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  • 1
    Publication Date: 2016-04-12
    Description: The control of magnetic Skyrmions confined in a nanometer scale disk using electric field pulses is studied by micromagnetic simulation. A stable Skyrmion can be created and annihilated by an electric field pulse depending on the polarity of the electric field. Moreover, the core direction of the Skyrmion can be switched using the same electric field pulses. Such creation and annihilation of Skyrmions, and its core switching do not require any magnetic field and precise control of the pulse length. This unconventional manipulation of magnetic texture using electric field pulses allows a robust way of controlling magnetic Skyrmions in nanodiscs, a path toward building ultralow power memory devices.
    Print ISSN: 0003-6951
    Electronic ISSN: 1077-3118
    Topics: Physics
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  • 2
    Publication Date: 2016-04-01
    Description: The dynamics of a magnetic domain wall (DW) under a transverse magnetic field H y are investigated in two-dimensional (2D) Co/Ni microstrips, where an interfacial Dzyaloshinskii-Moriya interaction (DMI) exists with DMI vector D lying in + y direction. The DW velocity exhibits asymmetric behavior for ± H y ; that is, the DW velocity becomes faster when H y is applied antiparallel to D . The key experimental results are reproduced in a 2D micromagnetic simulation, which reveals that the interfacial DMI suppresses the periodic change of the average DW angle φ even above the Walker breakdown and that H y changes φ , resulting in a velocity asymmetry. This suggests that the 2D DW motion, despite its microscopic complexity, simply depends on the average angle of the DW and thus can be described using a one-dimensional soliton model. These findings provide insight into the magnetic DW dynamics in 2D systems, which are important for emerging spin-orbitronic applications.
    Electronic ISSN: 2166-532X
    Topics: Mechanical Engineering, Materials Science, Production Engineering, Mining and Metallurgy, Traffic Engineering, Precision Mechanics
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  • 3
    Publication Date: 2003-04-12
    Description: Rapid turnover of the tumor suppressor protein p53 requires the MDM2 ubiquitin ligase, and both interact with p300-CREB-binding protein transcriptional coactivator proteins. p53 is stabilized by the binding of p300 to the oncoprotein E1A, suggesting that p300 regulates p53 degradation. Purified p300 exhibited intrinsic ubiquitin ligase activity that was inhibited by E1A. In vitro, p300 with MDM2 catalyzed p53 polyubiquitination, whereas MDM2 catalyzed p53 monoubiquitination. E1A expression caused a decrease in polyubiquitinated but not monoubiquitinated p53 in cells. Thus, generation of the polyubiquitinated forms of p53 that are targeted for proteasome degradation requires the intrinsic ubiquitin ligase activities of MDM2 and p300.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Grossman, Steven R -- Deato, Maria E -- Brignone, Chrystelle -- Chan, Ho Man -- Kung, Andrew L -- Tagami, Hideaki -- Nakatani, Yoshihiro -- Livingston, David M -- CA15751/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 2003 Apr 11;300(5617):342-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Cancer Biology, Dana-Farber Cancer Institute, Boston, MA 02115, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12690203" target="_blank"〉PubMed〈/a〉
    Keywords: Adenovirus E1A Proteins/metabolism ; Animals ; Catalysis ; Cells, Cultured ; E1A-Associated p300 Protein ; Embryo, Mammalian ; Fibroblasts/metabolism ; Humans ; Ligases/antagonists & inhibitors/metabolism ; Mice ; Nuclear Proteins/antagonists & inhibitors/*metabolism ; Proto-Oncogene Proteins/metabolism ; Proto-Oncogene Proteins c-mdm2 ; Recombinant Fusion Proteins/metabolism ; Recombinant Proteins/metabolism ; Trans-Activators/antagonists & inhibitors/*metabolism ; Transfection ; Tumor Cells, Cultured ; Tumor Suppressor Protein p53/*metabolism ; Ubiquitin-Protein Ligases ; Ubiquitins/*metabolism
    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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  • 4
    Publication Date: 2018-09-29
    Description: Author(s): H. Aratani, Y. Nakatani, H. Fujiwara, M. Kawada, Y. Kanai, K. Yamagami, S. Fujioka, S. Hamamoto, K. Kuga, T. Kiss, A. Yamasaki, A. Higashiya, T. Kadono, S. Imada, A. Tanaka, K. Tamasaku, M. Yabashi, T. Ishikawa, A. Yasui, Y. Saitoh, Y. Narumi, K. Kindo, T. Ebihara, and A. Sekiyama We present a detailed study on the 4 f ground-state symmetry of the pressure-induced superconductor CeCu 2 Ge 2 probed by soft x-ray absorption and hard x-ray photoemission spectroscopy. The revised Ce 4 f ground states are determined as | Γ 7 〉 = 0.45 | J z = ± 5 2 〉 − 0.55 | ∓ 3 2 〉 with Σ -type in-plane rotational symmetr... [Phys. Rev. B 98, 121113(R)] Published Fri Sep 28, 2018
    Keywords: Electronic structure and strongly correlated systems
    Print ISSN: 1098-0121
    Electronic ISSN: 1095-3795
    Topics: Physics
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  • 5
    Publication Date: 2008-09-27
    Description: Conventional semiconductor devices use electric fields to control conductivity, a scalar quantity, for information processing. In magnetic materials, the direction of magnetization, a vector quantity, is of fundamental importance. In magnetic data storage, magnetization is manipulated with a current-generated magnetic field (Oersted-Ampere field), and spin current is being studied for use in non-volatile magnetic memories. To make control of magnetization fully compatible with semiconductor devices, it is highly desirable to control magnetization using electric fields. Conventionally, this is achieved by means of magnetostriction produced by mechanically generated strain through the use of piezoelectricity. Multiferroics have been widely studied in an alternative approach where ferroelectricity is combined with ferromagnetism. Magnetic-field control of electric polarization has been reported in these multiferroics using the magnetoelectric effect, but the inverse effect-direct electrical control of magnetization-has not so far been observed. Here we show that the manipulation of magnetization can be achieved solely by electric fields in a ferromagnetic semiconductor, (Ga,Mn)As. The magnetic anisotropy, which determines the magnetization direction, depends on the charge carrier (hole) concentration in (Ga,Mn)As. By applying an electric field using a metal-insulator-semiconductor structure, the hole concentration and, thereby, the magnetic anisotropy can be controlled, allowing manipulation of the magnetization direction.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Chiba, D -- Sawicki, M -- Nishitani, Y -- Nakatani, Y -- Matsukura, F -- Ohno, H -- England -- Nature. 2008 Sep 25;455(7212):515-8. doi: 10.1038/nature07318.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Semiconductor Spintronics Project, Exploratory Research for Advanced Technology, Japan Science and Technology Agency, Sanban-cho 5, Chiyoda-ku, Tokyo 102-0075, Japan.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/18818654" 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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  • 6
    Publication Date: 2008-12-17
    Description: Might DNA sequence variation reflect germline genetic activity and underlying chromatin structure? We investigated this question using medaka (Japanese killifish, Oryzias latipes), by comparing the genomic sequences of two strains (Hd-rR and HNI) and by mapping approximately 37.3 million nucleosome cores from Hd-rR blastulae and 11,654 representative transcription start sites from six embryonic stages. We observed a distinctive approximately 200-base pair (bp) periodic pattern of genetic variation downstream of transcription start sites; the rate of insertions and deletions longer than 1 bp peaked at positions of approximately +200, +400, and +600 bp, whereas the point mutation rate showed corresponding valleys. This approximately 200-bp periodicity was correlated with the chromatin structure, with nucleosome occupancy minimized at positions 0, +200, +400, and +600 bp. These data exemplify the potential for genetic activity (transcription) and chromatin structure to contribute to molding the DNA sequence on an evolutionary time scale.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2757552/" 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/PMC2757552/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Sasaki, Shin -- Mello, Cecilia C -- Shimada, Atsuko -- Nakatani, Yoichiro -- Hashimoto, Shin-Ichi -- Ogawa, Masako -- Matsushima, Kouji -- Gu, Sam Guoping -- Kasahara, Masahiro -- Ahsan, Budrul -- Sasaki, Atsushi -- Saito, Taro -- Suzuki, Yutaka -- Sugano, Sumio -- Kohara, Yuji -- Takeda, Hiroyuki -- Fire, Andrew -- Morishita, Shinichi -- R01 GM037706/GM/NIGMS NIH HHS/ -- R01 GM037706-24/GM/NIGMS NIH HHS/ -- R01 GM37706/GM/NIGMS NIH HHS/ -- T32 CA009151/CA/NCI NIH HHS/ -- T32 CA09151/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 2009 Jan 16;323(5912):401-4. doi: 10.1126/science.1163183. Epub 2008 Dec 11.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Computational Biology, Graduate School of Frontier Sciences, University of Tokyo, Kashiwa, 277-0882, Japan.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/19074313" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Composition ; Base Sequence ; Chromatin/*physiology/ultrastructure ; DNA/chemistry/*genetics ; DNA Repair ; *Genetic Variation ; Genome ; INDEL Mutation ; Mutagenesis ; Mutation ; Nucleosomes/*physiology/ultrastructure ; Oryzias/embryology/*genetics ; Point Mutation ; Promoter Regions, Genetic ; *Transcription Initiation Site ; 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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  • 7
    Publication Date: 1993-07-23
    Description: Transcription initiation factor TFIIB recruits RNA polymerase II to the promoter subsequent to interaction with a preformed TFIID-promoter complex. The domains of TFIIB required for binding to the TFIID-promoter complex and for transcription initiation have been determined. The carboxyl-terminal two-thirds of TFIIB, which contains two direct repeats and two basic residue repeats, is sufficient for interaction with the TFIID-promoter complex. An extra 84-residue amino-terminal region, with no obvious known structural motifs, is required for basal transcription activity. Basic residues within the second basic repeat of TFIIB are necessary for stable interaction with the TFIID-promoter complex, whereas the basic character of the first basic repeat is not. Functional roles of other potential structural motifs are discussed in light of the present study.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Yamashita, S -- Hisatake, K -- Kokubo, T -- Doi, K -- Roeder, R G -- Horikoshi, M -- Nakatani, Y -- AI27397/AI/NIAID NIH HHS/ -- CA42567/CA/NCI NIH HHS/ -- GM45258/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1993 Jul 23;261(5120):463-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉National Institute of Neurological Diseases and Stroke, National Institutes of Health, Bethesda, MD 20892.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8332911" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Binding Sites ; DNA-Binding Proteins/*metabolism ; Drosophila ; Molecular Sequence Data ; Mutation ; *Promoter Regions, Genetic ; Protein Binding ; Transcription Factor TFIIB ; Transcription Factor TFIID ; Transcription Factors/*chemistry/*metabolism
    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: 2002-05-11
    Description: E2F-6 contributes to gene silencing in a manner independent of retinoblastoma protein family members. To better elucidate the molecular mechanism of repression by E2F-6, we have purified the factor from cultured cells. E2F-6 is found in a multimeric protein complex that contains Mga and Max, and thus the complex can bind not only to the E2F-binding site but also to Myc- and Brachyury-binding sites. Moreover, the complex contains chromatin modifiers such as a novel histone methyltransferase that modifies lysine 9 of histone H3, HP1gamma, and Polycomb group (PcG) proteins. The E2F-6 complex preferentially occupies target promoters in G0 cells rather than in G1 cells. These data suggest that these chromatin modifiers contribute to silencing of E2F- and Myc-responsive genes in quiescent cells.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ogawa, Hidesato -- Ishiguro, Kei-Ichiro -- Gaubatz, Stefan -- Livingston, David M -- Nakatani, Yoshihiro -- New York, N.Y. -- Science. 2002 May 10;296(5570):1132-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Dana-Farber Cancer Institute and Harvard Medical School, Boston, MA 02115, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12004135" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Binding Sites ; *Cell Cycle Proteins ; Chromatin/*metabolism ; Chromosomal Proteins, Non-Histone/metabolism ; *DNA-Binding Proteins ; Dimerization ; E2F Transcription Factors ; E2F6 Transcription Factor ; *G0 Phase ; G1 Phase ; *Gene Silencing ; HeLa Cells ; *Histone-Lysine N-Methyltransferase ; Histones/metabolism ; Humans ; Mass Spectrometry ; Methylation ; Methyltransferases/chemistry/metabolism ; Molecular Sequence Data ; Phosphoproteins/metabolism ; *Promoter Regions, Genetic ; Protein Footprinting ; Protein Methyltransferases ; *Proteins ; Proto-Oncogene Proteins c-myc/metabolism ; Recombinant Proteins/metabolism ; Retinoblastoma-Like Protein p130 ; Transcription Factors/chemistry/isolation & purification/*metabolism ; *Transcription, Genetic ; Two-Hybrid System Techniques
    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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  • 9
    Publication Date: 2013-06-05
    Description: Author(s): A. L. Gonzalez Oyarce, Y. Nakatani, and C. H. W. Barnes We study the static and dynamic behavior of transverse domain walls and 360 ∘ domain walls in a thin film of isotropic material including pinning effects caused by geometric defects in the form of triangular antinotches. In terms of the static interaction, our model reduces the domain walls to source... [Phys. Rev. B 87, 214403] Published Tue Jun 04, 2013
    Keywords: Magnetism
    Print ISSN: 1098-0121
    Electronic ISSN: 1095-3795
    Topics: Physics
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  • 10
    Publication Date: 2016-09-03
    Description: Author(s): A. Yamasaki, H. Fujiwara, S. Tachibana, D. Iwasaki, Y. Higashino, C. Yoshimi, K. Nakagawa, Y. Nakatani, K. Yamagami, H. Aratani, O. Kirilmaz, M. Sing, R. Claessen, H. Watanabe, T. Shirakawa, S. Yunoki, A. Naitoh, K. Takase, J. Matsuno, H. Takagi, A. Sekiyama, and Y. Saitoh In this study, we systematically investigate three-dimensional (3D) momentum ( ℏ k )-resolved electronic structures of Ruddlesden-Popper-type iridium oxides Sr n + 1 Ir n O 3 n + 1 using soft-x-ray (SX) angle-resolved photoemission spectroscopy (ARPES). Our results provide direct evidence of an insulator-to-meta… [Phys. Rev. B 94, 115103] Published Fri Sep 02, 2016
    Keywords: Electronic structure and strongly correlated systems
    Print ISSN: 1098-0121
    Electronic ISSN: 1095-3795
    Topics: Physics
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