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• Journal article
  Dang THT, Fagan RP, Fairweather NF, Tate EWet al., 2012,
  , Bioorganic & Medicinal Chemistry, Vol: 20, Pages: 614-621, ISSN: 1464-3391

  Clostridium difficile, a leading cause of hospital-acquired bacterial infection, is coated in a dense surface layer (S-layer) that is thought to provide both physicochemical protection and a scaffold for host-pathogen interactions. The key structural components of the S-layer are two proteins derived from a polypeptide precursor, SlpA, via proteolytic cleavage by the protease Cwp84. Here, we report the design, synthesis and in vivo characterization of a panel of protease inhibitors and activity-based probes (ABPs) designed to target S-layer processing in live C. difficile cells. Inhibitors based on substrate-mimetic peptides bearing a C-terminal Michael acceptor warhead were found to be promising candidates for further development.

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• Journal article
  Heal WP, Wright MH, Thinon E, Tate EWet al., 2012,
  , NATURE PROTOCOLS, Vol: 7, Pages: 105-117, ISSN: 1754-2189
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  • Citations: 88
• Journal article
  Heal WP, Tate EW, 2012,
  , ACTIVITY-BASED PROTEIN PROFILING, Vol: 324, Pages: 115-135, ISSN: 0340-1022
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  • Citations: 17
• Journal article
  Furse S, Brooks NJ, Seddon AM, Woscholski R, Templer RH, Tate EW, Gaffney PRJ, Ces Oet al., 2012,
  , Soft Matter
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• Journal article
  Bradshaw RT, Aronica PGA, Tate EW, Leatherbarrow RJ, Gould IRet al., 2012,
  , CHEMICAL SCIENCE, Vol: 3, Pages: 1503-1511, ISSN: 2041-6520
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  • Citations: 2
• Journal article
  Tate EW, Goss RJM, 2011,
  , Chem Commun (Camb), Vol: 47, Pages: 10869-10873
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• Journal article
  Delmotte A, Tate EW, Yaliraki SN, Barahona Met al., 2011,
  , PHYSICAL BIOLOGY, Vol: 8, ISSN: 1478-3975

  Despite the recognized importance of the multi-scale spatio-temporal organization of proteins, most computational tools can only access a limited spectrum of time and spatial scales, thereby ignoring the effects on protein behavior of the intricate coupling between the different scales. Starting from a physico-chemical atomistic network of interactions that encodes the structure of the protein, we introduce a methodology based on multi-scale graph partitioning that can uncover partitions and levels of organization of proteins that span the whole range of scales, revealing biological features occurring at different levels of organization and tracking their effect across scales. Additionally, we introduce a measure of robustness to quantify the relevance of the partitions through the generation of biochemically-motivated surrogate random graph models. We apply the method to four distinct conformations of myosin tail interacting protein, a protein from the molecular motor of the malaria parasite, and study properties that have been experimentally addressed such as the closing mechanism, the presence of conserved clusters, and the identification through computational mutational analysis of key residues for binding.

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• Journal article
  de la Riva L, Willing SE, Tate EW, Fairweather NFet al., 2011,
  , JOURNAL OF BACTERIOLOGY, Vol: 193, Pages: 3276-3285, ISSN: 0021-9193
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  • Citations: 45
• Journal article
  Serwa R, Tate EW, 2011,
  , Chemistry and Biology, Vol: 18, Pages: 407-409, ISSN: 1879-1301

  Activity-based protein profiling (ABPP) is emerging as a game-changing tool for drug discovery, target validation, and basic biology. In this issue, Chang et al. (2011) report the ABPP-facilitated discovery of JW480, a highly selective potent and orally bioavailable inhibitor of monoalkylglycerol ether hydrolase KIAA1363 that dramatically impairs in vivo growth of human prostate cancer cell lines.

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• Journal article
  Heal WP, Dang TH, Tate EW, 2011,
  , Chem Soc Rev, Vol: 40, Pages: 246-257, ISSN: 1460-4744

  The development and application of chemical technologies enabling direct analysis of enzyme activity in living systems has undergone explosive growth in recent years. Activity-based protein profiling (ABPP) is a key constituent of this broad field, and is among the most powerful and mature chemical proteomic technologies. This tutorial review introduces the essential features of ABPP and the design and application of activity-based probes (ABPs) from drug target elucidation and in vivo visualisation of enzyme activity to comprehensive profiling of the catalytic content of living systems, and the discovery of new biological pathways.

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