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  • Journal article
    Furse S, Brooks NJ, Seddon AM, Woscholski R, Templer RH, Tate EW, Gaffney PRJ, Ces Oet al., 2012,

    , Soft Matter
  • Journal article
    Bradshaw RT, Aronica PGA, Tate EW, Leatherbarrow RJ, Gould IRet al., 2012,

    , CHEMICAL SCIENCE, Vol: 3, Pages: 1503-1511, ISSN: 2041-6520
  • Journal article
    Tate EW, Goss RJM, 2011,

    , Chem Commun (Camb), Vol: 47, Pages: 10869-10873
  • 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.

  • 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
  • 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.

  • 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.

  • Journal article
    Heal WP, Jovanovic B, Bessin S, Wright MH, Magee AI, Tate EWet al., 2011,

    , CHEMICAL COMMUNICATIONS, Vol: 47, Pages: 4081-4083, ISSN: 1359-7345
  • Journal article
    Bradshaw RT, Patel BH, Tate EW, Leatherbarrow RJ, Gould IRet al., 2011,

    , PROTEIN ENGINEERING DESIGN & SELECTION, Vol: 24, Pages: 197-207, ISSN: 1741-0126
  • Journal article
    Berry AFH, Heal WP, Tarafder AK, Tolmachova T, Baron RA, Seabra MC, Tate EWet al., 2010,

    , CHEMBIOCHEM, Vol: 11, Pages: 771-773, ISSN: 1439-4227

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Request URL: http://www.imperial.ac.uk:80/respub/WEB-INF/jsp/search-t4-html.jsp Request URI: /respub/WEB-INF/jsp/search-t4-html.jsp Query String: id=870&limit=10&page=18&respub-action=search.html Current Millis: 1777183588211 Current Time: Sun Apr 26 07:06:28 BST 2026

Contact

Prof. Ed Tate
GSK Chair in Chemical Biology
Department of Chemistry
Molecular Sciences Research Hub, White City Campus,
82 Wood Lane, London, W12 0BZ

e.tate@imperial.ac.uk
Tel: +44 (0)20 759 + ext 43752 or 45821