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  • Journal article
    Dang THT, de la Riva L, Fagan RP, Storck EM, Heal WP, Janoir C, Fairweather NF, Tate EWet al., 2010,

    Chemical Probes of Surface Layer Biogenesis in <i>Clostridium difficile</i>

    , ACS CHEMICAL BIOLOGY, Vol: 5, Pages: 279-285, ISSN: 1554-8929
  • Journal article
    Wright MH, Heal WP, Mann DJ, Tate EWet al., 2010,

    Protein myristoylation in health and disease.

    , J Chem Biol, Vol: 3, Pages: 19-35, ISSN: 1864-6166

    N-myristoylation is the attachment of a 14-carbon fatty acid, myristate, onto the N-terminal glycine residue of target proteins, catalysed by N-myristoyltransferase (NMT), a ubiquitous and essential enzyme in eukaryotes. Many of the target proteins of NMT are crucial components of signalling pathways, and myristoylation typically promotes membrane binding that is essential for proper protein localisation or biological function. NMT is a validated therapeutic target in opportunistic infections of humans by fungi or parasitic protozoa. Additionally, NMT is implicated in carcinogenesis, particularly colon cancer, where there is evidence for its upregulation in the early stages of tumour formation. However, the study of myristoylation in all organisms has until recently been hindered by a lack of techniques for detection and identification of myristoylated proteins. Here we introduce the chemistry and biology of N-myristoylation and NMT, and discuss new developments in chemical proteomic technologies that are meeting the challenge of studying this important co-translational modification in living systems.
  • Journal article
    So S, Peeva LG, Tate EW, Leatherbarrow RJ, Livingston AGet al., 2010,

    Organic Solvent Nanofiltration: A New Paradigm in Peptide Synthesis

    , Org Process Res Dev, Vol: 14, Pages: 1313-1325
  • Journal article
    Thomas JC, Green JL, Howson RI, Simpson P, Moss DK, Martin SR, Holder AA, Cota E, Tate EWet al., 2010,

    Interaction and dynamics of the <i>Plasmodium</i> <i>falciparum</i> MTIP-MyoA complex, a key component of the invasion motor in the malaria parasite

    , MOLECULAR BIOSYSTEMS, Vol: 6, Pages: 494-498, ISSN: 1742-206X
  • Journal article
    So S, Peeva LG, Tate EW, Leatherbarrow RJ, Livingston AGet al., 2010,

    Membrane enhanced peptide synthesis

    , CHEMICAL COMMUNICATIONS, Vol: 46, Pages: 2808-2810, ISSN: 1359-7345
  • Journal article
    Heal WP, Tate EW, 2010,

    Getting a chemical handle on protein post-translational modification

    , ORGANIC & BIOMOLECULAR CHEMISTRY, Vol: 8, Pages: 731-738, ISSN: 1477-0520
  • Journal article
    Thongyoo P, Bonomelli C, Leatherbarrow RJ, Tate EWet al., 2009,

    Potent Inhibitors of β-Tryptase and Human Leukocyte Elastase Based on the MCoTI-II Scaffold

    , JOURNAL OF MEDICINAL CHEMISTRY, Vol: 52, Pages: 6197-6200, ISSN: 0022-2623
  • Journal article
    Heal WP, Wickramasinghe SR, Tate EW, 2008,

    Activity based chemical proteomics: profiling proteases as drug targets.

    , 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.
  • Journal article
    Busch GK, Tate EW, Gaffney PR, Rosivatz E, Woscholski R, Leatherbarrow RJet al., 2008,

    Specific N-terminal protein labelling: use of FMDV 3C pro protease and native chemical ligation

    , 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
  • Journal article
    Heal WP, Wickramasinghe SR, Leatherbarrow RJ, Tate EWet al., 2008,

    N-Myristoyl transferase-mediated protein labelling in vivo

    , Organic and Biomolecular Chemistry

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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