Colworth Medal

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Colworth Medal
Awarded foroutstanding research by a young biochemist of any nationality who has carried out the majority of their work in the UK or Republic of Ireland
Sponsored by Biochemical Society
Reward(s)£3000
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 and working mainly in the United Kingdom. The award is one of the most prestigious recognitions for young scientists in the UK, and was established by Tony James [3] 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.

Contents

The medal was first presented in 1963 [4] and many of those receiving the award are recognised as outstanding scientists achieving international reputations. [5] The lecture is published in Biochemical Society Transactions , previously Colworth Medal lectures were published in The Biochemical Journal .

Laureates

Source: [5]

See also

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References

  1. ↑ "colworth medal", New Scientist: 642–3, June 1971
  2. ↑ Goodwin, Trevor Walworth (1987), History of the Biochemical Society, 1911-1986, Biochemical Society, pp. 50, 66–67
  3. ↑ 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 .
  4. 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.
  5. 1 2 3 "The Colworth Medal". Biochemical Society. Archived from the original on 2014-05-06.
  6. ↑ "The Biochemical Society awards Birkbeck academic prestigious Colworth Medal". www.bbk.ac.uk. Retrieved 2021-12-28.
  7. ↑ "Colworth Medal | University of Sheffield". University of Sheffield. Retrieved 2018-02-11.
  8. ↑ "Colworth Medal | The Francis Crick Institute". The Francis Crick Institute. Retrieved 2016-03-31.
  9. ↑ "2016 Award Winners | Biochemical Society". www.biochemistry.org. Archived from the original on 2016-04-05. Retrieved 2016-03-31.
  10. ↑ "2015 Winners". www.biochemistry.org. Archived from the original on 2016-04-09. Retrieved 2016-03-31.
  11. ↑ 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.
  12. ↑ 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.
  13. ↑ 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.
  14. ↑ 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.
  15. ↑ 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.
  16. ↑ 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. S2CID   40978438.
  17. ↑ 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.
  18. ↑ 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.
  19. ↑ 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.
  20. ↑ 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.
  21. 1 2 3 4 5 6 7 8 "Past recipients of the Colworth Medal". Biochemical Society. 2013. Archived from the original on December 14, 2013.
  22. ↑ 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.
  23. ↑ Scrutton, N. S. (1999). "Colworth Medal Lecture. Enzymes in the quantum world". Biochemical Society Transactions. 27 (6): 767–79. doi:10.1042/bst0270767. PMID   10830100.
  24. ↑ 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.
  25. ↑ 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.
  26. ↑ 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.
  27. ↑ Stephens, L (1995). "Colworth Medal Lecture. Molecules mediating signals". Biochemical Society Transactions. 23 (2): 207–21. doi:10.1042/bst0230207. PMID   7672227.
  28. ↑ 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.
  29. ↑ 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. S2CID   7796865.
  30. ↑ 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.
  31. ↑ 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.
  32. ↑ Downes, C. P. (1989). "Twenty-fifth Colworth medal lecture. The cellular functions of myo-inositol". Biochemical Society Transactions. 17 (2): 259–68. doi:10.1042/bst0170259. PMID   2546836.
  33. ↑ Jeffreys, A. J. (1987). "Highly variable minisatellites and DNA fingerprints". Biochemical Society Transactions. 15 (3): 309–17. doi:10.1042/bst0150309. hdl: 2381/450 . PMID   2887471.
  34. ↑ 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.
  35. ↑ Oldfield, E (1988). "Spectroscopic studies of lipids and biological membranes. Twenty-first Colworth medal lecture". Biochemical Society Transactions. 16 (1): 1–10. doi:10.1042/bst0160001. PMID   3277879.
  36. ↑ 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.
  37. ↑ Rabbitts, T. H. (1983). "The human immunoglobulin genes. The nineteenth Colworth medal lecture". Biochemical Society Transactions. 11 (2): 119–26. doi:10.1042/bst0110119. PMID   6420211.
  38. ↑ 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.
  39. ↑ Laskey, R. A. (1981). "Molecular mechanisms of chromatin assembly". Biochemical Society Transactions. 9 (4): 263–70. doi:10.1042/bst0090263. PMID   6266896.
  40. ↑ 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.
  41. ↑ 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.
  42. ↑ 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.
  43. ↑ 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.
  44. ↑ 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.
  45. ↑ 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.
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  47. ↑ 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.
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  50. ↑ 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.
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