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• Journal article
  Thongyoo P, Bonomelli C, Leatherbarrow RJ, Tate EWet al., 2009,
  , JOURNAL OF MEDICINAL CHEMISTRY, Vol: 52, Pages: 6197-6200, ISSN: 0022-2623
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  • Citations: 110
• Journal article
  Heal WP, Wickramasinghe SR, Tate EW, 2008,
  , Curr Drug Discov Technol, Vol: 5, Pages: 200-212, ISSN: 1570-1638

  The pivotal role of proteases in many diseases has generated considerable interest in their basic biology, and in the potential to target them for chemotherapy. Although fundamental to the initiation and progression of diseases such as cancer, diabetes, arthritis and malaria, in many cases their precise role remains unknown. Activity-based chemical proteomics-an emerging field involving a combination of organic synthesis, biochemistry, cell biology, biophysics and bioinformatics-allows the detection, visualisation and activity quantification of whole families or selected sub-sets of proteases based upon their substrate specificity. This approach can be applied for drug target/lead identification and validation, the fundamentals of drug discovery. The activity-based probes discussed in this review contain three key features; a 'warhead' (binds irreversibly but selectively to the active site), a 'tag' (allowing enzyme 'handling', with a combination of fluorescent, affinity and/or radio labels), and a linker region between warhead and tag. From the design and synthesis of the linker arise some of the latest developments discussed here; not only can the physical properties (e.g., solubility, localisation) of the probe be tuned, but the inclusion of a cleavable moiety allows selective removal of tagged enzyme from affinity beads etc. The design and synthesis of recently reported probes is discussed, including modular assembly of highly versatile probes via solid phase synthesis. Recent applications of activity-based protein profiling to specific proteases (serine, threonine, cysteine and metalloproteases) are reviewed as are demonstrations of their use in the study of disease function in cancer and malaria.

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• Journal article
  Busch GK, Tate EW, Gaffney PR, Rosivatz E, Woscholski R, Leatherbarrow RJet al., 2008,
  , Chem.Commun.(Camb.), Pages: 3369-3371

  We report an effective strategy for generating N-terminal cysteinyl proteins by proteolytic cleavage using the enzyme 3C pro, suitable for a wide range of applications via native chemical ligation

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• Journal article
  Heal WP, Wickramasinghe SR, Leatherbarrow RJ, Tate EWet al., 2008,
  , Organic and Biomolecular Chemistry
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• Journal article
  Tate EW, 2008,
  , Journal of Chemical Biology, Vol: 1, Pages: 1-1

  Identification and quantification of multiple proteins from complex mixtures is a central theme in post-genomic biology. Despite recent progress in high-throughput proteomics, proteomic analysis of post-translationally modified (PTM) proteins remains particularly challenging. This mini-review introduces the emerging field of chemical proteomics and reviews recent advances in chemical proteomic technology that are offering striking new insights into the functional biology of post-translational modification.

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• Journal article
  Bowyer PW, Tate EW, Leatherbarrow RJ, Holder AA, Smith DF, Brown KAet al., 2008,
  , CHEMMEDCHEM, Vol: 3, Pages: 402-408, ISSN: 1860-7179
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  • Citations: 58
• Journal article
  Heal WP, Wickramasinghe SR, Bowyer PW, Holder AA, Smith DF, Leatherbarrow RJ, Tate EWet al., 2008,
  , Chem. Commun.
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• Journal article
  Thongyoo P, Roque-Rosell N, Leatherbarrow RJ, Tate EWet al., 2008,
  , ORGANIC & BIOMOLECULAR CHEMISTRY, Vol: 6, Pages: 1462-1470, ISSN: 1477-0520
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  • Citations: 130
• Journal article
  Bowyer PW, Gunaratne RS, Grainger M, Withers-Martinez C, Wickramsinghe SR, Tate EW, Leatherbarrow RJ, Brown KA, Holder AA, Smith DFet al., 2007,
  , BIOCHEMICAL JOURNAL, Vol: 408, Pages: 173-180, ISSN: 0264-6021
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  • Citations: 58
• Journal article
  Thongyoo P, Jaulent AM, Tate EW, Leatherbarrow RJet al., 2007,
  , CHEMBIOCHEM, Vol: 8, Pages: 1107-1109, ISSN: 1439-4227
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  • Citations: 43

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