality who has carried out the majority of their work in the UK or Republic of Ireland
Sponsor Biochemical Society
Reward £3000
Official website www.biochemistry.org/awards/thecolworthmedal.aspx

The Colworth Medal[1][2] is awarded annually by the Biochemical Society to an outstanding research biochemist under the age of 35[3] and working mainly in the United Kingdom. The award was established by Tony James[4] FRS at Unilever Research and Henry Arnstein of the Biochemical Society and takes its name from a Unilever research laboratory near Bedford in the UK, Colworth House.

The medal was first presented in 1963[5] and many of those receiving the award are recognised as outstanding scientists achieving international reputations.[6] The lecture is published in Biochemical Society Transactions, previously Colworth Medal lectures were published in The Biochemical Journal.

Laureates

Laureates of the medal[6] have included:

References

  1. ↑ "colworth medal", New Scientist, June 1971: 642–3
  2. ↑ Goodwin, Trevor Walworth (1987), History of the Biochemical Society, 1911-1986, Biochemical Society, pp. 50, 66–67
  3. ↑ Sarah Teichmann wins the 2011 Colworth Medal
  4. ↑ Gurr, M. (2012). "Anthony Trafford James. 6 March 1922 -- 7 December 2006". Biographical Memoirs of Fellows of the Royal Society 58: 129–150. doi:10.1098/rsbm.2011.0018.
  5. 1 2 Kornberg, H. L. (1966). "The role and control of the glyoxylate cycle in Escherichia coli". The Biochemical Journal 99 (1): 1–11. doi:10.1042/bj0990001. PMC 1264949. PMID 5337756.
  6. 1 2 3 "The Colworth Medal". Biochemical Society. Archived from the original on 2014-05-06.
  7. ↑ Smith, L. M.; May, R. C. (2013). "Mechanisms of microbial escape from phagocyte killing". Biochemical Society Transactions 41 (2): 475–90. doi:10.1042/BST20130014. PMID 23514140.
  8. ↑ Wu, L; Reddy, A. B. (2014). "Rethinking the clockwork: Redox cycles and non-transcriptional control of circadian rhythms". Biochemical Society Transactions 42 (1): 1–10. doi:10.1042/BST20130169. PMID 24450621.
  9. ↑ Perica, T; Marsh, J. A.; Sousa, F. L.; Natan, E; Colwell, L. J.; Ahnert, S. E.; Teichmann, S. A. (2012). "The emergence of protein complexes: Quaternary structure, dynamics and allostery. Colworth Medal Lecture". Biochemical Society Transactions 40 (3): 475–91. doi:10.1042/BST20120056. PMID 22616857.
  10. ↑ Dillingham, M. S. (2011). "Superfamily I helicases as modular components of DNA-processing machines". Biochemical Society Transactions 39 (2): 413–23. doi:10.1042/BST0390413. PMID 21428912.
  11. ↑ Hardingham, G. E. (2009). "Coupling of the NMDA receptor to neuroprotective and neurodestructive events". Biochemical Society Transactions 37 (Pt 6): 1147–60. doi:10.1042/BST0371147. PMC 2837198. PMID 19909238.
  12. ↑ Rouse, J (2009). "Control of genome stability by SLX protein complexes". Biochemical Society Transactions 37 (Pt 3): 495–510. doi:10.1042/BST0370495. PMID 19442243.
  13. ↑ Sargent, F (2007). "The twin-arginine transport system: Moving folded proteins across membranes". Biochemical Society Transactions 35 (Pt 5): 835–47. doi:10.1042/BST0350835. PMID 17956229.
  14. ↑ Boulton, S. J. (2006). "Cellular functions of the BRCA tumour-suppressor proteins". Biochemical Society Transactions 34 (Pt 5): 633–45. doi:10.1042/BST0340633. PMID 17052168.
  15. ↑ Collinson, I (2005). "The structure of the bacterial protein translocation complex SecYEG". Biochemical Society Transactions 33 (Pt 6): 1225–30. doi:10.1042/BST20051225. PMID 16246086.
  16. ↑ Naismith, J. H. (2004). "Chemical insights from structural studies of enzymes". Biochemical Society Transactions 32 (Pt 5): 647–54. doi:10.1042/BST0320647. PMID 15493979.
  17. 1 2 3 4 5 6 7 8 "Past recipeints of the Colworth Medal". Biochemical Society. 2013. Archived from the original on 2012-12-14.
  18. ↑ Alessi, D. R. (2001). "Discovery of PDK1, one of the missing links in insulin signal transduction. Colworth Medal Lecture". Biochemical Society Transactions 29 (Pt 2): 1–14. doi:10.1042/0300-5127:0290001. PMID 11356119.
  19. ↑ Scrutton, N. S. (1999). "Colworth Medal Lecture. Enzymes in the quantum world". Biochemical Society Transactions 27 (6): 767–79. PMID 10830100.
  20. ↑ Barford, D (1999). "Colworth Medal Lecture. Structural studies of reversible protein phosphorylation and protein phosphatases". Biochemical Society Transactions 27 (6): 751–66. doi:10.1042/bst0270751. PMID 10830099.
  21. ↑ Jackson, S. P. (1999). "Colworth Medal lecture. Detection, repair and signalling of DNA double-strand breaks". Biochemical Society Transactions 27 (2): 1–13. doi:10.1042/bst0270001. PMID 10093700.
  22. ↑ Pines, J (1996). "Cyclin from sea urchins to He Las: Making the human cell cycle". Biochemical Society Transactions 24 (1): 15–33. doi:10.1042/bst0240015. PMID 8674643.
  23. ↑ Stephens, L (1995). "Colworth Medal Lecture. Molecules mediating signals". Biochemical Society Transactions 23 (2): 207–21. doi:10.1042/bst0230207. PMID 7672227.
  24. ↑ Lamond, A. I. (1993). "2'-O-alkyloligoribonucleotides: Probes for studying the biochemistry and cell biology of RNA processing". Biochemical Society Transactions 21 (1): 1–8. doi:10.1042/bst0210001. PMID 8449268.
  25. ↑ Ferguson, M. A. (1992). "Colworth Medal Lecture. Glycosyl-phosphatidylinositol membrane anchors: The tale of a tail". Biochemical Society Transactions 20 (2): 243–56. doi:10.1042/bst0200243. PMID 1397606.
  26. ↑ Melton, D. W. (1990). "The use of gene targeting to develop animal models for human genetic diseases". Biochemical Society Transactions 18 (6): 1035–9. doi:10.1042/bst0181035. PMID 2088798.
  27. ↑ Pelham, H. R. (1989). "The selectivity of secretion: Protein sorting in the endoplasmic reticulum". Biochemical Society Transactions 17 (5): 795–802. doi:10.1042/bst0170795. PMID 2515980.
  28. ↑ Downes, C. P. (1989). "Twenty-fifth Colworth medal lecture. The cellular functions of myo-inositol". Biochemical Society Transactions 17 (2): 259–68. PMID 2546836.
  29. ↑ Jeffreys, A. J. (1987). "Highly variable minisatellites and DNA fingerprints". Biochemical Society Transactions 15 (3): 309–17. doi:10.1042/bst0150309. PMID 2887471.
  30. ↑ Houslay, M. D. (1986). "Insulin, glucagon and the receptor-mediated control of cyclic AMP concentrations in liver. Twenty-second Colworth medal lecture". Biochemical Society Transactions 14 (2): 183–93. doi:10.1042/bst0140183. PMID 3011541.
  31. ↑ Oldfield, E (1988). "Spectroscopic studies of lipids and biological membranes. Twenty-first Colworth medal lecture". Biochemical Society Transactions 16 (1): 1–10. PMID 3277879.
  32. ↑ Lilley, D. M. (1983). "Structural perturbation in supercoiled DNA: Hypersensitivity to modification by a single-strand-selective chemical reagent conferred by inverted repeat sequences". Nucleic Acids Research 11 (10): 3097–112. doi:10.1093/nar/11.10.3097. PMC 325951. PMID 6304622.
  33. ↑ Rabbitts, T. H. (1983). "The human immunoglobulin genes. The nineteenth Colworth medal lecture". Biochemical Society Transactions 11 (2): 119–26. PMID 6420211.
  34. ↑ Flavell, R. A. (1983). "The globin genes of rabbit and man. The eighteenth Colworth medal lecture". Biochemical Society Transactions 11 (2): 111–8. doi:10.1042/bst0110111. PMID 6198222.
  35. ↑ Laskey, R. A. (1981). "Molecular mechanisms of chromatin assembly". Biochemical Society Transactions 9 (4): 263–70. doi:10.1042/bst0090263. PMID 6266896.
  36. ↑ Hardingham, T (1981). "Proteoglycans: Their structure, interactions and molecular organization in cartilage". Biochemical Society Transactions 9 (6): 489–97. doi:10.1042/bst0090489. PMID 7308557.
  37. ↑ Cohen, P (1979). "The hormonal control of glycogen metabolism in mammalian muscle by multivalent phosphorylation". Biochemical Society Transactions 7 (3): 459–80. doi:10.1042/bst0070459. PMID 221283.
  38. ↑ Brownlee, G. G. (1979). "The Fourteenth Colworth Medal Lecture Sequencing eukaryotic genes or the anatomy of DNA". Biochemical Society Transactions 7 (2): 279–96. doi:10.1042/bst0070279. PMID 570938.
  39. ↑ Brammar, W. J. (1977). "The thirteenth Colworth Medal Lecture: The construction in vitro and exploitation of transducing derivatives of bacteriophage lambda". Biochemical Society Transactions 5 (6): 1633–52. doi:10.1042/bst0051633. PMID 340298.
  40. ↑ Trentham, D. R. (1977). "The twelfth Colworth Medal lecture. The adenosine triphosphatase reactions of myosin and actomyosin and their relation to energy transduction in muscle". Biochemical Society Transactions 5 (1): 5–22. doi:10.1042/bst0050005. PMID 142675.
  41. ↑ Williamson, A. R. (1972). "Extent and control of antibody diversity". The Biochemical Journal 130 (2): 325–33. doi:10.1042/bj1300325. PMC 1174411. PMID 4124148.
  42. ↑ Rees, D. A. (1972). "Shapely polysaccharides. The eighth Colworth medal lecture". The Biochemical Journal 126 (2): 257–73. doi:10.1042/bj1260257. PMC 1178377. PMID 4561024.
  43. ↑ Radda, G. K. (1971). "Enzyme and membrane conformation in biochemical control". The Biochemical Journal 122 (4): 385–96. doi:10.1042/bj1220385. PMC 1176792. PMID 4942951.
  44. ↑ Garland, P. B. (1970). "Biochemical applications of continuous culture: Energy-conservation mechanisms in Torulopsis utilis". The Biochemical Journal 118 (3): 329–39. doi:10.1042/bj1180329. PMC 1179196. PMID 4920880.
  45. ↑ Morris, L. J. (1970). "Mechanisms and stereochemistry in fatty acid metabolism". The Biochemical Journal 118 (5): 681–93. doi:10.1042/bj1180681g. PMC 1179276. PMID 4920387.
  46. ↑ Richmond, M. H. (1969). "Extrachromosomal elements and the spread of antibiotic resistance in bacteria". The Biochemical Journal 113 (2): 225–34. doi:10.1042/bj1130225. PMC 1184627. PMID 5808311.
  47. ↑ Tata, J. R. (1967). "The formation and distribution of ribosomes during hormone-induced growth and development". The Biochemical Journal 104 (1): 1–16. doi:10.1042/bj1040001. PMC 1270539. PMID 5340734.
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