{"id":11,"date":"2021-10-22T11:37:41","date_gmt":"2021-10-22T02:37:41","guid":{"rendered":"https:\/\/web.tohoku.ac.jp\/KineticControl\/?page_id=11"},"modified":"2023-05-02T20:54:13","modified_gmt":"2023-05-02T11:54:13","slug":"achievement","status":"publish","type":"page","link":"https:\/\/web.tohoku.ac.jp\/KineticControl\/achievement\/","title":{"rendered":"\u7814\u7a76\u6210\u679c"},"content":{"rendered":"\n

A01 (\u9f4b\u5c3e)<\/h2>\n\n\n\n

\u8ad6\u6587<\/h3>\n\n\n\n

(1)
Heat-Induced Conformational Transition Mechanism of Heat Shock Factor 1 Investigated by Tryptophan Probe
Soichiro Kawagoe, Munehiro Kumashiro, Takuya Mabuchi, Hiroyuki Kumeta, Koichiro Ishimori, Tomohide Saio
Biochemistry, 2022, 64(24), 2897. (doi: 10.1021\/acs.biochem.2c00492)<\/p>\n\n\n\n

(2)
Biophysical elucidation of neural network and chemical regeneration of neural tissue
Takahiro Muraoka, Tomohide Saio, Masaki Okumura
Biophys Physicobiol, 2022, 19, e190024. (doi: 10.2142\/biophysico.bppb-v19.0024)<\/p>\n\n\n\n

(3)
Structural and Kinetic Views of Molecular Chaperones in Multidomain Protein Folding
Soichiro Kawagoe, Koichiro Ishimori, Tomohide Saio
Int J Mol Sci, 2022, 23(5), 2485. (doi: 10.3390\/ijms23052485)<\/p>\n\n\n\n

(4)
Identification of an endoplasmic reticulum proteostasis modulator that enhances insulin production in pancreatic \u03b2 cells
Masato Miyake, Mitsuaki Sobajima, Kiyoe Kurahashi, Akira Shigenaga, Masaya Denda, Akira Otaka, Tomohide Saio, Naoki Sakane, Hidetaka Kosako, Seiichi Oyadomari
Cell Chem Biol, 2022, S2451-9456(22)00002-2. (doi: 10.1016\/j.chembiol.2022.01.002)<\/p>\n\n\n\n

(5)
C9orf72-derived arginine-rich poly-dipeptides impede phase modifiers
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*
Nature Commun. 2021, 12, 5301 (doi: 10.1038\/s41467-021-25560-0).<\/p>\n\n\n\n

(6)
Zinc-Dependent Oligomerization of Thermus thermophilus Trigger Factor Chaperone
Haojie Zhu, Motonori Matsusaki, Taiga Sugawara, Koichiro Ishimori*, and Tomohide Saio*
Biology 2021, 10, 1106.<\/p>\n\n\n\n

(7)
Functional Interplay Between P5 And PDI\/ERp72 To Drive Protein Folding
Motonori Matsusaki, Rina Okada, Yuya Tanikawa, Shingo Kanemura, Dai Ito, Yuxi Lin, Mai Watabe, Hiroshi Yamaguchi, Tomohide Saio, Young-Ho Lee, Kenji Inaba and Masaki Okumura* Biology 2021, 10, 1112.<\/p>\n\n\n\n

\u62db\u5f85\u8b1b\u6f14<\/h3>\n\n\n\n

(1)
\u65e5\u672c\u5316\u5b66\u4f1a\u7b2c102\u6625\u5b63\u5e74\u4f1a\u30012022\/3\/24\u3001\u30aa\u30f3\u30e9\u30a4\u30f3
\u9f4b\u5c3e \u667a\u82f1\u3000\u300c\u30bf\u30f3\u30d1\u30af\u8cea\u6db2\u6ef4\u306e\u5f62\u6210\u30fb\u5236\u5fa1\u30fb\u7834\u7dbb\u306e\u5206\u5b50\u30e1\u30ab\u30cb\u30ba\u30e0\u300d<\/p>\n\n\n\n

(2)
\u7b2c 22 \u56de\u65e5\u672c\u86cb\u767d\u8cea\u79d1\u5b66\u4f1a\u5e74\u4f1a\u30012022\/6\/9\u3001\u3064\u304f\u3070
\u9f4b\u5c3e \u667a\u82f1\u3000\u300c\u30b7\u30e3\u30da\u30ed\u30f3\u306b\u304a\u3051\u308b\u30ad\u30cd\u30c6\u30a3\u30af\u30b9\uff0d\u6d3b\u6027\u76f8\u95a2\u300d<\/p>\n\n\n\n

(3)
\u7b2c 74 \u56de \u65e5\u672c\u7d30\u80de\u751f\u7269\u5b66\u4f1a\u5e74\u4f1a\u30012022\/6\/30\u3001\u6771\u4eac
\u9f4b\u5c3e \u667a\u82f1\u3000\u300c\u5206\u5b50\u304b\u3089\u7406\u89e3\u3059\u308b\u76f8\u5206\u96e2\u5236\u5fa1\u3068\u7834\u7dbb\u300d<\/p>\n\n\n\n

(4)
International Symposium: Protein Folding, Aggregation, Misfolding Disease, and Disease Crosstalk\u30012022\/9\/2\u3001
\u97d3\u56fd\/\u30aa\u30f3\u30e9\u30a4\u30f3
Tomohide Saio \u300cStructural and kinetic views of regulators for protein folding and assembly\u300d<\/p>\n\n\n\n

(5)
2022 \u5e74\u5ea6 \u65e5\u672c\u5206\u5149\u5b66\u4f1aNMR\u5206\u5149\u90e8\u4f1a \u96c6\u4e2d\u8b1b\u7fa9\u30012022\/10\/18\u3001\u30aa\u30f3\u30e9\u30a4\u30f3
\u9f4b\u5c3e \u667a\u82f1\u3000\u300c\u76f8\u5206\u96e2\u5236\u5fa1\u3068\u5236\u5fa1\u7834\u7dbb\u306e\u5206\u5b50\u30e1\u30ab\u30cb\u30ba\u30e0\u300d<\/p>\n\n\n\n

(6)
2022 \u5e74\u5ea6 \u65e5\u672c\u5206\u5149\u5b66\u4f1aNMR\u5206\u5149\u90e8\u4f1a \u96c6\u4e2d\u8b1b\u7fa9\u30012022\/10\/18\u3001\u30aa\u30f3\u30e9\u30a4\u30f3
\u9f4b\u5c3e \u667a\u82f1\u3000\u300c\u76f8\u5206\u96e2\u5236\u5fa1\u3068\u5236\u5fa1\u7834\u7dbb\u306e\u5206\u5b50\u30e1\u30ab\u30cb\u30ba\u30e0\u300d<\/p>\n\n\n\n

(7)
The 1st IMEG Meeting of The Research Center for High Depth Omics\u30012023\/1\/16\u3001\u718a\u672c\/\u30aa\u30f3\u30e9\u30a4\u30f3
Tomohide Saio \u300cStructural insight into regulation and dysregulation of protein assembly and folding\u300d<\/p>\n\n\n\n

(8)
ZOOMinar on Molecular Bases of Proteinopathies\u30012023\/2\/13\u3001\u30aa\u30f3\u30e9\u30a4\u30f3
Tomohide Saio\u3000\u300cNMR investigation of the regulators in protein folding and assembly\u300d<\/p>\n\n\n\n

(9)
3rd India-Japan NMR WORK SHOP\u30012023\/2\/28\u3001\u672d\u5e4c
Tomohide Saio\u3000\u300cConformational distribution of a multi-domain protein enzyme investigated by paramagnetic NMR and ESR\u300d<\/p>\n\n\n\n

(10)
\u86cb\u767d\u7814\u30bb\u30df\u30ca\u30fc \u57fa\u790e\u304b\u3089\u5b66\u3076\u6700\u65b0NMR\u89e3\u6790\u6cd5\u3000\u7b2c6\u56de\u30ef\u30fc\u30af\u30b7\u30e7\u30c3\u30d7\u3000\u7d71\u5408\u578b\u69cb\u9020\u751f\u7269\u5b66\u7814\u7a76\u30012023\/3\/16\u3001\u30aa\u30f3\u30e9\u30a4\u30f3
\u9f4b\u5c3e \u667a\u82f1 \u300c\u5e38\u78c1\u6027\u30d7\u30ed\u30fc\u30d6\u3092\u7528\u3044\u305f\u30de\u30eb\u30c1\u30c9\u30e1\u30a4\u30f3\u30bf\u30f3\u30d1\u30af\u8cea\u306e\u69cb\u9020\u89e3\u6790\u300d<\/p>\n\n\n\n

(11)
\u65e5\u672c\u5316\u5b66\u4f1a\u7b2c103\u6625\u5b63\u5e74\u4f1a(2023)\u30012023\/3\/25\u3001\u91ce\u7530
\u9f4b\u5c3e \u667a\u82f1\u3000\u300c\u30e9\u30f3\u30bf\u30ce\u30a4\u30c9\u30bf\u30b0\u3092\u7528\u3044\u305f\u86cb\u767d\u8cea\u306e\u52d5\u7684\u69cb\u9020\u89e3\u6790\u300d<\/p>\n\n\n\n

(12)
ISMAR-APNMR2021\u30012021\/8\/25\u3001\u30aa\u30f3\u30e9\u30a4\u30f3
Tomohide Saio\u300cConformational Variation of a Multi-Domain Protein Enzyme Investigated by Paramagnetic Lanthanide Probe\u300d<\/p>\n\n\n\n

(13)
\u65e5\u672c\u30cf\u30a4\u30d1\u30fc\u30b5\u30fc\u30df\u30a2\u5b66\u4f1a\u7b2c38\u56de\u5927\u4f1a\u30012021\/9\/4\u3001\u30aa\u30f3\u30e9\u30a4\u30f3
\u9f4b\u5c3e\u667a\u82f1\u300c\u76f8\u5206\u96e2\u5236\u5fa1\u56e0\u5b50\u3068\u5206\u5b50\u30b7\u30e3\u30da\u30ed\u30f3\u306b\u3064\u3044\u3066\u306e\u52d5\u7684\u69cb\u9020\u89e3\u6790\u300d<\/p>\n\n\n\n

(14)
\u7b2c5\u56deLLPS\u7814\u7a76\u4f1a\u30012021\/9\/9\u3001\u30aa\u30f3\u30e9\u30a4\u30f3
\u9f4b\u5c3e\u667a\u82f1\u300c\u30b7\u30e3\u30da\u30ed\u30f3\u306b\u3088\u308b\u5206\u5b50\u96c6\u5408\u5236\u5fa1\u300d<\/p>\n\n\n\n

(15)
\u7b2c21\u56de\u82e5\u624bNMR\u7814\u7a76\u4f1a\u30012021\/9\/21\u3001\u30aa\u30f3\u30e9\u30a4\u30f3
\u9f4b\u5c3e\u667a\u82f1\u300c\u30e9\u30f3\u30bf\u30ce\u30a4\u30c9\u30d7\u30ed\u30fc\u30d6\u6cd5\u300d<\/p>\n\n\n\n

(16)
The 16th International Symposium of the Institute Network for Biomedical Sciences KEY FORUM 2021 International Symposium\u30012021\/11\/11\u3001\u30aa\u30f3\u30e9\u30a4\u30f3
Tomohide Saio\u300cMechanistic insight into chaperone-mediated protein homeostasis\u300d<\/p>\n\n\n\n

(17)
\u7b2c59\u56de\u65e5\u672c\u751f\u7269\u7269\u7406\u5b66\u4f1a\u5e74\u4f1a\u30012021\/11\/27\u3001\u30aa\u30f3\u30e9\u30a4\u30f3
\u9f4b\u5c3e\u667a\u82f1\u300cLarge-scale conformational distribution of a multi-domain protein enzyme investigated by NMR and EPR\u300d<\/p>\n\n\n\n

(18)
\u5206\u5b50\u751f\u7269\u5b66\u4f1a\u30ef\u30fc\u30af\u30b7\u30e7\u30c3\u30d7\u30012021\/12\/1\u3001\u6a2a\u6d5c
\u9f4b\u5c3e\u667a\u82f1\u300c\u591a\u91cf\u4f53\u5f62\u6210\u3092\u4ecb\u3057\u305f\u30b7\u30e3\u30da\u30ed\u30f3\u306e\u6a5f\u80fd\u5236\u5fa1\u300d<\/p>\n\n\n\n

(19)
Pacifichem 2021 (Symposium: #59, Biomolecular Structure and Dynamics: Recent Advances in NMR)\u30012021\/12\/18\u3001\u30aa\u30f3\u30e9\u30a4\u30f3
Tomohide Saio\u300cStructural and kinetic insights into a molecular chaperone for protein folding, translocation, and degradation\u300d<\/p>\n\n\n\n

(20)
Pacifichem 2021 (Chemical Tools to Measure and Control Protein Misfolding (#76))\u30012021\/12\/22\u3001\u30aa\u30f3\u30e9\u30a4\u30f3
Tomohide Saio\u300cNMR investigation of molecular chaperones manipulating protein folding\u300d<\/p>\n\n\n\n

\u53d7\u8cde<\/h3>\n\n\n\n

(1)
\u516c\u76ca\u8ca1\u56e3\u6cd5\u4eba\u30a2\u30b9\u30c6\u30e9\u30b9\u75c5\u614b\u4ee3\u8b1d\u7814\u7a76\u4f1a \u6700\u512a\u79c0\u7406\u4e8b\u9577\u8cde\u30012021\/10\/16
\u9f4b\u5c3e\u667a\u82f1\u300c\u6db2-\u6db2\u76f8\u5206\u96e2\u3068\u795e\u7d4c\u5909\u6027\u75be\u60a3\u306e\u52d5\u7684\u69cb\u9020\u57fa\u76e4\u300d<\/p>\n\n\n\n

<\/div>\n\n\n\n

B01 (\u5965\u6751)<\/h2>\n\n\n\n

\u8ad6\u6587<\/h3>\n\n\n\n

(1)
Biophysical elucidation of neural network and chemical regeneration of neural tissue
Takahiro Muraoka*, Tomohide Saio, and Masaki Okumura
Biophysics and Physicobiology<\/em><\/strong> 2022 19 e190024.<\/p>\n\n\n\n

(2)
Cysteine-based protein folding modulators for trapping intermediates and misfolded forms
Hayato Nishino, Mai Kitamura, Shunsuke Okada, Ryosuke Miyake, Masaki Okumura, and Takahiro Muraoka*
RSC adv <\/em><\/strong>2022 12 26658-26664.<\/p>\n\n\n\n

(3)
Atomistic structure of the interlocking claw-like amyloid fibril of full-length glucagon
Hyeongseop Jeong, Yuxi Lin, Jin Hae Kim, Wookyung Yu, Yunseok Heo, Hyung-Sik Won, Masaki Okumura, Young-Ho Lee*.
BioRxiv<\/em><\/strong> 2022 11.21.517306 https:\/\/doi.org\/10.1101\/2022.11.21.517306<\/p>\n\n\n\n

(4)
Elucidating the Peptide Degradation Mechanism by Insulin Degrading Enzyme
Tsubura Kuramochi, Shingo Kanemura, Ran Furukawa, Hiroshi Yamaguchi, Kenta Arai, Young-Ho Lee and Masaki Okumura*.
Peptide Science<\/em><\/strong> 2022 83-84.<\/p>\n\n\n\n

(5)
Oxidative Protein Folding Promotion by Imidazoyl-conjugated Thiol
Shunsuke Okada, Yosuke Matsumoto, Masaki Okumura, and Takahiro Muraoka*
Chem.Lett. <\/em><\/strong>2023 (52) 202-205.<\/p>\n\n\n\n

(6)
Dose-response relationship for the resistance of human insulin to degradation by insulin-degrading enzyme
Masaki Okumura*, Tsubura Kuramochi, Yuxi Lin, Ran Furukawa, Kenji Mizutani, Takeshi Yokoyama, Mingeun Kim, Mi Hee Lim, Hyon-Seung Yi, Kenta Arai, Hiroshi Yamaguchi, Hironobu Hojo, Michio Iwaoka, Yoshikazu Tanaka, Sam-Yong Park, Kenji Inaba, Shingo Kanemura, and Young-Ho Lee*.
BioRxiv<\/em><\/strong> 2023 04.08.536135 (https:\/\/doi.org\/10.1101\/2023.04.08.536135)<\/p>\n\n\n\n

(7)
Functional Interplay Between P5 And PDI\/ERp72 To Drive Protein Folding
Motonori Matsusaki, Rina Okada, Yuya Tanikawa, Shingo Kanemura, Dai Ito, Yuxi Lin, Mai Watabe, Hiroshi Yamaguchi, Tomohide Saio, Young-Ho Lee, Kenji Inaba and Masaki Okumura* Biology 10(11) 1112 <\/p>\n\n\n\n

\u8457\u66f8<\/h3>\n\n\n\n

(1)
\u5c0f\u80de\u4f53\u30b8\u30b9\u30eb\u30d5\u30a3\u30c9\u7d50\u5408\u89e6\u5a92\u30cd\u30c3\u30c8\u30ef\u30fc\u30af\u3092\u652f\u3048\u308b\u9175\u7d20\u7fa4\u306e\u69cb\u9020\u57fa\u76e4
\u91d1\u6751\u9032\u543e, \u7a32\u8449\u8b19\u6b21, \u5965\u6751\u6b63\u6a39
\u65e5\u672c\u7d50\u6676\u5b66\u4f1a\u8a8c64, 209-210 (2022)<\/p>\n\n\n\n

\u62db\u5f85\u8b1b\u6f14<\/h3>\n\n\n\n

(1)
Korea-Japan Joint Workshop on Biofunctional Chemistry\u30012022\/1\/12\u3001online (invited)
Masaki Okumura\u300cUnderstanding the proteostasis network in the endoplasmic reticulum\u300d<\/p>\n\n\n\n

(2)
\u7b2c22\u56de \u65e5\u672c\u86cb\u767d\u8cea\u79d1\u5b66\u4f1a\u30012022\/6\/8\u3001\u3064\u304f\u3070\uff08\u4f9d\u983c\u8b1b\u6f14\uff09
\u5965\u6751\u6b63\u6a39\u300c\u5404\u968e\u5c64\u306b\u304a\u3051\u308b\u9178\u5316\u7684\u30d5\u30a9\u30fc\u30eb\u30c7\u30a3\u30f3\u30b0\u89e6\u5a92\u30b7\u30b9\u30c6\u30e0\u306e\u7406\u89e3\u300d<\/p>\n\n\n\n

(3)
\u7b2c15\u56de \u5c0f\u80de\u4f53\u30b9\u30c8\u30ec\u30b9\u7814\u7a76\u4f1a\u30012022\/7\/31\u3001\u4eac\u90fd
\u5965\u6751\u6b63\u6a39\u300cPDI\u30d5\u30a1\u30df\u30ea\u30fc\u30e1\u30f3\u30d0\u30fcPDIA6\u306e\u65b0\u898f\u69cb\u9020\u3068\u6a5f\u80fd\u300d<\/p>\n\n\n\n

(4)
Protein Folding, Aggregation, Misfolding Disease, and Disease Crosstalk  Korea\u30012022\/9\/2\u3001(invited)
Masaki Okumura\u300cStructural insights into the protein control system mechanism by PDI family, the endoplasmic reticulum-resident chaperone\/enzyme\u300d<\/p>\n\n\n\n

(5)
Redox Week in Sendai  Sendai\u30012022\/10\/31\u3001(invited)
Masaki Okumura\u300cProtein Disulfide Isomerase family; their molecular actions and functions\u300d<\/p>\n\n\n\n

(6)
\u7b2c95\u56de \u65e5\u672c\u751f\u5316\u5b66\u4f1a\u30012022\/11\/9\u3001\u540d\u53e4\u5c4b\uff08\u4f9d\u983c\u8b1b\u6f14\uff09
\u5965\u6751\u6b63\u6a39\u300c\u5c0f\u80de\u4f53\u5185\u306b\u304a\u3051\u308b\u9178\u5316\u7684\u30d5\u30a9\u30fc\u30eb\u30c7\u30a3\u30f3\u30b0\u89e6\u5a92\u30cd\u30c3\u30c8\u30ef\u30fc\u30af\u306e\u7406\u89e3\u300d<\/p>\n\n\n\n

(7)
\u7b2c45\u56de \u65e5\u672c\u5206\u5b50\u751f\u7269\u5b66\u4f1a\u30012022\/11\/30\u3001\u5e55\u5f35\uff08\u4f9d\u983c\u8b1b\u6f14\uff09
\u5965\u6751\u6b63\u6a39\u300cPDI\u30d5\u30a1\u30df\u30ea\u30fc\u306e\u30b7\u30e3\u30da\u30ed\u30f3\u6a5f\u80fd\u306e\u7406\u89e3\uff1a\u30d7\u30ed\u30c6\u30aa\u30b9\u30bf\u30b9\u3068\u795e\u7d4c\u5909\u6027\u75be\u60a3\u300d<\/p>\n\n\n\n

(8)
\u7b2c45\u56de \u65e5\u672c\u5206\u5b50\u751f\u7269\u5b66\u4f1a\u30012022\/12\/1\u3001\u5e55\u5f35\uff08\u4f9d\u983c\u8b1b\u6f14\uff09
\u5965\u6751\u6b63\u6a39\u300c\u30db\u30ed\u30b0\u30e9\u30d5\u30a3\u30c3\u30af\u9855\u5fae\u93e1\u3092\u7528\u3044\u305f\u76f8\u5206\u96e2\u89b3\u5bdf\u4f8b\u306e\u7d39\u4ecb\u300d<\/p>\n\n\n\n

(9)
\u7b2c4\u56de\u795e\u6238\u5b66\u9662\u5927\u5b66\u30bb\u30df\u30ca\u30fc \u77e5\u306e\u5275\u9020\u30bb\u30df\u30ca\u30fc\u30012023\/1\/23\u3001\u795e\u6238\uff08\u4f9d\u983c\u8b1b\u6f14\uff09
\u5965\u6751\u6b63\u6a39\u300c\u5404\u751f\u7269\u5b66\u7684\u968e\u5c64\u306b\u304a\u3051\u308b\u30bf\u30f3\u30d1\u30af\u8cea\u54c1\u8cea\u7ba1\u7406\u306e\u7406\u89e3\u300d<\/p>\n\n\n\n

(10)
Zoominar “Amyloid Symposium”\u30012023\/2\/6\u3001online (invited)
Masaki Okumura\u300cUnderstanding the mechanism by which Protein Disulfide Isomerase (PDI) family guide proper oxidative folding\u300d<\/p>\n\n\n\n

(11)
\u65e5\u672c\u5316\u5b66\u4f1a \u7b2c103\u6625\u5b63\u5e74\u4f1a\u30012023\/3\/25\u3001\u91ce\u7530\uff08\u4f9d\u983c\u8b1b\u6f14\uff09
\u5965\u6751\u6b63\u6a39\u300c\u57fa\u8cea\u89e6\u5a92\u306b\u304a\u3051\u308bPDI\u9175\u7d20\u7fa4\u306e\u52d5\u7684\u4f1a\u5408\u4f53\u5f62\u6210\u306e\u7406\u89e3\u300d<\/p>\n\n\n\n

(12)
\u7b2c5\u56deLLPS\u7814\u7a76\u4f1a\u30012021\/9\/9\u3001\u30aa\u30f3\u30e9\u30a4\u30f3
\u5965\u6751\u6b63\u6a39\u300c\u5c0f\u80de\u4f53\u5185\u3067\u6db2\u6ef4\u3092\u5f62\u6210\u3059\u308b\u56e0\u5b50\u306e\u751f\u7406\u5b66\u7684\u6a5f\u80fd\u306e\u7406\u89e3\u300d<\/p>\n\n\n\n

(13)
\u5206\u5b50\u751f\u7269\u5b66\u4f1a\u30ef\u30fc\u30af\u30b7\u30e7\u30c3\u30d7\u30012022\/12\/1\u3001\u6a2a\u6d5c
\u5965\u6751\u6b63\u6a39\u300cPDI family\u306e\u52d5\u7684\u306a\u4f1a\u5408\u306b\u3088\u308b\u5c0f\u80de\u4f53\u5185\u30bf\u30f3\u30d1\u30af\u8cea\u54c1\u8cea\u7ba1\u7406\u306e\u7406\u89e3\u300d<\/p>\n\n\n\n

<\/div>\n\n\n\n

C01 (\u6751\u5ca1)<\/h2>\n\n\n\n

\u8ad6\u6587<\/h3>\n\n\n\n

(1)
Efficient Protein Incorporation and Release by a Jigsaw-Shaped Self-Assembling Peptide Hydrogel for Injured Brain Regeneration
Atsuya Yaguchi, Mio Oshikawa, Go Watanabe, Hirotsugu Hiramatsu, Noriyuki Uchida, Chikako Hara, Naoko Kaneko, Kazunobu Sawamoto, Takahiro Muraoka* and Itsuki Ajioka*
Nature Commun, 2021<\/strong>, 12<\/em>, 6623 (doi: 10.1038\/s41467-021-26896-3).<\/p>\n\n\n\n

(2)
Stabilization of Bicelles Using Metal-Binding Peptide for Extended Blood Circulation
Yuichiro Takagi, Noriyuki Uchida, Yasutaka Anraku and Takahiro Muraoka
Chem. Commun.<\/em>\u00a02022<\/strong>,\u00a058<\/em>, 5164\u20135167 (doi: 10.1039\/D2CC01058E).<\/p>\n\n\n\n

(3)
Self-Assembling Molecular Medicine for the Subacute Phase of Ischemic Stroke
Takahiro Muraoka and Itsuki Ajioka
Neurochem. Res.<\/em>\u00a02022<\/strong>,\u00a047<\/em>, 2488\u20132498 (doi: 10.1007\/s11064-022-03638-5).<\/p>\n\n\n\n

(4)
Cysteine-Based Protein Folding Modulators for Trapping Intermediates and Misfolded Forms
Hayato Nishino, Mai Kitamura, Shunsuke Okada, Ryosuke Miyake, Masaki Okumura and Takahiro Muraoka
RSC Adv.<\/em>\u00a02022<\/strong>,\u00a012<\/em>, 26658\u201326664 (doi: 10.1039\/D2RA04044A).<\/p>\n\n\n\n

(5)
Amphiphilic Peptide-tagged N-Cadherin Forms Radial Glial-like Fibers that Enhance Neuronal Migration in Injured Brain and Promote Sensorimotor Recovery
Yuya Ohno, Chikako Nakajima, Itsuki Ajioka, Takahiro Muraoka, Atsuya Yaguchi, Teppei Fujioka, Saori Akimoto, Misaki Matsuo, Ahmed Lotfy, Sayuri Nakamura, Vicente Herranz-P\u00e9rez, Jos\u00e9 Manuel Garc\u00eda-Verdugo, Noriyuki Matsukawa, Naoko Kaneko and Kazunobu Sawamoto
Biomaterials<\/em>\u00a02023<\/strong>,\u00a0294<\/em>, 122003 (10.1016\/j.biomaterials.2023.122003).<\/p>\n\n\n\n

(6)
Coacervate Formation of Elastin-like Polypeptides in Explicit Aqueous Solution Using Coarse-Grained Molecular Dynamics Simulations
Takuya Mabuchi, Junko Kijima, Yukino Yamashita, Erika Miura and Takahiro Muraoka
Macromolecules<\/em>\u00a02023<\/strong>,\u00a056<\/em>, 794\u2013805 (10.1021\/acs.macromol.2c02195).<\/p>\n\n\n\n

(7)
Oxidative Protein Folding Promotion by Imidazoyl-Conjugated Thiol
Shunsuke Okada, Yosuke Matsumoto, Masaki Okumura and Takahiro Muraoka
Chem. Lett.<\/em>\u00a02023<\/strong>,\u00a052<\/em>, 202\u2013205 (10.1246\/cl.220537).<\/p>\n\n\n\n

(8)
ROS-Triggered Gel\u2013Sol Transition and Kinetics-Controlled Cargo Release by Methionine-Containing Peptides
Yoshika Hara, Atsuya Yaguchi, Hirotsugu Hiramatsu and Takahiro Muraoka
ChemBioChem<\/em>\u00a02023<\/strong>, accepted (10.1002\/cbic.202200798, selected as a Very Important Paper (VIP), highlighted in\u00a0ChemBioTalents 2022).<\/p>\n\n\n\n

(9)
Endocytosis-Like Vesicle Fission Mediated by a Membrane-Expanding Molecular Machine Enables Virus Encapsulation for In Vivo Delivery
Noriyuki Uchida, Yunosuke Ryu, Yuichiro Takagi, Ken Yoshizawa, Kotono Suzuki, Yasutaka Anraku, Itsuki Ajioka, Naofumi Shimokawa, Masahiro Takagi, Norihisa Hoshino, Tomoyuki Akutagawa, Teruhiko Matsubara, Toshinori Sato, Yuji Higuchi, Hiroaki Ito, Masamune Morita and Takahiro Muraoka
J. Am. Chem. Soc.<\/em>\u00a02023<\/strong>, accepted (10.1021\/jacs.2c12348).<\/p>\n\n\n\n

\u62db\u5f85\u8b1b\u6f14<\/h3>\n\n\n\n

(1)
\u7b2c6\u56deABC-InFO\u8b1b\u6f14\u4f1a\u30012021\/9\/22\u3001\u30aa\u30f3\u30e9\u30a4\u30f3
\u6751\u5ca1\u8cb4\u535a\u300c\u751f\u304d\u305f\u7d30\u80de\u819c\u3067\u6a5f\u80fd\u3059\u308b\u4eba\u5de5\u30a4\u30aa\u30f3\u30c1\u30e3\u30cd\u30eb\u300d<\/p>\n\n\n\n

(2)
\u5206\u5b50\u751f\u7269\u5b66\u4f1a\u30ef\u30fc\u30af\u30b7\u30e7\u30c3\u30d7\u30012022\/12\/1\u3001\u6a2a\u6d5c
\u6751\u5ca1\u8cb4\u535a\u300c\u5408\u6210\u5316\u5b66\u30a2\u30d7\u30ed\u30fc\u30c1\u306b\u3088\u308b\u30b8\u30b9\u30eb\u30d5\u30a3\u30c9\u7d50\u5408\u7570\u6027\u5316\u9175\u7d20\u306e\u6a21\u5023\u300d<\/p>\n\n\n\n

(3)
Pacifichem 2021 (Peptide Self-Assembly: Chemistry and Nanotechnology (#106))\u30012022\/12\/16\u3001\u30aa\u30f3\u30e9\u30a4\u30f3
Takahiro Muraoka\u300cGlycine Substitution Effects on Supramolecular Morphology and Thermal Response of Self-Assembling Peptides\u300d<\/p>\n\n\n\n

(4)
\u7b2c3\u56de\u30bf\u30bf\u30d0\u30a4\u30aa\u5206\u5b50\u30af\u30e9\u30d6
\u6751\u5ca1\u8cb4\u535a\u300c\u81ea\u5df1\u96c6\u5408\u6027\u30da\u30d7\u30c1\u30c9\u3092\u7528\u3044\u305f\u795e\u7d4c\u7d44\u7e54\u518d\u751f\u300d<\/p>\n\n\n\n

(5)
\u86cb\u767d\u8cea\u79d1\u5b66\u4f1a\u300c\u30ad\u30cd\u30c6\u30a3\u30af\u30b9\u304b\u3089\u7406\u89e3\u3059\u308b\u751f\u547d\u30b7\u30b9\u30c6\u30e0\u300d\u30ef\u30fc\u30af\u30b7\u30e7\u30c3\u30d7\u30012022\/6\/8\u3001\u7b51\u6ce2\uff08\u4f9d\u983c\u8b1b\u6f14\uff09
\u6751\u5ca1\u8cb4\u535a\u300c\u30ad\u30cd\u30c6\u30a3\u30af\u30b9\u64cd\u4f5c\u306b\u57fa\u3065\u304f\u9178\u5316\u7684\u86cb\u767d\u8cea\u30d5\u30a9\u30fc\u30eb\u30c7\u30a3\u30f3\u30b0\u5236\u5fa1\u300d<\/p>\n\n\n\n

(6)
Neuro2022\u30012022\/7\/2\u3001\u6c96\u7e04
\u6751\u5ca1\u8cb4\u535a\u300cNeurochemistry from Supramolecular Chemistry\u300d<\/p>\n\n\n\n

(7)
Protein Folding, Aggregation, Misfolding Disease, and Disease Crosstalk\u30012022\/9\/2\u3001\u97d3\u56fd\uff08\u30cf\u30a4\u30d6\u30ea\u30c3\u30c9\uff09
\u6751\u5ca1\u8cb4\u535a\u300cRegulated folding and assembly of polypeptides for designing ECM-mimetic biomaterials\u300d<\/p>\n\n\n\n

(8)
CREST\u300c\u7d30\u80de\u5916\u5fae\u7c92\u5b50\u300d\u9818\u57df\u4e3b\u50ac\u3000\u7b2c1\u56de CREST\u30fb\u3055\u304d\u304c\u3051\u9818\u57df\u6a2a\u65ad\u30b7\u30f3\u30dd\u30b8\u30a6\u30e0 ~\u30b3\u30ed\u30ca\u95a2\u9023\u7814\u7a76\u3092\u4e2d\u5fc3\u306b~\u30012022\/10\/14\u3001\u30aa\u30f3\u30e9\u30a4\u30f3\uff08\u4f9d\u983c\u8b1b\u6f14\uff09
\u6751\u5ca1\u8cb4\u535a\u300c\u30a6\u30a4\u30eb\u30b9\u5149\u6355\u6349\u6750\u6599\u300d<\/p>\n\n\n\n

(9)
\u7b2c31\u56de\u30dd\u30ea\u30de\u30fc\u6750\u6599\u30d5\u30a9\u30fc\u30e9\u30e0\u30012022\/11\/15\u3001\u6771\u4eac
\u77e2\u53e3\u6566\u4e5f\u30fb\u5e73\u677e\u5f18\u55e3\u30fb\u5473\u5ca1\u9038\u6a39\u30fb\u6751\u5ca1\u8cb4\u535a\u300c\u9ad8\u6b21\u69cb\u9020\u8ee2\u79fb\u7279\u6027\u3092\u6709\u3059\u308b\u81ea\u5df1\u96c6\u5408\u6027\u30da\u30d7\u30c1\u30c9\u306e\u958b\u767a\u3068\u4e9c\u6025\u6027\u671f\u8133\u6897\u585e\u6cbb\u7642\u3078\u306e\u5fdc\u7528\u300d<\/p>\n\n\n\n

(10)
\u5206\u5b50\u751f\u7269\u5b66\u4f1a\u30012022\/11\/30\u3001\u5343\u8449\uff08\u4f9d\u983c\u8b1b\u6f14\uff09
\u6751\u5ca1\u8cb4\u535a\u300c\u591a\u6bb5\u968e\u53cd\u5fdc\u5236\u5fa1\u306b\u3088\u308b\u30bf\u30f3\u30d1\u30af\u8cea\u30d5\u30a9\u30fc\u30eb\u30c7\u30a3\u30f3\u30b0\u4fc3\u9032\u300d<\/p>\n\n\n\n

(11)
ZOOMinar series on \u201cMolecular Basis of Proteinopathies\u201d\u3001 2023\/2\/6\u3001\u30aa\u30f3\u30e9\u30a4\u30f3
\u6751\u5ca1\u8cb4\u535a\u300cFunctional assembly of polypeptides for injured brain regeneration\u300d<\/p>\n\n\n\n

(12)
\u4ee4\u548c4\u5e74\u5ea6\u6771\u5317\u5730\u533a\u5148\u7aef\u9ad8\u5206\u5b50\u30bb\u30df\u30ca\u30fc\u30012023\/3\/7\u3001\u4ed9\u53f0
\u6751\u5ca1\u8cb4\u535a\u300c\u819c\u5909\u5f62\u5206\u5b50\u6a5f\u68b0\u306e\u958b\u767a\u3068\u751f\u4f53\u5185\u8f38\u9001\u3078\u306e\u5fdc\u7528\u300d<\/p>\n\n\n\n

(13)
\u65e5\u672c\u5316\u5b66\u4f1a \u7b2c103\u6625\u5b63\u5927\u4f1a\uff082023\uff09\u30012023\/3\/25\u3001\u91ce\u7530\uff08\u4f9d\u983c\u8b1b\u6f14\uff09
\u6751\u5ca1\u8cb4\u535a\u300c\u901f\u5ea6\u8ad6\u52b9\u679c\u3092\u5229\u7528\u3059\u308b\u591a\u6bb5\u968e\u86cb\u767d\u8cea\u30d5\u30a9\u30fc\u30eb\u30c7\u30a3\u30f3\u30b0\u4fc3\u9032\u300d<\/p>\n\n\n\n

\u53d7\u8cde<\/h3>\n\n\n\n

(1)
\u7b2c3\u56de\uff082021\u5e74\u5ea6\uff09\u7269\u8cea\u30fb\u30c7\u30d0\u30a4\u30b9\u5171\u540c\u7814\u7a76\u8cde\u30012021\/9\/28
\u6751\u5ca1\u8cb4\u535a\u300c\u53ef\u8996\u5149\u5fdc\u7b54\u819c\u5909\u5f62\u5206\u5b50\u306e\u958b\u767a\u3068 \u7d30\u80de\u5236\u5fa1 \u3078\u306e\u5c55\u958b\u300d<\/p>\n\n\n\n

<\/div>\n\n\n\n

C01 (\u99ac\u6e15)<\/h2>\n\n\n\n

\u8ad6\u6587<\/h3>\n\n\n\n

(1)
Switching Type I\/Type II Reactions by Turning a Photoredox Catalyst into a Photo-Driven Artificial Metalloenzyme
Y. Okamoto*, T. Mabuchi, K. Nakane, A. Ueno, and S. Sato*
ACS Catalysis<\/em>, 13, 4134-4141 (2023). (https:\/\/doi.org\/10.1021\/acscatal.2c05946<\/a>)<\/p>\n\n\n\n

(2)
Coacervate Formation of Elastin-like Polypeptides in Explicit Aqueous Solution Using Coarse-Grained Molecular Dynamics Simulations
T. Mabuchi*, J. Kijima, Y. Yamashita, E. Miura, and T. Muraoka*
Macromolecules<\/em>, 56, 794-805 (2023). (https:\/\/doi.org\/10.1021\/acs.macromol.2c02195<\/a>)<\/p>\n\n\n\n

(3)
Deep Learning to Reveal the Distribution and Diffusion of Water Molecules in Fuel Cell Catalyst Layers
G. Li, Y. Zhu, Y. Guo*, T. Mabuchi, D. Li, S. F. Huang, S. Wang, H. Sun, and T. Tokumasu
ACS Applied Materials & Interfaces<\/em>, 15, 5099-5108 (2023). (https:\/\/doi.org\/10.1021\/acsami.2c17198<\/a>)<\/p>\n\n\n\n

(4)
Growth mechanism study of boron nitride atomic layer deposition by experiment and density functional theory
N. Uene*, T. Mabuchi, M. Zaitsu, Y. Jin, S. Yasuhara, and T. Tokumasu
Computational Materials Science<\/em>, 217, 111919 (2023). (https:\/\/doi.org\/10.1016\/j.commatsci.2022.111919<\/a>)<\/p>\n\n\n\n

(5)
Heat-Induced Conformational Transition Mechanism of Heat Shock Factor 1 Investigated by Tryptophan Probe
S. Kawagoe, M. Kumashiro, T. Mabuchi, H. Kumeta, K. Ishimori*, and T. Saio*
Biochemistry<\/em>, 61, 2897-2908 (2022). (https:\/\/doi.org\/10.1021\/acs.biochem.2c00492<\/a>)<\/p>\n\n\n\n

(6)
Morphology Evolution and Adsorption Behavior of Ionomers from Solution to Pt\/C Substrates
Y. Guo*, T. Mabuchi, G. Li, and T. Tokumasu, Macromolecules<\/em>, 55, 4245-4255 (2022).(https:\/\/doi.org\/10.1021\/acs.macromol.2c00533<\/a>)<\/p>\n\n\n\n

(7)
Molecular Simulation Study of CO2<\/sub> Adsorption on Lanthanum-Based Metal Organic Framework
I. H. Putra, F. Yulia, I. A. Zulkarnain, R. Ruliandini, A. Zulys, T. Mabuchi, W. Gon\u00e7alves, and Nasruddin*
Russian Journal of Physical Chemistry A<\/em>, 96, 3007-3014 (2022). (https:\/\/doi.org\/10.1134\/S0036024422130040<\/a>)<\/p>\n\n\n\n

(8)
Revealing the anticorrelation behavior mechanism between the Grotthuss and vehicular diffusions for proton transport in concentrated acid solutions
T. Mabuchi*, Journal of Physical Chemistry B<\/em>, 126, 3319-3326 (2022). (https:\/\/doi.org\/10.1021\/acs.jpcb.1c09742<\/a>)<\/p>\n\n\n\n

(9)
Bio-Metal-Organic Framework-based Cobalt Glutamate for CO2\/N2 Separation: Experimental and multi-objective Optimization with a Neural Network
F. Yulia, A. Zulys, B. B. Saha, T. Mabuchi, W. Gon\u00e7alves, and Nasruddin*
Process Safety and Environmental Protection<\/em>, 162, 998-1014 (2022). (https:\/\/doi.org\/10.1016\/j.psep.2022.04.076<\/a>)<\/p>\n\n\n\n

(10)
Reactive force-field molecular dynamics simulation for the surface reaction of SiH (x = 2\u20134) species on Si(1 0 0)-(2 \u00d7 1):H surfaces in chemical vapor deposition processes
N. Uene*, T. Mabuchi, M. Zaitsu, S. Yasuhara, and T. Tokumasu
Computational Materials Science<\/em>, 204, 111193 (2022). (https:\/\/doi.org\/10.1016\/j.commatsci.2022.111193<\/a>)<\/p>\n\n\n\n

(11)
Prediction of the adsorption properties of liquid at solid surfaces with molecular scale surface roughness via encoding-decoding convolutional neural networks
G. Li, Y. Guo*, T. Mabuchi, D. Surblys, T. Ohara, and T. Tokumasu
Journal of Molecular Liquids<\/em>, 349, 118489 (2022). (https:\/\/doi.org\/10.1016\/j.molliq.2022.118489<\/a>)<\/p>\n\n\n\n

(12)
Prediction of nanoscale thermal transport and adsorption of liquid containing surfactant at solid-liquid interface via deep learning
Y. Guo, G. Li*, T. Mabuchi, D. Surblys, T. Ohara, and T. Tokumasu
Journal of Colloid and Interface Science<\/em>, 613, 587-596 (2022). (https:\/\/doi.org\/10.1016\/j.jcis.2022.01.037<\/a>)<\/p>\n\n\n\n

(13)
Influence of Ionomer Loading and Substrate Wettability on the Morphology of Ionomer Thin Films Using Coarse-Grained Solvent Evaporation Simulations
Takuya Mabuchi*, Sheng-Feng Huang, and Takashi Tokumasu
Macromolecules 2021, 54, 115 (doi: 10.1021\/acs.macromol.0c01303).<\/p>\n\n\n\n

\u62db\u5f85\u8b1b\u6f14<\/h3>\n\n\n\n

(1)
\u5206\u5b50\u30b7\u30df\u30e5\u30ec\u30fc\u30b7\u30e7\u30f3\u3092\u7528\u3044\u305f\u751f\u4f53\u9ad8\u5206\u5b50\u3068\u5408\u6210\u9ad8\u5206\u5b50\u306b\u95a2\u3059\u308b\u7814\u7a76
2022\u5e74\u5ea6\u7b2c2\u56de\u9759\u96fb\u6c17\u30fb\u9ad8\u96fb\u5727\u30fb\u653e\u96fb\u30fb\u30d7\u30e9\u30ba\u30de\u82e5\u624b\u7814\u7a76\u59d4\u54e1\u4f1a\/\u7814\u7a76\u4f1a\uff0c\u5bae\u57ce\u770c\uff08\u30cf\u30a4\u30d6\u30ea\u30c3\u30c9\uff09
2022\u5e7412\u670812\u65e5<\/p>\n\n\n\n

(2)
\u71c3\u6599\u96fb\u6c60\u89e6\u5a92\u30a4\u30f3\u30af\u5206\u5b50\u30b7\u30df\u30e5\u30ec\u30fc\u30b7\u30e7\u30f3
\u30c8\u30e8\u30bf\u3068\u6771\u5317\u5927\u5b66\u304c\u5922\u898b\u308b\u30df\u30e9\u30a4\uff0c\u5bae\u57ce\u770c\uff0c2022\u5e7410\u670814\u65e5<\/p>\n\n\n\n

(3)
Molecular Simulation of Phase Separation Phenomena for Engineering Applications
6th International Joint Conference on Science and Technology (IJCST) 2022,
Jakarta, Indonesia (online), September 28-29 (2022).<\/p>\n\n\n\n

(4)
Multiscale Modeling and Simulation of Ionomer Self-Assembly for Polymer Electrolyte Fuel Cells
JAIST\u71c3\u6599\u96fb\u6c60\u7814\u7a76\u4f1a\u30012021\/5\/21\u3001\u30aa\u30f3\u30e9\u30a4\u30f3<\/p>\n\n\n\n

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A01 (\u9f4b\u5c3e) \u8ad6\u6587 (1)Heat-Induced Conformational Transition Mechanism of Heat Shock Factor 1 Investigated by Tryptop […]<\/p>\n

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