{"id":60,"date":"2015-12-08T11:52:17","date_gmt":"2015-12-08T02:52:17","guid":{"rendered":"https:\/\/www2.tagen.tohoku.ac.jp\/lab\/takahashi-s\/?page_id=60"},"modified":"2025-01-22T11:13:23","modified_gmt":"2025-01-22T02:13:23","slug":"2011%e5%b9%b4%ef%bd%9e2016%e5%b9%b4","status":"publish","type":"page","link":"https:\/\/www2.tagen.tohoku.ac.jp\/lab\/takahashi-s\/achievements\/2011%e5%b9%b4%ef%bd%9e2016%e5%b9%b4\/","title":{"rendered":"2011\u5e74\uff5e2020\u5e74"},"content":{"rendered":"<h2 style=\"text-align: center\">\u00a0<strong>2020<\/strong><\/h2>\n<ul>\n<li><b>Subekti D. R. G.<\/b>, *<b>Kamagata K.<\/b>,\u00a0<span lang=\"DE\">\u201cThe disordered DNA-binding domain of p53 is indispensable for forming an encounter complex to and jumping along DNA<\/span><span lang=\"DE\">\u201d<\/span><span lang=\"EN-US\">,\u00a0<\/span><span lang=\"EN-US\"><i>Biochem. Biophys. Res. Commun.<\/i>, 534<\/span><span lang=\"DE\"><span lang=\"DE\"><span lang=\"DE\">, 21-26, 2021.<\/span><\/span><\/span><\/li>\n<li>*<b>Kamagata K<\/b>., Ouchi K., Tan C., Mano E., Mandali S., <b>Wu Y<\/b>., Takada S., <b>Takahashi S<\/b>., *Johnson R. C.,<br \/>\n<span lang=\"DE\">&#8220;<span lang=\"DE\">The HMGB chromatin protein Nhp6A can bypass obstacles when traveling on DNA<\/span><span lang=\"DE\">&#8220;<\/span><span lang=\"DE\">, Nucleic Acids Research,<\/span>\u00a048, 10820-10831, 2020. \u00a0\u00a0<\/span><\/li>\n<li>Nobuo Shimamoto, Mikito Toda, Shigetoshi Nara, Tamiki Komatsuzaki, <b>Kiyoto Kamagata<\/b>, Takashi Kinebuchi &amp; Tomizawa<br \/>\n<span lang=\"DE\">\u201cDependence of DNA length on binding affinity between TrpR and trpO of DNA<\/span><span lang=\"DE\">\u201d<\/span><span lang=\"EN-US\">,\u00a0<i>Scientific Reports<\/i>,\u00a0<\/span><span lang=\"DE\"><span lang=\"DE\">10, 15624, 2020.<\/span><\/span><\/li>\n<li><b>Subekti D. R. G., Murata A., Itoh Y., Takahashi S., Kamagata K<\/b>.,<span lang=\"DE\">\u201c<\/span><span lang=\"EN-US\">Transient binding and jumping dynamics of p53 along DNA revealed by sub-millisecond resolved single-molecule fluorescence tracking<\/span><span lang=\"DE\">\u201d<\/span><span lang=\"EN-US\">,\u00a0<i>Scientific Reports<\/i>,\u00a0<\/span><span lang=\"DE\"><span lang=\"DE\"><span lang=\"DE\">10, 13697, 2020.<\/span><\/span><\/span><\/li>\n<li>Muraoka T, Noguchi D, Kasai RS, Sato K, Sasaki R, Tabata KV, Ekimoto T, Ikeguchi M,<b>\u00a0Kamagata K<\/b>, Hoshino N, Noji H, Akutagawa T, Ichimura K, Kinbara K.,&#8221;A synthetic ion channel with anisotropic ligand response.&#8221;,\u00a0Nat Commun. 2020 Jun 10;11(1):2924.<\/li>\n<li>\n<div class=\"gmail_default\"><strong>Kamagata K*, \u00a0Itoh Y, Subekti DRG<\/strong><\/div>\n<div class=\"gmail_default\">\n<p><span style=\"color: #000000\">How p53 Molecules Solve the Target DNA Search Problem: A Review\u00a0<\/span><em>int. J. Mol. Sci.\u00a02020,\u00a021(3), 1031<\/em><\/p>\n<p>&nbsp;<\/p>\n<\/div>\n<\/li>\n<li>\n<div class=\"gmail_default\"><strong>Kiyoto Kamagata*, Saori Kanbayashi, Masaya Honda, Yuji Itoh, Hiroto Takahashi,<\/strong> Tomoshi Kameda, Fumi Nagatsugi, and <strong>Satoshi Takahashi<\/strong>\u201cLiquid-like droplet formation by tumor suppressor p53 induced by multivalent electrostatic interactions between two disordered domains\u201d\u00a0<em>Scientific Reports<\/em>\u00a010, 580 (2020)<\/div>\n<\/li>\n<\/ul>\n<h2 style=\"text-align: center\"><span style=\"font-size: 16px\">\u00a0<\/span><strong>2019<\/strong><span style=\"font-size: 16px\">\u00a0<\/span><\/h2>\n<ul>\n<li><strong>Kiyoto Kamagata, Eriko Mano, Yuji Itoh,<\/strong>, Takuro Wakamoto, Ryo Kitahara, <strong>Saori Kanbayashi, Hiroto Takahashi, Agato Murata,<\/strong> Tomoshi Kameda,\u201cRational design using sequence information only produces a peptide that binds to the intrinsically disordered region of \u00a0p53\u201d, <em>Scientific Reports<\/em>, 9,8584 (2019)<\/li>\n<\/ul>\n<h2 style=\"text-align: center\">\u00a0<strong>2018<\/strong><\/h2>\n<ul>\n<li><strong>Hiroyuki Oikawa,\u00a0 Takumi Takahashi,\u00a0 Supawich Kamonprasertsuk\u00a0 and\u00a0 Satoshi Takahashi, <\/strong>&#8220;Microsecond resolved single-molecule FRET time series measurements based on the line confocal optical system combined with hybrid photodetectors&#8221;<strong>,\u00a0<\/strong><em>Phys. Chem. Chem. Phys.<\/em>, 2018,\u00a0<strong>20<\/strong>, 3277-3285 DOI:\u00a0<a href=\"https:\/\/doi.org\/10.1039\/C7CP06268K\" target=\"_blank\" rel=\"noopener\">10.1039\/C7CP06268K<\/a><\/li>\n<li><strong>Kamagata K., Mano E., Ouchi K., Kanbayashi S.,<\/strong> Johnson R.C.,\u00a0\u201cHigh Free-Energy Barrier of 1D Diffusion Along DNA by Architectural DNA-Binding Proteins\u201d, <em>J.Mol.Biol<\/em>., 430,655-667.(2018)<\/li>\n<li><strong>Satoshi Takahashi<\/strong>, <strong>Aya Yoshida<\/strong>, <strong>Hiroyuki Oikawa<\/strong>, \u201cHypothesis: structural heterogeneity of the unfolded proteins originating from the coupling of the local clusters and the long-range distance distribution\u201d, Biophysical Reviews, 10(2), 363-373, 2018.<\/li>\n<li><strong>Itoh Y.,Murata A., \u00a0*Takahashi S., *Kamagata K<\/strong>., \u201cIntrinsically disordered domain of tumor suppressor p53 facilitates target search by ultrafast transfer between different DNA strands\u201d, <em>Nucleic Acid Res<\/em>., 46, 7261-7269, (2018)<\/li>\n<\/ul>\n<h2 style=\"text-align: center\">\u00a0<strong>2017<\/strong><\/h2>\n<ul>\n<li>Kazumasa Sakurai, Masanori Yagi, Tsuyoshi Konuma, <strong>Satoshi Takahashi<\/strong>, Chiaki Nishimura, Yuji Goto, \u201cNon-Native \u03b1-Helices in the Initial Folding Intermediate Facilitate the Ordered Assembly of the \u03b2-Barrel in \u03b2-Lactoglobulin\u201d, Biochemistry, 56(36), 4799-4807, 2017.<\/li>\n<li><strong>Subekti D. R. G., Murata A., Itoh Y., Fukuchi S., Takahashi H., Kanbayashi S., *Takahashi S., *Kamagata K<\/strong>., \u201cDisordered linker in p53 participates in non-specific binding to and 1D sliding along DNA revealed by single-molecule fluorescence measurements\u201d, <i>Biochemistry,\u00a0<\/i><span lang=\"EN-US\">56 (32), 4134-4144, (<\/span>2017\uff09DOI: 10.1021\/acs.biochem.7b00292<\/li>\n<li><strong>Agato Murata, Yuji Itoh, Eriko Mano, Saori Kanbayashi, Chihiro Igarashi, Hiroto Takahashi, \u00a0Satoshi Takahashi, Kiyoto Kamagata<\/strong>&#8220;One-Dimensional Search Dynamics of Tumor Suppressor p53 Regulated by a Disordered C-Terminal Domain&#8221;, <em>Biophysical<\/em>\u00a0<em>Journal, Vol.112, Issue 11, <\/em>2301-2314\uff082017\uff09<\/li>\n<li>Takuhiro Otosu, Kunihiko Ishii, <strong>Hiroyuki Oikawa<\/strong>, Munehito Arai, <strong>Satoshi Takahashi<\/strong>, and Tahei Tahara, &#8220;Highly Heterogeneous nature of the Native and Unfolded States of the B Domain of Protein A Revealed by Two-Dimensional Fluorescence Lifetime Correlation Spectroscopy&#8221;,<em> J. Phys. Chem.B<\/em>,121(22), 5463-5473\uff082017\uff09<\/li>\n<li>Daiki Tatsumi, Kei Nanatani, Yuto Koike, <strong>Kiyoto Kamagata, Satoshi Takahashi<\/strong>, Ayumu Konno, Tadaomi Furuta, Minoru Sakurai, Nobuyuki Uozumi, &#8220;Probing native metal ion association sites through quenching of fluorophores in the nucleotide-binding domains of the ABC transporter MsbA&#8221;, <em>Biochemical Journal<\/em>,474,12,1993-2007\uff082017\uff09<\/li>\n<li><strong>Kiyoto K<\/strong><strong>amagata, Agato Murata, Yuji Itoh, Satoshi Takahashi,\u00a0<\/strong>&#8220;Characterization of \u00a0facilitated diffusion of tumor suppressor p53 along DNA using single-molecule fluorescence imaging&#8221;,\u00a0<em>Journal of Photochemistry and Photobiology C: Photochemistry Reviews, <\/em>30,36-50\uff082017\uff09\u3000<a id=\"ddDoi\" class=\"S_C_ddDoi\" href=\"http:\/\/dx.doi.org\/10.1016\/j.jphotochemrev.2017.01.004\" target=\"doilink\" rel=\"noopener\">10.1016\/j.jphotochemrev.2017.01.004<\/a><\/li>\n<li><span lang=\"EN-US\"><span lang=\"EN-US\">Masakazu Furuta, Tomotsumi Fujisawa, Hiroyasu Urago, Takahiro Eguchi, Tkahito Shingae,<strong> Satoshi Takahashi, <\/strong>Ewan W. Blanch and Masashi Unno.<sup>\u00a0<\/sup>\u201cRaman optical activity of tetra-alanine in the poly(L-proline) II type peptide conformation<\/span><\/span><span lang=\"EN-US\"><span lang=\"EN-US\"><span lang=\"EN-US\">\u201d,<em>Phys.Chem.Chem.Phys<\/em>., 19, 2078-2086\uff082017\uff0910.1039\/c6cp07828a<br \/>\n<\/span><\/span><\/span><span lang=\"EN-US\"><br \/>\n<\/span><\/li>\n<li><strong>Igarashi C.,\u00a0Murata A.,\u00a0Itoh Y.,\u00a0Subekti D. R. G., Takahashi S., Kamagata K.,<\/strong> &#8220;DNA garden:<span lang=\"EN-US\">A simple method for producing arrays of stretchable DNA for single-molecule fluorescence imaging of DNA binding proteins\u201d,B<\/span><span lang=\"EN-US\"><em>ull. Chem. Soc. Jpn<\/em>., 90, 34-43\uff082017\uff09 \u00a0 \u00a010.1246\/bcsj.20160298<\/span><\/li>\n<\/ul>\n<h2 style=\"text-align: center\">\u00a0<strong>2016<\/strong><\/h2>\n<ul>\n<li><strong>Masataka Saito<\/strong>, <strong>Supawich Kamonprasertsuk<\/strong>, Satomi Suzuki, Kei Nanatani, <strong>Hiroyuki Oikawa<\/strong>, Keiichiro Kushiro, Madoka Takai, Po-Ting Chen, Eric Hsin-Liang Chen, Rita Pei-Yeh Chen, and <strong>Satoshi Takahashi,\u00a0<\/strong>&#8220;Significant Heterogeneity and Slow Dynamics of the Unfolded Ubiquitin Detected by Confocal Method of Single-Molecule Fluorescence Spectroscopy&#8221;<em> J. Phys. Chem. B,\u00a0<\/em>120 (34), 8818-8829\uff082016), doi<strong>:\u00a0<\/strong>10.1021\/acs.jpcb.6b05481<\/li>\n<li><strong>Yuji Itoh, Agato Murata<\/strong>, Seiji Sakamoto, Kei Nanatani, Takehiko Wada, <strong>Satoshi Takahashi, Kiyoto Kamagata<\/strong>,\u00a0&#8220;Activation of p53 Facilitates the Target Search in DNA by Enhancing the Target Recognition Probability&#8221;, <em>J. Mol. Biol.<\/em>\u00a0,\u00a0428, 2916\u20132930(2016),\u00a0<a id=\"ddDoi\" class=\"S_C_ddDoi\" href=\"http:\/\/dx.doi.org\/10.1016\/j.jmb.2016.06.001\" target=\"doilink\" rel=\"noopener\">doi:10.1016\/j.jmb.2016.06.001<\/a><\/li>\n<li>Toshitaka Matsui, Shusuke Nambu, Celia W. Goulding,\u00a0<strong>Satoshi Takahashi<\/strong>, Hiroshi Fujii, and Masao Ikeda-Saito,\u00a0&#8220;Unique coupling of mono- and dioxygenase chemistries in a single active site promotes heme degradation&#8221; <em>Proc. Natl. Acad. Sci. USA,\u00a0<\/em>113, 3779\u20133784(2016)<\/li>\n<\/ul>\n<h2 style=\"text-align: center\">\u00a0<strong>2015\u00a0<\/strong><\/h2>\n<ul>\n<li>Tsuyoshi Konuma, Kazumasa Sakurai, Masanori Yagi, Yuji Goto, Teturo Fujisawa, <strong>Satoshi Takahashi <\/strong>&#8220;Highly Collapsed Conformation of the Initial Folding Intermediates of \u03b2-Lactoglobulin with Non-Native \u03b1-Helix&#8221; <em>Journal of Molecular Biology<\/em>, 427(19):3158-65 (2015)<\/li>\n<li><strong>Agato Murata<\/strong>, <strong>Yuji Ito<\/strong>, Risa Kashima, <strong>Saori Kanbayashi<\/strong>, Kei Nanatani, <strong>Chihiro Igarashi<\/strong>, Masaki Okumura, Kenji Inaba, Takashi Tokino, <strong>Satoshi Takahashi<\/strong>, <strong>Kiyoto Kamagata<\/strong> &#8220;One-dimensional sliding of p53 along DNA is accelerated in the presence of Ca2+ or Mg2+ at millimolar concentrations&#8221;<br \/>\n<em>Journal of Molecular Biology,<\/em>Volume 427, Issue 16, 14 August, 2663-2678 (2015\uff09<\/li>\n<li><strong>Hiroyuki Oikawa, Kiyoto Kamagata<\/strong> ,Munehito Arai, and <strong>Satoshi Takahashi<\/strong> &#8220;Complexity of the Folding Transition of the B domain of Protein A Revealed by the High-Speed Tracking of Single-Molecule Fluorescence Time Series&#8221; <em>The Journal of Physical Chemistry B, <\/em>119(20), 6081-6091<em>\u00a0<\/em>(2015)<\/li>\n<\/ul>\n<h2 style=\"text-align: center\">\u00a0<strong>2013<\/strong><\/h2>\n<ul>\n<li>I.I. Rze\u017anicka, H.Horino, N. Kikkawa, S. Sakaguchi, A.Morita, <strong>S. Takahashi<\/strong>, T. Komeda,\u00a0H. Fukumura, T. Yamada, M. Kawai &#8220;Tip-enhanced Raman spectroscopy of 4,4\u2032-bipyridine and 4,4\u2032-bipyridine N,N&#8217;-dioxide\u00a0adsorbed on gold thin films&#8221;<em> Surface Science<\/em> (2013)<\/li>\n<li>Atsuko Deguchi, Takeshi Tomita,Tsutomu Omori, Akiko Komatsu, Umeharu Ohto, <strong>Satoshi Takahashi,<\/strong> Natsuko Tanimura, Sachiko Akashi-Takamura, Kensuke Miyake and Yoshiro Maru &#8220;Serum Amyloid A3 Binds MD-2 To Activate p38 and NF-kB Pathways in a MyD88-Dependent Manner&#8221;<em> J. Immunology <\/em>\uff082013\uff09<\/li>\n<li><strong>Hiroyuki Oikawa<\/strong>, <strong>Yuta Suzuki, Masataka Saito, Kiyoto Kamagata<\/strong>, Munehiro Arai and<strong> Satoshi Takahashi<\/strong> &#8220;Microsecond dynamics of an unfolded protein by a line confocal tracking of single molecule fluorescence&#8221; Scientific Reports 3, Article number:2151, doi:10.1038\/srep02151<\/li>\n<li>Shusuke Nambu, Toshitaka Matsui, Celia W. Goulding, <b>Satoshi Takahashi, <\/b>and Masao Ikeda-Saito &#8220;A New Way to Degrade Heme -THE MYCOBACTERIUM TUBERCULOSIS ENZYME MhuD CATALYZES HEME DEGRADATION\u00a0WITHOUT GENERATING CO*-&#8220;\u3000<em>JBC <\/em>, 288, No.14, pp, 10101-10109, 2013<\/li>\n<li>Yusuke Miyashita, Tetsuichi Wazawa, George Mogami, <strong>Satoshi Takahashi<\/strong>, Yoshihiro Sambongi, and Makoto Suzuki &#8220;Hydration-State Change of horse Heart Cytochrome <em>c <\/em>Corresponding to Trifluoroacetic-Acid-Induced unfolding&#8221; <em>Biophysical Journal<\/em> Volume 104 January 2013 163-172<\/li>\n<\/ul>\n<h2 style=\"text-align: center\">\u00a0<strong>2012<\/strong><\/h2>\n<ul>\n<li><strong>Kamagata K, Kawaguchi T<\/strong>, Iwahashi Y, Baba A, Fujimoto K, Komatsuzaki T, Sambongi Y, Goto Y, <strong>Takahashi S<\/strong> &#8220;Long-Term Observation of Fluorescence of Free SingleMolecules To Explore Protein-Folding Energy Landscapes&#8221;<em> J. Am. Chem. Soc. <\/em>134, 11525-11532 (2012)<\/li>\n<\/ul>\n<h2 style=\"text-align: center\">\u00a0<strong>2011\u00a0<\/strong><\/h2>\n<ul>\n<li>Tsuyoshi Konuma, Tetsunari Kimura, Shuzo Matsumoto, Yuji Goto, Tetsuro Fujisawa, Alan R.Fersht and\u00a0<strong>Satoshi Takahashi<\/strong>\u00a0&#8220;Time-Resolved Small-Angle X-ray Scattering Study of the Folding Dynamics of Barnase&#8221;<em> J.Mol.Biol.<\/em> 405,1284-1294 (2011)<\/li>\n<\/ul>\n","protected":false},"excerpt":{"rendered":"<p>\u00a02020 Subekti D. R. G., *Kamagata K.,\u00a0\u201cThe disordered DNA-bind&#8230;<\/p>\n","protected":false},"author":1,"featured_media":0,"parent":37,"menu_order":0,"comment_status":"closed","ping_status":"closed","template":"","meta":{"footnotes":""},"class_list":["post-60","page","type-page","status-publish","hentry"],"_links":{"self":[{"href":"https:\/\/www2.tagen.tohoku.ac.jp\/lab\/takahashi-s\/wp-json\/wp\/v2\/pages\/60","targetHints":{"allow":["GET"]}}],"collection":[{"href":"https:\/\/www2.tagen.tohoku.ac.jp\/lab\/takahashi-s\/wp-json\/wp\/v2\/pages"}],"about":[{"href":"https:\/\/www2.tagen.tohoku.ac.jp\/lab\/takahashi-s\/wp-json\/wp\/v2\/types\/page"}],"author":[{"embeddable":true,"href":"https:\/\/www2.tagen.tohoku.ac.jp\/lab\/takahashi-s\/wp-json\/wp\/v2\/users\/1"}],"replies":[{"embeddable":true,"href":"https:\/\/www2.tagen.tohoku.ac.jp\/lab\/takahashi-s\/wp-json\/wp\/v2\/comments?post=60"}],"version-history":[{"count":57,"href":"https:\/\/www2.tagen.tohoku.ac.jp\/lab\/takahashi-s\/wp-json\/wp\/v2\/pages\/60\/revisions"}],"predecessor-version":[{"id":1092,"href":"https:\/\/www2.tagen.tohoku.ac.jp\/lab\/takahashi-s\/wp-json\/wp\/v2\/pages\/60\/revisions\/1092"}],"up":[{"embeddable":true,"href":"https:\/\/www2.tagen.tohoku.ac.jp\/lab\/takahashi-s\/wp-json\/wp\/v2\/pages\/37"}],"wp:attachment":[{"href":"https:\/\/www2.tagen.tohoku.ac.jp\/lab\/takahashi-s\/wp-json\/wp\/v2\/media?parent=60"}],"curies":[{"name":"wp","href":"https:\/\/api.w.org\/{rel}","templated":true}]}}