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  • 1
    Publication Date: 2014-10-07
    Description: Author(s): T. Kurihara, K. Nakamura, K. Yamaguchi, Y. Sekine, Y. Saito, M. Nakajima, K. Oto, H. Watanabe, and T. Suemoto We demonstrate enhancement of the spin precession of orthoferrite ErFeO3 using the magnetic near-field produced by a split-ring resonator (SRR), using the terahertz pump-optical Faraday probe measurement. The precession amplitude was enhanced by ∼8 times when the resonance frequency of spin precessi... [Phys. Rev. B 90, 144408] Published Mon Oct 06, 2014
    Keywords: Magnetism
    Print ISSN: 1098-0121
    Electronic ISSN: 1095-3795
    Topics: Physics
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  • 2
    Publication Date: 2013-04-06
    Description: Author(s): J. Burnett, T. Lindström, M. Oxborrow, Y. Harada, Y. Sekine, P. Meeson, and A. Ya. Tzalenchuk Slow noise processes, with characteristic timescales ∼1 s, have been studied in planar superconducting resonators. A frequency-locked loop is employed to track deviations of the resonator center frequency with high precision and bandwidth. Comparative measurements are made in varying microwave drive... [Phys. Rev. B 87, 140501] Published Fri Apr 05, 2013
    Keywords: Superfluidity and superconductivity
    Print ISSN: 1098-0121
    Electronic ISSN: 1095-3795
    Topics: Physics
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  • 3
    Publication Date: 2015-10-15
    Description: Selenocysteine (Sec), the 21 st amino acid in translation, uses its specific tRNA (tRNA Sec ) to recognize the UGA codon. The Sec-specific elongation factor SelB brings the selenocysteinyl-tRNA Sec (Sec-tRNA Sec ) to the ribosome, dependent on both an in-frame UGA and a Sec-insertion sequence (SECIS) in the mRNA. The bacterial SelB binds mRNA through its C-terminal region, for which crystal structures have been reported. In this study, we determined the crystal structure of the full-length SelB from the bacterium Aquifex aeolicus , in complex with a GTP analog, at 3.2-Å resolution. SelB consists of three EF-Tu-like domains (D1–3), followed by four winged-helix domains (WHD1–4). The spacer region, connecting the N- and C-terminal halves, fixes the position of WHD1 relative to D3. The binding site for the Sec moiety of Sec-tRNA Sec is located on the interface between D1 and D2, where a cysteine molecule from the crystallization solution is coordinated by Arg residues, which may mimic Sec binding. The Sec-binding site is smaller and more exposed than the corresponding site of EF-Tu. Complex models of Sec-tRNA Sec , SECIS RNA, and the 70S ribosome suggest that the unique secondary structure of tRNA Sec allows SelB to specifically recognize tRNA Sec and characteristically place it at the ribosomal A-site.
    Print ISSN: 0305-1048
    Electronic ISSN: 1362-4962
    Topics: Biology
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  • 4
    Publication Date: 2011-03-08
    Description: Author(s): S. Faniel, T. Matsuura, S. Mineshige, Y. Sekine, and T. Koga We report the determination of the intrinsic spin-orbit interaction (SOI) parameters for In_{0.53} Ga_{0.47} As/In_{0.52} Al_{0.48} As quantum wells (QWs) from the analysis of the weak antilocalization effect. We show that the Dresselhaus SOI is mostly negligible in this system and that the intrinsi... [Phys. Rev. B 83, 115309] Published Mon Mar 07, 2011
    Keywords: Semiconductors II: surfaces, interfaces, microstructures, and related topics
    Print ISSN: 1098-0121
    Electronic ISSN: 1095-3795
    Topics: Physics
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  • 5
    Publication Date: 2011-12-28
    Description: Author(s): S. Mineshige, S. Kawabata, S. Faniel, J. Waugh, Y. Sekine, and T. Koga [Phys. Rev. B 84, 233305] Published Tue Dec 27, 2011
    Keywords: Semiconductors II: surfaces, interfaces, microstructures, and related topics
    Print ISSN: 1098-0121
    Electronic ISSN: 1095-3795
    Topics: Physics
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  • 6
    Publication Date: 2014-11-19
    Description: Dense hydrous magnesium silicates (DHMSs) may play an important role in water transport during planetary accretion and as water reservoirs in the Earth’s deep mantle. We show that the dynamic decomposition products of antigorite, Mg 3 Si 2 O 5 (OH) 4 , can be interpreted as containing the newly discovered, dense hydrous silicate, phase H (MgSiO 4 H 2 ). The Hugoniot for phase H was calculated based on the Hugoniots for its constituent oxides and equation of state data derived from first-principles calculations. The measured antigorite Hugoniot, previously suggested to decompose into high-pressure phases without generating fluid H 2 O, was compared with those derived from calculations involving phase H. Sound velocity data were also compared to confirm that the dynamic breakdown product of antigorite at pressures above ~40 GPa is most likely phase H plus MgO without formation of fluid H 2 O.
    Print ISSN: 0003-004X
    Electronic ISSN: 1945-3027
    Topics: Geosciences
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  • 7
    Publication Date: 2007-10-20
    Description: A computational analysis of the nuclear genome of a red alga, Cyanidioschyzon merolae, identified 11 transfer RNA (tRNA) genes in which the 3' half of the tRNA lies upstream of the 5' half in the genome. We verified that these genes are expressed and produce mature tRNAs that are aminoacylated. Analysis of tRNA-processing intermediates for these genes indicates an unusual processing pathway in which the termini of the tRNA precursor are ligated, resulting in formation of a characteristic circular RNA intermediate that is then processed at the acceptor stem to generate the correct termini.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Soma, Akiko -- Onodera, Akinori -- Sugahara, Junichi -- Kanai, Akio -- Yachie, Nozomu -- Tomita, Masaru -- Kawamura, Fujio -- Sekine, Yasuhiko -- New York, N.Y. -- Science. 2007 Oct 19;318(5849):450-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Life Science, College of Science, Rikkyo (St. Paul's) University, Toshima, Tokyo 171-8501, Japan.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17947580" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; DNA, Algal/chemistry/genetics ; *Genes ; Methionine-tRNA Ligase/metabolism ; Molecular Sequence Data ; Nucleic Acid Conformation ; RNA/chemistry/genetics/*metabolism ; RNA Processing, Post-Transcriptional ; RNA, Algal/*genetics/metabolism ; RNA, Transfer/*genetics/metabolism ; RNA, Transfer, Amino Acyl/metabolism ; Rhodophyta/*genetics/metabolism ; Transcription, Genetic
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 8
    Publication Date: 2015-03-13
    Description: Detection of sodium-salt-rich ice grains emitted from the plume of the Saturnian moon Enceladus suggests that the grains formed as frozen droplets from a liquid water reservoir that is, or has been, in contact with rock. Gravitational field measurements suggest a regional south polar subsurface ocean of about 10 kilometres thickness located beneath an ice crust 30 to 40 kilometres thick. These findings imply rock-water interactions in regions surrounding the core of Enceladus. The resulting chemical 'footprints' are expected to be preserved in the liquid and subsequently transported upwards to the near-surface plume sources, where they eventually would be ejected and could be measured by a spacecraft. Here we report an analysis of silicon-rich, nanometre-sized dust particles (so-called stream particles) that stand out from the water-ice-dominated objects characteristic of Saturn. We interpret these grains as nanometre-sized SiO2 (silica) particles, initially embedded in icy grains emitted from Enceladus' subsurface waters and released by sputter erosion in Saturn's E ring. The composition and the limited size range (2 to 8 nanometres in radius) of stream particles indicate ongoing high-temperature (〉90 degrees C) hydrothermal reactions associated with global-scale geothermal activity that quickly transports hydrothermal products from the ocean floor at a depth of at least 40 kilometres up to the plume of Enceladus.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hsu, Hsiang-Wen -- Postberg, Frank -- Sekine, Yasuhito -- Shibuya, Takazo -- Kempf, Sascha -- Horanyi, Mihaly -- Juhasz, Antal -- Altobelli, Nicolas -- Suzuki, Katsuhiko -- Masaki, Yuka -- Kuwatani, Tatsu -- Tachibana, Shogo -- Sirono, Sin-iti -- Moragas-Klostermeyer, Georg -- Srama, Ralf -- England -- Nature. 2015 Mar 12;519(7542):207-10. doi: 10.1038/nature14262.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory for Atmospheric and Space Physics, University of Colorado, Boulder, Colorado 80303, USA. ; 1] Institut fur Geowissenschaften, Universitat Heidelberg, 69120 Heidelberg, Germany [2] Institut fur Raumfahrtsysteme, Universitat Stuttgart, 70569 Stuttgart, Germany. ; Department of Complexity Science and Engineering, University of Tokyo, Kashiwa 277-8561, Japan. ; Laboratory of Ocean-Earth Life Evolution Research, JAMSTEC, Yokosuka 237-0061, Japan. ; 1] Laboratory for Atmospheric and Space Physics, University of Colorado, Boulder, Colorado 80303, USA [2] Institute for Particle and Nuclear Physics, Wigner RCP, 1121 Budapest, Hungary. ; European Space Agency, ESAC, E-28691 Madrid, Spain. ; Research and Development Center for Submarine Resources, JAMSTEC, Yokosuka 237-0061, Japan. ; Graduate School of Environmental Studies, Tohoku University, Sendai 980-8579, Japan. ; Department of Natural History Sciences, Hokkaido University, Sapporo 060-0810, Japan. ; Graduate School of Environmental Sciences, Nagoya University, Nagoya 464-8601, Japan. ; Institut fur Raumfahrtsysteme, Universitat Stuttgart, 70569 Stuttgart, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/25762281" target="_blank"〉PubMed〈/a〉
    Print ISSN: 0028-0836
    Electronic ISSN: 1476-4687
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
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  • 9
    Publication Date: 2015-04-11
    Description: The integrated stress response (ISR) modulates messenger RNA translation to regulate the mammalian unfolded protein response (UPR), immunity, and memory formation. A chemical ISR inhibitor, ISRIB, enhances cognitive function and modulates the UPR in vivo. To explore mechanisms involved in ISRIB action, we screened cultured mammalian cells for somatic mutations that reversed its effect on the ISR. Clustered missense mutations were found at the amino-terminal portion of the delta subunit of guanine nucleotide exchange factor (GEF) eIF2B. When reintroduced by CRISPR-Cas9 gene editing of wild-type cells, these mutations reversed both ISRIB-mediated inhibition of the ISR and its stimulatory effect on eIF2B GEF activity toward its substrate, the translation initiation factor eIF2, in vitro. Thus, ISRIB targets an interaction between eIF2 and eIF2B that lies at the core of the ISR.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4538794/" target="_blank"〉〈img src="https://static.pubmed.gov/portal/portal3rc.fcgi/4089621/img/3977009" border="0"〉〈/a〉   〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4538794/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Sekine, Yusuke -- Zyryanova, Alisa -- Crespillo-Casado, Ana -- Fischer, Peter M -- Harding, Heather P -- Ron, David -- 084812/Wellcome Trust/United Kingdom -- 084812/Z/08/Z/Wellcome Trust/United Kingdom -- 100140/Wellcome Trust/United Kingdom -- New York, N.Y. -- Science. 2015 May 29;348(6238):1027-30. doi: 10.1126/science.aaa6986. Epub 2015 Apr 9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉University of Cambridge, Cambridge Institute for Medical Research (CIMR), the Wellcome Trust MRC Institute of Metabolic Science and NIHR Cambridge Biomedical Research Centre, Cambridge CB2 0XY, UK. dr360@medschl.cam.ac.uk ys412@cam.ac.uk. ; University of Cambridge, Cambridge Institute for Medical Research (CIMR), the Wellcome Trust MRC Institute of Metabolic Science and NIHR Cambridge Biomedical Research Centre, Cambridge CB2 0XY, UK. ; Division of Medicinal Chemistry and Structural Biology, School of Pharmacy, Centre for Biomolecular Sciences, University of Nottingham, Nottingham NG7 2RD, UK.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/25858979" target="_blank"〉PubMed〈/a〉
    Keywords: Acetamides/*pharmacology ; Animals ; CHO Cells ; Caspase 9 ; Clustered Regularly Interspaced Short Palindromic Repeats/genetics ; Cricetulus ; Cyclohexylamines/*pharmacology ; Drug Resistance/*genetics ; Eukaryotic Initiation Factor-2/*metabolism ; Eukaryotic Initiation Factor-2B/*genetics/metabolism ; Genetic Testing ; Memory/*drug effects ; Mutation, Missense ; Nootropic Agents/*pharmacology ; Protein Biosynthesis/drug effects ; Unfolded Protein Response/*drug effects/immunology
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 10
    Publication Date: 2013-07-16
    Description: Selenocysteine (Sec) is translationally incorporated into proteins in response to the UGA codon. The tRNA specific to Sec (tRNA Sec ) is first ligated with serine by seryl-tRNA synthetase (SerRS). In the present study, we determined the 3.1 Å crystal structure of the tRNA Sec from the bacterium Aquifex aeolicus , in complex with the heterologous SerRS from the archaeon Methanopyrus kandleri . The bacterial tRNA Sec assumes the L-shaped structure, from which the long extra arm protrudes. Although the D-arm conformation and the extra-arm orientation are similar to those of eukaryal/archaeal tRNA Sec s, A. aeolicus tRNA Sec has unique base triples, G14:C21:U8 and C15:G20a:G48, which occupy the positions corresponding to the U8:A14 and R15:Y48 tertiary base pairs of canonical tRNAs. Methanopyrus kandleri SerRS exhibited serine ligation activity toward A. aeolicus tRNA Sec in vitro . The SerRS N-terminal domain interacts with the extra-arm stem and the outer corner of tRNA Sec . Similar interactions exist in the reported tRNA Ser and SerRS complex structure from the bacterium Thermus thermophilus . Although the catalytic C-terminal domain of M. kandleri SerRS lacks interactions with A. aeolicus tRNA Sec in the present complex structure, the conformational flexibility of SerRS is likely to allow the CCA terminal region of tRNA Sec to enter the SerRS catalytic site.
    Print ISSN: 0305-1048
    Electronic ISSN: 1362-4962
    Topics: Biology
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