{"id":93,"date":"2014-03-22T14:33:47","date_gmt":"2014-03-22T05:33:47","guid":{"rendered":"http:\/\/barato.sci.hokudai.ac.jp\/~stchem\/?page_id=93"},"modified":"2022-09-16T14:49:32","modified_gmt":"2022-09-16T05:49:32","slug":"presented-paper","status":"publish","type":"page","link":"https:\/\/wwwchem.sci.hokudai.ac.jp\/~stchem\/presen-project\/presented-paper\/","title":{"rendered":"\u767a\u8868\u8ad6\u6587"},"content":{"rendered":"

2022\u5e74\u5ea6<\/h2>
1.<\/span><\/td>

Heme binding to cold shock protein D, CspD, from Vibrio cholerae<\/em><\/strong><\/p>

Dayeon Nam, Wataru Motegi, Koichiro Ishimori, Takeshi Uchida<\/p>

Biochem. Biophys. Res. Commun.<\/em>, 2022<\/strong>, 624<\/em>, 151-156<\/p><\/td><\/tr>

2.<\/span><\/td>

Converting cytochrome\u00a0c<\/em>\u00a0into a DyP-like metalloenzyme<\/strong><\/p>

Issei Omura, Koichiro Ishimori, Takeshi Uchida<\/p>

Dalton Trans.<\/em>, 2022<\/strong>, 51<\/em>, 12641-12649<\/p><\/td><\/tr>

3.<\/span><\/td>

Metal sensing by a glycine\u2013histidine repeat sequence regulates the heme degradation activity of PM0042 from\u00a0Pasteurella multocida<\/em><\/strong><\/p>

Takeshi Uchida, Kazuki Ota, Akinobu Tatsumi, Syota Takeuchi, Koichiro Ishimori<\/p>

Inorg. Chem.<\/em>, 2022<\/strong>, 61<\/em>, 13543-13553<\/p><\/td><\/tr><\/tbody><\/table>

2021\u5e74\u5ea6<\/h2>
1.<\/span><\/td>

Radical transfer but not heme distal residues is essential for pH dependence of dye-decolorizing activity of peroxidase from Vibrio cholerae<\/em><\/strong><\/p>

Takeshi Uchida, Issei Omura, Sayaka Umetsu, Koichiro Ishimori<\/p>

J. Inorg. Biochem.<\/em>, <\/span>2021<\/strong>,\u00a0<\/span>219<\/em>, 111422 (8 pages)<\/span><\/p><\/td><\/tr>

2.<\/span><\/td>

Conformational ensemble of a multidomain protein explored by Gd3+<\/sup>\u00a0electron paramagnetic resonance<\/strong><\/p>

Tomohide Saio, Soya Hiramatsu, Mizue Asada, Hiroshi Nakagawa, Kazumi Shimizu, Hiroyuki Kumeta, Toshikazu Nakamura, Koichiro Ishimori<\/p>

Biophys. J.<\/em>,\u00a02021<\/strong>, 120<\/em>, 2943-2951<\/p><\/td><\/tr>

3.<\/span><\/td>

Zinc-dependent oligomerization of thermus thermophilus<\/em> trigger factor chaperone<\/strong><\/p>

Haojie Zhu, Motonori Matsusaki, Taiga Sugawara, Koichiro Ishimori, Tomohide Saio<\/p>

Biology<\/em>,\u00a02021<\/strong>, 10<\/em>, 1106-1106 (13 pages)<\/p><\/td><\/tr>

4.<\/span><\/td>

Functional cooperativity between the trigger factor chaperone and the ClpXP proteolytic complex<\/strong><\/p>

Kamran Rizzolo, Angela Yeou Hsiung Yu, Adedeji Ologbenla, Sa Rang Kim, Haojie Zhu, Koichiro Ishimori, Guillaume Thibault, Elisa Leung, Yi Wen Zhang, Mona Teng, Marta Haniszewski, Noha Miah, Sadhna Phanse, Zoran Minic, Sukyeong Lee, Julio Diaz Caballero, Mohan Babu, Francis T. F. Tsai, Tomohide Saio, Walid A. Houry<\/p>

Nat. Commun.<\/em>, 2021<\/strong>, 12<\/em>, 281 (18 pages)<\/p><\/td><\/tr>

5.<\/span><\/td>

C9orf72-derived arginine-rich poly-dipeptides impede phase modifiers<\/strong><\/p>

Hitoki Nanaura, Honoka Kawamukai, Ayano Fujiwara, Takeru Uehara, Yuichiro Aiba, Mari Nakanishi, Tomo Shiota, Masaki Hibino, Pattama Wiriyasermkul, Sotaro Kikuchi, Riko Nagata, Masaya Matsubayashi, Yoichi Shinkai, Tatsuya Niwa, Taro Mannen, Naritaka Morikawa, Naohiko Iguchi, Takao Kiriyama, Ken Morishima, Rintaro Inoue, Masaaki Sugiyama, Takashi Oda, Noriyuki Kodera, Sachiko Toma-Fukai, Mamoru Sato, Hideki Taguchi, Shushi Nagamori, Osami Shoji, Koichiro Ishimori, Hiroyoshi Matsumura, Kazuma Sugie, Tomohide Saio, Takuya Yoshizawa, Eiichiro Mori<\/p>

Nat. Commun.<\/em>, 2021<\/strong>, 12<\/em>, 531 (12 pages)<\/p><\/td><\/tr>

6.<\/span><\/td>

Regulation of the expression of the nickel uptake system in Vibrio cholerae<\/em> by iron and heme via Fur<\/strong><\/p>

Kazuyoshi Muranishi, Koichiro Ishimori, Takeshi Uchida<\/p>

J. Inorg. Biochem.<\/em>, 2022<\/strong>,\u00a0228<\/em>, 111713 (9 pages)<\/p><\/td><\/tr>

7.<\/span><\/td>

Structural and kinetic views of molecular chaperones in multidomain protein folding<\/strong><\/p>

Soichiro Kawagoe, Koichiro Ishimori, Tomohide Saio<\/p>

Int. J. Mol. Sci., 2022<\/strong>, 23<\/em>, 2485 (13 pages)<\/p><\/td><\/tr><\/tbody><\/table>

2020\u5e74\u5ea6<\/h2>
1.<\/span><\/td>

Biophysical research in Hokkaido University, Japan<\/strong><\/p>

Tomoyasu Aizawa, Makoto Demura, Kazutoshi Gohara, Hisashi Haga, Koichiro Ishimori, Masataka Kinjo, Tamiki Komatsuzaki, Katsumi Maenaka, Min Yao<\/p>

Biophys. Rev., <\/em>2020<\/strong>, 12, 233-236<\/p><\/td><\/tr>

2.<\/span><\/td>

Spectroscopic characterization of Halorhodopsin reconstituted into nanodisks using native lipids<\/strong><\/p>

Ayumi Yamamoto, Takashi Tsukamoto, Kenshiro Suzuki, Eri Hashimoto, Yoshihiro Kobashigawa, Kousuke Shibasaki, Takeshi Uchida, Fuyuhiko Inagaki, Makoto Demura, Koichiro Ishimori<\/p>

Biophys. J<\/em>., 2020<\/strong>, 118, 2853-2865<\/p><\/td><\/tr>

3.<\/span><\/td>

Osmotic pressure effects identify dehydration upon cytochrome c<\/em>-cytochrome c<\/em> oxidase complex formation contributing to a specific electron pathway formation<\/strong><\/p>

Wataru Sato, Seiji Hitaoka, Takeshi Uchida, Kyoko Shinzawa-Itoh, Kazunari Yoshizawa, Shinya Yoshikawa, Koichiro Ishimori<\/p>

Biochem. J., <\/em>2020<\/strong>, 477, 1565-1578<\/p><\/td><\/tr>

4.<\/span><\/td>

Mechanistic insights into heme-mediated transcriptional regulation via a bacterial manganese-<\/strong>binding iron regulator, iron response regulator (Irr)<\/p>

Dayeon Nam, Yuki Matsumoto, Takeshi Uchida, Mark R. O’Brian, Koichiro Ishimori<\/p>

J.\u00a0<\/em>Biol. Chem., <\/em>2020<\/strong>, 295, 11316-11325<\/span><\/p><\/td><\/tr>

5.<\/span><\/td>

Distance distribution between two iodine atoms derived from small-angle x-ray scattering interferometry for analyzing a conformational ensemble of heavy atom-labeled small molecules<\/strong><\/p>

Yuya Taguchi, Tomohide Saio, Daisuke Kohda<\/p>

J. <\/em>Phys. Chem. Lett.,<\/em> 2020<\/strong>, 25, 5451-5456<\/span><\/p><\/td><\/tr>

6.\u00a0<\/span><\/td>

Dynamics of proteins with different molecular structures under solution condition<\/strong><\/p>

Rintaro Inoue, Takashi Oda, Hiroshi Nakagawa, Taiki Tominaga, Tomohide Saio, Yukinobu Kawakita, Masahiro Shimizu, Aya Okuda, Ken Morishima, Nobuhiro Sato, Reiko Urade, Mamoru Sato, Masaaki Sugiyama<\/p>

Sci. Rep.,<\/em> 2020<\/strong>, 10, 21678 (10 pages)<\/p><\/td><\/tr>

7.<\/span><\/td>

Functional cooperativity between the trigger factor chaperone and the ClpXP proteolytic complex<\/strong><\/p>

Kamran Rizzolo, Angela Yeou Hsiung Yu, Adedeji Ologbenla, Sa Rang Kim, Haojie Zhu, Koichiro Ishimori, Guillaume Thibault, Elisa Leung, Yi Wen Zhang, Mona Teng, Marta Haniszewski, Noha Miah, Sadhna Phanse, Zoran Minic, Sukyeong Lee, Julio Diaz Caballero, Mohan Babu, Francis T. F. Tsai, Tomohide Saio, Walid A. Houry<\/p>

Nat. Commun.,<\/em> 2021<\/strong>, 12, 281 (18 pages)<\/p><\/td><\/tr>

8.<\/span><\/td>

Deuteration aiming for neutron scattering<\/strong><\/p>

Aya Okuda, Rintaro Inoue, Ken Morishima, Tomohide Saio, Yasuhiro Yunoki, Maho Yagi-Utsumi, Hirokazu Yagi, Masahiro Shimizu, Nobuhiro Sato, Reiko Urade, Koichi Kato, Masaaki Sugiyama<\/p>

Biophys. Physicobiol.,<\/em> 2021<\/strong>, 18, 16-27<\/p><\/td><\/tr>

9.<\/span><\/td>

A unique leucine-valine adhesive motif supports structure and function of protein disulfide isomerase P5 via dimerization<\/strong><\/p>

Masaki Okumura, Shingo Kanemura, Motonori Matsusaki, Misaki Kinoshita, Tomohide Saio, Dai Ito, Chihiro Hirayama, Hiroyuki Kumeta, Mai Watabe, Yuta Amagai, Young-Ho Lee, Shuji Akiyama, Kenji Inaba<\/p>

Structure<\/em>, 2021<\/strong>, 29, 1-14<\/p><\/td><\/tr>

10.<\/span><\/td>

\u91d1\u5c5e\u30bb\u30f3\u30b7\u30f3\u30b0<\/p>

\u77f3\u68ee\u6d69\u4e00\u90ce<\/p>

\u751f\u547d\u91d1\u5c5e\u30c0\u30a4\u30ca\u30df\u30af\u30b9\u3000\u7b2c4\u7ae0\u3000\u7b2c3\u7bc0\u3001\u682a\u5f0f\u4f1a\u793e\u30a8\u30cc\u30fb\u30c6\u30a3\u30fc\u30fb\u30a8\u30b9 (2021)<\/p><\/td><\/tr>

11.<\/span><\/td>

Biological phase separation: cell biology meets biophysics<\/strong><\/p>

  1. Yoshizawa, R.S. Nozawa, T.Z. Jia, Tomohide Saio, E. Mori<\/li><\/ol>

    Biophys. Rev.,<\/em> 2020<\/strong>, 12, 519-539<\/p><\/td><\/tr>

12.<\/span><\/td>

Solution NMR spectroscopy for investigation of liquid-liquid phase separation<\/strong><\/p>

Tomohide Saio, M. Okumura, Y.Ho. Lee<\/p>

  1. Korean Mag. Res. Soc.<\/em>, 2020<\/strong>, 24, 47-52<\/li><\/ol><\/td><\/tr>
13.<\/span><\/td>

\u76f8\u5206\u96e2\u751f\u7269\u5b66:\u76f8\u5206\u96e2\u30e1\u30ac\u30cd\u306e\u30b9\u30b9\u30e1 \u691c\u51fa\u6280\u8853:\u5929\u7136\u5909\u6027\u30bf\u30f3\u30d1\u30af\u8cea\u306e\u69cb\u9020\u751f\u7269\u5b66<\/p>

\u5c0f\u7530\u9686, \u9f4b\u5c3e\u667a\u82f1<\/p>

\u751f\u7269\u5de5\u5b66\u4f1a\u8a8c, 2020<\/strong>, 98, 232-235<\/p><\/td><\/tr>

14.<\/span><\/td>

\u4e2d\u6027\u5b50\u6eb6\u6db2\u6563\u4e71-\u73fe\u5728\u30fb\u904e\u53bb\u30fb\u672a\u6765-<\/p>

\u6749\u5c71\u6b63\u660e, \u4e95\u4e0a\u502b\u592a\u90ce, \u4e2d\u5ddd\u6d0b, \u9f4b\u5c3e\u667a\u82f1<\/p>

\u6ce2\u7d0b, 2020<\/strong>, 30, 16-25<\/p><\/td><\/tr><\/tbody><\/table>

2019\u5e74\u5ea6<\/h2>
1.<\/span><\/td>

Dynamic assembly of protein disulfide isomerase in catalysis of oxidative folding<\/strong><\/p>

Masaki Okumura, Kentaro Noi, Shingo Kanemura, Misaki Kinoshita, Tomohide Saio, Yuichi Inoue, Takaaki Hikima, Shuji Akiyama, Teru Ogura, and Kenji Inaba<\/p>

Nat. Chem. Biol., 2019<\/b>, 15, 499-509<\/p><\/td><\/tr>

2.<\/span><\/td>

Accelerating structural life science by paramagnetic lanthanide probe methods<\/strong><\/p>

Tomohide Saio and Koichiro Ishimori<\/p>

Biochim. Biophys. Acta. Gen. Subj., in press.<\/p><\/td><\/tr>

3.<\/span><\/td>

\u7acb\u4f53\u69cb\u9020\u304b\u3089\u660e\u3089\u304b\u306b\u3059\u308b\u5206\u5b50\u30b7\u30e3\u30da\u30ed\u30f3\u306e\u4f5c\u7528\u6a5f\u5e8f<\/strong><\/p>

\u6589\u5c3e\u667a\u82f1, <\/span>\u77f3\u68ee \u6d69\u4e00\u90ce<\/p>

\u751f\u7269\u7269\u7406<\/span>, 2019<\/b>, 59, 197-201<\/p><\/td><\/tr>

4.<\/span><\/td>

\u30b3\u30ec\u30e9\u83cc\u306e\u30d8\u30e0\u7372\u5f97\u6a5f\u69cb\u3068\u751f\u5408\u6210\u7cfb<\/strong><\/p>

\u5185\u7530\u3000\u6bc5<\/p>

\u751f\u5316\u5b66<\/span>, 2019<\/b>, 91, 404-408<\/p><\/td><\/tr>

5.<\/span><\/td>

Specific heme binding to heme regulatory motifs in iron regulatory proteins and its functional significance<\/strong><\/p>

Yudai Nishitani, Hirotaka Okutani, Yukiko Takeda, Takeshi Uchida, Kazuhiro Iwai, and Koichiro Ishimori<\/p>

J. Inorg. Biochem., 2019<\/b>, 198, 110726 (11 pages)<\/p><\/td><\/tr>

6.\u00a0<\/span><\/td>

Structural basis for heme transfer reaction in heme uptake machinery from Corynebacteria<\/i><\/strong><\/p>

Norifumi Muraki, Chihiro Kitatsuji, Yasunori Okamoto, Takeshi Uchida, Koichiro Ishimori, and Shigetoshi Aono<\/p>

Chem. Commun., 2019<\/b>, 55, 13864-13867<\/p><\/td><\/tr>

7.<\/span><\/td>

Role of conserved arginine in the heme distal site of HutZ from Vibrio cholerae<\/i> in the heme degradation reaction<\/strong><\/p>

Takeshi Uchida, Nobuhiko Dojun, Kazuki Ota, Yukari Sekine, Yuina Nakamura, Sayaka Umetsu, and Koichiro Ishimori<\/p>

Arch. Biochem. Biophys., 2019<\/b>, 677, 108165 (15 pages)<\/p><\/td><\/tr>

8.<\/span><\/td>

A single mutation converts Alr5027 from cyanobacteria Nostoc<\/i> sp. PCC 7120 to a heme-binding protein with heme-degrading ability<\/strong><\/p>

Nobuhiko Dojun, Kazuyoshi Muranishi, Koichiro Ishimori, and Takeshi Uchida<\/p>

J. Inorg. Biochem, 2020<\/b>, 203, 110916 (11 pages)<\/p><\/td><\/tr><\/tbody><\/table>

2018\u5e74\u5ea6<\/h2>
1.<\/span><\/td>

Functional metagenomic approach to identify overlooked antibiotic resistance mutations in bacterial rRNA<\/strong><\/p>

Kentaro Miyazaki and Kei Kitahara<\/p>

Sci. Rep., 2018<\/b>, 8, 5179<\/p><\/td><\/tr>

2.<\/span><\/td>

Oligomerization of a molecular chaperone modulates its activity<\/strong><\/p>

Tomohide Saio, Soichiro Kawagoe, Koichiro Ishimori, and Charalampos G. Kalodimos<\/p>

eLife, 2018<\/b>, 7, e35731<\/p><\/td><\/tr>

3.<\/span><\/td>

Uncovering dehydration in cytochrome c<\/i> refolding from urea- and guanidine hydrochloride-denatured unfolded state by high pressure spectroscopy<\/strong><\/p>

Shohei Konno, Kentaro Doi, and Koichiro Ishimori<\/p>

Biophys. Physicobiol., 2019<\/b>, 16, 18-27<\/p><\/td><\/tr>

4.<\/span><\/td>

Subunit-subunit interactions play a key role in the heme-degradation reaction of HutZ from Vibrio cholerae<\/i><\/strong><\/p>

Takeshi Uchida, Kazuki Ota, Yukari Sekine, Nobuhiko Dojun, and Koichiro Ishimori<\/p>

Dalton. Trans., 2019<\/b>, 48, 3973-3983<\/p><\/td><\/tr>

5.<\/span><\/td>

Role of His63 in HutZ from Vibrio cholerae<\/i> in the heme degradation reaction and heme binding<\/strong><\/p>

Takeshi Uchida, Nobuhiko Dojun, Yukari Sekine, and Koichiro Ishimori<\/p>

Dalton. Trans., 2019<\/b>, 48, 5408-5416<\/p><\/td><\/tr><\/tbody><\/table>

2017\u5e74\u5ea6<\/h2>
1.<\/span><\/td>

HmuS from Yersinia pseudotuberculosis is a non-canonical heme-degrading enzyme to acquire iron from heme<\/strong><\/span><\/p>

Masato Onzuka, Yukari Sekine, Takeshi Uchida, Koichiro Ishimori, and Shin-ichi Ozaki<\/span><\/p>

Biochimica et Biophysica Acta (BBA)<\/em>\u00a01861, (2017), 1870-1878
<\/em><\/span><\/p><\/td><\/tr>

2.<\/span><\/td>

The Iron Chaperone Protein CyaY from Vibrio cholerae<\/em> is a Heme-Binding Protein<\/strong><\/span><\/p>

Takeshi Uchida, Noriyuki Kobayashi, Souichiro Muneta, and Koichiro Ishimori<\/span><\/p>

Biochemistry<\/em> 2017<\/strong>, 56, 2425<\/span><\/p><\/td><\/tr>

3.<\/span><\/td>

Heme iron coordination structure of heme transport protein HutB from Vibrio cholerae<\/em><\/span><\/strong><\/p>

Takeshi Uchida, Takumi Funamizu, Mariko Ogura, and Koichiro Ishimori<\/span><\/p>

Bull. Chem. Soc. Jpn.<\/em>, 2017<\/strong>, 90, 924-930<\/span><\/p><\/td><\/tr>

4.<\/span><\/td>

Heme Proximal Hydrogen Bonding between His170 and Asp132 Plays an Essential Role in the Heme Degradation Reaction by HutZ from\u00a0Vibrio cholerae<\/em><\/strong><\/span><\/p>

Takeshi Uchida, Nobuhiko Dojun, Yukari Sekine, and Koichiro Ishimori<\/span><\/p>

Biochemistry<\/em>\u00a02017<\/strong>, 56, 2723-2734<\/span><\/p><\/td><\/tr>

5.<\/span><\/td>

Reaction intermediates in the heme degradation reaction by HutZ from\u00a0Vibrio cholerae<\/i><\/strong><\/p>

Takeshi Uchida, Yukari Sekine, Nobuhiko Dojun,\u00a0Ariel Lewis,\u00a0Izumi Ishigami,\u00a0Toshitaka Matsui,\u00a0Syun-Ru Yeh,\u00a0 and \u00a0Koichiro Ishimori\u00a0<\/p>

Dalton Trans.,\u00a02017<\/b>, 46, 8104-8109\u00a0<\/p><\/td><\/tr>

6.\u00a0<\/span><\/td>

Heme binding to porphobilinogen deaminase from Vibrio cholerae<\/i> decelerates the formation of 1-hydroxymethylbilane<\/strong><\/p>

Takeshi Uchida, Takumi Funamizu, Minghao Chen, Yoshikazu Tanaka,and Koichiro Ishimori<\/span><\/p>

ACS Chem. Biol., 2018<\/b>, 13, 750-760<\/p><\/td><\/tr>

7.<\/span><\/td>

Redox-dependent axial ligand replacement and its functional significance in heme-bound iron regulatory proteins<\/strong><\/p>

Mariko Ogura, Ryosuke Endo, Haruto Ishikawa, Yukiko Takeda, Takeshi Uchida, Kazuhiro Iwai, Kazuo Kobayashi, and Koichiro Ishimori<\/span><\/p>

J. Inorg. Biochem., 2018<\/b>, 182, 238-248<\/p><\/td><\/tr>

8.<\/span><\/td>

Polyethylene Glycol Promotes Autoxidation of Cytochrome c<\/strong><\/p>

Wataru Sato, Takeshi Uchida, Tomohide Saio, and Koichiro Ishimori<\/span><\/p>

Biochim. Biophys. Acta., Gen. Subj., 2018<\/b>, 1862, 1339-1349<\/p><\/td><\/tr><\/tbody><\/table>

 <\/p>

2016\u5e74\u5ea6<\/h2>
1.<\/td>

Energetic Mechanism of Cytochrome\u00a0c\u00a0– Cytochrome\u00a0c\u00a0Oxidase Electron Transfer Complex Formation under Turnover Conditions Revealed by Mutational Effects and Docking Simulation
<\/strong><\/span><\/p>

Wataru Sato,\u00a0Seiji Hitaoka,\u00a0Kaoru Inoue,\u00a0Mizue Imai,\u00a0Tomohide Saio,Takeshi Uchida,\u00a0Kyoko Shinzawa-Itoh,\u00a0Shinya Yoshikawa,Kazunari Yoshizawa and\u00a0Koichiro Ishimori<\/span><\/p>

J. Biol. Chem.<\/em>,\u00a02016<\/strong>, 291, 15320
<\/em><\/span><\/p><\/td><\/tr>

2.<\/td>

Structural Characterization of Heme Environmental Mutants of CgHmuT that Shuttles Heme Molecules to Heme Transporter<\/strong>s<\/span><\/p>

Norifumi Muraki, Chihiro Kitatsuji, Mariko Ogura, Takeshi Uchida, Koichiro Ishimori, and Shigetoshi Aono<\/span><\/p>

Int. J. Mol. Sci.<\/em>\u00a02016<\/b>,\u00a017<\/em>(6), 829\u00a0<\/span><\/p><\/td><\/tr>

3.<\/td>

Redox-Dependent Dynamics in Heme-Bound Bacterial Iron Response Regulator (Irr) Protein<\/span><\/strong><\/p>

Kazuo Kobayashi, Megumi Nakagaki, Haruto Ishikawa, Kazuhiro Iwai, Mark R. O\u2019Brian and Koichiro Ishimori<\/span><\/p>

Biochemistry<\/i>,\u00a02016<\/strong>,\u00a055(29), 4047<\/span><\/p><\/td><\/tr>

4.<\/td>

Energetic basis on interactions between ferredoxin and ferredoxin NADP+<\/sup>\u00a0reductase at varying physiological conditions<\/span><\/strong><\/p>

Misaki Kinoshita, Ju Yaen Kim, Satoshi Kume, Yuxi Lin, K. Hun Mok, Yosky Kataoka, Koichiro Ishimori, Natalia Markova, Genji Kurisu, Toshiharu Hase, Young-Ho Lee<\/span><\/p>

Biochem. Biophys. Res. Commun.<\/em>, 2017<\/strong>, 428, 909<\/span><\/p><\/td><\/tr>

5.<\/td>

Dual role of the active-center cysteine in human peroxiredoxin 1: Peroxidase activity and heme binding<\/span><\/strong><\/p>

Yuta Watanabe,\u00a0Koichiro Ishimori,\u00a0Takeshi Uchida<\/span><\/p>

Biochem. Biophys. Res. Commun.,<\/em>\u00a02017<\/strong>, 483, 930\u00a0<\/span><\/p><\/td><\/tr>

6.<\/td>

Iron Chelators Inhibit the Heme-Degradation Reaction by HutZ from\u00a0Vibrio cholerae<\/em><\/span><\/strong><\/p>

Nobuhiko Dojun,\u00a0\u00a0Yukari Sekine, \u00a0Koichiro Ishimori\u00a0and\u00a0Takeshi Uchida<\/span><\/p>

Dalton Trans.<\/i>, 2017,46,<\/strong> 5147\u00a0<\/span><\/p><\/td><\/tr><\/tbody><\/table>

 <\/p>

 <\/p>

2015\u5e74\u5ea6<\/h2>
1.<\/span><\/td>

A dye-decolorizing peroxidase from Vibrio cholerae<\/span><\/strong><\/p>

T. Uchida, M. Sasaki, Y. Tanaka, K. Ishimori<\/span><\/p>

Biochemistry<\/em>,\u00a02015<\/strong>, 54, 6610
<\/em><\/span><\/p><\/td><\/tr>

2.<\/span><\/td>

Investigation of the redox-dependent modulation of structure and dynamics in human cytochrome\u00a0c<\/em><\/span><\/strong><\/p>

M. Imai,\u00a0T. Saio,\u00a0H. Kumeta,\u00a0T. Uchida,\u00a0F. Inagaki,\u00a0K. Ishimori<\/span><\/p>

Biochem. Biophys. Res. Commun.<\/em>,\u00a02016<\/strong>, 469, 978\u00a0<\/span><\/p><\/td><\/tr>

3.<\/span><\/td>

Conformational disorder of the most immature Cu,Zn-superoxide dismutase leading to amyotrophic lateral sclerosis<\/span><\/strong><\/p>

Y. Furukawa,\u00a0I. Anzai,\u00a0S. Akiyama,\u00a0M. Imai, F. J. C. Cruz,\u00a0T. Saio,\u00a0K. Nagasawa,\u00a0T. Nomura, K. Ishimori<\/span><\/p>

J. Biol. Chem.<\/em>, 2016<\/strong>,\u00a0291, 4144.<\/span><\/p>

DOI: 10.1074\/jbc.M115.683763<\/span><\/p><\/td><\/tr>

4.<\/span><\/td>

Protein oxidation mediated by heme-induced active site conversion specific for heme-regulated transcription factor, iron response regulator<\/span><\/strong><\/p>

C. Kitatsuji,\u00a0K. Izumi,\u00a0S. Nambu,\u00a0M. Kurogochi,\u00a0T. Uchida,\u00a0S. Nishimura,\u00a0K. Iwai,\u00a0M. R. O\u2019Brian,\u00a0M. Ikeda-Saito, K. Ishimori<\/span><\/p>

Sci. Rep.<\/em>,\u00a02016<\/strong>, 6:18703, 1<\/span><\/p>

\u00a0<\/span><\/p><\/td><\/tr>

5.<\/span><\/td>

Cytoplasmic heme-binding protein (HutX) from Vibrio cholerae is an intracellular heme transport protein for the heme-degrading enzyme, HutZ<\/strong><\/span>\u00a0<\/p>

Yukari Sekine, Takehito Tanzawa, Yoshikazu Tanaka, Koichiro Ishimori, Takeshi Uchida<\/span><\/p>

Biochemistry,<\/em><\/span>\u00a02016<\/strong>, 55(6), 884<\/span><\/p>

DOI:\u00a010.1021\/acs.biochem.5b01273<\/span><\/p>

 <\/p><\/td><\/tr>

6.<\/span><\/td>

Amorphous aggregation of cytochrome\u00a0c<\/i>\u00a0with inherently low amyloidogenicity is characterized by the metastability of supersaturation and the phase diagram<\/strong><\/span><\/p>

Yuxi Lin,\u00a0J\u00f3zsef Kardos,\u00a0Mizue Imai,\u00a0Tatsuya Ikenoue,\u00a0Misaki Kinoshita,\u00a0Toshihiko Sugiki,\u00a0Koichiro Ishimori,Yuji Goto, and\u00a0Young-Ho Lee<\/span><\/p>

Langmuir,<\/em> 2016<\/strong>,\u00a032(8), 2010<\/span><\/p><\/td><\/tr>

7.<\/span><\/td>

Haem-dependent dimerization of PGRMC1\/Sigma-2 receptor facilitates cancer proliferation and chemoresistance<\/strong><\/span><\/p>

Yasuaki Kabe,Takanori Nakane,Ikko Koike,Tatsuya Yamamoto,Yuki Sugiura,Erisa Harada,Kenji Sugase,Tatsuro Shimamura,Mitsuyo Ohmura,Kazumi Muraoka,Ayumi Yamamoto,Takeshi Uchida,So Iwata,Yuki Yamaguchi,Elena Krayukhina,Masanori Noda,Hiroshi Handa,Koichiro Ishimori,Susumu Uchiyama,Takuya Kobayashi&\u00a0Makoto Suematsu<\/span><\/p>

Nature Communications, 2016,<\/strong> 7,\u00a011030<\/span><\/p><\/td><\/tr><\/tbody><\/table>

\u00a0<\/span><\/p>

\u00a0<\/span><\/p>

2014\u5e74<\/span><\/h2>
1.<\/span><\/td>

Spectroscopic studies on HasA from Yersinia pseudotuberculosis<\/em><\/span><\/strong><\/p>

S. Ozaki, T. Sato, Y. Sekine, C. T. Migita, T. Uchida and K. Ishimori<\/span><\/p>

J. Inorg. Biochem.<\/em>, 2014<\/strong>, 138, 31<\/span><\/p><\/td><\/tr>

2.<\/span><\/td>

Molecular Mechanism for Heme-Mediated Inhibition\u00a0of 5-Aminolevulinic Acid Synthase 1<\/span><\/strong><\/p>

C. Kitatsuji, M. Ogura, T. Uchida, K. Ishimori and S. Aono<\/span><\/p>

Bull. Chem. Soc. Jpn.<\/em>, 2014<\/strong>, 87, 997<\/span><\/p><\/td><\/tr>

3.<\/span><\/td>

Heme-binding properties of HupD functioning as a substrate-binding protein in a <\/span>heme-uptake ABC-transporter system in Listeria monocytogenes<\/span><\/strong><\/p>

Y. Okamoto, H. Sawai, M. Ogura, T. Uchida, K. Ishimori, T. Hayashi and S. Aono<\/span><\/p>

Bull. Chem. Soc. Jpn.<\/em>,<\/span><\/p><\/td><\/tr>

4.<\/span><\/td>

Unique Heme Environmental Structures in Heme-regulated Proteins Using <\/span>Heme as the Signaling Molecule<\/span><\/strong><\/p>

K. Ishimori and Y. Watanabe<\/span><\/p>

Chem. Lett.<\/em>, 2014<\/strong>, 43, 1680<\/span><\/p>

\uff08Chem. Lett. \u8a8c\u306e\u8868\u7d19\u3092\u98fe\u308a\u307e\u3057\u305f\uff01\uff09<\/span><\/strong><\/span><\/p><\/td><\/tr><\/tbody><\/table>

\u00a0<\/span><\/p>

\u00a0<\/span><\/p>

2013\u5e74<\/span><\/h2>
1.<\/span><\/td>

Sequence and Temperature Dependence of the End-to-End Collision Dynamics of Single-Stranded DNA<\/span><\/strong><\/p>

T. Uzawa, T. Isoshima, Y. Ito, K. Ishimori, D. E. Makarov and K. W. Plaxco<\/span><\/p>

Biophys. J.<\/em>, 2013<\/strong>, 104, 2485<\/span><\/p><\/td><\/tr><\/tbody><\/table>

\u00a0<\/span><\/p>

2012\u5e74<\/span><\/h2>
1.<\/span><\/td>

Effects of the bHLH Domain on Axial Coordination of heme in the PAS-A Domain of Neuronal PAS Domain Protein 2 (NPAS2): Conversion from His119\/Cys170 Coordination to His119\/His171 Coordination<\/span><\/strong><\/p>

T. Uchida, I. Sagami, T. Shimizu, K. Ishimori, and T. Kitagawa<\/span><\/p>

J. Inorg. Biochem.<\/em>, 2012<\/strong>, 108, 188<\/span><\/p><\/td><\/tr>

2.<\/span><\/td>

The Structural Investigation on Small Methane Clusters Described by Two Different Potentials<\/span><\/strong><\/p>

H. Takeuchi<\/span><\/p>

Comput. Theor. Chem.<\/em>, 2012<\/strong>, 986, 48<\/span><\/p><\/td><\/tr>

3.<\/span><\/td>

Function of Heme Regulatory Motif in the Oxidative Modification for Transcriptional Regulation <\/span><\/strong><\/p>

T. Tatsukawa, T. Uchida, and K. Ishimori<\/span><\/p>

Peptide Sci.<\/em>, 2012<\/strong>, 2011, 191<\/span><\/p><\/td><\/tr>

4.<\/span><\/td>

A Heme Degradation Enzyme, HutZ, from Vibrio\u00a0<\/span><\/strong>cholerae<\/b><\/span><\/p>

T. Uchida, Y. Sekine, T. Matsui, M. Ikeda-Saito, and K. Ishimori<\/span><\/p>

Chem. Commun.<\/em>, 2012<\/strong>, 48, 6741<\/span><\/p><\/td><\/tr>

5.<\/span><\/td>

Structural Features of Small Benzene Clusters (C6H6)n (n \u2264 30) As Investigated with the All-Atom OPLS Potential<\/span><\/strong><\/p>

H. Takeuchi<\/span><\/p>

J. Phys. Chem. A<\/em>, 2012<\/strong>, 116, 10172<\/span><\/p><\/td><\/tr>

6.<\/span><\/td>

The Structural Investigation on Small Methane Clusters Described by Two Different Potentials<\/strong><\/span><\/p>

H. Takeuchi<\/span><\/p>

Comput. Theor. Chem.<\/em>, 2012<\/strong>, 986, 48<\/span><\/p><\/td><\/tr><\/tbody><\/table>

\u00a0<\/span><\/p>

2011\u5e74<\/span><\/h2>
1.<\/span><\/td>

Probing Phenylalanine Environments in Oligomeric Structures with Pentafluorophenylalanine and Cyclohexylalanine<\/span><\/strong><\/p>

T. Nomura, R. Kamada, I. Ito, K. Sakamoto, Y. Chuman, K. Ishimori, Y. Shimohigashi, K. Sakaguchi<\/span><\/p>

Biopolymer, 2011<\/strong>, 95, 410<\/span><\/p><\/td><\/tr>

2.<\/span><\/td>

A Theoretical Investigation on Optimal Structures of Ethane Clusters (C2H6)n with n \u2264 25 and Their Building-up Principle<\/span><\/strong><\/p>

H. Takeuchi<\/span><\/p>

J. Comput. Chem., 2011<\/strong>, 32, 1345<\/span><\/p><\/td><\/tr>

3.<\/span><\/td>

Unusual Heme Binding in the Bacterial Iron Response Regulator Protein (Irr): Spectral Characterization of Heme Binding to Heme Regulatory Motif<\/span><\/strong><\/p>

H. Ishikawa, M. Nakagaki, A. Bamba, T. Uchida, H. Hori, M. R. O\u2019Brian, K. Iwai, and K. Ishimori<\/span><\/p>

Biochemistry, 2011<\/strong>, 50, 1016<\/span><\/p><\/td><\/tr>

4.<\/span><\/td>

NMR Basis for Interprotein Electron Transfer Gating between Cytochrome c \u2013 Cytochrome c Oxidase<\/strong>\u00a0<\/span><\/p>

K. Sakamoto, M. Kamiya, M. Imai, K. Shinzawa-Ito, T. Uchida, K. Kawano, S. Yoshikawa, and K. Ishimori<\/span><\/p>

Proc. Natl. Acad. Sci. U.S.A., 2011<\/strong>, 108, 12271<\/span><\/p><\/td><\/tr>

5.<\/span><\/td>

Identification and Functional and Spectral Characterizations of a Novel Globin-Coupled Histidine Kinase from Anaeromixobacter sp. Fw109-5<\/span><\/strong><\/p>

K. Kitanishi, K. Kobayashi, T. Uchida, K. Ishimori, J. Igarashi, and T. Shimizu<\/span><\/p>

J. Biol. Chem., 2011<\/strong>, 286, 35522<\/span><\/p><\/td><\/tr>

6.<\/span><\/td>

Theoretical Investigation on Structural Properties of Ethylene Clusters (C2H4)n (n \u2264 25)<\/span><\/strong><\/p>

H. Takeuchi<\/span><\/p>

Comput.Theor. Chem., 2011<\/strong>, 970, 48<\/span><\/p><\/td><\/tr><\/tbody><\/table>

\u00a0<\/span><\/p>

2010\u5e74<\/span><\/h2>
1.<\/span><\/td>

Molecular Oxygen Regulates the Enzymatic Activity of a Heme-containing Diguanylate Cyclase (HemDGC) for the Synthesis of Cyclic Di-GMP<\/span>
H. Sawai, S. Yoshioka, T. Uchida, M. Hyodo, Y. Hayakawa, K. Ishimori, and S. Aono<\/span>
Biochimica et Biophysica Acta, Vol. 1804, No. 1, 166-172 (2010).<\/span><\/p><\/td><\/tr>

2.<\/span><\/td>

Global Minimum Geometries of Acetylene Clusters (HCCH)n with n \u2264 55 Obtained by a Heuristic Method Combined with Geometrical Perturbations<\/span>
H. Takeuchi<\/span>
J. Comput. Chem., Vol. 31, No. 8, 1699-1706 (2010).<\/span><\/p><\/td><\/tr>

3.<\/span><\/td>

Redox-controlled Backbone Dynamics of Human Cytochrome c Revealed by 15N NMR Relaxation Measurements<\/span>
K. Sakamoto, M. Kamiya, T. Uchida, K. Kawano, and K. Ishimori<\/span>
Biochem. Biophys. Res. Commun., Vol. 398, 231-236 (2010).<\/span><\/p><\/td><\/tr>

4.<\/span><\/td>

Global Minimum Geometries of Acetylene Clusters (HCCH)n with n \u2264 55 Obtained by a Heuristic Method Combined with Geometrical Perturbations<\/span>
H. Takeuchi<\/span>
J. Comput. Chem., Vol. 31, 1699-1706 (2010).<\/span><\/p><\/td><\/tr>

5.<\/span><\/td>

Molecular Oxygen Regulates the Enzymatic Activity of a Heme-containing Diguanylate Cyclase (HemDGC) for the Synthesis of Cyclic di-GMP<\/span>
H. Sawai, S. Yoshioka, T. Uchida, M. Hyodo, Y. Hayakawa, K. Ishimori, and S.<\/span>
Aono <\/span>
Biochim. Biophys. Acta, Vol. 1804, 166-172 (2010).<\/span><\/p><\/td><\/tr><\/tbody><\/table>

\u00a0<\/span><\/p>

2009\u5e74<\/span><\/h2>
1.<\/span><\/td>

Optical Manipulation of Proteins in Aqueous Solution<\/span>
Y. Tsuboi, T. Shoji, M. Nishino, S. Masuda, K. Ishimori, and N. Kitamura<\/span>
App. Sur. Sci., Vol. 255, 9906\u20139908 (2009)<\/span><\/p><\/td><\/tr><\/tbody><\/table>","protected":false},"excerpt":{"rendered":"

2022\u5e74\u5ea61.Heme binding to cold shock protein D, CspD, from Vibrio choleraeDayeon Nam, Wataru Motegi, Koichiro Is […]<\/p>\n","protected":false},"author":1,"featured_media":0,"parent":55,"menu_order":10,"comment_status":"closed","ping_status":"closed","template":"","meta":{"footnotes":""},"_links":{"self":[{"href":"https:\/\/wwwchem.sci.hokudai.ac.jp\/~stchem\/wp-json\/wp\/v2\/pages\/93"}],"collection":[{"href":"https:\/\/wwwchem.sci.hokudai.ac.jp\/~stchem\/wp-json\/wp\/v2\/pages"}],"about":[{"href":"https:\/\/wwwchem.sci.hokudai.ac.jp\/~stchem\/wp-json\/wp\/v2\/types\/page"}],"author":[{"embeddable":true,"href":"https:\/\/wwwchem.sci.hokudai.ac.jp\/~stchem\/wp-json\/wp\/v2\/users\/1"}],"replies":[{"embeddable":true,"href":"https:\/\/wwwchem.sci.hokudai.ac.jp\/~stchem\/wp-json\/wp\/v2\/comments?post=93"}],"version-history":[{"count":35,"href":"https:\/\/wwwchem.sci.hokudai.ac.jp\/~stchem\/wp-json\/wp\/v2\/pages\/93\/revisions"}],"predecessor-version":[{"id":1833,"href":"https:\/\/wwwchem.sci.hokudai.ac.jp\/~stchem\/wp-json\/wp\/v2\/pages\/93\/revisions\/1833"}],"up":[{"embeddable":true,"href":"https:\/\/wwwchem.sci.hokudai.ac.jp\/~stchem\/wp-json\/wp\/v2\/pages\/55"}],"wp:attachment":[{"href":"https:\/\/wwwchem.sci.hokudai.ac.jp\/~stchem\/wp-json\/wp\/v2\/media?parent=93"}],"curies":[{"name":"wp","href":"https:\/\/api.w.org\/{rel}","templated":true}]}}