小川 治夫

Last Update: 2021/06/29 19:25:35

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Name(Kanji/Kana/Abecedarium Latinum)
小川 治夫/オガワ ハルオ/Ogawa, Haruo
Primary Affiliation(Org1/Job title)
Graduate School of Pharmaceutical Sciences/Associate Professor
Faculty
Org1 Job title
薬学部
Academic Degree
Field(Japanese) Field(English) University(Japanese) University(English) Method
博士(理学) 東京工業大学
修士(理学) 東京工業大学
Personal Profile
(Japanese)
細胞膜に存在する膜タンパク質は、細胞外から細胞に情報を伝達する上で重要な役割を果たします。この「膜タンパク質」の作動機構に興味があり、極低温電子顕微鏡やX線結晶学を用いて機構解明に取り組んでいます。
(English)
Membrane proteins exist in the cell membrane play key role in transmitting information from outside the cell into the cell. I am interested in the mechanism of "membrane protein", and am working to elucidate this mechanism using cryo-electron microscope and/or X-ray crystallography.
Language of Instruction
Language(japanese) Language(english) Code
日本語 Japanese jpn
ORCID ID
https://orcid.org/0000-0001-5515-1533
researchmap URL
https://researchmap.jp/haru_9000
Published Papers
Author Author(Japanese) Author(English) Title Title(Japanese) Title(English) Bibliography Bibliography(Japanese) Bibliography(English) Publication date Refereed paper Language Publishing type Disclose
Yoshiki Kabashima, Haruo Ogawa, Rie Nakajima, Chikashi Toyoshima Yoshiki Kabashima, Haruo Ogawa, Rie Nakajima, Chikashi Toyoshima Yoshiki Kabashima, Haruo Ogawa, Rie Nakajima, Chikashi Toyoshima What ATP binding does to the Ca2+ pump and how nonproductive phosphoryl transfer is prevented in the absence of Ca2. What ATP binding does to the Ca2+ pump and how nonproductive phosphoryl transfer is prevented in the absence of Ca2. What ATP binding does to the Ca2+ pump and how nonproductive phosphoryl transfer is prevented in the absence of Ca2. Proceedings of the National Academy of Sciences of the United States of America, 117, 31, 18448-18458 Proceedings of the National Academy of Sciences of the United States of America, 117, 31, 18448-18458 Proceedings of the National Academy of Sciences of the United States of America, 117, 31, 18448-18458 2020/08/04 Refereed English Research paper(scientific journal) Disclose to all
Haruo Ogawa, Nagomi Kurebayashi, Toshiko Yamazawa, Takashi Murayama Haruo Ogawa, Nagomi Kurebayashi, Toshiko Yamazawa, Takashi Murayama Haruo Ogawa, Nagomi Kurebayashi, Toshiko Yamazawa, Takashi Murayama Regulatory mechanisms of ryanodine receptor/Ca2+ release channel revealed by recent advancements in structural studies. Regulatory mechanisms of ryanodine receptor/Ca2+ release channel revealed by recent advancements in structural studies. Regulatory mechanisms of ryanodine receptor/Ca2+ release channel revealed by recent advancements in structural studies. Journal of muscle research and cell motility Journal of muscle research and cell motility Journal of muscle research and cell motility 2020/02/10 Refereed English Research paper(scientific journal) Disclose to all
Toshiko Yamazawa, Haruo Ogawa, Takashi Murayama, Maki Yamaguchi, Hideto Oyamada, Junji Suzuki, Nagomi Kurebayashi, Kazunori Kanemaru, Katsuji Oguchi, Takashi Sakurai, Masamitsu Iino Toshiko Yamazawa, Haruo Ogawa, Takashi Murayama, Maki Yamaguchi, Hideto Oyamada, Junji Suzuki, Nagomi Kurebayashi, Kazunori Kanemaru, Katsuji Oguchi, Takashi Sakurai, Masamitsu Iino Toshiko Yamazawa, Haruo Ogawa, Takashi Murayama, Maki Yamaguchi, Hideto Oyamada, Junji Suzuki, Nagomi Kurebayashi, Kazunori Kanemaru, Katsuji Oguchi, Takashi Sakurai, Masamitsu Iino Insights into channel modulation mechanism of RYR1 mutants using Ca2+ imaging and molecular dynamics. Insights into channel modulation mechanism of RYR1 mutants using Ca2+ imaging and molecular dynamics. Insights into channel modulation mechanism of RYR1 mutants using Ca2+ imaging and molecular dynamics. The Journal of general physiology, 152, 1 The Journal of general physiology, 152, 1 The Journal of general physiology, 152, 1 2020/01/06 Refereed English Research paper(scientific journal) Disclose to all
Naoki Tsunekawa, Haruo Ogawa, Junko Tsueda, Toshihiko Akiba, Chikashi Toyoshima Naoki Tsunekawa, Haruo Ogawa, Junko Tsueda, Toshihiko Akiba, Chikashi Toyoshima Naoki Tsunekawa, Haruo Ogawa, Junko Tsueda, Toshihiko Akiba, Chikashi Toyoshima Mechanism of the E2 to E1 transition in Ca2+ pump revealed by crystal structures of gating residue mutants. Mechanism of the E2 to E1 transition in Ca2+ pump revealed by crystal structures of gating residue mutants. Mechanism of the E2 to E1 transition in Ca2+ pump revealed by crystal structures of gating residue mutants. Proceedings of the National Academy of Sciences of the United States of America, 115, 50, 12722-12727 Proceedings of the National Academy of Sciences of the United States of America, 115, 50, 12722-12727 Proceedings of the National Academy of Sciences of the United States of America, 115, 50, 12722-12727 2018/12/11 Refereed English Research paper(scientific journal) Disclose to all
Takashi Murayama, Nagomi Kurebayashi, Mari Ishigami-Yuasa, Shuichi Mori, Yukina Suzuki, Ryunosuke Akima, Haruo Ogawa, Junji Suzuki, Kazunori Kanemaru, Hideto Oyamada, Yuji Kiuchi, Masamitsu Iino, Hiroyuki Kagechika, Takashi Sakurai Takashi Murayama, Nagomi Kurebayashi, Mari Ishigami-Yuasa, Shuichi Mori, Yukina Suzuki, Ryunosuke Akima, Haruo Ogawa, Junji Suzuki, Kazunori Kanemaru, Hideto Oyamada, Yuji Kiuchi, Masamitsu Iino, Hiroyuki Kagechika, Takashi Sakurai Takashi Murayama, Nagomi Kurebayashi, Mari Ishigami-Yuasa, Shuichi Mori, Yukina Suzuki, Ryunosuke Akima, Haruo Ogawa, Junji Suzuki, Kazunori Kanemaru, Hideto Oyamada, Yuji Kiuchi, Masamitsu Iino, Hiroyuki Kagechika, Takashi Sakurai Efficient High-Throughput Screening by Endoplasmic Reticulum Ca2+ Measurement to Identify Inhibitors of Ryanodine Receptor Ca2+-Release Channels. Efficient High-Throughput Screening by Endoplasmic Reticulum Ca2+ Measurement to Identify Inhibitors of Ryanodine Receptor Ca2+-Release Channels. Efficient High-Throughput Screening by Endoplasmic Reticulum Ca2+ Measurement to Identify Inhibitors of Ryanodine Receptor Ca2+-Release Channels. Molecular pharmacology, 94, 1, 722-730 Molecular pharmacology, 94, 1, 722-730 Molecular pharmacology, 94, 1, 722-730 2018/07 Refereed English Research paper(scientific journal) Disclose to all
Eisuke Sato, Maho Morita, Haruo Ogawa, Masato Iwatsuki, Rei Hokari, Aki Ishiyama, Satoshi Ōmura, Arihiro Iwasaki, Kiyotake Suenaga Eisuke Sato, Maho Morita, Haruo Ogawa, Masato Iwatsuki, Rei Hokari, Aki Ishiyama, Satoshi Ōmura, Arihiro Iwasaki, Kiyotake Suenaga Eisuke Sato, Maho Morita, Haruo Ogawa, Masato Iwatsuki, Rei Hokari, Aki Ishiyama, Satoshi Ōmura, Arihiro Iwasaki, Kiyotake Suenaga Design, synthesis and anti-malarial activities of synthetic analogs of biselyngbyolide B, a Ca2+ pump inhibitor from marine cyanobacteria. Design, synthesis and anti-malarial activities of synthetic analogs of biselyngbyolide B, a Ca2+ pump inhibitor from marine cyanobacteria. Design, synthesis and anti-malarial activities of synthetic analogs of biselyngbyolide B, a Ca2+ pump inhibitor from marine cyanobacteria. Bioorganic & medicinal chemistry letters, 28, 3, 298-301 Bioorganic & medicinal chemistry letters, 28, 3, 298-301 Bioorganic & medicinal chemistry letters, 28, 3, 298-301 2018/02/01 Refereed English Research paper(scientific journal) Disclose to all
Takashi Murayama, Haruo Ogawa, Nagomi Kurebayashi, Seiko Ohno, Minoru Horie, Takashi Sakurai Takashi Murayama, Haruo Ogawa, Nagomi Kurebayashi, Seiko Ohno, Minoru Horie, Takashi Sakurai Takashi Murayama, Haruo Ogawa, Nagomi Kurebayashi, Seiko Ohno, Minoru Horie, Takashi Sakurai A tryptophan residue in the caffeine-binding site of the ryanodine receptor regulates Ca2+ sensitivity. A tryptophan residue in the caffeine-binding site of the ryanodine receptor regulates Ca2+ sensitivity. A tryptophan residue in the caffeine-binding site of the ryanodine receptor regulates Ca2+ sensitivity. Communications biology, 1, 98-98 Communications biology, 1, 98-98 Communications biology, 1, 98-98 2018 Refereed English Research paper(scientific journal) Disclose to all
Takashi Murayama, Nagomi Kurebayashi, Haruo Ogawa, Toshiko Yamazawa, Hideto Oyamada, Junji Suzuki, Kazunori Kanemaru, Katsuji Oguchi, Masamitsu Iino, Takashi Sakurai Takashi Murayama, Nagomi Kurebayashi, Haruo Ogawa, Toshiko Yamazawa, Hideto Oyamada, Junji Suzuki, Kazunori Kanemaru, Katsuji Oguchi, Masamitsu Iino, Takashi Sakurai Takashi Murayama, Nagomi Kurebayashi, Haruo Ogawa, Toshiko Yamazawa, Hideto Oyamada, Junji Suzuki, Kazunori Kanemaru, Katsuji Oguchi, Masamitsu Iino, Takashi Sakurai Genotype-Phenotype Correlations of Malignant Hyperthermia and Central Core Disease Mutations in the Central Region of the RYR1 Channel. Genotype-Phenotype Correlations of Malignant Hyperthermia and Central Core Disease Mutations in the Central Region of the RYR1 Channel. Genotype-Phenotype Correlations of Malignant Hyperthermia and Central Core Disease Mutations in the Central Region of the RYR1 Channel. Human mutation, 37, 11, 1231-1241 Human mutation, 37, 11, 1231-1241 Human mutation, 37, 11, 1231-1241 2016/11 Refereed English Research paper(scientific journal) Disclose to all
Yimeng Zhao, Haruo Ogawa, Shin-Ichiro Yonekura, Hiroaki Mitsuhashi, Satomi Mitsuhashi, Ichizo Nishino, Chikashi Toyoshima, Shoichi Ishiura Yimeng Zhao, Haruo Ogawa, Shin-Ichiro Yonekura, Hiroaki Mitsuhashi, Satomi Mitsuhashi, Ichizo Nishino, Chikashi Toyoshima, Shoichi Ishiura Yimeng Zhao, Haruo Ogawa, Shin-Ichiro Yonekura, Hiroaki Mitsuhashi, Satomi Mitsuhashi, Ichizo Nishino, Chikashi Toyoshima, Shoichi Ishiura Functional analysis of SERCA1b, a highly expressed SERCA1 variant in myotonic dystrophy type 1 muscle. Functional analysis of SERCA1b, a highly expressed SERCA1 variant in myotonic dystrophy type 1 muscle. Functional analysis of SERCA1b, a highly expressed SERCA1 variant in myotonic dystrophy type 1 muscle. Biochimica et biophysica acta, 1852, 10 Pt A, 2042-7 Biochimica et biophysica acta, 1852, 10 Pt A, 2042-7 Biochimica et biophysica acta, 1852, 10 Pt A, 2042-7 2015/10 Refereed English Research paper(scientific journal) Disclose to all
Haruo Ogawa, Flemming Cornelius, Ayami Hirata, Chikashi Toyoshima Haruo Ogawa, Flemming Cornelius, Ayami Hirata, Chikashi Toyoshima Haruo Ogawa, Flemming Cornelius, Ayami Hirata, Chikashi Toyoshima Sequential substitution of K(+) bound to Na(+),K(+)-ATPase visualized by X-ray crystallography. Sequential substitution of K(+) bound to Na(+),K(+)-ATPase visualized by X-ray crystallography. Sequential substitution of K(+) bound to Na(+),K(+)-ATPase visualized by X-ray crystallography. Nature communications, 6, 8004-8004 Nature communications, 6, 8004-8004 Nature communications, 6, 8004-8004 2015/08/10 Refereed English Research paper(scientific journal) Disclose to all
Maho Morita, Haruo Ogawa, Osamu Ohno, Takao Yamori, Kiyotake Suenaga, Chikashi Toyoshima Maho Morita, Haruo Ogawa, Osamu Ohno, Takao Yamori, Kiyotake Suenaga, Chikashi Toyoshima Maho Morita, Haruo Ogawa, Osamu Ohno, Takao Yamori, Kiyotake Suenaga, Chikashi Toyoshima Biselyngbyasides, cytotoxic marine macrolides, are novel and potent inhibitors of the Ca(2+) pumps with a unique mode of binding. Biselyngbyasides, cytotoxic marine macrolides, are novel and potent inhibitors of the Ca(2+) pumps with a unique mode of binding. Biselyngbyasides, cytotoxic marine macrolides, are novel and potent inhibitors of the Ca(2+) pumps with a unique mode of binding. FEBS letters, 589, 13, 1406-11 FEBS letters, 589, 13, 1406-11 FEBS letters, 589, 13, 1406-11 2015/06/04 Refereed English Research paper(scientific journal) Disclose to all
Michael Habeck, Haim Haviv, Adriana Katz, Einat Kapri-Pardes, Sophie Ayciriex, Andrej Shevchenko, Haruo Ogawa, Chikashi Toyoshima, Steven J D Karlish Michael Habeck, Haim Haviv, Adriana Katz, Einat Kapri-Pardes, Sophie Ayciriex, Andrej Shevchenko, Haruo Ogawa, Chikashi Toyoshima, Steven J D Karlish Michael Habeck, Haim Haviv, Adriana Katz, Einat Kapri-Pardes, Sophie Ayciriex, Andrej Shevchenko, Haruo Ogawa, Chikashi Toyoshima, Steven J D Karlish Stimulation, inhibition, or stabilization of Na,K-ATPase caused by specific lipid interactions at distinct sites. Stimulation, inhibition, or stabilization of Na,K-ATPase caused by specific lipid interactions at distinct sites. Stimulation, inhibition, or stabilization of Na,K-ATPase caused by specific lipid interactions at distinct sites. The Journal of biological chemistry, 290, 8, 4829-42 The Journal of biological chemistry, 290, 8, 4829-42 The Journal of biological chemistry, 290, 8, 4829-42 2015/02/20 Refereed English Research paper(scientific journal) Disclose to all
Hiroki Takai, Koji Masuda, Tomohiro Sato, Yuriko Sakaguchi, Takeo Suzuki, Tsutomu Suzuki, Ryo Koyama-Nasu, Yukiko Nasu-Nishimura, Yuki Katou, Haruo Ogawa, Yasuyuki Morishita, Hiroko Kozuka-Hata, Masaaki Oyama, Tomoki Todo, Yasushi Ino, Akitake Mukasa, Nobuhito Saito, Chikashi Toyoshima, Katsuhiko Shirahige, Tetsu Akiyama Hiroki Takai, Koji Masuda, Tomohiro Sato, Yuriko Sakaguchi, Takeo Suzuki, Tsutomu Suzuki, Ryo Koyama-Nasu, Yukiko Nasu-Nishimura, Yuki Katou, Haruo Ogawa, Yasuyuki Morishita, Hiroko Kozuka-Hata, Masaaki Oyama, Tomoki Todo, Yasushi Ino, Akitake Mukasa, Nobuhito Saito, Chikashi Toyoshima, Katsuhiko Shirahige, Tetsu Akiyama Hiroki Takai, Koji Masuda, Tomohiro Sato, Yuriko Sakaguchi, Takeo Suzuki, Tsutomu Suzuki, Ryo Koyama-Nasu, Yukiko Nasu-Nishimura, Yuki Katou, Haruo Ogawa, Yasuyuki Morishita, Hiroko Kozuka-Hata, Masaaki Oyama, Tomoki Todo, Yasushi Ino, Akitake Mukasa, Nobuhito Saito, Chikashi Toyoshima, Katsuhiko Shirahige, Tetsu Akiyama 5-Hydroxymethylcytosine plays a critical role in glioblastomagenesis by recruiting the CHTOP-methylosome complex. 5-Hydroxymethylcytosine plays a critical role in glioblastomagenesis by recruiting the CHTOP-methylosome complex. 5-Hydroxymethylcytosine plays a critical role in glioblastomagenesis by recruiting the CHTOP-methylosome complex. Cell reports, 9, 1, 48-60 Cell reports, 9, 1, 48-60 Cell reports, 9, 1, 48-60 2014/10/09 Refereed English Research paper(scientific journal) Disclose to all
Ryuta Kanai, Haruo Ogawa, Bente Vilsen, Flemming Cornelius, Chikashi Toyoshima Ryuta Kanai, Haruo Ogawa, Bente Vilsen, Flemming Cornelius, Chikashi Toyoshima Ryuta Kanai, Haruo Ogawa, Bente Vilsen, Flemming Cornelius, Chikashi Toyoshima Crystal structure of a Na+-bound Na+,K+-ATPase preceding the E1P state. Crystal structure of a Na+-bound Na+,K+-ATPase preceding the E1P state. Crystal structure of a Na+-bound Na+,K+-ATPase preceding the E1P state. Nature, 502, 7470, 201-6 Nature, 502, 7470, 201-6 Nature, 502, 7470, 201-6 2013/10/10 Refereed English Research paper(scientific journal) Disclose to all
Chikashi Toyoshima, Shiho Iwasawa, Haruo Ogawa, Ayami Hirata, Junko Tsueda, Giuseppe Inesi Chikashi Toyoshima, Shiho Iwasawa, Haruo Ogawa, Ayami Hirata, Junko Tsueda, Giuseppe Inesi Chikashi Toyoshima, Shiho Iwasawa, Haruo Ogawa, Ayami Hirata, Junko Tsueda, Giuseppe Inesi Crystal structures of the calcium pump and sarcolipin in the Mg2+-bound E1 state. Crystal structures of the calcium pump and sarcolipin in the Mg2+-bound E1 state. Crystal structures of the calcium pump and sarcolipin in the Mg2+-bound E1 state. Nature, 495, 7440, 260-4 Nature, 495, 7440, 260-4 Nature, 495, 7440, 260-4 2013/03/14 Refereed English Research paper(scientific journal) Disclose to all
Takashi Okuda, Chieko Osawa, Haruhiko Yamada, Kengo Hayashi, Shizue Nishikawa, Tomoko Ushio, Yuji Kubo, Motoyasu Satou, Haruo Ogawa, Tatsuya Haga Takashi Okuda, Chieko Osawa, Haruhiko Yamada, Kengo Hayashi, Shizue Nishikawa, Tomoko Ushio, Yuji Kubo, Motoyasu Satou, Haruo Ogawa, Tatsuya Haga Takashi Okuda, Chieko Osawa, Haruhiko Yamada, Kengo Hayashi, Shizue Nishikawa, Tomoko Ushio, Yuji Kubo, Motoyasu Satou, Haruo Ogawa, Tatsuya Haga Transmembrane topology and oligomeric structure of the high-affinity choline transporter. Transmembrane topology and oligomeric structure of the high-affinity choline transporter. Transmembrane topology and oligomeric structure of the high-affinity choline transporter. The Journal of biological chemistry, 287, 51, 42826-34 The Journal of biological chemistry, 287, 51, 42826-34 The Journal of biological chemistry, 287, 51, 42826-34 2012/12/14 Refereed English Research paper(scientific journal) Disclose to all
Naoki Okamoto, Haruo Ogawa, Chikashi Toyoshima Naoki Okamoto, Haruo Ogawa, Chikashi Toyoshima Naoki Okamoto, Haruo Ogawa, Chikashi Toyoshima A new method for establishing stable cell lines and its use for large-scale production of human guanylyl cyclase-B receptor and of the extracellular domain. A new method for establishing stable cell lines and its use for large-scale production of human guanylyl cyclase-B receptor and of the extracellular domain. A new method for establishing stable cell lines and its use for large-scale production of human guanylyl cyclase-B receptor and of the extracellular domain. Biochemical and biophysical research communications, 426, 2, 260-5 Biochemical and biophysical research communications, 426, 2, 260-5 Biochemical and biophysical research communications, 426, 2, 260-5 2012/09/21 Refereed English Research paper(scientific journal) Disclose to all
Kunio S Misono, John S Philo, Tsutomu Arakawa, Craig M Ogata, Yue Qiu, Haruo Ogawa, Howard S Young Kunio S Misono, John S Philo, Tsutomu Arakawa, Craig M Ogata, Yue Qiu, Haruo Ogawa, Howard S Young Kunio S Misono, John S Philo, Tsutomu Arakawa, Craig M Ogata, Yue Qiu, Haruo Ogawa, Howard S Young Structure, signaling mechanism and regulation of the natriuretic peptide receptor guanylate cyclase. Structure, signaling mechanism and regulation of the natriuretic peptide receptor guanylate cyclase. Structure, signaling mechanism and regulation of the natriuretic peptide receptor guanylate cyclase. The FEBS journal, 278, 11, 1818-29 The FEBS journal, 278, 11, 1818-29 The FEBS journal, 278, 11, 1818-29 2011/06 Refereed English Research paper(scientific journal) Disclose to all
Haruo Ogawa, Yue Qiu, John S Philo, Tsutomu Arakawa, Craig M Ogata, Kunio S Misono Haruo Ogawa, Yue Qiu, John S Philo, Tsutomu Arakawa, Craig M Ogata, Kunio S Misono Haruo Ogawa, Yue Qiu, John S Philo, Tsutomu Arakawa, Craig M Ogata, Kunio S Misono Reversibly bound chloride in the atrial natriuretic peptide receptor hormone-binding domain: possible allosteric regulation and a conserved structural motif for the chloride-binding site. Reversibly bound chloride in the atrial natriuretic peptide receptor hormone-binding domain: possible allosteric regulation and a conserved structural motif for the chloride-binding site. Reversibly bound chloride in the atrial natriuretic peptide receptor hormone-binding domain: possible allosteric regulation and a conserved structural motif for the chloride-binding site. Protein science : a publication of the Protein Society, 19, 3, 544-57 Protein science : a publication of the Protein Society, 19, 3, 544-57 Protein science : a publication of the Protein Society, 19, 3, 544-57 2010/03 Refereed English Research paper(scientific journal) Disclose to all
Haruo Ogawa, Takehiro Shinoda, Flemming Cornelius, Chikashi Toyoshima Haruo Ogawa, Takehiro Shinoda, Flemming Cornelius, Chikashi Toyoshima Haruo Ogawa, Takehiro Shinoda, Flemming Cornelius, Chikashi Toyoshima Crystal structure of the sodium-potassium pump (Na+,K+-ATPase) with bound potassium and ouabain. Crystal structure of the sodium-potassium pump (Na+,K+-ATPase) with bound potassium and ouabain. Crystal structure of the sodium-potassium pump (Na+,K+-ATPase) with bound potassium and ouabain. Proceedings of the National Academy of Sciences of the United States of America, 106, 33, 13742-7 Proceedings of the National Academy of Sciences of the United States of America, 106, 33, 13742-7 Proceedings of the National Academy of Sciences of the United States of America, 106, 33, 13742-7 2009/08/18 Refereed English Research paper(scientific journal) Disclose to all
Takehiro Shinoda, Haruo Ogawa, Flemming Cornelius, Chikashi Toyoshima Takehiro Shinoda, Haruo Ogawa, Flemming Cornelius, Chikashi Toyoshima Takehiro Shinoda, Haruo Ogawa, Flemming Cornelius, Chikashi Toyoshima Crystal structure of the sodium-potassium pump at 2.4 A resolution. Crystal structure of the sodium-potassium pump at 2.4 A resolution. Crystal structure of the sodium-potassium pump at 2.4 A resolution. Nature, 459, 7245, 446-50 Nature, 459, 7245, 446-50 Nature, 459, 7245, 446-50 2009/05/21 Refereed English Research paper(scientific journal) Disclose to all
Haruo Ogawa, Yue Qiu, Liming Huang, Suk-Wah Tam-Chang, Howard S Young, Kunio S Misono Haruo Ogawa, Yue Qiu, Liming Huang, Suk-Wah Tam-Chang, Howard S Young, Kunio S Misono Haruo Ogawa, Yue Qiu, Liming Huang, Suk-Wah Tam-Chang, Howard S Young, Kunio S Misono Structure of the atrial natriuretic peptide receptor extracellular domain in the unbound and hormone-bound states by single-particle electron microscopy. Structure of the atrial natriuretic peptide receptor extracellular domain in the unbound and hormone-bound states by single-particle electron microscopy. Structure of the atrial natriuretic peptide receptor extracellular domain in the unbound and hormone-bound states by single-particle electron microscopy. The FEBS journal, 276, 5, 1347-55 The FEBS journal, 276, 5, 1347-55 The FEBS journal, 276, 5, 1347-55 2009/03 Refereed English Research paper(scientific journal) Disclose to all
Chikashi Toyoshima, Yoshiyuki Norimatsu, Shiho Iwasawa, Takeo Tsuda, Haruo Ogawa Chikashi Toyoshima, Yoshiyuki Norimatsu, Shiho Iwasawa, Takeo Tsuda, Haruo Ogawa Chikashi Toyoshima, Yoshiyuki Norimatsu, Shiho Iwasawa, Takeo Tsuda, Haruo Ogawa How processing of aspartylphosphate is coupled to lumenal gating of the ion pathway in the calcium pump. How processing of aspartylphosphate is coupled to lumenal gating of the ion pathway in the calcium pump. How processing of aspartylphosphate is coupled to lumenal gating of the ion pathway in the calcium pump. Proceedings of the National Academy of Sciences of the United States of America, 104, 50, 19831-6 Proceedings of the National Academy of Sciences of the United States of America, 104, 50, 19831-6 Proceedings of the National Academy of Sciences of the United States of America, 104, 50, 19831-6 2007/12/11 Refereed English Research paper(scientific journal) Disclose to all
Kunio Misono, Haruo Ogawa, Yue Qiu, Craig M Ogata Kunio Misono, Haruo Ogawa, Yue Qiu, Craig M Ogata Kunio Misono, Haruo Ogawa, Yue Qiu, Craig M Ogata [ANP receptor structure and signal transduction mechanism: a novel hormone-induced rotation mechanism for transmembrane signaling]. [ANP receptor structure and signal transduction mechanism: a novel hormone-induced rotation mechanism for transmembrane signaling]. [ANP receptor structure and signal transduction mechanism: a novel hormone-induced rotation mechanism for transmembrane signaling]. Tanpakushitsu kakusan koso. Protein, nucleic acid, enzyme, 50, 9, 1078-87 Tanpakushitsu kakusan koso. Protein, nucleic acid, enzyme, 50, 9, 1078-87 Tanpakushitsu kakusan koso. Protein, nucleic acid, enzyme, 50, 9, 1078-87 2005/08 Refereed Japanese Research paper(scientific journal) Disclose to all
Kunio S Misono, Haruo Ogawa, Yue Qiu, Craig M Ogata Kunio S Misono, Haruo Ogawa, Yue Qiu, Craig M Ogata Kunio S Misono, Haruo Ogawa, Yue Qiu, Craig M Ogata Structural studies of the natriuretic peptide receptor: a novel hormone-induced rotation mechanism for transmembrane signal transduction. Structural studies of the natriuretic peptide receptor: a novel hormone-induced rotation mechanism for transmembrane signal transduction. Structural studies of the natriuretic peptide receptor: a novel hormone-induced rotation mechanism for transmembrane signal transduction. Peptides, 26, 6, 957-68 Peptides, 26, 6, 957-68 Peptides, 26, 6, 957-68 2005/06 Refereed English Research paper(scientific journal) Disclose to all
Haruo Ogawa, Yue Qiu, Craig M Ogata, Kunio S Misono Haruo Ogawa, Yue Qiu, Craig M Ogata, Kunio S Misono Haruo Ogawa, Yue Qiu, Craig M Ogata, Kunio S Misono Crystal structure of hormone-bound atrial natriuretic peptide receptor extracellular domain: rotation mechanism for transmembrane signal transduction. Crystal structure of hormone-bound atrial natriuretic peptide receptor extracellular domain: rotation mechanism for transmembrane signal transduction. Crystal structure of hormone-bound atrial natriuretic peptide receptor extracellular domain: rotation mechanism for transmembrane signal transduction. The Journal of biological chemistry, 279, 27, 28625-31 The Journal of biological chemistry, 279, 27, 28625-31 The Journal of biological chemistry, 279, 27, 28625-31 2004/07/02 Refereed English Research paper(scientific journal) Disclose to all
Shinji Asano, Ayumi Yoshida, Hiroaki Yashiro, Yusuke Kobayashi, Anna Morisato, Haruo Ogawa, Noriaki Takeguchi, Magotoshi Morii Shinji Asano, Ayumi Yoshida, Hiroaki Yashiro, Yusuke Kobayashi, Anna Morisato, Haruo Ogawa, Noriaki Takeguchi, Magotoshi Morii Shinji Asano, Ayumi Yoshida, Hiroaki Yashiro, Yusuke Kobayashi, Anna Morisato, Haruo Ogawa, Noriaki Takeguchi, Magotoshi Morii The cavity structure for docking the K(+)-competitive inhibitors in the gastric proton pump. The cavity structure for docking the K(+)-competitive inhibitors in the gastric proton pump. The cavity structure for docking the K(+)-competitive inhibitors in the gastric proton pump. The Journal of biological chemistry, 279, 14, 13968-75 The Journal of biological chemistry, 279, 14, 13968-75 The Journal of biological chemistry, 279, 14, 13968-75 2004/04/02 Refereed English Research paper(scientific journal) Disclose to all
Yue Qiu, Haruo Ogawa, Masaru Miyagi, Kunio S Misono Yue Qiu, Haruo Ogawa, Masaru Miyagi, Kunio S Misono Yue Qiu, Haruo Ogawa, Masaru Miyagi, Kunio S Misono Constitutive activation and uncoupling of the atrial natriuretic peptide receptor by mutations at the dimer interface. Role of the dimer structure in signalling. Constitutive activation and uncoupling of the atrial natriuretic peptide receptor by mutations at the dimer interface. Role of the dimer structure in signalling. Constitutive activation and uncoupling of the atrial natriuretic peptide receptor by mutations at the dimer interface. Role of the dimer structure in signalling. The Journal of biological chemistry, 279, 7, 6115-23 The Journal of biological chemistry, 279, 7, 6115-23 The Journal of biological chemistry, 279, 7, 6115-23 2004/02/13 Refereed English Research paper(scientific journal) Disclose to all
Haruo Ogawa, Xiaolun Zhang, Yue Qiu, Craig M Ogata, Kunio S Misono Haruo Ogawa, Xiaolun Zhang, Yue Qiu, Craig M Ogata, Kunio S Misono Haruo Ogawa, Xiaolun Zhang, Yue Qiu, Craig M Ogata, Kunio S Misono Crystallization and preliminary X-ray analysis of the atrial natriuretic peptide (ANP) receptor extracellular domain complex with ANP: use of ammonium sulfate as the cryosalt. Crystallization and preliminary X-ray analysis of the atrial natriuretic peptide (ANP) receptor extracellular domain complex with ANP: use of ammonium sulfate as the cryosalt. Crystallization and preliminary X-ray analysis of the atrial natriuretic peptide (ANP) receptor extracellular domain complex with ANP: use of ammonium sulfate as the cryosalt. Acta crystallographica. Section D, Biological crystallography, 59, Pt 10, 1831-3 Acta crystallographica. Section D, Biological crystallography, 59, Pt 10, 1831-3 Acta crystallographica. Section D, Biological crystallography, 59, Pt 10, 1831-3 2003/10 Refereed English Research paper(scientific journal) Disclose to all
Haruo Ogawa, Chikashi Toyoshima Haruo Ogawa, Chikashi Toyoshima Haruo Ogawa, Chikashi Toyoshima Homology modeling of the cation binding sites of Na+K+-ATPase. Homology modeling of the cation binding sites of Na+K+-ATPase. Homology modeling of the cation binding sites of Na+K+-ATPase. Proceedings of the National Academy of Sciences of the United States of America, 99, 25, 15977-82 Proceedings of the National Academy of Sciences of the United States of America, 99, 25, 15977-82 Proceedings of the National Academy of Sciences of the United States of America, 99, 25, 15977-82 2002/12/10 Refereed English Research paper(scientific journal) Disclose to all

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