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  • Conference paper
    Maioli V, Gorlitz F, Warren S, Kumar S, French PMW, Chennell G, Sardini A, Carling D, Alwes F, Dunsby CWet al., 2016,

    Three-dimensional fluorescence imaging by stage-scanning oblique plane microscopy

    , Conference on Three-Dimensional and Multidimensional Microscopy - Image Acquisition and Processing XXIII, Publisher: SPIE, ISSN: 0277-786X
  • Journal article
    Byrne B, Alguel Y, Scull NJ, Craven G, Armstrong A, Iwata S, Diallinas G, Amillis S, Capaldi S, Cameron AD, Lambrinidis G, Mikros Eet al., 2016,

    Structure of eukaryotic purine/Hþ symporter UapA suggests a role for homodimerization in transport activity

    , Nature Communications, Vol: 7, Pages: 1-9, ISSN: 2041-1723

    The uric acid/xanthine H+ symporter, UapA, is a high-affinity purine transporter from the filamentous fungus Aspergillus nidulans. Here we present the crystal structure of a genetically stabilized version of UapA (UapA-G411VΔ1–11) in complex with xanthine. UapA is formed from two domains, a core domain and a gate domain, similar to the previously solved uracil transporter UraA, which belongs to the same family. The structure shows UapA in an inward-facing conformation with xanthine bound to residues in the core domain. Unlike UraA, which was observed to be a monomer, UapA forms a dimer in the crystals with dimer interactions formed exclusively through the gate domain. Analysis of dominant negative mutants is consistent with dimerization playing a key role in transport. We postulate that UapA uses an elevator transport mechanism likely to be shared with other structurally homologous transporters including anion exchangers and prestin.

  • Journal article
    Miller RM, Poulos AS, Robles ESJ, Brooks NJ, Ces O, Cabral JTet al., 2016,

    Isothermal Crystallization Kinetics of Sodium Dodecyl Sulfate–Water Micellar Solutions

    , Crystal Growth & Design, Vol: 16, Pages: 3379-3388, ISSN: 1528-7505

    The crystallization mechanisms and kinetics of micellar sodium dodecyl sulfate (SDS) solutions in water, under isothermal conditions, were investigated experimentally by a combination of reflection optical microscopy (OM), differential scanning calorimetry (DSC), and attenuated total reflection Fourier transform infrared spectroscopy (ATR-FTIR). The rates of nucleation and growth were estimated from OM and DSC across temperatures ranging from 20 to −6 °C for 20% SDS-H2O, as well as for 10 and 30% SDS-H2O at representative temperatures of 6, 2, and −2 °C. A decrease in temperature increased both nucleation and growth rates, and the combined effect of the two processes on the morphology was quantified via both OM and ATR-FTIR. Needles, corresponding to the hemihydrate polymorph, become the dominant crystal form at ≤ −2 °C, while platelets, the monohydrate, predominate at higher temperatures. Above 8 °C, crystallization was only observed if seeded from crystals generated at lower temperatures. Our results provide quantitative and morphological insight into the crystallization of ubiquitous micellar SDS solutions and its phase stability below room temperature.

  • Journal article
    sherlock B, Yu F, Stone J, Warren S, Paterson C, Neil MAA, French PMW, Dunsby CWet al., 2016,

    Tunable fibre-coupled multiphoton microscopy with a negative curvature fibre

    , Journal of Biophotonics, Vol: 9, Pages: 715-720, ISSN: 1864-0648

    Negative curvature fibre (NCF) guides light in its core by inhibiting the coupling of core andcladding modes. In this work, an NCF was designed and fabricated to transmit ultrashort opticalpulses for multiphoton microscopy with low group velocity dispersion (GVD) at 800 nm. Itsattenuation was measured to be <0.3 dB.m-1over the range 600-850 nm and the GVD was-180±70 fs2.m-1at 800 nm. Using an average fibre output power of ~20 mW and pulserepetition rate of 80 MHz, the NCF enabled pulses with a duration of <200 fs to be transmittedthrough a length of 1.5 m of fibre over a tuning range of 180 nm without the need for dispersioncompensation. In a 4 m fibre, temporal and spectral pulse widths were maintained to within10% of low power values up to the maximum fibre output power achievable with the lasersystem used of 278 mW at 700 nm, 808 mW at 800 nm and 420 mW at 860 nm. When coupledto a multiphoton microscope, it enabled imaging of ex vivo tissue using excitation wavelengthsfrom 740 nm to 860 nm without any need for adjustments to the set-up.

  • Conference paper
    Madej B, Dickson C, Skjevik A, Yang L, Gould I, Walker Ret al., 2016,

    Expansion of the Amber Lipid14 force field: Enabling complex membrane molecular dynamics

    , Publisher: AMER CHEMICAL SOC, ISSN: 0065-7727
  • Conference paper
    Yang L, Madej B, Skjevik A, Dickson C, Wang H, Gould I, Walker Ret al., 2016,

    Extension of the Amber Lipid14 force field to glycolipids: Parameterization and validation

    , Publisher: AMER CHEMICAL SOC, ISSN: 0065-7727
  • Journal article
    Lanyon-Hogg T, Masumoto N, Bodakh G, Konitsiotis AD, Thinon E, Rodgers UR, Owens RJ, Magee AI, Tate EWet al., 2016,

    Synthesis and characterisation of 5-acyl-6,7-dihydrothieno[3,2-c]pyridine inhibitors of Hedgehog acyltransferase

    , Data in Brief, Vol: 7, Pages: 257-281, ISSN: 2352-3409

    In this data article we describe synthetic and characterisation data for four members of the 5-acyl-6,7-dihydrothieno[3,2-c]pyridine (termed “RU-SKI”) class of inhibitors of Hedgehog acyltransferase, including associated NMR spectra for final compounds. RU-SKI compounds were selected for synthesis based on their published high potencies against the enzyme target. RU-SKI 41 (9a), RU-SKI 43 (9b), RU-SKI 101 (9c), and RU-SKI 201 (9d) were profiled for activity in the related article “Click chemistry armed enzyme linked immunosorbent assay to measure palmitoylation by Hedgehog acyltransferase” (Lanyon-Hogg et al., 2015) [1]. 1H NMR spectral data indicate different amide conformational ratios between the RU-SKI inhibitors, as has been observed in other 5-acyl-6,7-dihydrothieno[3,2-c]pyridines. The synthetic and characterisation data supplied in the current article provide validated access to the class of RU-SKI inhibitors.

  • Journal article
    Haase S, Zimmermann D, Olshina MA, Wilkinson M, Fisher F, Tan YH, Stewart RJ, Tonkin CJ, Wong W, Kovar DR, Baum Jet al., 2015,

    Disassembly activity of actin depolymerization factor (ADF) is associated with distinct cellular processes in apicomplexan parasites.

    , Molecular Biology of the Cell, Vol: 26, Pages: 3001-3012, ISSN: 1939-4586

    Proteins of the actin depolymerizing factor (ADF)/cofilin family have been shown to be crucial for the motility and survival of apicomplexan parasites. However, the mechanisms by which ADF proteins fulfill their function remains poorly understood. In this study we sought to investigate the comparative activities of ADF proteins from Toxoplasma gondii and Plasmodium falciparum, the human malaria parasite, using a conditional T. gondii ADF-knockout line complemented with ADF variants from either species. We show that P. falciparum ADF1 can fully restore native TgADF activity, demonstrating functional conservation between parasites. Strikingly, mutation of a key basic residue (Lys(72)), previously implicated in disassembly in PfADF1, had no detectable phenotypic effect on parasite growth, motility or development. In contrast, organelle segregation was severely impaired when complementing with a TgADF mutant lacking the corresponding residue (Lys(68)). Biochemical analyses of each ADF protein confirmed the reduced ability of lysine mutants to mediate actin depolymerization via filament disassembly though not severing, in contrast to previous reports. These data suggest that actin filament disassembly is essential for apicomplexan parasite development but not for motility as well as pointing to genus-specific coevolution between ADF proteins and their native actin.

  • Journal article
    McCarthy NL, Ces O, Law RV, Seddon JM, Brooks NJet al., 2015,

    Separation of liquid domains in model membranes induced with high hydrostatic pressure

    , EUROPEAN BIOPHYSICS JOURNAL WITH BIOPHYSICS LETTERS, Vol: 44, Pages: S115-S115, ISSN: 0175-7571
  • Journal article
    McCarthy NLC, Ces O, Law RV, Seddon JM, Brooks NJet al., 2015,

    Separation of liquid domains in model membranes induced with high hydrostatic pressure.

    , Chem Commun (Camb), Vol: 51, Pages: 8675-8678

    We have imaged the formation of membrane microdomains immediately after their induction using a novel technology platform coupling high hydrostatic pressure to fluorescence microscopy. After formation, the ordered domains are small and highly dynamic. This will enhance links between model lipid assemblies and dynamic processes in cellular membranes.

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.

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