Oxford, Oxfordshire, United Kingdom

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Department of Chemistry
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Department of Engineering Science
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Department of Physics
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Publication History View all

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    ABSTRACT: Standard techniques for computed tomography imaging are not directly applicable to a carbonate rock because of the geometric complexity of its pore space. In this study, we first characterized the pore structure in Majella limestone with 30 per cent porosity. Microtomography data acquired on this rock was partitioned into three distinct domains: macropores, solid grains, and an intermediate domain made up of voxels of solid embedded with micropores below the resolution. A morphological analysis of the microtomography images shows that in Majella limestone both the solid and intermediate domains are interconnected in a manner similar to that reported previously in a less porous limestone. We however show that the macroporosity in Majella limestone is fundamentally different, in that it has a percolative backbone which may contribute significantly to its permeability. We then applied for the first time 3-D-volumetric digital image correlation (DIC) to characterize the mode of mechanical failure in this limestone. Samples were triaxially deformed over a wide range of confining pressures. Tomography imaging was performed on these samples before and after deformation. Inelastic compaction was observed at all tested pressures associated with both brittle and ductile behaviors. Our DIC analysis reveals the structure of compacting shear bands in Majella limestone deformed in the transitional regime. It also indicates an increase of geometric complexity with increasing confinement-from a planar shear band, to a curvilinear band, and ultimately to a diffuse multiplicity of bands, before shear localization is inhibited as the failure mode completes the transition to delocalized cataclastic flow.
    12/2015; 200(2-2):699-717. DOI:10.1093/gji/ggu414
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    ABSTRACT: CTP synthase (CTPsyn) is a metabolic enzyme responsible for the de novo synthesis of the nucleotide CTP. Several recent studies have shown that CTPsyn forms filamentous subcellular structures known as cytoophidia in bacteria, yeast, fruit flies and humans. However, it remains elusive whether and how CTPsyn and cytoophidia play a role during development. Here, we show that cytoophidia are abundant in the neuroepithelial stem cells in Drosophila optic lobes. Optic lobes are underdeveloped in CTPsyn mutants as well as in CTPsyn RNAi. Moreover, overexpressing CTPsyn impairs the development of optic lobes, specifically by blocking the transition from neuroepithelium to neuroblast. Taken together, our results indicate that CTPsyn is critical for optic lobe homeostasis in Drosophila. Copyright © 2015 The Authors. Published by Elsevier Ltd.. All rights reserved.
    Journal of Genetics and Genomics 05/2015; 3(5). DOI:10.1016/j.jgg.2015.04.006

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  • Address
    University of Oxford, University Offices, Wellington Square, OX1 2JD, Oxford, Oxfordshire, United Kingdom
  • Head of Institution
    The Rt Hon the Lord Patten of Barnes, CH
  • Website
    http://www.ox.ac.uk
  • Phone
    +44 1865 270000
  • Fax
    +44 1865 270708
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BMJ (online) 01/2010; 340:c1900.
176 Downloads
 
Trials 07/2015; DOI:10.1186/s13063-015-0818-7
174 Downloads

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