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Wyszukujesz frazę ""Dohmae, Naoshi"" wg kryterium: Autor


Tytuł:
Comparative proteomic analysis of glomerular proteins in IgA nephropathy and IgA vasculitis with nephritis.
Autorzy:
Kaga H; Department of Hematology, Nephrology, and Rheumatology, Akita University Graduate School of Medicine, Akita, Japan.
Matsumura H; Department of Life Science, Graduate School of Engineering Science, Akita University, Akita, Japan. .
Saito A; Department of Hematology, Nephrology, and Rheumatology, Akita University Graduate School of Medicine, Akita, Japan.
Saito M; Department of Hematology, Nephrology, and Rheumatology, Akita University Graduate School of Medicine, Akita, Japan.
Abe F; Department of Hematology, Nephrology, and Rheumatology, Akita University Graduate School of Medicine, Akita, Japan.
Suzuki T; Biomolecular Characterization Unit, RIKEN Center for Sustainable Resource Science, Wako, Japan.
Dohmae N; Biomolecular Characterization Unit, RIKEN Center for Sustainable Resource Science, Wako, Japan.
Odaka M; Department of Life Science, Graduate School of Engineering Science, Akita University, Akita, Japan.
Komatsuda A; Department of Internal Medicine, Ogachi Central Hospital, Yuzawa, Japan.
Wakui H; Emeritus Professor, Akita University, Akita, Japan.
Takahashi N; Department of Hematology, Nephrology, and Rheumatology, Akita University Graduate School of Medicine, Akita, Japan.
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Źródło:
Clinical proteomics [Clin Proteomics] 2023 May 13; Vol. 20 (1), pp. 21. Date of Electronic Publication: 2023 May 13.
Typ publikacji:
Journal Article
Czasopismo naukowe
Tytuł:
C-mannosylation regulates stabilization of RAMP1 protein and RAMP1-mediated cell migration.
Autorzy:
Mizuta H; Department of Applied Chemistry, Faculty of Science and Technology, Keio University, Yokohama, Japan.
Takakusaki A; Department of Applied Chemistry, Faculty of Science and Technology, Keio University, Yokohama, Japan.
Suzuki T; Biomolecular Characterization Unit, RIKEN Center for Sustainable Resource Science, Wako, Japan.
Otake K; Department of Applied Chemistry, Faculty of Science and Technology, Keio University, Yokohama, Japan.
Dohmae N; Biomolecular Characterization Unit, RIKEN Center for Sustainable Resource Science, Wako, Japan.
Simizu S; Department of Applied Chemistry, Faculty of Science and Technology, Keio University, Yokohama, Japan.
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Źródło:
The FEBS journal [FEBS J] 2023 Jan; Vol. 290 (1), pp. 196-208. Date of Electronic Publication: 2022 Aug 17.
Typ publikacji:
Journal Article; Research Support, Non-U.S. Gov't
MeSH Terms:
Thrombospondins*
Receptors, Cytokine*
Glycosylation ; Cell Membrane ; Cell Movement
Czasopismo naukowe
Tytuł:
Comparative proteomic analysis of glomerular proteins in primary and bucillamine-induced membranous nephropathy.
Autorzy:
Kaga H; Department of Hematology, Nephrology, and Rheumatology, Akita University Graduate School of Medicine, Akita, Japan.
Matsumura H; Department of Life Science, Graduate School of Engineering Science, Akita University, 1-1 Tegatagakuen-machi, Akita City, Akita, 010-8502, Japan. .
Suzuki T; Biomolecular Characterization Unit, RIKEN Center for Sustainable Research Science, Wako, Japan.
Dohmae N; Biomolecular Characterization Unit, RIKEN Center for Sustainable Research Science, Wako, Japan.
Odaka M; Department of Life Science, Graduate School of Engineering Science, Akita University, 1-1 Tegatagakuen-machi, Akita City, Akita, 010-8502, Japan.
Komatsuda A; Department of Internal Medicine, Ogachi Central Hospital, Yuzawa, Japan.
Takahashi N; Department of Hematology, Nephrology, and Rheumatology, Akita University Graduate School of Medicine, Akita, Japan.
Wakui H; Department of Life Science, Graduate School of Engineering Science, Akita University, 1-1 Tegatagakuen-machi, Akita City, Akita, 010-8502, Japan.
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Źródło:
Clinical proteomics [Clin Proteomics] 2022 Jul 14; Vol. 19 (1), pp. 26. Date of Electronic Publication: 2022 Jul 14.
Typ publikacji:
Journal Article
Czasopismo naukowe
Tytuł:
Mammalian HEMK1 methylates glutamine residue of the GGQ motif of mitochondrial release factors.
Autorzy:
Fang Q; Cellular Memory Laboratory, RIKEN Cluster for Pioneering Research, RIKEN, Wako, Saitama, 351-0198, Japan.; Graduate School of Science and Engineering, Saitama University, Saitama, 338-8570, Japan.
Kimura Y; RNA Systems Biochemistry Laboratory, RIKEN Cluster for Pioneering Research, Wako, Saitama, 351-0198, Japan.; Department of Computational Biology and Medical Sciences, Graduate School of Frontier Sciences, The University of Tokyo, Kashiwa, Chiba, 277-8561, Japan.
Shimazu T; Cellular Memory Laboratory, RIKEN Cluster for Pioneering Research, RIKEN, Wako, Saitama, 351-0198, Japan.
Suzuki T; Biomolecular Characterization Unit, Technology Platform Division, RIKEN Center for Sustainable Resource Science, Wako, Saitama, 351-0198, Japan.
Yamada A; Cellular Memory Laboratory, RIKEN Cluster for Pioneering Research, RIKEN, Wako, Saitama, 351-0198, Japan.
Dohmae N; Biomolecular Characterization Unit, Technology Platform Division, RIKEN Center for Sustainable Resource Science, Wako, Saitama, 351-0198, Japan.
Iwasaki S; RNA Systems Biochemistry Laboratory, RIKEN Cluster for Pioneering Research, Wako, Saitama, 351-0198, Japan.; Department of Computational Biology and Medical Sciences, Graduate School of Frontier Sciences, The University of Tokyo, Kashiwa, Chiba, 277-8561, Japan.
Shinkai Y; Cellular Memory Laboratory, RIKEN Cluster for Pioneering Research, RIKEN, Wako, Saitama, 351-0198, Japan. .; Graduate School of Science and Engineering, Saitama University, Saitama, 338-8570, Japan. .
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Źródło:
Scientific reports [Sci Rep] 2022 Mar 08; Vol. 12 (1), pp. 4104. Date of Electronic Publication: 2022 Mar 08.
Typ publikacji:
Journal Article; Research Support, Non-U.S. Gov't
MeSH Terms:
Glutamine*/metabolism
Peptide Termination Factors*/metabolism
Animals ; Humans ; Amino Acid Motifs ; HeLa Cells ; Mammals/metabolism ; Mitochondrial Proteins/genetics ; Mitochondrial Proteins/metabolism
Czasopismo naukowe
Tytuł:
Clathrin adapters AP-1 and GGA2 support expression of epidermal growth factor receptor for cell growth.
Autorzy:
Uemura T; Department of Anatomy and Histology, Fukushima Medical University School of Medicine, 1 Hikarigaoka, Fukushima, Fukushima, 960-1295, Japan.
Suzuki T; Biomolecular Characterization Unit, RIKEN Center for Sustainable Resource Science, 2-1 Hirosawa, Wako, Saitama, 351-0198, Japan.
Dohmae N; Biomolecular Characterization Unit, RIKEN Center for Sustainable Resource Science, 2-1 Hirosawa, Wako, Saitama, 351-0198, Japan.
Waguri S; Department of Anatomy and Histology, Fukushima Medical University School of Medicine, 1 Hikarigaoka, Fukushima, Fukushima, 960-1295, Japan. .
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Źródło:
Oncogenesis [Oncogenesis] 2021 Nov 19; Vol. 10 (11), pp. 80. Date of Electronic Publication: 2021 Nov 19.
Typ publikacji:
Journal Article
Czasopismo naukowe
Tytuł:
Discovery of a small protein-encoding cis-regulatory overlapping gene of the tumor suppressor gene Scribble in humans.
Autorzy:
Nomura Y; Biomolecular Characterization Unit, RIKEN Center for Sustainable Resource Science, 2-1 Hirosawa, Wako, Saitama, 351-0198, Japan. .
Dohmae N; Biomolecular Characterization Unit, RIKEN Center for Sustainable Resource Science, 2-1 Hirosawa, Wako, Saitama, 351-0198, Japan. dohmae@riken.jp.
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Źródło:
Communications biology [Commun Biol] 2021 Sep 17; Vol. 4 (1), pp. 1098. Date of Electronic Publication: 2021 Sep 17.
Typ publikacji:
Journal Article
MeSH Terms:
Membrane Proteins/*genetics
Open Reading Frames/*genetics
Tumor Suppressor Proteins/*genetics
Cell Line, Tumor ; Humans ; Membrane Proteins/metabolism ; Tumor Suppressor Proteins/metabolism
Czasopismo naukowe
Tytuł:
Regulation of mammalian 3D genome organization and histone H3K9 dimethylation by H3K9 methyltransferases.
Autorzy:
Fukuda K; Cellular Memory Laboratory, RIKEN Cluster for Pioneering Research, Wako, Japan. .
Shimura C; Cellular Memory Laboratory, RIKEN Cluster for Pioneering Research, Wako, Japan.
Miura H; Laboratory for Developmental Epigenetics, RIKEN Center for Biosystems Dynamics Research, Kobe, Japan.
Tanigawa A; Laboratory for Developmental Epigenetics, RIKEN Center for Biosystems Dynamics Research, Kobe, Japan.
Suzuki T; Biomolecular Characterization Unit, Technology Platform Division, RIKEN Center for Sustainable Resource Science, Wako, Japan.
Dohmae N; Biomolecular Characterization Unit, Technology Platform Division, RIKEN Center for Sustainable Resource Science, Wako, Japan.
Hiratani I; Laboratory for Developmental Epigenetics, RIKEN Center for Biosystems Dynamics Research, Kobe, Japan.
Shinkai Y; Cellular Memory Laboratory, RIKEN Cluster for Pioneering Research, Wako, Japan. .
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Źródło:
Communications biology [Commun Biol] 2021 May 13; Vol. 4 (1), pp. 571. Date of Electronic Publication: 2021 May 13.
Typ publikacji:
Journal Article; Research Support, Non-U.S. Gov't
MeSH Terms:
DNA Methylation*
Chromatin/*metabolism
Fibroblasts/*metabolism
Histone-Lysine N-Methyltransferase/*metabolism
Histones/*metabolism
Lysine/*metabolism
Mouse Embryonic Stem Cells/*metabolism
Animals ; Chromatin/chemistry ; Chromatin/genetics ; Fibroblasts/cytology ; Genome ; Histone-Lysine N-Methyltransferase/genetics ; Histones/chemistry ; Histones/genetics ; Lysine/chemistry ; Lysine/genetics ; Mice ; Mouse Embryonic Stem Cells/cytology
Czasopismo naukowe
Tytuł:
The role of transcriptional repressor activity of LexA in salt-stress responses of the cyanobacterium Synechocystis sp. PCC 6803.
Autorzy:
Takashima K; Graduate School of Science and Engineering, Saitama University, 255 Shimo-Okubo, Saitama, 338-8570, Japan.
Nagao S; Graduate School of Science and Engineering, Saitama University, 255 Shimo-Okubo, Saitama, 338-8570, Japan.
Kizawa A; Graduate School of Science and Engineering, Saitama University, 255 Shimo-Okubo, Saitama, 338-8570, Japan.; Department of Biological Sciences, Faculty of Science and Engineering, Chuo University, 1-13-27 Kasuga, Bunkyo-ku, Tokyo, 112-8551, Japan.
Suzuki T; Biomolecular Characterization Unit, RIKEN Center for Sustainable Resource Science, 2-1 Hirosawa, Wako, Saitama, 351-0198, Japan.
Dohmae N; Biomolecular Characterization Unit, RIKEN Center for Sustainable Resource Science, 2-1 Hirosawa, Wako, Saitama, 351-0198, Japan.
Hihara Y; Graduate School of Science and Engineering, Saitama University, 255 Shimo-Okubo, Saitama, 338-8570, Japan. .
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Źródło:
Scientific reports [Sci Rep] 2020 Oct 15; Vol. 10 (1), pp. 17393. Date of Electronic Publication: 2020 Oct 15.
Typ publikacji:
Journal Article; Research Support, Non-U.S. Gov't
MeSH Terms:
Bacterial Proteins/*physiology
Repressor Proteins/*physiology
Salt Stress/*physiology
Serine Endopeptidases/*physiology
Synechocystis/*physiology
Genes, Bacterial ; Promoter Regions, Genetic ; Protein Processing, Post-Translational ; Sequence Analysis, RNA/methods ; Synechocystis/genetics
Czasopismo naukowe
Tytuł:
Genetic incorporation of non-canonical amino acid photocrosslinkers in Neisseria meningitidis: New method provides insights into the physiological function of the function-unknown NMB1345 protein.
Autorzy:
Takahashi H; National Institute of Infectious Diseases, Department of Bacteriology I, Shinjuku-ku, Japan.
Dohmae N; Biomolecular Characterization Unit, RIKEN Center for Sustainable Resource Science, Wako, Japan.
Kim KS; Division of Pediatric Infectious Diseases, Department of Pediatrics, School of Medicine, Johns Hopkins University, Baltimore, Maryland, United States of America.
Shimuta K; National Institute of Infectious Diseases, Department of Bacteriology I, Shinjuku-ku, Japan.
Ohnishi M; National Institute of Infectious Diseases, Department of Bacteriology I, Shinjuku-ku, Japan.
Yokoyama S; RIKEN Structural Biology Laboratory, Yokohama, Japan.; RIKEN Cluster for Science, Technology and Innovation Hub, Yokohama, Japan.
Yanagisawa T; RIKEN Structural Biology Laboratory, Yokohama, Japan.; RIKEN Cluster for Science, Technology and Innovation Hub, Yokohama, Japan.
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Źródło:
PloS one [PLoS One] 2020 Aug 31; Vol. 15 (8), pp. e0237883. Date of Electronic Publication: 2020 Aug 31 (Print Publication: 2020).
Typ publikacji:
Journal Article; Research Support, Non-U.S. Gov't
MeSH Terms:
Light*
Amino Acids/*genetics
Cross-Linking Reagents/*metabolism
Neisseria meningitidis/*genetics
Bacterial Proteins/genetics ; Bacterial Proteins/isolation & purification ; Brain/blood supply ; Endocytosis ; Endothelial Cells/microbiology ; Fimbriae, Bacterial/metabolism ; Humans ; Microvessels/pathology ; Mutation/genetics ; Plasmids/genetics
Czasopismo naukowe
Tytuł:
Author Correction: A spatial similarity of stereochemical environments formed by amino acid residues defines a common epitope of two non-homologous proteins.
Autorzy:
Nakashima K; Institute of Neuroscience, Tokushima Bunri University, Kagawa, 769-2193, Japan. .
Iwashita S; Institute of Neuroscience, Tokushima Bunri University, Kagawa, 769-2193, Japan. .; Department of Pharmacy, Iwaki Meisei University, Fukushima, 970-8551, Japan. .
Suzuki T; Biomolecular Characterization Unit, RIKEN Center for Sustainable Resource Science, Saitama, 351-0198, Japan.
Kato C; Institute of Neuroscience, Tokushima Bunri University, Kagawa, 769-2193, Japan.
Kohno T; Department of Biochemistry, Kitasato University School of Medicine, Kanagawa, 242-0374, Japan.
Kamei Y; Laboratory of Molecular Nutrition, Graduate School of Environmental and Life Science, Kyoto Prefectural University, Kyoto, 606-0823, Japan.
Sasaki M; Department of Basic Veterinary Medicine, Obihiro University of Agriculture and Veterinary Medicine, Hokkaido, 080-8555, Japan.
Urayama O; Faculty of Health Sciences, Tsukuba International University, Ibaraki, 300-0051, Japan.
Ohno-Iwashita Y; Department of Pharmacy, Iwaki Meisei University, Fukushima, 970-8551, Japan.
Dohmae N; Biomolecular Characterization Unit, RIKEN Center for Sustainable Resource Science, Saitama, 351-0198, Japan.
Song SY; Institute of Neuroscience, Tokushima Bunri University, Kagawa, 769-2193, Japan. .
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Źródło:
Scientific reports [Sci Rep] 2020 Jul 01; Vol. 10 (1), pp. 11091. Date of Electronic Publication: 2020 Jul 01.
Typ publikacji:
Published Erratum
Tytuł:
Cryo-EM structure of the volume-regulated anion channel LRRC8D isoform identifies features important for substrate permeation.
Autorzy:
Nakamura R; Department of Biological Sciences, Graduate School of Science, The University of Tokyo, 7-3-1 Hongo, Bunkyo-ku, Tokyo, Japan.
Numata T; Department of Physiology, Graduate School of Medical Sciences, Fukuoka University, 7-45-1 Nanakuma, Johnan-ku, Fukuoka, Japan.
Kasuya G; Division of Integrative Physiology, Department of Physiology, Jichi Medical University, 3311-1 Yakushiji, Shimotsuke-shi, Tochigi, Japan. .
Yokoyama T; Laboratory for Protein Functional and Structural Biology, RIKEN Center for Biosystems Dynamics Research, 1-7-22 Suehiro-cho, Tsurumi-ku, Yokohama-shi, Kanagawa, Japan.
Nishizawa T; Department of Biological Sciences, Graduate School of Science, The University of Tokyo, 7-3-1 Hongo, Bunkyo-ku, Tokyo, Japan.
Kusakizako T; Department of Biological Sciences, Graduate School of Science, The University of Tokyo, 7-3-1 Hongo, Bunkyo-ku, Tokyo, Japan.
Kato T; Department of Biological Sciences, Graduate School of Science, The University of Tokyo, 7-3-1 Hongo, Bunkyo-ku, Tokyo, Japan.
Hagino T; Department of Biological Sciences, Graduate School of Science, The University of Tokyo, 7-3-1 Hongo, Bunkyo-ku, Tokyo, Japan.
Dohmae N; Biomolecular Characterization Unit, RIKEN Center for Sustainable Resource Science, 2-1 Hirosawa, Wako-shi, Saitama, Japan.
Inoue M; Laboratory of Cell Signaling, Graduate School of Pharmaceutical Sciences, The University of Tokyo, 7-3-1 Hongo, Bunkyo-ku, Tokyo, Japan.
Watanabe K; Laboratory of Cell Signaling, Graduate School of Pharmaceutical Sciences, The University of Tokyo, 7-3-1 Hongo, Bunkyo-ku, Tokyo, Japan.
Ichijo H; Laboratory of Cell Signaling, Graduate School of Pharmaceutical Sciences, The University of Tokyo, 7-3-1 Hongo, Bunkyo-ku, Tokyo, Japan.
Kikkawa M; Department of Cell Biology and Anatomy, Graduate School of Medicine, The University of Tokyo, 7-3-1 Hongo, Bunkyo-ku, Tokyo, Japan.
Shirouzu M; Laboratory for Protein Functional and Structural Biology, RIKEN Center for Biosystems Dynamics Research, 1-7-22 Suehiro-cho, Tsurumi-ku, Yokohama-shi, Kanagawa, Japan.
Jentsch TJ; Physiology and Pathology of Ion Transport, Leibniz-Forschungsinstitut für Molekulare Pharmakologie (FMP) and Max-Delbrück-Centrum für Molekulare Medizin, D-13125, Berlin, Germany.
Ishitani R; Department of Biological Sciences, Graduate School of Science, The University of Tokyo, 7-3-1 Hongo, Bunkyo-ku, Tokyo, Japan.
Okada Y; Department of Molecular Cell Physiology, Kyoto Prefectural University of Medicine, Kyoto, Japan. .; Department of Cell Physiology, National Institute for Physiological Sciences, Okazaki, Japan. .
Nureki O; Department of Biological Sciences, Graduate School of Science, The University of Tokyo, 7-3-1 Hongo, Bunkyo-ku, Tokyo, Japan. .
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Źródło:
Communications biology [Commun Biol] 2020 May 15; Vol. 3 (1), pp. 240. Date of Electronic Publication: 2020 May 15.
Typ publikacji:
Journal Article; Research Support, Non-U.S. Gov't
MeSH Terms:
Signal Transduction*
Ion Transport/*physiology
Cryoelectron Microscopy ; Protein Domains ; Protein Isoforms/chemistry ; Protein Isoforms/ultrastructure ; Voltage-Dependent Anion Channels/chemistry ; Voltage-Dependent Anion Channels/ultrastructure
Czasopismo naukowe
Tytuł:
Structure of a cyanobacterial photosystem I surrounded by octadecameric IsiA antenna proteins.
Autorzy:
Akita F; Research Institute for Interdisciplinary Science and Graduate School of Natural Science and Technology, Okayama University, Okayama, 700-8530, Japan. fusamichi_.; Japan Science and Technology Agency, PRESTO, Saitama, 332-0012, Japan. fusamichi_.
Nagao R; Research Institute for Interdisciplinary Science and Graduate School of Natural Science and Technology, Okayama University, Okayama, 700-8530, Japan.
Kato K; Research Institute for Interdisciplinary Science and Graduate School of Natural Science and Technology, Okayama University, Okayama, 700-8530, Japan.
Nakajima Y; Research Institute for Interdisciplinary Science and Graduate School of Natural Science and Technology, Okayama University, Okayama, 700-8530, Japan.
Yokono M; Nippon Flour Mills Co., Ltd., Innovation Center, Kanagawa, 243-0041, Japan.
Ueno Y; Graduate School of Science, Kobe University, Hyogo, 657-8501, Japan.
Suzuki T; Biomolecular Characterization Unit, RIKEN Center for Sustainable Resource Science, Saitama, 351-0198, Japan.
Dohmae N; Biomolecular Characterization Unit, RIKEN Center for Sustainable Resource Science, Saitama, 351-0198, Japan.
Shen JR; Research Institute for Interdisciplinary Science and Graduate School of Natural Science and Technology, Okayama University, Okayama, 700-8530, Japan. .
Akimoto S; Graduate School of Science, Kobe University, Hyogo, 657-8501, Japan. .
Miyazaki N; Life Science Center for Survival Dynamics, Tsukuba Advanced Research Alliance (TARA), University of Tsukuba, Ibaraki, 305-8577, Japan. .; Institute for Protein Research, Osaka University, Osaka, 565-0871, Japan. .
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Źródło:
Communications biology [Commun Biol] 2020 May 11; Vol. 3 (1), pp. 232. Date of Electronic Publication: 2020 May 11.
Typ publikacji:
Journal Article; Research Support, Non-U.S. Gov't
MeSH Terms:
Bacterial Proteins/*genetics
Light-Harvesting Protein Complexes/*genetics
Photosystem I Protein Complex/*genetics
Bacterial Proteins/chemistry ; Bacterial Proteins/metabolism ; Light-Harvesting Protein Complexes/chemistry ; Light-Harvesting Protein Complexes/metabolism ; Photosystem I Protein Complex/chemistry ; Photosystem I Protein Complex/metabolism ; Thermosynechococcus/genetics ; Thermosynechococcus/metabolism
SCR Organism:
Thermosynechococcus vulcanus
Czasopismo naukowe
Tytuł:
Protein Arginine N -methyltransferases 5 and 7 Promote HIV-1 Production.
Autorzy:
Murakami H; Viral Infectious Disease Unit, RIKEN, 2-1 Hirosawa, Wako, Saitama 351-0198, Japan.; Laboratory of Animal Health II, School of Veterinary Medicine, Azabu University, 1-17-71 Fuchinobe, Chuo-ku, Sagamihara, Kanagawa 252-5201, Japan.
Suzuki T; Biomolecular Characterization Unit, RIKEN CSRS, 2-1 Hirosawa, Wako, Saitama 351-0198, Japan.
Tsuchiya K; AIDS Clinical Center, National Center for Global Health and Medicine, 1-21-1 Toyama, Shinjuku-ku, Tokyo 162-8655, Japan.
Gatanaga H; AIDS Clinical Center, National Center for Global Health and Medicine, 1-21-1 Toyama, Shinjuku-ku, Tokyo 162-8655, Japan.
Taura M; Division of Hematopoiesis, Joint Research Center for Human Retrovirus Infection, Kumamoto University, 2-2-1 Honjo, Chuo-ku, Kumamoto 860-0811, Japan.
Kudo E; Division of Hematopoiesis, Joint Research Center for Human Retrovirus Infection, Kumamoto University, 2-2-1 Honjo, Chuo-ku, Kumamoto 860-0811, Japan.
Okada S; Division of Hematopoiesis, Joint Research Center for Human Retrovirus Infection, Kumamoto University, 2-2-1 Honjo, Chuo-ku, Kumamoto 860-0811, Japan.
Takei M; Viral Infectious Disease Unit, RIKEN, 2-1 Hirosawa, Wako, Saitama 351-0198, Japan.; Nakamura Laboratory, Baton Zone Program, RIKEN Cluster for Science, Technology and Innovation Hub, 2-1 Hirosawa, Wako, Saitama 351-0198, Japan.; Nihon University School of Medicine, 30-1 Oyaguchi, Itabashi, Tokyo 173-8610, Japan.
Kuroda K; Nihon University School of Medicine, 30-1 Oyaguchi, Itabashi, Tokyo 173-8610, Japan.
Yamamoto T; Nihon University School of Medicine, 30-1 Oyaguchi, Itabashi, Tokyo 173-8610, Japan.
Hagiwara K; Viral Infectious Disease Unit, RIKEN, 2-1 Hirosawa, Wako, Saitama 351-0198, Japan.
Dohmae N; AIDS Clinical Center, National Center for Global Health and Medicine, 1-21-1 Toyama, Shinjuku-ku, Tokyo 162-8655, Japan.
Aida Y; Viral Infectious Disease Unit, RIKEN, 2-1 Hirosawa, Wako, Saitama 351-0198, Japan.; Nakamura Laboratory, Baton Zone Program, RIKEN Cluster for Science, Technology and Innovation Hub, 2-1 Hirosawa, Wako, Saitama 351-0198, Japan.; Nihon University School of Medicine, 30-1 Oyaguchi, Itabashi, Tokyo 173-8610, Japan.
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Źródło:
Viruses [Viruses] 2020 Mar 23; Vol. 12 (3). Date of Electronic Publication: 2020 Mar 23.
Typ publikacji:
Journal Article; Research Support, Non-U.S. Gov't
MeSH Terms:
Host-Pathogen Interactions*
Virus Replication*
HIV Infections/*metabolism
HIV Infections/*virology
HIV-1/*physiology
Protein-Arginine N-Methyltransferases/*metabolism
Amino Acid Sequence ; Carrier Proteins ; Cell Line ; Cells, Cultured ; Gene Knockdown Techniques ; Humans ; Macrophages/virology ; Protein Binding ; Protein-Arginine N-Methyltransferases/chemistry ; vpr Gene Products, Human Immunodeficiency Virus/metabolism
Czasopismo naukowe
Tytuł:
Three YXXL Sequences of a Bovine Leukemia Virus Transmembrane Protein are Independently Required for Fusion Activity by Controlling Expression on the Cell Membrane.
Autorzy:
Matsuura R; Viral Infectious Diseases Unit, RIKEN, 2-1 Hirosawa, Wako, Saitama 351-0198, Japan.; Biomolecular Characterization Unit, RIKEN Center for Sustainable Resource Science, 2-1 Hirosawa, Wako, Saitama 351-0198, Japan.; Laboratory of Viral Infectious Diseases, Department of Computational Biology and Medical Sciences, Graduate School of Frontier Sciences, The University of Tokyo, 2-1 Hirosawa, Wako, Saitama 351-0198, Japan.
Inabe K; Viral Infectious Diseases Unit, RIKEN, 2-1 Hirosawa, Wako, Saitama 351-0198, Japan.
Otsuki H; Viral Infectious Diseases Unit, RIKEN, 2-1 Hirosawa, Wako, Saitama 351-0198, Japan.
Kurokawa K; Live Cell Super-Resolution Imaging Research Team, RIKEN Center for Advanced Photonics, 2-1 Hirosawa, Wako, Saitama 351-0198, Japan.
Dohmae N; Biomolecular Characterization Unit, RIKEN Center for Sustainable Resource Science, 2-1 Hirosawa, Wako, Saitama 351-0198, Japan.
Aida Y; Viral Infectious Diseases Unit, RIKEN, 2-1 Hirosawa, Wako, Saitama 351-0198, Japan.; Laboratory of Viral Infectious Diseases, Department of Computational Biology and Medical Sciences, Graduate School of Frontier Sciences, The University of Tokyo, 2-1 Hirosawa, Wako, Saitama 351-0198, Japan.; Nakamura Laboratory, Baton Zone program, Riken Cluster for Science, Technology and Innovation Hub, 2-1 Hirosawa, Wako, Saitama 351-0198, Japan.
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Źródło:
Viruses [Viruses] 2019 Dec 10; Vol. 11 (12). Date of Electronic Publication: 2019 Dec 10.
Typ publikacji:
Journal Article; Research Support, Non-U.S. Gov't
MeSH Terms:
Amino Acid Motifs*
Host-Pathogen Interactions*
Membrane Fusion*
Cell Membrane/*metabolism
Cell Membrane/*virology
Leukemia Virus, Bovine/*physiology
Viral Envelope Proteins/*genetics
Viral Envelope Proteins/*metabolism
Amino Acid Sequence ; Animals ; Cattle ; Cell Line ; Cells, Cultured ; Fluorescent Antibody Technique ; Gene Expression ; Humans ; Mutation ; Protein Transport ; Viral Envelope Proteins/chemistry ; Virus Attachment ; Virus Release
Czasopismo naukowe
Tytuł:
Structural basis for oligomerization of the prokaryotic peptide transporter PepT So2 .
Autorzy:
Nagamura R; Department of Biological Sciences, Graduate School of Science, The University of Tokyo, 7-3-1 Hongo, Bunkyo-ku, Tokyo 113-0033, Japan.
Fukuda M; Department of Biological Sciences, Graduate School of Science, The University of Tokyo, 7-3-1 Hongo, Bunkyo-ku, Tokyo 113-0033, Japan.
Kawamoto A; Institute for Protein Research, Osaka University, 3-2 Yamadaoka, Suita, Osaka 565-0871, Japan.
Matoba K; Institute for Protein Research, Osaka University, 3-2 Yamadaoka, Suita, Osaka 565-0871, Japan.
Dohmae N; RIKEN Advanced Science Institute, 2-1 Hirosawa, Wako-shi, Saitama 351-0198, Japan.
Ishitani R; Department of Biological Sciences, Graduate School of Science, The University of Tokyo, 7-3-1 Hongo, Bunkyo-ku, Tokyo 113-0033, Japan.
Takagi J; Institute for Protein Research, Osaka University, 3-2 Yamadaoka, Suita, Osaka 565-0871, Japan.
Nureki O; Department of Biological Sciences, Graduate School of Science, The University of Tokyo, 7-3-1 Hongo, Bunkyo-ku, Tokyo 113-0033, Japan.
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Źródło:
Acta crystallographica. Section F, Structural biology communications [Acta Crystallogr F Struct Biol Commun] 2019 May 01; Vol. 75 (Pt 5), pp. 348-358. Date of Electronic Publication: 2019 Apr 24.
Typ publikacji:
Journal Article
MeSH Terms:
Bacterial Proteins/*chemistry
Carrier Proteins/*chemistry
Shewanella/*chemistry
Amino Acid Sequence ; Bacterial Proteins/genetics ; Bacterial Proteins/metabolism ; Binding Sites ; Carrier Proteins/genetics ; Carrier Proteins/metabolism ; Cloning, Molecular ; Cryoelectron Microscopy ; Crystallography, X-Ray ; Escherichia coli/genetics ; Escherichia coli/metabolism ; Gene Expression ; Genetic Vectors/chemistry ; Genetic Vectors/metabolism ; Models, Molecular ; Protein Binding ; Protein Conformation, alpha-Helical ; Protein Conformation, beta-Strand ; Protein Interaction Domains and Motifs ; Protein Multimerization ; Recombinant Fusion Proteins/chemistry ; Recombinant Fusion Proteins/genetics ; Recombinant Fusion Proteins/metabolism ; Shewanella/metabolism ; Substrate Specificity
Czasopismo naukowe
Tytuł:
Tri-methylation of ATF7IP by G9a/GLP recruits the chromodomain protein MPP8.
Autorzy:
Tsusaka T; Cellular Memory Laboratory, RIKEN Cluster for Pioneering Research, Wako, 351-0198, Japan.; Department of Diabetes, Endocrinology and Nutrition, Graduate School of Medicine, Kyoto University, Kyoto, 606-8507, Japan.
Kikuchi M; Laboratory for Epigenetics Drug Discovery, RIKEN Center for Biosystems Dynamics Research, Yokohama, 230-0045, Japan.
Shimazu T; Cellular Memory Laboratory, RIKEN Cluster for Pioneering Research, Wako, 351-0198, Japan.
Suzuki T; Biomolecular Characterization Unit, Technology Platform Division, RIKEN Center for Sustainable Resource Science, Wako, 351-0198, Japan.
Sohtome Y; Synthetic Organic Chemistry Laboratory, RIKEN Cluster for Pioneering Research, Wako, 351-0198, Japan.; RIKEN Center for Sustainable Resource Science, Wako, 351-0198, Japan.
Akakabe M; Synthetic Organic Chemistry Laboratory, RIKEN Cluster for Pioneering Research, Wako, 351-0198, Japan.; RIKEN Center for Sustainable Resource Science, Wako, 351-0198, Japan.
Sodeoka M; Synthetic Organic Chemistry Laboratory, RIKEN Cluster for Pioneering Research, Wako, 351-0198, Japan.; RIKEN Center for Sustainable Resource Science, Wako, 351-0198, Japan.
Dohmae N; Biomolecular Characterization Unit, Technology Platform Division, RIKEN Center for Sustainable Resource Science, Wako, 351-0198, Japan.
Umehara T; Laboratory for Epigenetics Drug Discovery, RIKEN Center for Biosystems Dynamics Research, Yokohama, 230-0045, Japan.
Shinkai Y; Cellular Memory Laboratory, RIKEN Cluster for Pioneering Research, Wako, 351-0198, Japan. .
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Źródło:
Epigenetics & chromatin [Epigenetics Chromatin] 2018 Oct 04; Vol. 11 (1), pp. 56. Date of Electronic Publication: 2018 Oct 04.
Typ publikacji:
Journal Article; Research Support, Non-U.S. Gov't
MeSH Terms:
Protein Processing, Post-Translational*
Histone-Lysine N-Methyltransferase/*metabolism
Phosphoproteins/*metabolism
Repressor Proteins/*metabolism
Animals ; Cells, Cultured ; Embryonic Stem Cells/metabolism ; HEK293 Cells ; Humans ; Methylation ; Mice
Czasopismo naukowe
Tytuł:
Novel function of HATs and HDACs in homologous recombination through acetylation of human RAD52 at double-strand break sites.
Autorzy:
Yasuda T; Research Center for Radiation Emergency Medicine, National Institute of Radiological Sciences (NIRS), Anagawa, Inage-ku, Chiba, Japan.
Kagawa W; Program in Chemistry and Life Science, Department of Interdisciplinary Science and Engineering, School of Science and Engineering, Meisei University, Hodokubo, Hino-shi, Tokyo, Japan.
Ogi T; Department of Genetics, Research Institute of Environmental Medicine, Nagoya University, Furo-cho, Chikusa-ku, Nagoya, Japan.
Kato TA; Department of Environmental and Radiological Health Sciences, Colorado State University, Fort Collins, CO, United States of America.
Suzuki T; Biomolecular Characterization Unit, RIKEN Center for Sustainable Resource Science, Hirosawa, Wako, Saitama, Japan.
Dohmae N; Biomolecular Characterization Unit, RIKEN Center for Sustainable Resource Science, Hirosawa, Wako, Saitama, Japan.
Takizawa K; Research Center for Radiation Emergency Medicine, National Institute of Radiological Sciences (NIRS), Anagawa, Inage-ku, Chiba, Japan.
Nakazawa Y; Department of Genetics, Research Institute of Environmental Medicine, Nagoya University, Furo-cho, Chikusa-ku, Nagoya, Japan.; Department of Genome Repair, Atomic Bomb Disease Institute, Nagasaki University, Sakamoto, Nagasaki, Japan.
Genet MD; Department of Environmental and Radiological Health Sciences, Colorado State University, Fort Collins, CO, United States of America.
Saotome M; Program in Chemistry and Life Science, Department of Interdisciplinary Science and Engineering, School of Science and Engineering, Meisei University, Hodokubo, Hino-shi, Tokyo, Japan.
Hama M; Department of Basic Medical Sciences for Radiation Damage, NIRS, National Institutes for Quantum and Radiation Sciences and Technology (QST), Anagawa, Inage-ku, Chiba, Japan.
Konishi T; Department of Basic Medical Sciences for Radiation Damage, NIRS, National Institutes for Quantum and Radiation Sciences and Technology (QST), Anagawa, Inage-ku, Chiba, Japan.
Nakajima NI; Research Center for Charged Particle Therapy, NIRS, Anagawa, Inage-ku, Chiba, Japan.
Hazawa M; Research Center for Radiation Emergency Medicine, National Institute of Radiological Sciences (NIRS), Anagawa, Inage-ku, Chiba, Japan.; Cell-Bionomics Research Unit, Innovative Integrated Bio-Research Core, Institute for Frontier Science Initiative, Kanazawa University, Kakuma-machi, Kanazawa, Japan.
Tomita M; Radiation Safety Research Center, Nuclear Technology Research Laboratory, Central Research Institute of Electric Power Industry, Iwado Kita, Komae-shi, Tokyo, Japan.
Koike M; Research Center for Radiation Protection, NIRS, 4-9-1 Anagawa, Inage-ku, Chiba, Japan.
Noshiro K; Research Center for Radiation Emergency Medicine, National Institute of Radiological Sciences (NIRS), Anagawa, Inage-ku, Chiba, Japan.
Tomiyama K; Research Center for Radiation Emergency Medicine, National Institute of Radiological Sciences (NIRS), Anagawa, Inage-ku, Chiba, Japan.
Obara C; Research Center for Radiation Emergency Medicine, National Institute of Radiological Sciences (NIRS), Anagawa, Inage-ku, Chiba, Japan.
Gotoh T; Research Center for Radiation Emergency Medicine, National Institute of Radiological Sciences (NIRS), Anagawa, Inage-ku, Chiba, Japan.
Ui A; Genome regulation and Molecular pharmacogenomics, School of Bioscience and Biotechnology, Tokyo University of Technology, Katakuramachi, Hachioji City, Tokyo, Japan.
Fujimori A; Research Center for Charged Particle Therapy, NIRS, Anagawa, Inage-ku, Chiba, Japan.; International Open Laboratory (IOL), NIRS, Anagawa, Inage-ku, Chiba, Japan.
Nakayama F; Department of Basic Medical Sciences for Radiation Damage, NIRS, National Institutes for Quantum and Radiation Sciences and Technology (QST), Anagawa, Inage-ku, Chiba, Japan.
Hanaoka F; Faculty of Science, Gakushuin University, Mejiro, Toshima-ku, Tokyo, Japan.
Sugasawa K; Biosignal Research Center, and Graduate School of Science, Kobe University, Rokkodai-cho, Nada-ku, Kobe, Japan.
Okayasu R; International Open Laboratory (IOL), NIRS, Anagawa, Inage-ku, Chiba, Japan.
Jeggo PA; International Open Laboratory (IOL), NIRS, Anagawa, Inage-ku, Chiba, Japan.; Genome Damage and Stability Centre, University of Sussex, Brighton, United Kingdom.
Tajima K; Research Center for Radiation Emergency Medicine, National Institute of Radiological Sciences (NIRS), Anagawa, Inage-ku, Chiba, Japan.
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Źródło:
PLoS genetics [PLoS Genet] 2018 Mar 28; Vol. 14 (3), pp. e1007277. Date of Electronic Publication: 2018 Mar 28 (Print Publication: 2018).
Typ publikacji:
Journal Article; Research Support, Non-U.S. Gov't
MeSH Terms:
DNA Breaks, Double-Stranded*
Homologous Recombination*
Histone Acetyltransferases/*physiology
Histone Deacetylases/*physiology
Rad52 DNA Repair and Recombination Protein/*metabolism
Acetylation ; Ataxia Telangiectasia Mutated Proteins/metabolism ; Histone Acetyltransferases/genetics ; Histone Deacetylases/genetics ; Humans ; Microscopy, Fluorescence ; Two-Hybrid System Techniques
Czasopismo naukowe
Tytuł:
Topological analysis of DPY19L3, a human C-mannosyltransferase.
Autorzy:
Niwa Y; Department of Applied Chemistry, Faculty of Science and Technology, Keio University, Yokohama, Japan.
Nakano Y; Department of Applied Chemistry, Faculty of Science and Technology, Keio University, Yokohama, Japan.
Suzuki T; Biomolecular Characterization Unit, RIKEN Center for Sustainable Resource Science, Wako, Japan.
Yamagishi M; Department of Applied Chemistry, Faculty of Science and Technology, Keio University, Yokohama, Japan.
Otani K; Department of Applied Chemistry, Faculty of Science and Technology, Keio University, Yokohama, Japan.
Dohmae N; Biomolecular Characterization Unit, RIKEN Center for Sustainable Resource Science, Wako, Japan.
Simizu S; Department of Applied Chemistry, Faculty of Science and Technology, Keio University, Yokohama, Japan.
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Źródło:
The FEBS journal [FEBS J] 2018 Mar; Vol. 285 (6), pp. 1162-1174. Date of Electronic Publication: 2018 Feb 16.
Typ publikacji:
Journal Article; Research Support, Non-U.S. Gov't
MeSH Terms:
Asparagine/*metabolism
Endoplasmic Reticulum/*metabolism
Mannosyltransferases/*metabolism
Membrane Proteins/*metabolism
Amino Acid Sequence ; Asparagine/chemistry ; Asparagine/genetics ; Binding Sites/genetics ; Computer Simulation ; Glycosylation ; HEK293 Cells ; Humans ; Mannose/metabolism ; Mannosyltransferases/chemistry ; Mannosyltransferases/genetics ; Membrane Proteins/chemistry ; Membrane Proteins/genetics ; Mutation ; Protein Domains ; Sequence Homology, Amino Acid
Czasopismo naukowe
Tytuł:
Dpy-19 like 3-mediated C -mannosylation and expression levels of RPE-spondin in human tumor cell lines.
Autorzy:
Morishita S; Department of Applied Chemistry, Faculty of Science and Technology, Keio University, Yokohama, Kanagawa 223-8522, Japan.
Suzuki T; Biomolecular Characterization Unit, RIKEN Center for Sustainable Resource Science, Wako, Saitama 351-0198, Japan.
Niwa Y; Department of Applied Chemistry, Faculty of Science and Technology, Keio University, Yokohama, Kanagawa 223-8522, Japan.
Dohmae N; Biomolecular Characterization Unit, RIKEN Center for Sustainable Resource Science, Wako, Saitama 351-0198, Japan.
Simizu S; Department of Applied Chemistry, Faculty of Science and Technology, Keio University, Yokohama, Kanagawa 223-8522, Japan.
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Źródło:
Oncology letters [Oncol Lett] 2017 Aug; Vol. 14 (2), pp. 2537-2544. Date of Electronic Publication: 2017 Jun 22.
Typ publikacji:
Journal Article
Czasopismo naukowe
Tytuł:
Protein lysine methyltransferase SMYD3 is involved in tumorigenesis through regulation of HER2 homodimerization.
Autorzy:
Yoshioka Y; Section of Hematology/Oncology, Department of Medicine, The University of Chicago, 5841 S. Maryland Ave, MC2115, Chicago, Illinois, 60637.; Department of Surgical Oncology, Graduate School of Medicine, The University of Tokyo, 7-3-1 Hongo, Bunkyo-ku, Tokyo, 113-8654, Japan.
Suzuki T; Biomolecular Characterization Unit, RIKEN Center for Sustainable Resource Science, 2-1 Hirosawa, Wako, Saitama, 351-0198, Japan.
Matsuo Y; OncoTherapy Science Inc., 3-2-1 Sakado, Takatsu-ku, Kawasaki, Kanagawa, 213-0012, Japan.
Tsurita G; Department of Surgery, IMSUT Hospital, Institute of Medical Science, The University of Tokyo, 4-6-1 Shirokanedai, Minato-ku, Tokyo, 108-8639, Japan.
Watanabe T; Department of Surgical Oncology, Graduate School of Medicine, The University of Tokyo, 7-3-1 Hongo, Bunkyo-ku, Tokyo, 113-8654, Japan.
Dohmae N; Biomolecular Characterization Unit, RIKEN Center for Sustainable Resource Science, 2-1 Hirosawa, Wako, Saitama, 351-0198, Japan.
Nakamura Y; Section of Hematology/Oncology, Department of Medicine, The University of Chicago, 5841 S. Maryland Ave, MC2115, Chicago, Illinois, 60637.; Department of Surgery, The University of Chicago, 5841 S. Maryland Ave, MC2115, Chicago, Illinois, 60637.
Hamamoto R; Section of Hematology/Oncology, Department of Medicine, The University of Chicago, 5841 S. Maryland Ave, MC2115, Chicago, Illinois, 60637.
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Źródło:
Cancer medicine [Cancer Med] 2017 Jul; Vol. 6 (7), pp. 1665-1672. Date of Electronic Publication: 2017 Jun 22.
Typ publikacji:
Journal Article
MeSH Terms:
Protein Multimerization*
Cell Transformation, Neoplastic/*metabolism
Histone-Lysine N-Methyltransferase/*metabolism
Receptor, ErbB-2/*metabolism
Cell Line, Tumor ; Cell Transformation, Neoplastic/genetics ; Gene Expression ; Gene Expression Regulation, Neoplastic ; Gene Knockdown Techniques ; Histone-Lysine N-Methyltransferase/chemistry ; Histone-Lysine N-Methyltransferase/genetics ; Humans ; Methylation ; Microsatellite Repeats ; Phosphorylation ; Polymorphism, Genetic ; Protein Binding ; RNA Interference ; RNA, Small Interfering/genetics ; Receptor, ErbB-2/chemistry ; Receptor, ErbB-2/genetics ; Recombinant Fusion Proteins/metabolism
Czasopismo naukowe

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