Recent Muon g-2 Result in Deflected Anomaly-Mediated Supersymmetry Breaking

We study the deflected anomaly-mediated supersymmetry breaking (AMSB) scenario in the light of the recent result of the muon g-2 from Brookhaven E821 experiment. The E821 result suggests the deviation from the SM prediction, though there remain unsettled uncertainties. We find that the supersymmetric contribution to the muon g-2 can be \mathcal{O}(10^{-9}), large enough to fill the deviation, with other experimental constraints satisfied. In particular, the Higgs mass and b \to s \gamma put severe constraints on the model and large \tan\beta is favored to enhance the muon g-2.Comment: 13 pages, 6 figure

Normally-OFF Two-Dimensional Hole Gas Diamond MOSFETs Through Nitrogen-Ion Implantation

Diamond is a promising material for power applications owing to its excellent physical properties. Two-dimensional hole gas (2DHG) diamond metal-oxide- semiconductor field-effect transistors (MOSFETs) with hydrogen-terminated (C-H) channel have high current densities and high breakdown fields but often show normally-ON operation. From the viewpoint of safety, normally-OFF operation is required for power applications. In this letter, we used ion implantation to form a shallow and thin nitrogen-doped layer below the C-H channel region, which realized normally-OFF operation. Nitrogen-ion implanted length is fixed at 5 or 10 μm. Nitrogen is a deep donor (1.7 eV) and the nitrogen-doped layer prevents hole accumulation near the surface. The threshold voltage was as high as -2.5 V and no obvious dependence on the threshold voltage of nitrogenion implanted length is observed. The breakdown field was 2.7 MV/cm at room temperature. Of 64 devices with a common gate length, 75% showed normally-OFF operation. We confirmed the threshold voltage shift by a thin and shallow nitrogen-doped layer formed by ion implantation

Toward Bringing Stability in Afghanistan : A Review of the Peacebuilding Strategy

Contributors ii Introduction: A Need for 'Change' in the Peacebuilding Strategy for Afghanistan / Yuji Uesugi 1 Chapter 1: What Was Wrong With Afghanistan? Reflection upon the Past and Prospect for the Future / Hideaki Shinoda 13 Chapter 2: Examining Regime Change Dynamics in Afghanistan through Relationships between States and Armed Groups / Tatsuo Yamane 25 Chapter 3: Security Sector Reform in Afghanistan / Masoon Stanekzai and Masaki Kudo 39 Chapter 4: Assessing the Role of DDR in Afghanistan: Internal Security Provision and External Environment / Shamsul Hadi Shams 55 Chapter 5: Impact of Illicit Drugs on the Afghan Peacebuilding Process and the Establishment of the Rule of Law / Miwa Kato 77 Chapter 6: Transitional Justice in the Afghan Peacebuilding Process: The Potential and Limitations / Madoka Futamura 101 Chapter 7: Japanese Assistance to the Security Sector in Afghanistan / Nobutaka Miyahara 119 Chapter 8: Breaking the Vicious Cycle of Insecurity: Counter-insurgency in Afghanistan / Yuji Uesugi 13

Fosfomycin Biosynthesis <i>via</i> Transient Cytidylylation of 2‑Hydroxyethylphosphonate by the Bifunctional Fom1 Enzyme

Fosfomycin is a wide-spectrum phosphonate antibiotic that is used clinically to treat cystitis, tympanitis, <i>etc</i>. Its biosynthesis starts with the formation of a carbon–phosphorus bond catalyzed by the phosphoenolpyruvate phosphomutase Fom1. We identified an additional cytidylyltransferase (CyTase) domain at the Fom1 <i>N</i>-terminus in addition to the phosphoenolpyruvate phosphomutase domain at the Fom1 <i>C</i>-terminus. Here, we demonstrate that Fom1 is bifunctional and that the Fom1 CyTase domain catalyzes the cytidylylation of the 2-hydroxyethylphosphonate (HEP) intermediate to produce cytidylyl-HEP. On the basis of this new function of Fom1, we propose a revised fosfomycin biosynthetic pathway that involves the transient CMP-conjugated intermediate. The identification of a biosynthetic mechanism <i>via</i> such transient cytidylylation of a biosynthetic intermediate fundamentally advances the understanding of phosphonate biosynthesis in nature. The crystal structure of the cytidylyl-HEP-bound CyTase domain provides a basis for the substrate specificity and reveals unique catalytic elements not found in other members of the CyTase family

Identification and characterization of endo-α-, exo-α-, and exo-β-d-arabinofuranosidases degrading lipoarabinomannan and arabinogalactan of mycobacteria

Abstract The cell walls of pathogenic and acidophilic bacteria, such as Mycobacterium tuberculosis and Mycobacterium leprae, contain lipoarabinomannan and arabinogalactan. These components are composed of d-arabinose, the enantiomer of the typical l-arabinose found in plants. The unique glycan structures of mycobacteria contribute to their ability to evade mammalian immune responses. In this study, we identified four enzymes (two GH183 endo-d-arabinanases, GH172 exo-α-d-arabinofuranosidase, and GH116 exo-β-d-arabinofuranosidase) from Microbacterium arabinogalactanolyticum. These enzymes completely degraded the complex d-arabinan core structure of lipoarabinomannan and arabinogalactan in a concerted manner. Furthermore, through biochemical characterization using synthetic substrates and X-ray crystallography, we elucidated the mechanisms of substrate recognition and anomer-retaining hydrolysis for the α- and β-d-arabinofuranosidic bonds in both endo- and exo-mode reactions. The discovery of these d-arabinan-degrading enzymes, along with the understanding of their structural basis for substrate specificity, provides valuable resources for investigating the intricate glycan architecture of mycobacterial cell wall polysaccharides and their contribution to pathogenicity