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• Journal article
  Yusuf NA, Green JL, Wall RJ, Knuepfer E, Moon RW, Schulte-Huxel C, Stanway RR, Martin SR, Howell SA, Douse CH, Cota E, Tate EW, Tewari R, Holder AAet al., 2015,
  , Journal of Biological Chemistry, Vol: 290, Pages: 12147-12164, ISSN: 1083-351X

  Myosin B (MyoB) is one of the two short class XIV myosinsencoded in the Plasmodium genome. Class XIV myosins arecharacterized by a catalytic “head,” a modified “neck,” and theabsence of a “tail” region. Myosin A (MyoA), the other class XIVmyosin in Plasmodium, has been established as a component ofthe glideosome complex important in motility and cell invasion,but MyoB is not well characterized. We analyzed the propertiesof MyoB using three parasite species as follows: Plasmodiumfalciparum, Plasmodium berghei, and Plasmodium knowlesi.MyoB is expressed in all invasive stages (merozoites, ookinetes,and sporozoites) of the life cycle, and the protein is found in adiscrete apical location in these polarized cells. In P. falciparum,MyoB is synthesized very late in schizogony/merogony, and itslocation in merozoites is distinct from, and anterior to, that of arange of known proteins present in the rhoptries, rhoptry neckor micronemes. Unlike MyoA, MyoB is not associated withglideosome complex proteins, including the MyoA light chain,myosin A tail domain-interacting protein (MTIP). A uniqueMyoB light chain (MLC-B) was identified that contains a calmodulin-likedomain at the C terminus and an extended N-terminalregion. MLC-B localizes to the same extreme apical polein the cell as MyoB, and the two proteins form a complex. Wepropose that MLC-B is a MyoB-specific light chain, and for theshort class XIV myosins that lack a tail region, the atypical myosinlight chains may fulfill that role.

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• Journal article
  Masumoto N, Lanyon-Hogg T, Rodgers UR, Konitsiotis AD, Magee AI, Tate EWet al., 2015,
  , Biochemical Society Transactions, Vol: 43, Pages: 246-252, ISSN: 1470-8752

  Since the identification of the membrane-bound O-acyltransferase (MBOATs) protein family in the early2000s, three distinct members [porcupine (PORCN), hedgehog (Hh) acyltransferase (HHAT) and ghrelin Oacyltransferase(GOAT)] have been shown to acylate specific proteins or peptides. In this review, topologydetermination, development of assays to measure enzymatic activities and discovery of small moleculeinhibitors are compared and discussed for each of these enzymes.

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• Journal article
  Ciepla P, Magee AI, Tate EW, 2015,
  , BIOCHEMICAL SOCIETY TRANSACTIONS, Vol: 43, Pages: 262-267, ISSN: 0300-5127
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  • Citations: 15
• Journal article
  Wright MH, Paape D, Storck EM, Serwa RA, Smith DF, Tate EWet al., 2015,
  , CHEMISTRY & BIOLOGY, Vol: 22, Pages: 342-354, ISSN: 1074-5521
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  • Citations: 71
• Journal article
  Lanyon-Hogg T, Ritzefeld M, Masumoto N, Magee AI, Rzepa HS, Tate EWet al., 2015,
  , Journal of Organic Chemistry, Vol: 80, Pages: 4370-4377, ISSN: 1520-6904

  2-Substituted N-acyl-piperidine is a widespread and important structuralmotif, found in approximately 500 currently available structures, and present in nearly30 pharmaceutically active compounds. Restricted rotation of the acyl substituent insuch molecules can give rise to two distinct chemical environments. Here wedemonstrate, using NMR studies and density functional theory modeling of the lowestenergy structures of 5-acyl-6,7-dihydrothieno[3,2-c]pyridine derivatives, that the amideE:Z equilibrium is affected by non-covalent interactions between the amide oxygen andadjacent aromatic protons. Structural predictions were used to design molecules that promote either the E- or Z-amideconformation, enabling preparation of compounds with a tailored conformational ratio, as proven by NMR studies. Analysis ofthe available X-ray data of a variety of published N-acyl-piperidine-containing compounds further indicates that these moleculesare also clustered in the two observed conformations. This finding emphasizes that directed conformational isomerism hassignificant implications for the design of both small molecules and larger amide-containing molecular architectures.

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• Journal article
  Konitsiotis AD, Jovanovic B, Ciepla P, Spitaler M, Lanyon-Hogg T, Tate EW, Magee AIet al., 2015,
  , JOURNAL OF BIOLOGICAL CHEMISTRY, Vol: 290, Pages: 3293-3307
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  • Citations: 51
• Journal article
  Tate EW, Kalesh KA, Lanyon-Hogg T, Storck EM, Thinon Eet al., 2015,
  , CURRENT OPINION IN CHEMICAL BIOLOGY, Vol: 24, Pages: 48-57, ISSN: 1367-5931
  • Cite
  • Citations: 91
• Journal article
  Douse CH, Vrielink N, Zhang W, Cota E, Tate EWet al., 2015,
  , CHEMMEDCHEM, Vol: 10, Pages: 134-143, ISSN: 1860-7179
  • Cite
  • Citations: 18
• Journal article
  Kalesh KA, Clulow JA, Tate EW, 2015,
  , CHEMICAL COMMUNICATIONS, Vol: 51, Pages: 5497-5500, ISSN: 1359-7345
  • Cite
  • Citations: 29
• Journal article
  Furse S, Mak L, Tate EW, Templer RH, Ces O, Woscholski R, Gaffney PRJet al., 2015,
  , ORGANIC & BIOMOLECULAR CHEMISTRY, Vol: 13, Pages: 2001-2011, ISSN: 1477-0520
  • Cite
  • Citations: 8

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