{"id":11,"date":"2019-03-19T18:46:28","date_gmt":"2019-03-19T09:46:28","guid":{"rendered":"https:\/\/nishi-lab.bs.teu.ac.jp\/?page_id=11"},"modified":"2022-04-17T16:56:59","modified_gmt":"2022-04-17T07:56:59","slug":"%e7%a0%94%e7%a9%b6%e6%a5%ad%e7%b8%be","status":"publish","type":"page","link":"https:\/\/nishi-lab.bs.teu.ac.jp\/?page_id=11","title":{"rendered":"\u7814\u7a76\u696d\u7e3e"},"content":{"rendered":"\n

\u539f\u8457\u8ad6\u6587 (Peer-reviewed)<\/strong><\/p>\n\n\n\n

  1. Mizuho Okamoto, Masanori Shimogishi, Akari Nakamura, Yusuke Suga, Kyosuke Sugawara, Michio Sato, Ryotaro Nishi<\/strong>, Akiko Fujisawa, Yorihiro Yamamoto and Misato Kashiba, Differentiation of THP-1 monocytes to macrophages increased mitochondrial DNA copy number but did not increase expression of mitochondrial respiratory proteins or mitochondrial transcription factor A, Archives of Biochemistry and Biophysics<\/strong>, 2021, 15, 108988<\/li>
  2. Misaki Matsui, Ryo Sakasai, Masako Abe, Yusuke Kimura, Shoki Kajita, Wakana Torii, Yoko Katsuki, Masamichi Ishiai, Kuniyoshi Iwabuchi, Minoru Takata and Ryotaro Nishi*<\/strong>,\u00a0USP42 enhances homologous recombination repair by promoting R-loop resolution with a DNA-RNA helicase DHX9, Oncogenesis<\/strong>, 2020, 9, 60, *Corresponding author<\/li>
  3. Ryotaro Nishi<\/strong>*<\/sup>, Paul W. G. Wijnhoven, Yusuke Kimura, Misaki Matsui, Rebecca Konietzny, Qian Wu, Keisuke Nakamura, Tom L. Blundell, and Benedikt M. Kessler,\u00a0The deubiquitylating enzyme UCHL3 regulates Ku80 retention at sites of DNA damage, Scientific Reports<\/strong>,2018, 8, 17891,*Corresponding author<\/li>
  4. Ryotaro Nishi<\/strong>. Balancing act: To be, or not to be ubiquitylated.\u00a0Mutation Research\/Fundamental and Molecular Mechanisms of Mutagenesis<\/strong>, 803-805, 43-50, 2017<\/li>
  5. Tomohumi Nakamura, Kouichi Murakami, Haruto Tada, Yoshihiko Uehara, Jumpei Nogami, Kazumitsu Maehara, Yasuyuki Ohkawa, Hisato Saitoh, Hideo Nishitani, Tetsuya Ono,\u00a0Ryotaro Nishi<\/strong>, Masayuki Yokoi, Wataru Sakai, and Kaoru Sugasawa, Thymine DNA glycosylase modulates the DNA damage response and gene expression by base excision repair-dependent and -independent mechanisms.\u00a0Genes to Cells<\/strong>, 22 (4), 392-405, 2017<\/li>
  6. Mayu Isono,\u00a0Atsuko Niimi,\u00a0Takahiro Oike,\u00a0Yoshihiko Hagiwara,\u00a0Hiro Sato,\u00a0Ryota Sekine,\u00a0Yukari Yoshida,\u00a0Shin-Ya Isobe,\u00a0Chikashi Obuse,\u00a0Ryotaro Nishi<\/strong>,\u00a0Elena Petricci,\u00a0Shinichiro Nakada,\u00a0Takashi Nakano and Atsushi Shibata. BRCA1 directs the repair pathway to homologous recombination by promoting 53BP1 dephosphorylation.\u00a0Cell Reports<\/strong>, 18 (2), 520-532, 2017<\/li>
  7. Paul Wijnhoven,\u00a0Rebecca\u00a0Konietzny, Andrew N. Blackford, Jonathan Travers, Benedikt M. Kessler,\u00a0Ryotaro Nishi*<\/strong>\u00a0and Stephen P. Jackson*.\u00a0USP4 Auto-Deubiquitylation Promotes Homologous Recombination.\u00a0Molecular Cell<\/strong>, 60 (3), 362-373, 2015, *Corresponding authors<\/li>
  8. Masaki Akita, Yon-Soo Tak, Tsutomu shimura, Syota Matsumoto, Yuki Okuda-Shimizu, Yuichiro Shimizu,\u00a0Ryotaro Nishi<\/strong>, Hisato Saitoh, Shigenori Iwai, Toshio Mori, Tsuyoshi Ikura, Wataru Sakai, Fumio Hanaoka and Kaoru Sugasawa. SUMOylation of xeroderma pigmentosum group C protein regulates DNA damage recognition during nucleotide excision repair.\u00a0Scientific Reports,\u00a0<\/strong>5, 10984, 2015<\/li>
  9. Syota Matsumoto, Eric S. Fisher, Takeshi Yasuda, Naoshi Dohmae, Shigenori Iwai, Toshio Mori,\u00a0Ryotaro Nishi<\/strong>, Ken-ichi Yoshino, Wataru Sakai, Fumio Hanaoka, Nicolas H, Thom\u00e4 and Kaoru Sugasawa. Functional regulation of the DNA damage-recognition factor DDB2 by ubiquitination and interaction with xeroderma pigmentosum group C protein.\u00a0Nucleic Acids Research<\/strong>, 43 (3), 1700-1713, 2015<\/li>
  10. Ryotaro Nishi<\/strong>, Paul Wijnhoven, Carlos le Sage, Jorrit Tjeertes, Yaron Galanty, Josep V. Forment, Michael J. Clague, Sylvie Urb\u00e9 and Stephen P Jackson. Systematic characterization of deubiquitylating enzymes for roles in maintaining genome integrity.\u00a0Nature Cell Biology<\/strong>, 16 (10), 1016-1026, 2014<\/li>
  11. Ryotaro Nishi*<\/strong>, Wataru Sakai*, Daisuke Tone, Fumio Hanaoka and Kaoru Sugasawa. Structure-function analysis of the EF-hand protein centrin-2 for its intracellular localization and nucleotide excision repair.\u00a0Nucleic Acids Research<\/strong>, 41 (14), 6917-6929, 2013\u00a0*; equally contributing author<\/li>
  12. Niina Tanaka, Miki Goto, Azusa Kawasaki, Takashi Sasano, Ko Eto,\u00a0Ryotaro Nishi,<\/strong>\u00a0Kaoru Sugasawa, Shinichi Abe and Hisato Saitoh. An EF-hands protein, centrin-1, is an EGTA-sensitive SUMO-interacting protein in mouse testis.\u00a0Cell Biochemistry and Function,<\/strong>\u00a028 (7), 604-612, 2010<\/li>
  13. Kaoru Sugasawa, Jun-ichi Akagi,\u00a0Ryotaro Nishi<\/strong>, Shigenori Iwai and Fumio Hanaoka. Two-step recognition of DNA damage for mammalian nucleotide excision repair: Directional binding of the XPC complex and DNA strand scanning.\u00a0Molecular Cell<\/strong>, 36 (4), 642-653, 2009<\/li>
  14. Ryotaro Nishi<\/strong>, Sergey Alekseev, Christoffel Dinant, Deborah Hoogstraten, Adriaan B. Houtsmuller, Jan H. J. Hoeijmakers, Wim Vermeulen, Fumio Hanaoka and Kaoru Sugasawa. UV-DDB dependent regulation of nucleotide excision repair kinetics in living cells.\u00a0DNA Repair<\/strong>, 8 (6), 767-776, 2009<\/li>
  15. Gentaro Yasuda*,\u00a0Ryotaro Nishi*<\/strong>, Eriko Watanabe, Toshio Mori, Shigenori Iwai, Donata Orioli, Miria Stefanini, Fumio Hanaoka, and Kaoru Sugasawa.\u00a0In vivo<\/em>\u00a0destabilization and functional defects of the xeroderma pigmentosum C protein caused by a pathogenic missense mutation.\u00a0Molecular and Cellular Biology,<\/strong>\u00a027 (19), 6606-6614, 2007\u00a0*; equally contributing author<\/li>
  16. Ryotaro Nishi<\/strong>, Yuki Okuda, Eriko Watanabe, Toshio Mori, Shigenori Iwai, Chikahide Masutani, Kaoru Sugasawa, and Fumio Hanaoka. Centrin 2 stimulates nucleotide excision repair by interacting with xeroderma pigmentosum group C protein.\u00a0Molecular and Cellular Biology<\/strong>, 25 (13), 5664-5674, 2005<\/li>
  17. Kaoru Sugasawa, Yuki Okuda, Masafumi Saijo,\u00a0Ryotaro Nishi<\/strong>,\u00a0Noriyuki Matsuda, Gilbert Chu, Toshio Mori, Shigenori Iwai, Keiji Tanaka, Kiyoji Tanaka, and Fumio Hanaoka.\u00a0UV-induced ubiquitylation of XPC protein mediated by UV-DDB-ubiquitin ligase complex.\u00a0Cell<\/strong>,121 (3), 387-400, 2005<\/li>
  18. Yuki Okuda,\u00a0Ryotaro Nishi<\/strong>, Jessica M.Y. Ng, Wim Vermeulen, Gijsbertus T.J. van der Horst, Toshio Mori, Jan H.J. Hoeijmakers, Fumio Hanaoka and Kaoru Sugasawa.\u00a0Relative levels of the two mammalian Rad23 homologs determine and stability of the xeroderma pigmentosum group C protein complex.\u00a0DNA Repair<\/strong>,\u00a03 (10), 1285-1295, 2004<\/li><\/ol>\n\n\n\n

    \u65e5\u672c\u8a9e\u7dcf\u8aac<\/strong><\/p>\n\n\n\n

    1. \u897f\u3000\u826f\u592a\u90ce<\/strong>\u3001\u300cDNA\u4e8c\u91cd\u9396\u5207\u65ad\u5fdc\u7b54\u3092\u5236\u5fa1\u3059\u308b\u8131\u30e6\u30d3\u30ad\u30c1\u30f3\u5316\u9175\u7d20\u7fa4\u300d\u3001\u653e\u751f\u7814\u30cb\u30e5\u30fc\u30b9\u30012016<\/li>
    2. \u897f\u3000\u826f\u592a\u90ce<\/strong>\u3001\u300cDNA\u640d\u50b7\u5fdc\u7b54\u306bH1\u30ea\u30f3\u30ab\u30fc\u30d2\u30b9\u30c8\u30f3\u304c\u95a2\u4e0e\u3057\u3066\u3044\u305f\uff01\u300d\u3001\u5b9f\u9a13\u533b\u5b66\u30012016\u3001Vol. 34, No. 4, 2\u6708<\/li>
    3. \u897f\u3000\u826f\u592a\u90ce<\/strong>, \u83c5\u6fa4\u3000\u85ab\u3000\u7d2b\u5916\u7dda\u306b\u3088\u308bDNA\u640d\u50b7\u306e\u4fee\u5fa9\u6a5f\u69cb \u86cb\u767d\u8cea\u6838\u9178\u9175\u7d20, 51, 2126-2133, 2006, 11<\/li><\/ol>\n\n\n\n

      \u5b66\u4f1a\u767a\u8868\uff08\u62db\u5f85\u8b1b\u6f14\u306e\u307f\u8868\u793a\uff09<\/strong><\/p>\n\n\n\n

      1. Ryotaro Nishi<\/strong>, DNA\u4e8c\u672c\u9396\u5207\u65ad\u4fee\u5fa9\u3068\u6838\u5185\u69cb\u9020\u4f53\u306e\u30af\u30ed\u30b9\u30c8\u30fc\u30af\u306e\u89e3\u660e, Genome Damage Network, Kyoto, 2019\/03\/11-12<\/li>
      2. Misaki Matsui, Yusuke Kimura, Masako Abe, Syoki Kajita, Wakana Torii, Masamichi Ishiai, Minoru Takata and Ryotaro Nishi<\/strong>, \u65b0\u898fnuclear speckle\u56e0\u5b50USP42\u306f\u76f8\u540c\u7d44\u63db\u3048\u4fee\u5fa9\u3092\u5236\u5fa1\u3059\u308b, \u65e5\u672c\u653e\u5c04\u7dda\u5f71\u97ff\u5b66\u4f1a\u7b2c61\u56de\u5927\u4f1a, \u9577\u5d0e, 2018\/11\/07<\/li>
      3. Ryotaro Nishi<\/strong>, \u30bf\u30f3\u30d1\u30af\u8cea\u30e6\u30d3\u30ad\u30c1\u30f3\u5316\u306e\u6642\u7a7a\u9593\u7684\u5236\u5fa1\u304b\u3089\u7d10\u89e3\u304fDNA\u4e8c\u91cd\u9396\u5207\u65ad\u4fee\u5fa9\u6a5f\u69cb, \u65e5\u672c\u653e\u5c04\u7dda\u5f71\u97ff\u5b66\u4f1a\u7b2c61\u56de\u5927\u4f1a, \u9577\u5d0e, 2018\/11\/08<\/li>
      4. \u677e\u4e95 \u7f8e\u54b2, \u6728\u6751\u7950\u8f14, \u5b89\u500d\u660c\u5b50, \u77f3\u5408\u6b63\u9053, \u5800\u5229\u884c, \u9ad8\u7530\u7a70, Stephen P Jackson, \u897f\u826f\u592a\u90ce<\/strong>, \u6838\u5185\u69cb\u9020\u4f53\u306b\u5c40\u5728\u3059\u308b\u56e0\u5b50\u306b\u3088\u308b\u76f8\u540c\u7d44\u63db\u3048\u4fee\u5fa9\u5236\u5fa1, \u7b2c40\u56de\u65e5\u672c\u5206\u5b50\u751f\u7269\u5b66\u4f1a\u5e74\u4f1a\uff082017\u5e74\u5ea6\u751f\u547d\u79d1\u5b66\u7cfb\u5b66\u4f1a\u5408\u540c\u5e74\u6b21\u5927\u4f1a\uff09, \u795e\u6238, 2017\/12 \/06-09<\/li>
      5. Ryotaro Nishi<\/strong>, Paul Wijnhoven, Yusuke Kimura, Misaki Matsui, Keisuke Nakamura, Rebecca Konietny, Qian Wu, Toshiyuki Hori, Tom Blundell, Benedikt M Kessler and Stephen P Jackson, A deubiquitylating enzyme, UCHL3, enhances non-homologous end-joining by regulating Ku ubiquitylation, The 33rd<\/sup> International Symposium of Radiation Biology Center, Hotel Co-op Inn Kyoto, Kyoto, 2017\/12\/04-05<\/li>
      6. \u677e\u4e95 \u7f8e\u54b2, \u6728\u6751\u7950\u8f14, \u5b89\u500d\u660c\u5b50, \u77f3\u5408\u6b63\u9053, \u5800\u5229\u884c, \u9ad8\u7530\u7a70, Stephen P Jackson, \u897f\u826f\u592a\u90ce<\/strong>, \u6838\u5185\u69cb\u9020\u4f53\u306b\u3088\u308bDNA\u4e8c\u672c\u9396\u5207\u65ad\u5fdc\u7b54\u5236\u5fa1\u6a5f\u69cb\u306e\u89e3\u660e, \u65e5\u672c\u653e\u5c04\u7dda\u5f71\u97ff\u5b66\u4f1a\u7b2c60\u56de\u5927\u4f1a, \u5343\u8449, 2017\/10\/25-28<\/li>
      7. \u897f\u3000\u826f\u592a\u90ce<\/strong>, Ubiquitin carboxyl-terminal hydrolase family\u306b\u3088\u308bDNA\u4e8c\u91cd\u9396\u5207\u65ad\u5fdc\u7b54\u5236\u5fa1\u6a5f\u69cb, \u5e73\u621029\u5e74\u5ea6\u5c02\u9580\u7814\u7a76\u4f1a\u3000\u82e5\u624b\u653e\u5c04\u7dda\u751f\u7269\u7814\u7a76\u4f1a\u4e3b\u50ac, \u6771\u4eac, 2017\/09\/02-03<\/li>
      8. Ryotaro Nishi<\/strong>, Yusuke Kimura, Misaki Matsui and Stephen P Jackson, DNA double-strand break repair and responses regulated by UCH family deubiquitylating enzymes, \u65e5\u672c\u653e\u5c04\u7dda\u5f71\u97ff\u5b66\u4f1a\u7b2c59\u56de\u5927\u4f1a, \u5e83\u5cf6, 2016\/10\/26-28<\/li>
      9. Ryotaro Nishi, <\/strong>DNA double-strand break repair and responses regulated by UCH family deubiquitylating enzymes, The 32rd RBC International Symposium \u201cGrowing Edge of Radiation Biology, from principles to applications., Coop-Inn Kyoto, Kyoto, 2016\/09\/01-02<\/li>
      10. Paul Wijnhoven, Rebecca Konietzny, Andrew N. Blackford, Jonathan Travers, Benedikt M. Kessler, Ryotaro Nishi*<\/sup><\/strong> and Stephen P. Jackson*<\/sup>, DNA\u4e8c\u91cd\u9396\u5207\u65ad\u4fee\u5fa9\u306b\u95a2\u4e0e\u3059\u308b\u8131\u30e6\u30d3\u30ad\u30c1\u30f3\u5316\u9175\u7d20\u3092\u4ecb\u3057\u305f\u30b2\u30ce\u30e0\u5b89\u5b9a\u6027\u7dad\u6301\u6a5f\u69cb, BMB2015, \u7b2c38\u56de\u65e5\u672c\u5206\u5b50\u751f\u7269\u5b66\u4f1a\u5e74\u4f1a, \u7b2c88\u56de\u65e5\u672c\u751f\u5316\u5b66\u5927\u4f1a\u5408\u540c\u5927\u4f1a, \u795e\u6238, 2015\/12\/03<\/li>
      11. Ryotaro Nishi<\/strong>, \u8131\u30e6\u30d3\u30ad\u30c1\u30f3\u5316\u9175\u7d20\u306b\u3088\u308bDNA\u4e8c\u91cd\u9396\u5207\u65ad\u4fee\u5fa9\u5236\u5fa1\u6a5f\u69cb, \u653e\u5c04\u7dda\u5f71\u97ff\u5b66\u4f1a\u653e\u5c04\u7dda\u30ef\u30fc\u30af\u30b7\u30e7\u30c3\u30d7\u301c\u672a\u6765\u306b\u7e4b\u3050\u653e\u5c04\u7dda\u7814\u7a76\u301c, \u5bcc\u5c71, 2015\/10\/16<\/li>
      12. Ryotaro Nishi<\/strong>, Paul Wijnhoven, Carlos le Sage, Jorrit Tjeertes, Yaron Galanty, Josep V. Forment, Michael J. Clague, Sylvie Urb\u00e9 and Stephen P Jackson, \u8131\u30e6\u30d3\u30ad\u30c1\u30f3\u5316\u9175\u7d20\u306b\u3088\u308bDNA\u4e8c\u91cd\u9396\u5207\u65ad\u5fdc\u7b54\u306e\u5236\u5fa1\u6a5f\u69cb, \u7fa4\u99ac\u5927\u5b66\u7b2c\uff12\u56deGenome Damage Discussion Group\u516c\u958b\u30bb\u30df\u30ca\u30fc, \u7fa4\u99ac\u30012015\/6\/29<\/li>
      13. Ryotaro Nishi<\/strong>, Paul Wijnhoven, Carlos le Sage, Jorrit Tjeertes, Yaron Galanty, Josep V. Forment, Michael J. Clague, Sylvie Urb\u00e9 and Stephen P Jackson, DUB-mediated regulation of DNA double-strand break repair, Cambridge Cell Cycle Club, University of Cambridge, United Kingdom, 2015\/02\/26<\/li>
      14. Ryotaro Nishi<\/strong>, Paul Wijnhoven, Carlos le Sage, Jorrit Tjeertes, Yaron Galanty, Josep V. Forment, Michael J. Clague, Sylvie Urb\u00e9 and Stephen P Jackson, Systematic characterization of deubiquitylating enzymes in DNA double-strand break repair, Cambridge 3R seminar series, Cambridge LMB, United Kingdom, 2014<\/li>
      15. Ryotaro Nishi<\/strong>, Sergey Alekseev, Christoffel Dinant, Deborah Hoogstraten, Adriaan B. Houtsmuller, Jan H. J. Hoeijmakers, Wim Vermeulen, Fumio Hanaoka and Kaoru Sugasawa, \u30cc\u30af\u30ec\u30aa\u30c1\u30c9\u9664\u53bb\u4fee\u5fa9\u56e0\u5b50\u306e\u7d30\u80de\u5185\u52d5\u614b\u3068\u305d\u306e\u5236\u5fa1\u6a5f\u69cb\u306e\u89e3\u6790, The 30th<\/sup> Annual Meeting of the Molecular Biology Society of Japan, Yokohama, Japan, 2007\/12\/13<\/li><\/ol>\n","protected":false},"excerpt":{"rendered":"

        \u539f\u8457\u8ad6\u6587 (Peer-reviewed) Mizuho Okamoto, Masanori Shimogishi, Akari Nakamura, Yusuke Suga, Kyosuke Sugawara, …<\/p>\n","protected":false},"author":3,"featured_media":0,"parent":0,"menu_order":0,"comment_status":"closed","ping_status":"closed","template":"","meta":{"footnotes":""},"class_list":["post-11","page","type-page","status-publish","hentry"],"_links":{"self":[{"href":"https:\/\/nishi-lab.bs.teu.ac.jp\/index.php?rest_route=\/wp\/v2\/pages\/11","targetHints":{"allow":["GET"]}}],"collection":[{"href":"https:\/\/nishi-lab.bs.teu.ac.jp\/index.php?rest_route=\/wp\/v2\/pages"}],"about":[{"href":"https:\/\/nishi-lab.bs.teu.ac.jp\/index.php?rest_route=\/wp\/v2\/types\/page"}],"author":[{"embeddable":true,"href":"https:\/\/nishi-lab.bs.teu.ac.jp\/index.php?rest_route=\/wp\/v2\/users\/3"}],"replies":[{"embeddable":true,"href":"https:\/\/nishi-lab.bs.teu.ac.jp\/index.php?rest_route=%2Fwp%2Fv2%2Fcomments&post=11"}],"version-history":[{"count":8,"href":"https:\/\/nishi-lab.bs.teu.ac.jp\/index.php?rest_route=\/wp\/v2\/pages\/11\/revisions"}],"predecessor-version":[{"id":402,"href":"https:\/\/nishi-lab.bs.teu.ac.jp\/index.php?rest_route=\/wp\/v2\/pages\/11\/revisions\/402"}],"wp:attachment":[{"href":"https:\/\/nishi-lab.bs.teu.ac.jp\/index.php?rest_route=%2Fwp%2Fv2%2Fmedia&parent=11"}],"curies":[{"name":"wp","href":"https:\/\/api.w.org\/{rel}","templated":true}]}}