The publication feed below is often incomplete and out of date; for an up to date summary of our publications please see Google Scholar or Pub Med

Search or filter publications

Filter by type:

Filter by publication type

Filter by year:



  • Showing results for:
  • Reset all filters

Search results

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

    Mutational Locally Enhanced Sampling (MULES) for quantitative prediction of the effects of mutations at protein-protein interfaces

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

    Highlights from the 46th EUCHEM Conference on stereochemistry, Bürgenstock, Switzerland, May 2011.

    , Chem Commun (Camb), Vol: 47, Pages: 10869-10873
  • Journal article
    Delmotte A, Tate EW, Yaliraki SN, Barahona Met al., 2011,

    Protein multi-scale organization through graph partitioning and robustness analysis: application to the myosin-myosin light chain interaction

    , 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,

    Roles of Cysteine Proteases Cwp84 and Cwp13 in Biogenesis of the Cell Wall of <i>Clostridium difficile</i>

    , JOURNAL OF BACTERIOLOGY, Vol: 193, Pages: 3276-3285, ISSN: 0021-9193
  • Journal article
    Serwa R, Tate EW, 2011,

    Activity-based profiling for drug discovery

    , 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,

    Activity-based probes: discovering new biology and new drug targets.

    , 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,

    Bioorthogonal chemical tagging of protein cholesterylation in living cells

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

    Comparing experimental and computational alanine scanning techniques for probing a prototypical protein-protein interaction

    , 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,

    Rapid Multilabel Detection of Geranylgeranylated Proteins by Using Bioorthogonal Ligation Chemistry

    , CHEMBIOCHEM, Vol: 11, Pages: 771-773, ISSN: 1439-4227
  • Journal article
    Brannigan JA, Smith BA, Yu Z, Brzozowski AM, Hodgkinson MR, Maroof A, Price HP, Meier F, Leatherbarrow RJ, Tate EW, Smith DF, Wilkinson AJet al., 2010,

    N-Myristoyltransferase from Leishmania donovani: Structural and Functional Characterisation of a Potential Drug Target for Visceral Leishmaniasis

    , Journal of Molecular Biology, Vol: 396, Pages: 985-999, ISSN: 1089-8638

    N-Myristoyltransferase (NMT) catalyses the attachment of the 14-carbon saturated fatty acid, myristate, to the amino-terminal glycine residue of a subset of eukaryotic proteins that function in multiple cellular processes, including vesicular protein trafficking and signal transduction. In these pathways, N-myristoylation facilitates association of substrate proteins with membranes or the hydrophobic domains of other partner peptides. NMT function is essential for viability in all cell types tested to date, demonstrating that this enzyme has potential as a target for drug development. Here, we provide genetic evidence that NMT is likely to be essential for viability in insect stages of the pathogenic protozoan parasite, Leishmania donovani, causative agent of the tropical infectious disease, visceral leishmaniasis. The open reading frame of L. donovaniNMT has been amplified and used to overproduce active recombinant enzyme in Escherichia coli, as demonstrated by gel mobility shift assays of ligand binding and peptide-myristoylation activity in scintillation proximity assays. The purified protein has been crystallized in complex with the non-hydrolysable substrate analogue S-(2-oxo)pentadecyl-CoA, and its structure was solved by molecular replacement at 1.4 Å resolution. The structure has as its defining feature a 14-stranded twisted β-sheet on which helices are packed so as to form an extended and curved substrate-binding groove running across two protein lobes. The fatty acyl-CoA is largely buried in the N-terminal lobe, its binding leading to the loosening of a flap, which in unliganded NMT structures, occludes the protein substrate binding site in the carboxy-terminal lobe. These studies validate L. donovani NMT as a potential target for development of new therapeutic agents against visceral leishmaniasis.

This data is extracted from the Web of Science and reproduced under a licence from Thomson Reuters. You may not copy or re-distribute this data in whole or in part without the written consent of the Science business of Thomson Reuters.

Request URL: Request URI: /respub/WEB-INF/jsp/search-t4-html.jsp Query String: id=870&limit=10&page=17&respub-action=search.html Current Millis: 1719074827795 Current Time: Sat Jun 22 17:47:07 BST 2024