{"id":66,"date":"2015-12-08T11:55:03","date_gmt":"2015-12-08T02:55:03","guid":{"rendered":"https:\/\/www2.tagen.tohoku.ac.jp\/lab\/takahashi-s\/?page_id=66"},"modified":"2025-01-22T11:14:59","modified_gmt":"2025-01-22T02:14:59","slug":"2000%e5%b9%b4%ef%bd%9e2010%e5%b9%b4","status":"publish","type":"page","link":"https:\/\/www2.tagen.tohoku.ac.jp\/lab\/takahashi-s\/achievements\/2000%e5%b9%b4%ef%bd%9e2010%e5%b9%b4\/","title":{"rendered":"2000\u5e74\uff5e2010\u5e74"},"content":{"rendered":"<h2 style=\"text-align: center\">2008<\/h2>\n<ul>\n<li>Uzawa, T., Nishimura, C., Akiyama, S., Ishimori, K., <u><strong>Takahashi, S<\/strong><\/u>.*, Dyson, H. J., Wright, P. E.*<br \/>\n&#8220;Hierarchical folding mechanism of apomyoglobin revealed by ultra-fast H\/D exchange coupled with 2D NMR\u201d <em>Proc. Natl. Acad. Sci. USA. <\/em>105, 13859-13864 (2008) [<a href=\"http:\/\/www.pnas.org\/content\/early\/2008\/09\/06\/0804033105\">Abstract<\/a>]<\/li>\n<li>Kimura,T., Maeda, A., Nishiguchi, S., Ishimori, K., Morishima, I., Konno, T., Goto, Y., <u><strong>Takahashi, S<\/strong><\/u>.* \u201cDehydration of mainchain amides in the final folding step of single chain monellin revealed by time-resolved infrared spectroscopy\u201d<br \/>\n<em>Proc. Natl. Acad. Sci. USA<\/em>. 105, 13391-13396 (2008)[<a href=\"http:\/\/www.pnas.org\/content\/105\/36\/13391\">Abstract<\/a>]<\/li>\n<\/ul>\n<h2 style=\"text-align: center\">2007<\/h2>\n<ul>\n<li>Kinoshita, M. ,Kamagata, K., Maeda, A., Goto, Y., Komatsuzaki, T., <u><strong>Takahashi, S<\/strong><\/u>.* \u201cDevelopment of a technique for the investigation of folding dynamics of single proteins for extended time periods<em>\u201d Proc. Natl. Acad. Sci. USA,<\/em> 104,10453-10458 (2007\uff09[<a href=\"http:\/\/www.pnas.org\/content\/104\/25\/10453.full\">Abstract<\/a>]<\/li>\n<li>Nishiguchi, S., Goto, Y., <u><strong>Takahashi, S<\/strong><\/u>.\u201cSolvation and desolvation dynamics in apomyoglobin folding monitored by time-resolved infrared spectroscopy\u201d<br \/>\n<em>J. Mol. Biol.<\/em> 373,491-502 (2007)\u00a0[<a href=\"http:\/\/www.sciencedirect.com\/science?_ob=ArticleURL&amp;_udi=B6WK7-4PFW6JB-1&amp;_user=143915&amp;_coverDate=08%2F19%2F2007&amp;_rdoc=1&amp;_fmt=&amp;_orig=search&amp;_sort=d&amp;view=c&amp;_acct=C000011799&amp;_version=1&amp;_urlVersion=0&amp;_userid=143915&amp;md5=e2469824080acfca11709bd6d6d62f1b\">Abstract<\/a>]<\/li>\n<li>Matsumoto,S., Yane, A., Nakashima, S., Hashida, M., Fujita, M., Goto, Y., <u><strong>Takahashi, S<\/strong><\/u>.\u201cA Rapid Flow Mixer with 11-ms Mixing Time Microfabricated by a Pulsed-laser Ablation Technique: Observation of a Barrier-limited Collapse in Cytochrome c Folding\u201d<br \/>\n<em>J. Am. Chem. Soc. <\/em>129, 3840-3841 (2007)\u00a0[<a href=\"http:\/\/pubs.acs.org\/doi\/abs\/10.1021\/ja0660958\">Abstract<\/a>]<\/li>\n<li>Lee,Y. H., Tamura, K., Maeda, M., Hoshino, M., Sakurai, K.,<u><strong>Takahashi, S<\/strong><\/u>., Ikegami, T., Hase, T., Goto, Y.\u201cCores and pH-dependent Dynamics of Ferredoxin-NADP+ Reductase Revealed by Hydrogen \/ Deuterium Exchange\u201d<em>J. Biol. Chem.<\/em> : 282,5959-5967 (2007)\u00a0[<a href=\"http:\/\/www.jbc.org\/cgi\/content\/abstract\/282\/8\/5959\">Abstract<\/a>]<\/li>\n<\/ul>\n<h2 style=\"text-align: center\">2006<\/h2>\n<ul>\n<li>Iwata, K., Fujiwara, T., Matsuki, Y., Akutsu, H., <u><strong>Takahashi, S<\/strong><\/u>., Naiki, H., Goto, Y. \u201c3D structure of amyloid protofilaments of beta2-microglobulin fragment probed by solid-state NMR\u201d Proc. Natl. Acad. Sci. USA, 103,18119-18124 (2006) [<a href=\"http:\/\/www.pnas.org\/content\/103\/48\/18119.full\">Abstract<\/a>]<\/li>\n<li>Uzawa, T., Kimura, T., Ishimori, K., Morishima, I., Matsui, T., Ikeda-Saito, M., <u><strong>Takahashi, S<\/strong><\/u>., Akiyama, S., Fujisawa, T. \u201cTime-resolved small-angle X-ray scattering investigation of the folding dynamics of heme oxygenase: Implication of the scaling relationship for the submillisecond intermediates of protein folding\u201d J. Mol. Biol. : 357,997-1008 (2006)\u00a0[<a href=\"http:\/\/www.sciencedirect.com\/science?_ob=ArticleURL&amp;_udi=B6WK7-4J3NX17-1&amp;_user=127492&amp;_coverDate=03%2F31%2F2006&amp;_rdoc=29&amp;_fmt=high&amp;_orig=browse&amp;_srch=doc-info(%23toc%236899%232006%23996429996%23619223%23FLA%23display%23Volume)&amp;_cdi=6899&amp;_sort=d&amp;_docanchor=&amp;_ct=33&amp;_acct=C000009858&amp;_version=1&amp;_urlVersion=0&amp;_userid=127492&amp;md5=2e47df5c715f3659dba74e05ddf2da92\">Abstract<\/a>]<\/li>\n<\/ul>\n<h2 style=\"text-align: center\">2005<\/h2>\n<ul>\n<li>Yamaguchi, K., <u><strong>Takahashi, S<\/strong><\/u>., Kawai, T., Naiki, H., Goto, Y. \u201cSeeding-dependent propagation and maturation of amyloid fibril conformation\u201d J. Mol. Biol. : 352, 952-960 (2005)\u00a0[<a href=\"http:\/\/www.sciencedirect.com\/science?_ob=ArticleURL&amp;_udi=B6WK7-4GTVW54-1&amp;_user=127492&amp;_coverDate=09%2F30%2F2005&amp;_alid=1000677102&amp;_rdoc=1&amp;_fmt=high&amp;_orig=search&amp;_cdi=6899&amp;_sort=r&amp;_docanchor=&amp;view=c&amp;_ct=42&amp;_acct=C000009858&amp;_version=1&amp;_urlVersion=0&amp;_userid=127492&amp;md5=3a136ee02fa3da113e04eb9de16138cd\">Abstract<\/a>]<\/li>\n<li>Shintaku, M., Matsuura, K., Yoshioka, S., <u><strong>Takahashi, S<\/strong><\/u>., Ishimori, K., Morishima, I. \u201cAbsence of a detectable intermediate in the compound I formation of horseradish peroxidase at ambient temperature\u201d J. Biol. Chem. :280, 40934-40938 (2005)\u00a0[<a href=\"http:\/\/www.jbc.org\/cgi\/content\/abstract\/280\/49\/40934?maxtoshow=&amp;HITS=10&amp;hits=10&amp;RESULTFORMAT=&amp;fulltext=Absence+of+a+detectable+intermediate+in+the+compound+I+formation+of+horseradish+&amp;andorexactfulltext=and&amp;searchid=1&amp;FIRSTINDEX=0&amp;sortspec=relevance&amp;resourcetype=HWCIT\">Abstract<\/a>]<\/li>\n<li>Kameda, A., Hoshino, M., Higurashi, T., <u><strong>Takahashi, S<\/strong><\/u>., Naiki, H., Goto, Y.<br \/>\n\u201cNuclear magnetic resonance characterization of the refolding intermediate of beta2-microglobulin trapped by non-native prolyl peptide bond\u201d J. Mol. Biol. : 348, 383-397 (2005)\u00a0[<a href=\"http:\/\/www.sciencedirect.com\/science?_ob=ArticleURL&amp;_udi=B6WK7-4FNW1K6-2&amp;_user=143915&amp;_handle=V-WA-A-W-WB-MsSAYVW-UUA-U-AAACWDZEEE-AAAWYCDDEE-WDBCUYVZ-WB-U&amp;_fmt=summary&amp;_coverDate=04%2F29%2F2005&amp;_rdoc=13&amp;_orig=browse&amp;_srch=%23toc%236899%232005%23996519997%23591288!&amp;_cdi=6899&amp;view=c&amp;_acct=C000011799&amp;_version=1&amp;_urlVersion=0&amp;_userid=143915&amp;md5=d570c5cb17be4d12e7953ba84ccaa72a\">Abstract<\/a>]<\/li>\n<li>Kimura, T., Akiyama, S., Uzawa, T., Ishimori, K., Morishima, I., Fujisawa, T., <u><strong>Takahashi, S<\/strong><\/u><strong>.<\/strong><br \/>\n\u201cSpecifically collapsed intermediate in the early stage of the folding of ribonuclease A\u201d<br \/>\nJ. Mol. Biol. : 350, 349-362 (2005)\u00a0[<a href=\"http:\/\/www.sciencedirect.com\/science?_ob=ArticleURL&amp;_udi=B6WK7-4G643JH-3&amp;_user=127492&amp;_coverDate=07%2F08%2F2005&amp;_alid=1000682034&amp;_rdoc=1&amp;_fmt=high&amp;_orig=search&amp;_cdi=6899&amp;_sort=r&amp;_docanchor=&amp;view=c&amp;_ct=102&amp;_acct=C000009858&amp;_version=1&amp;_urlVersion=0&amp;_userid=127492&amp;md5=658c2a8b3c29c241448b2f0428052003\">Abstract<\/a>]<\/li>\n<li>Wadai, H., Yamaguchi, K., <u><strong>Takahashi, S<\/strong><\/u>., Kanno, T., Kawai, T., Naiki, H., Goto Y.<br \/>\n\u201cStereospecific amyloid-like fibril formation by a peptide fragment of beta2-microglobulin.\u201d<br \/>\nBiochemistry : 44, 157-164 (2005)\u00a0[<a href=\"http:\/\/pubs.acs.org\/doi\/abs\/10.1021\/bi0485880\">Abstract<\/a>]<\/li>\n<li>Kimura, T., Uzawa, T., Ishimori, K., Morishima, I., <u><strong>Takahashi, S<\/strong><\/u>., Konno, T., Akiyama, S., Fujisawa, T. \u201cSpecific collapse followed by slow hydrogen-bond formation of beta-sheet in the folding of single-chain monellin.\u201d Proc. Natl. Acad. Sci. USA. 102, 2748-2753 (2005)\u00a0[<a href=\"http:\/\/www.pnas.org\/gca?allch=&amp;gca=pnas%3B102%2F8%2F2748#top-1\">Abstract<\/a>]<\/li>\n<\/ul>\n<h2 style=\"text-align: center\">2004<\/h2>\n<ul>\n<li>Uzawa, T., Akiyama, S., Kimura, T., <u><strong>Takahashi, S<\/strong><\/u>.*, Ishimori, K., Morishima, I., Fujisawa, T.*<br \/>\n&#8220;Collapse and search dynamics of apomyoglobin folding revealed by submillisecond observations of alpha-helical content and compactness.&#8221; Proc. Natl. Acad. Sci. USA. 101, 1171-1176 (2004)\u00a0[<a href=\"http:\/\/www.pnas.org\/gca?allch=&amp;gca=pnas%3B101%2F5%2F1171#top-1\">Abstract<\/a>]<\/li>\n<li>Inuzuka, T., Yun, B. G., Ishikawa, H., <u><strong>Takahashi, S<\/strong><\/u>., Hori, H., Matts, R. L., Ishimori, K., Morishima, I. \u201cIdentification of crucial histidines for heme binding in the N-terminal domain of the heme-regulated eIF2alpha kinase.\u201d J. Biol. Chem. 279, 6778-6682 (2004) [<a href=\"http:\/\/www.jbc.org\/cgi\/content\/abstract\/279\/8\/6778?maxtoshow=&amp;HITS=10&amp;hits=10&amp;RESULTFORMAT=&amp;fulltext=Identification+of+crucial+histidines+for+heme+binding+in+the+N-terminal+domain+o&amp;andorexactfulltext=and&amp;searchid=1&amp;FIRSTINDEX=0&amp;sortspec=relevance&amp;resourcetype=HWCIT\">Abstract<\/a>]<\/li>\n<li>Matsuura, K., Yoshioka, S., <u><strong>Takahashi S<\/strong><\/u>, Ishimori K, Mogi T, Hori H, Morishima I.<br \/>\n\u201cDioxygen reduction by bo-type quinol oxidase from Escherichia coli studied by submillisecond-resolved freeze-quench EPR spectroscopy.\u201d Biochemistry43, 2288-2296 (2004)\u00a0[<a href=\"http:\/\/pubs.acs.org\/doi\/abs\/10.1021\/bi0355490?prevSearch=Dioxygen%2Breduction%2Bby%2Bbo-type%2Bquinol%2Boxidase%2Bfrom%2BEscherichia%2Bcoli%2Bstudied%2Bby%2Bsubmillisecond-resolved%2Bfreeze-quench%2BEPR%2Bspectroscopy&amp;searchHistoryKey=\">Abstract<\/a>]<\/li>\n<li>Matsuura, K., Tosha, T., Yoshioka, S., <u><strong>Takahashi, S<\/strong><\/u>., Ishimori, K., Morishima, I.<br \/>\n\u201cStructuraland functional characterization of &#8220;laboratory evolved&#8221; cytochrome P450cam mutants showing enhanced naphthalene oxygenation activity.\u201d Biochem. Biophys. Res. Commun. 323, 1209-1215 (2004)\u00a0[<a href=\"http:\/\/www.sciencedirect.com\/science?_ob=ArticleURL&amp;_udi=B6WBK-4DB576B-3&amp;_user=127492&amp;_rdoc=1&amp;_fmt=&amp;_orig=search&amp;_sort=d&amp;_docanchor=&amp;view=c&amp;_acct=C000009858&amp;_version=1&amp;_urlVersion=0&amp;_userid=127492&amp;md5=b31f81f0e12f7130f25cb0a8f54cab10\">Abstract<\/a>]<\/li>\n<li>Ishikawa, H., <u><strong>Takahashi, S<\/strong><\/u>., Ishimori, K., Morishima, I. \u201cSteric effects of isoleucine 107 on heme reorientation reaction in human myoglobin.\u201d Biochem. Biophys. Res. Commun. 324, 1095-1100 (2004)\u00a0[<a href=\"http:\/\/www.sciencedirect.com\/science?_ob=ArticleURL&amp;_udi=B6WBK-4DGW3M9-8&amp;_user=127492&amp;_rdoc=1&amp;_fmt=&amp;_orig=search&amp;_sort=d&amp;_docanchor=&amp;view=c&amp;_acct=C000009858&amp;_version=1&amp;_urlVersion=0&amp;_userid=127492&amp;md5=9b791b27dc50af4bff01b4095440286b\">Abstract<\/a>]<\/li>\n<li>Kumita, H., Matsuura, K., Hino, T., <u><strong>Takahashi, S<\/strong><\/u>., Hori, H., Fukumori, Y., Morishima, I., Shiro, Y.<br \/>\n\u201cNO reduction by nitric-oxide reductase from denitrifying bacterium Pseudomonas aeruginosa: characterization of reaction intermediates that appear in the single turnover cycle.\u201d<br \/>\nJ. Biol. Chem. : 279,55247-55254 (2004)\u00a0[<a href=\"http:\/\/www.jbc.org\/cgi\/content\/abstract\/279\/53\/55247?maxtoshow=&amp;HITS=10&amp;hits=10&amp;RESULTFORMAT=&amp;fulltext=NO+reduction+by+nitric-oxide+reductase+from+denitrifying+bacterium+Pseudomonas+a&amp;andorexactfulltext=and&amp;searchid=1&amp;FIRSTINDEX=0&amp;sortspec=relevance&amp;resourcetype=HWCIT\">Abstract<\/a>]<\/li>\n<li>Ban, T., Hoshino, M., <u><strong>Takahashi, S<\/strong><\/u>., Hamada, D., Hasegawa, K., Naiki, H., Goto, Y. \u201cDirect observation of Abeta amyloid fibril growth and inhibition.\u201d J. Mol. Biol. : 344, 757-767 (2004)\u00a0[<a href=\"http:\/\/www.ncbi.nlm.nih.gov\/pubmed\/15533443?dopt=Abstract\">Abstract<\/a>]<\/li>\n<li>Egawa, T., Hishiki, T., Ichikawa, Y., Kanamori, Y., Shimada, H.,<u><strong>Takahashi, S<\/strong><\/u>., Kitagawa, T., Ishimura, Y. \u201cRefolding processes of cytochrome P450cam from ferric and ferrous acid forms to the native conformation. Formations of folding intermediates with non-native heme coordination state.\u201d J. Biol. Chem. : 279, 32008-32017 (2004)\u00a0[<a href=\"http:\/\/www.jbc.org\/cgi\/content\/abstract\/279\/31\/32008?maxtoshow=&amp;HITS=10&amp;hits=10&amp;RESULTFORMAT=&amp;andorexactfulltext=and&amp;searchid=1&amp;FIRSTINDEX=0&amp;sortspec=relevance&amp;volume=279&amp;firstpage=32008&amp;resourcetype=HWCIT\">Abstract<\/a>]<\/li>\n<\/ul>\n<h2 style=\"text-align: center\">2003<\/h2>\n<ul>\n<li>Tosha, T., Yoshioka, S., <u><strong>Takahashi, S<\/strong><\/u>., Ishimori, K., Shimada, H., Morishima, I. \u201cNMR study on the structural changes of cytochrome P450cam upon the complex formation with putidaredoxin. Functional significance of the putidaredoxin-induced structural changes.\u201d<br \/>\nJ. Biol. Chem. 278, 39809-39821 (2003)\u00a0[<a href=\"http:\/\/www.jbc.org\/cgi\/content\/abstract\/278\/41\/39809?maxtoshow=&amp;HITS=10&amp;hits=10&amp;RESULTFORMAT=&amp;andorexactfulltext=and&amp;searchid=1&amp;FIRSTINDEX=0&amp;sortspec=relevance&amp;volume=278&amp;firstpage=39809&amp;resourcetype=HWCIT\">Abstract<\/a>]<\/li>\n<li>Egawa, T., Yoshioka, S.,<u> <strong>Takahashi, S<\/strong><\/u>., Hori, H., Nagano, S., Shimada, H., Ishimori, K., Morishima, I., Suematsu, M., Ishimura, Y. \u201cKinetic and spectroscopic characterization of a hydroperoxy compound in the reaction of native myoglobin with hydrogen peroxide.\u201d J. Biol. Chem. 278, 41597-41606 (2003)\u00a0[<a href=\"http:\/\/www.jbc.org\/cgi\/content\/abstract\/278\/43\/41597?maxtoshow=&amp;HITS=10&amp;hits=10&amp;RESULTFORMAT=&amp;andorexactfulltext=and&amp;searchid=1&amp;FIRSTINDEX=0&amp;sortspec=relevance&amp;volume=278&amp;firstpage=41597&amp;resourcetype=HWCIT\">Abstract<\/a>]<\/li>\n<li>Tanaka, M., Matsuura, K., Yoshioka, S., <u><strong>Takahashi, S<\/strong><\/u>., Ishimori, K., Hori, H., Morishima, I.<br \/>\n\u201cActivationof Hydrogen Peroxide in Horseradish Peroxidase Occurs within ~300\u03bcs Observed by a New Freeze-Quench Device\u201d Biophys. J. (2003). 84, 1998-2004.\u00a0[<a href=\"http:\/\/www.pubmedcentral.nih.gov\/articlerender.fcgi?tool=pubmed&amp;pubmedid=12609902\">Abstract<\/a>]<\/li>\n<\/ul>\n<h2 style=\"text-align: center\">2002<\/h2>\n<ul>\n<li>Akiyama, S., <u><strong>Takahashi, S<\/strong><\/u>., Kimura, T., Ishimori, K., Morishima, I., Nishikawa, Y.,Fujisama, T.,<br \/>\n\u201cConformational Landscape of Cytochrome c Folding Studied by Microsecond-Resolved Small Angle X-ray Scattering\u201d Proc. Natl. Acad. Sci. U. S. A.. 99. 1329-1334 (2002)\u00a0[<a href=\"http:\/\/www.pnas.org\/gca?allch=&amp;gca=pnas%3B99%2F3%2F1329\">Abstract<\/a>]<\/li>\n<li>Kimura, T., <u><strong>Takahashi, S<\/strong><\/u>., Akiyama, S., Uzawa, T., Ishimori, K., Morishima, I. \u201cDirect Observation of the Multi-step Helix Formation of Poly-L-glutamic acids\u201d J. Am. Chem. Soc. (2002). 124, 11596-11597.\u00a0[<a href=\"http:\/\/pubs.acs.org\/doi\/abs\/10.1021\/ja026639f\">Abstract<\/a>]<\/li>\n<li>Yoshioka, S., Tosha, T.,<u> <strong>Takahashi, S<\/strong><\/u>., Ishimori, K., Morishima, I. \u201cRoles of the Proximal Hydrogen Bonding Network in Cytochrome P450cam-Catalyzed Oxygenation\u201d<br \/>\nJ. Am. Chem. Soc. 124, 14571-14579 (2002)\u00a0[<a href=\"http:\/\/pubs.acs.org\/doi\/abs\/10.1021\/ja0265409\">Abstract<\/a>]<\/li>\n<li>Ishikawa, H., Yun, B.-G., <u><strong>Takahashi, S<\/strong><\/u>., Hori, H., Matts, R. L., Ishimori, K., Morishima, I. \u201cNO-induced Activation Mechanism of the Heme-regulated eIF2 Kinase\u201d J. Am. Chem. Soc. 124, 13696-13697 (2002)\u00a0[<a href=\"http:\/\/pubs.acs.org\/doi\/abs\/10.1021\/ja0272336\">Abstract<\/a>]<\/li>\n<li>Tosha, T., Yoshioka, S., <u><strong>Takahashi, S<\/strong><\/u>., Hori, H., Ishimori, K., Morishima, I. \u201cMolecular Mechanism of Electron Transfer Reaction in Cytochrome P450cam-Putidaredoxin: Roles of Gln360 at the Heme Proximal Site\u201d Biochemistry 41, 13883-13893 (2002)\u00a0[<a href=\"http:\/\/pubs.acs.org\/doi\/abs\/10.1021\/bi0261037?prevSearch=%255Bauthor%253A%2BTosha%252C%2BT%255D&amp;searchHistoryKey=\">Abstract<\/a>]<\/li>\n<\/ul>\n<h2 style=\"text-align: center\">2001<\/h2>\n<ul>\n<li>Ishikawa, H., Uchida, T., <u><strong>Takahashi, S<\/strong><\/u>., Ishimori, K., Morishima, I. \u201cLigand Migration in Human Myoglobin: Steric Effects of Isoleucine 107(G8) on O2 and CO Binding\u201d Biophys. J. 80, 1507-1517 (2001)\u00a0[<a href=\"http:\/\/www.pubmedcentral.nih.gov\/articlerender.fcgi?tool=pubmed&amp;pubmedid=11222311\">Abstract<\/a>]<\/li>\n<li>Shibata, Y., Ishikawa, H., <u><strong>Takahashi, S<\/strong><\/u>., Morishima, I. \u201cTime-Resolved Hole-Burning Study on Myoglobin: Fluctuation of Restricted Water within Distal Pocket\u201d Biophys. J. 80, 1013-1023 (2001)\u00a0[<a href=\"http:\/\/www.pubmedcentral.nih.gov\/articlerender.fcgi?tool=pubmed&amp;pubmedid=11159468\">Abstract<\/a>]<\/li>\n<li>Yamamoto, K., Ishikawa, H., <u><strong>Takahashi, S<\/strong><\/u>., Ishimori, K., Morishima, I., Nakajima, H., Aono, S. \u201cBinding of CO at the Pro2 Side Is Crucial for the Activation of CO-Sensing Transcriptional Activator CooA &#8211; H1-NMR Spectroscopic Studies\u201d J. Biol. Chem. 276, 11473-11476 (2001)\u00a0[<a href=\"http:\/\/www.jbc.org\/cgi\/content\/abstract\/276\/15\/11473?maxtoshow=&amp;HITS=10&amp;hits=10&amp;RESULTFORMAT=&amp;andorexactfulltext=and&amp;searchid=1&amp;FIRSTINDEX=0&amp;sortspec=relevance&amp;volume=276&amp;firstpage=11473&amp;resourcetype=HWCIT\">Abstract<\/a>]<\/li>\n<li>Yoshioka, S., <u><strong>Takahashi, S<\/strong><\/u>., Hori, H., Ishimori, K., Morishima, I. \u201cProximal Cysteine Residue Is Essential for the Enzymatic Activities of Cytochrome P450cam\u201d<br \/>\nEur. J. Biochem. 268, 252-259 (2001)\u00a0[<a href=\"http:\/\/www3.interscience.wiley.com\/journal\/118990627\/abstract?CRETRY=1&amp;SRETRY=0\">Abstract<\/a>]<\/li>\n<\/ul>\n<h2 style=\"text-align: center\">2000<\/h2>\n<ul>\n<li>Akiyama, S., <u><strong>Takahashi, S<\/strong><\/u>.,Ishimori, K., Morishima, I. \u201cStepwise Formation of Alpha-Helices During Cytochrome c Folding\u201d Nat. Struct. Biol. 7, 514-520 (2000)\u00a0[<a href=\"http:\/\/www.nature.com\/nsmb\/journal\/v7\/n6\/full\/nsb0600_514.html\">Abstract<\/a>]<\/li>\n<li>Ihara, M., Shintaku, M., <u><strong>Takahashi, S<\/strong><\/u>., Ishimori, K., Morishima, I. \u201cConversion of an Electron-Transfer Protein into an Oxygen Binding Protein: The Axial Cytochrome b5 Mutant with an Unusually High O2 Affinity\u201d J. Am. Chem. Soc. 122, 11535-11536 (2000)\u00a0[<a href=\"http:\/\/pubs.acs.org\/doi\/abs\/10.1021\/ja002914r\">Abstract<\/a>]<\/li>\n<li>Ihara, M., <u><strong>Takahashi, S<\/strong><\/u>., Ishimori, K., Morishima, I. \u201cFunctions of Fluctuation in the Heme-Binding Loops of Cytochrome b5 Revealed in the Process of Heme Incorporation\u201d Biochemistry 39, 5961-5970 (2000)\u00a0[<a href=\"http:\/\/pubs.acs.org\/doi\/abs\/10.1021\/bi9922289\">Abstract<\/a>]<\/li>\n<li>Yoshioka, S., <u><strong>Takahashi, S<\/strong><\/u>., Ishimori, K., Morishima, I. \u201cRoles of the Axial Push Effect in Cytochrome P450cam Studied with the Site-Directed Mutagenesis at the Heme Proximal Site\u201d J. Inorg. Biochem. 81, 141-151 (2000)\u00a0[<a href=\"http:\/\/www.sciencedirect.com\/science?_ob=ArticleURL&amp;_udi=B6TGG-417WD0D-3&amp;_user=127492&amp;_rdoc=1&amp;_fmt=&amp;_orig=search&amp;_sort=d&amp;_docanchor=&amp;view=c&amp;_acct=C000009858&amp;_version=1&amp;_urlVersion=0&amp;_userid=127492&amp;md5=24f0b27010fa21a4aacdfd3ac412ffd8\">Abstract<\/a>]<\/li>\n<li>Han, S., <u><strong>Takahashi, S<\/strong><\/u>., Rousseau, D. L. \u201cTime Dependence of the Catalytic Intermediates in Cytochrome c Oxidase\u201d J. Biol. Chem. 275, 1910-1919 (2000)\u00a0[<a href=\"http:\/\/www.jbc.org\/cgi\/content\/abstract\/275\/3\/1910?maxtoshow=&amp;HITS=10&amp;hits=10&amp;RESULTFORMAT=&amp;andorexactfulltext=and&amp;searchid=1&amp;FIRSTINDEX=0&amp;sortspec=relevance&amp;volume=275&amp;firstpage=1910&amp;resourcetype=HWCIT\">Abstract<\/a>]<\/li>\n<\/ul>\n","protected":false},"excerpt":{"rendered":"<p>2008 Uzawa, T., Nishimura, C., Akiyama, S., Ishimori, K., Taka&#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-66","page","type-page","status-publish","hentry"],"_links":{"self":[{"href":"https:\/\/www2.tagen.tohoku.ac.jp\/lab\/takahashi-s\/wp-json\/wp\/v2\/pages\/66","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=66"}],"version-history":[{"count":4,"href":"https:\/\/www2.tagen.tohoku.ac.jp\/lab\/takahashi-s\/wp-json\/wp\/v2\/pages\/66\/revisions"}],"predecessor-version":[{"id":1093,"href":"https:\/\/www2.tagen.tohoku.ac.jp\/lab\/takahashi-s\/wp-json\/wp\/v2\/pages\/66\/revisions\/1093"}],"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=66"}],"curies":[{"name":"wp","href":"https:\/\/api.w.org\/{rel}","templated":true}]}}