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1. Full Text Molecular mechanism of the Mg2+ channel MgtE
by Nureki, O
ACTA CRYSTALLOGRAPHICA A-FOUNDATION AND ADVANCES, ISSN 2053-2733, 2017, Volume 73, Issue a2, pp. C151 - C151
X-ray crystallography | channel | Patch clamp method | CRYSTALLOGRAPHY | CHEMISTRY, MULTIDISCIPLINARY
Conference Proceeding
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2. Full Text Structural insights into the competitive inhibition of the ATP-gated P2X receptor channel
by Kasuya, Go and Yamaura, Toshiaki and Ma, Xiao-Bo and Nakamura, Ryoki and Takemoto, Mizuki and Nagumo, Hiromitsu and Tanaka, Eiichi and Dohmae, Naoshi and Nakane, Takanori and Yu, Ye and Ishitani, Ryuichiro and Matsuzaki, Osamu and Hattori, Motoyuki and Nureki, Osamu
Nature Communications, ISSN 2041-1723, 12/2017, Volume 8, Issue 1, pp. 876 - 10
P2X receptors are non-selective cation channels gated by extracellular ATP, and the P2X7 receptor subtype plays a crucial role in the immune and nervous... 
EXTRACELLULAR ATP | P-2X RECEPTOR | MOLECULAR-DYNAMICS | DESENSITIZATION | MULTIDISCIPLINARY SCIENCES | EQUILIBRIUM | INVOLVEMENT | ION-CHANNEL | PURINERGIC RECEPTOR | MEMBRANE-PROTEINS | BINDING | Hypertension | Competition | Electrophysiology | Arthritis | Channels | Receptors | Computation | Rheumatoid arthritis | Computer applications | Cations | Inhibition | Mutation | ATP | Crystal structure | Conformation | Structure-function relationships | Index Medicus
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3. Full Text Structural basis for dynamic mechanism of proton-coupled symport by the peptide transporter POT
by Shintaro Doki and Hideaki E. Kato and Nicolae Solean and Masayo Iwaki and Michio Koyama and Motoyuki Hattori and Norihiko Iwase and Tomoya Tsukazaki and Yuji Sugita and Hideki Kandori and Simon Newstead and Ryuichiro Ishitani and Osamu Nureki
Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, 7/2013, Volume 110, Issue 28, pp. 11343 - 11348
Proton-dependent oligopeptide transporters (POTs) are major facilitator super-family (MFS) proteins that mediate the uptake of peptides and peptide-like... 
Proteins | Biochemical mechanisms | Hydrogen bonds | Counterflow | Ions | Functional analysis | Sulfates | Binding sites | Carboxylates | Crystal structure | X-ray crystallography | Membrane transporter | Molecular dynamics simulation | CRYSTAL-STRUCTURE | MULTIDISCIPLINARY SCIENCES | molecular dynamics simulation | ESCHERICHIA-COLI | LACY | FAMILY | LACTOSE PERMEASE | SUBSTRATE | membrane transporter | ALTERNATING ACCESS | BETA-LACTAM ANTIBIOTICS | HUMAN DIPEPTIDE TRANSPORTER | OLIGOPEPTIDE TRANSPORTER | Protons | Alanine - analogs & derivatives | Carrier Proteins - metabolism | Peptides - metabolism | Models, Molecular | Alanine - metabolism | Carrier Proteins - chemistry | Protein Conformation | Ion Transport | Molecular Dynamics Simulation | Peptides | Carrier proteins | Drug interactions | Physiological aspects | Dosage and administration | Research | Structure | Statins | Molecules | Membranes | Small intestine | Index Medicus | Biological Sciences
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4. Full Text Genome-scale transcriptional activation by an engineered CRISPR-Cas9 complex
by Konermann, Silvana and Brigham, Mark D and Trevino, Alexandro E and Joung, Julia and Abudayyeh, Omar O and Barcena, Clea and Hsu, Patrick D and Habib, Naomi and Gootenberg, Jonathan S and Nishimasu, Hiroshi and Nureki, Osamu and Zhang, Feng
Nature, ISSN 0028-0836, 01/2015, Volume 517, Issue 7536, pp. 583 - 588
Systematic interrogation of gene function requires the ability to perturb gene expression in a robust and generalizable manner. Here we describe... 
RAF INHIBITION | MELANOMA | RNA | PATHWAY | HUMAN-CELLS | MULTIDISCIPLINARY SCIENCES | RESISTANCE | PROTEIN-COUPLED RECEPTORS | TARGET DNA | CAS9 | CANCER | Transcriptional Activation - genetics | Genetic Testing | RNA, Untranslated - metabolism | Humans | DNA, Complementary - genetics | Genetic Loci - genetics | RNA, Untranslated - genetics | Melanoma - genetics | DNA, Complementary - biosynthesis | Indoles - pharmacology | Clustered Regularly Interspaced Short Palindromic Repeats - genetics | Gene Expression Regulation, Neoplastic - genetics | Genetic Engineering - methods | Reproducibility of Results | Gene Library | CRISPR-Associated Proteins - genetics | Up-Regulation - genetics | Sulfonamides - pharmacology | CRISPR-Cas Systems - genetics | Genome, Human - genetics | Proto-Oncogene Proteins B-raf - antagonists & inhibitors | Drug Resistance, Neoplasm - genetics | RNA, Untranslated - biosynthesis | CRISPR-Associated Proteins - metabolism | Melanoma - drug therapy | Cell Line, Tumor | Drug Resistance, Neoplasm - drug effects | Enzymes | Nucleotide sequence | Genetic research | Genomes | Genetic aspects | Genetic engineering | Genetic transcription | Research | Proteins | Transcription factors | Genomics | Melanoma | Epigenetics | Drug resistance | Gene expression | Crystal structure | Index Medicus
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5. Full Text Crystal structure of a claudin provides insight into the architecture of tight junctions
by Suzuki, Hiroshi and Nishizawa, Tomohiro and Tani, Kazutoshi and Yamazaki, Yuji and Tamura, Atsushi and Ishitani, Ryuichiro and Dohmae, Naoshi and Tsukita, Sachiko and Nureki, Osamu and Fujiyoshi, Yoshinori
Science, ISSN 0036-8075, 2014, Volume 344, Issue 6181, pp. 304 - 307
Tight junctions are cell-cell adhesion structures in epithelial cell sheets that surround organ compartments in multicellular organisms and regulate the... 
TRANSPORT | STRANDS | MULTIDISCIPLINARY SCIENCES | OCCLUDIN | CHANNELS | MUTATIONS | MEMBRANE-PROTEINS | Protein Structure, Tertiary | Amino Acid Sequence | Protein Structure, Secondary | Models, Molecular | Molecular Sequence Data | Crystallography, X-Ray | Static Electricity | Protein Folding | Amino Acid Motifs | Tight Junctions - chemistry | Tight Junctions - physiology | Animals | Claudins - chemistry | Protein Conformation | Mice | Protein Subunits - chemistry | Junctional complexes (Epithelium) | Cell research | Cell adhesion | Crystals | Cell junctions | Physiological aspects | Research | Structure | Homeowners | Cells | Crystal structure | Cell adhesion & migration | Index Medicus
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6. Full Text Engineered Cpf1 variants with altered PAM specificities
by Gao, Linyi and Cox, David B T and Yan, Winston X and Manteiga, John C and Schneider, Martin W and Yamano, Takashi and Nishimasu, Hiroshi and Nureki, Osamu and Crosetto, Nicola and Zhang, Feng
Nature Biotechnology, ISSN 1087-0156, 08/2017, Volume 35, Issue 8, pp. 789 - 792
The RNA-guided endonuclease Cpf1 is a promising tool for genome editing in eukaryotic cells1-7. However, the utility of the commonly used Acidaminococcus sp.... 
RNA-GUIDED ENDONUCLEASE | CAS9 | RECOGNITION | CRISPR-CAS9 NUCLEASES | BIOTECHNOLOGY & APPLIED MICROBIOLOGY | HUMAN-CELLS | Genetic Engineering - methods | Endonucleases - genetics | Humans | Bacterial Proteins - genetics | HEK293 Cells | Mutagenesis, Site-Directed - methods | Acidaminococcus - genetics | Genetic Variation - genetics | Acidaminococcus - enzymology | Nucleotide sequencing | Observations | Genetic variation | Methods | DNA sequencing | Eukaryotes | Mutagenesis | Tissue engineering | Editing | Genomes | Mutation | Endonuclease | Ribonucleic acid--RNA | In vitro methods and tests | Deoxyribonucleic acid--DNA | Index Medicus
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7. Full Text Light-induced structural changes and the site of O=O bond formation in PSII caught by XFEL
by Suga, Michihiro and Akita, Fusamichi and Sugahara, Michihiro and Kubo, Minoru and Nakajima, Yoshiki and Nakane, Takanori and Yamashita, Keitaro and Umena, Yasufumi and Nakabayashi, Makoto and Yamane, Takahiro and Nakano, Takamitsu and Suzuki, Mamoru and Masuda, Tetsuya and Inoue, Shigeyuki and Kimura, Tetsunari and Nomura, Takashi and Yonekura, Shinichiro and Yu, Long-Jiang and Sakamoto, Tomohiro and Motomura, Taiki and Chen, Jing-Hua and Kato, Yuki and Noguchi, Takumi and Tono, Kensuke and Joti, Yasumasa and Kameshima, Takashi and Hatsui, Takaki and Nango, Eriko and Tanaka, Rie and Naitow, Hisashi and Matsuura, Yoshinori and Yamashita, Ayumi and Yamamoto, Masaki and Nureki, Osamu and Yabashi, Makina and Ishikawa, Tetsuya and Iwata, So and Shen, Jian-Ren
Nature, ISSN 0028-0836, 03/2017, Volume 543, Issue 7643, pp. 131 - 135
Photosystem II (PSII) is a huge membrane-protein complex consisting of 20 different subunits with a total molecular mass of 350 kDa for a monomer. It catalyses... 
OXYGEN-EVOLVING COMPLEX | ROOM-TEMPERATURE | PROTON RELEASE | MECHANISM | MULTIDISCIPLINARY SCIENCES | PHOTOSYSTEM-II | X-RAY-DIFFRACTION | PHOTOSYNTHETIC WATER OXIDATION | INFRARED-SPECTROSCOPY | OXIDIZING COMPLEX | S-STATE TRANSITIONS | Protons | Temperature | Nonheme Iron Proteins - metabolism | Electron Transport - radiation effects | Cyanobacteria - chemistry | Crystallography - methods | Oxygen - metabolism | Fourier Analysis | Time Factors | Lasers | Light | Oxygen - chemistry | Water - chemistry | Nonheme Iron Proteins - chemistry | Biocatalysis - radiation effects | Water - metabolism | Models, Molecular | Nonheme Iron Proteins - radiation effects | Manganese - chemistry | Photosystem II Protein Complex - metabolism | Manganese - metabolism | Photosystem II Protein Complex - radiation effects | Photosystem II Protein Complex - chemistry | Oxygen - radiation effects | Electrons | Chemical bonds | Physiological aspects | Photosystem II | Structure | Photosynthesis research | Membrane proteins | Datasets | Ligands | Fourier transforms | Binding sites | Index Medicus
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8. Full Text Crystal structure of the channelrhodopsin light-gated cation channel
by Kato, Hideaki E and Zhang, Feng and Yizhar, Ofer and Ramakrishnan, Charu and Nishizawa, Tomohiro and Hirata, Kunio and Ito, Jumpei and Aita, Yusuke and Tsukazaki, Tomoya and Hayashi, Shigehiko and Hegemann, Peter and Maturana, Andrés D and Ishitani, Ryuichiro and Deisseroth, Karl and Nureki, Osamu
Nature, ISSN 0028-0836, 02/2012, Volume 482, Issue 7385, pp. 369 - 374
Channelrhodopsins (ChRs) are light-gated cation channels derived from algae that have shown experimental utility in optogenetics; for example, neurons... 
OPTICAL CONTROL | ACTIVATION | PROTEIN | HALOBACTERIUM-HALOBIUM | OPTOGENETICS | MULTIDISCIPLINARY SCIENCES | PHOTOCYCLE | GREEN-ALGAE | RHODOPSIN | BACTERIORHODOPSIN | EXCITABLE CELLS | Cations - metabolism | Ion Channel Gating - radiation effects | Ion Channels - genetics | Crystallography, X-Ray | Retinaldehyde - metabolism | Rhodopsin - radiation effects | Chlamydomonas reinhardtii - genetics | Cattle | Recombinant Fusion Proteins - radiation effects | Light | Binding Sites | Ion Channels - chemistry | Rhodopsin - chemistry | Models, Molecular | Recombinant Fusion Proteins - chemistry | Static Electricity | Chlamydomonas reinhardtii - chemistry | Animals | Rhodopsin - genetics | Schiff Bases - chemistry | Recombinant Fusion Proteins - genetics | Protein Conformation | Ion Channels - radiation effects | Mutation | Bacteriorhodopsins - chemistry | Design | Proteins | Signal transduction | Amino acids | Index Medicus
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9. Full Text Real-space and real-Time dynamics of CRISPR-Cas9 visualized by high-speed atomic force microscopy
by Shibata, Mikihiro and Nishimasu, Hiroshi and Kodera, Noriyuki and Hirano, Seiichi and Ando, Toshio and Uchihashi, Takayuki and Nureki, Osamu
Nature Communications, ISSN 2041-1723, 12/2017, Volume 8, Issue 1, pp. 1430 - 9
The CRISPR-associated endonuclease Cas9 binds to a guide RNA and cleaves double-stranded DNA with a sequence complementary to the RNA guide. The Cas9-RNA... 
IMMUNITY | COMPLEX | ENDONUCLEASE | RNA | CRYSTAL-STRUCTURE | MULTIDISCIPLINARY SCIENCES | INTERROGATION | SYSTEMS | CAS9 | CLEAVAGE | TARGET DNA RECOGNITION | Atomic force microscopy | CRISPR | Nucleotide sequence | Double-stranded RNA | Genomes | Real time | Ribonucleic acid--RNA | Microscopy | High speed | Cleavage | Nuclease | Endonuclease | Atomic structure | Deoxyribonucleic acid--DNA | Conformation | Index Medicus
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10. Full Text Crystal structure of autotaxin and insight into GPCR activation by lipid mediators
by Okudaira, Shinichi and Hama, Kotaro and Aoki, Junken and Nishimasu, Hiroshi and Dohmae, Naoshi and Mihara, Emiko and Nureki, Osamu and Takagi, Junichi and Inoue, Asuka and Ishitani, Ryuichiro
Nature Structural & Molecular Biology, ISSN 1545-9993, 02/2011, Volume 18, Issue 2, pp. 205 - 212
Autotaxin (ATX, also known as Enpp2) is a secreted lysophospholipase D that hydrolyzes lysophosphatidylcholine to generate lysophosphatidic acid (LPA), a lipid... 
DOMAIN | CELL MOTILITY | BIOCHEMISTRY & MOLECULAR BIOLOGY | IDENTIFICATION | CELL BIOLOGY | SECRETED LYSOPHOSPHOLIPASE-D | NUCLEOTIDE PYROPHOSPHATASES/PHOSPHODIESTERASES | BIOPHYSICS | LYSOPHOSPHATIDIC ACID | PHOSPHODIESTERASE | CATALYTIC SITE | EXPRESSION | BLOOD | Amino Acid Sequence | Cell Line | Lysophospholipids - metabolism | Receptors, G-Protein-Coupled - metabolism | Lysophospholipids - chemistry | Humans | Models, Molecular | Molecular Sequence Data | Multienzyme Complexes - metabolism | Substrate Specificity | Crystallography, X-Ray | Pyrophosphatases - chemistry | Phosphodiesterase I - chemistry | Multienzyme Complexes - chemistry | Pyrophosphatases - metabolism | Phosphoric Diester Hydrolases | Animals | Phosphodiesterase I - metabolism | Hydrophobic and Hydrophilic Interactions | Protein Conformation | Mice | Binding Sites | Physiological aspects | Lipids | Cell receptors | Research | Phospholipases | Structure | Enzymes | Signal transduction | Cellular biology | Molecular biology | Crystal structure | Index Medicus
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11. Full Text Structure and function of Zucchini endoribonuclease in piRNA biogenesis
by Nishimasu, Hiroshi and Ishizu, Hirotsugu and Saito, Kuniaki and Fukuhara, Satoshi and Kamatani, Miharu K and Bonnefond, Luc and Matsumoto, Naoki and Nishizawa, Tomohiro and Nakanaga, Keita and Aoki, Junken and Ishitani, Ryuichiro and Siomi, Haruhiko and Siomi, Mikiko C and Nureki, Osamu
Nature, ISSN 0028-0836, 11/2012, Volume 491, Issue 7423, pp. 284 - 287
PIWI-interacting RNAs (piRNAs) silence transposons to maintain genome integrity in animal germ lines(1-4). piRNAs are classified as primary and secondary... 
REPLACEMENT | GERMLINE | SMALL RNAS | MECHANISM | NUAGE FORMATION | CRYSTAL-STRUCTURE | MULTIDISCIPLINARY SCIENCES | PHOSPHOLIPASE-D FAMILY | DROSOPHILA | GENOME | PIWI | Endoribonucleases - chemistry | RNA, Small Interfering - genetics | Catalytic Domain | Biocatalysis | Endoribonucleases - metabolism | Gene Silencing | Models, Molecular | Molecular Sequence Data | Crystallography, X-Ray | Structure-Activity Relationship | Drosophila Proteins - chemistry | Drosophila Proteins - metabolism | Drosophila melanogaster - genetics | RNA, Small Interfering - chemistry | Animals | Base Sequence | RNA, Small Interfering - biosynthesis | DNA Transposable Elements - genetics | Drosophila melanogaster - enzymology | Protein Conformation | RNA, Small Interfering - metabolism | Synthesis | Molecular genetics | RNA | Drosophila | Physiological aspects | Genetic aspects | Ribonuclease | Research | Structure | Enzymes | Biosynthesis | Crystal structure | Index Medicus
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12. Full Text Somatic RHOA mutation in angioimmunoblastic T cell lymphoma
by Sakata-Yanagimoto, Mamiko and Enami, Terukazu and Yoshida, Kenichi and Shiraishi, Yuichi and Ishii, Ryohei and Miyake, Yasuyuki and Muto, Hideharu and Tsuyama, Naoko and Sato-Otsubo, Aiko and Okuno, Yusuke and Sakata, Seiji and Kamada, Yuhei and Nakamoto-Matsubara, Rie and Tran, Nguyen Bich and Izutsu, Koji and Sato, Yusuke and Ohta, Yasunori and Furuta, Junichi and Shimizu, Seiichi and Komeno, Takuya and Sato, Yuji and Ito, Takayoshi and Noguchi, Masayuki and Noguchi, Emiko and Sanada, Masashi and Chiba, Kenichi and Tanaka, Hiroko and Suzukawa, Kazumi and Nanmoku, Toru and Hasegawa, Yuichi and Nureki, Osamu and Miyano, Satoru and Nakamura, Naoya and Takeuchi, Kengo and Ogawa, Seishi and Chiba, Shigeru
Nature Genetics, ISSN 1061-4036, 2014, Volume 46, Issue 2, pp. 171 - 175
Angioimmunoblastic T cell lymphoma (AITL) is a distinct subtype of peripheral T cell lymphoma characterized by generalized lymphadenopathy and frequent... 
FREQUENT | ALIGNMENT | GTPASES | PHOSPHORYLATION | FORM | CRYSTAL-STRUCTURE | GENES | GENETICS & HEREDITY | TET2 | GENOME | FAMILY | NIH 3T3 Cells | Immunoblastic Lymphadenopathy - genetics | Jurkat Cells | Humans | Lymphoma, T-Cell, Peripheral - genetics | Molecular Sequence Data | Bromodeoxyuridine | Isocitrate Dehydrogenase - genetics | Proto-Oncogene Proteins - genetics | rhoA GTP-Binding Protein - genetics | DNA-Binding Proteins - genetics | Sequence Analysis, DNA | Mutation, Missense - genetics | DNA (Cytosine-5-)-Methyltransferases - genetics | Exome - genetics | Animals | Base Sequence | Lymphoma, T-Cell, Peripheral - pathology | Mice | Genetic aspects | Non-Hodgkin's lymphomas | Research | Gene mutations | Health aspects | Risk factors | Medical research | Lymphocytes | Lymphomas | Genomes | Mutation | Gene expression | Tumors | Index Medicus
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