{"id":164,"date":"2015-12-08T15:38:18","date_gmt":"2015-12-08T06:38:18","guid":{"rendered":"https:\/\/www2.tagen.tohoku.ac.jp\/lab\/takahashi-s\/?page_id=164"},"modified":"2015-12-08T15:42:53","modified_gmt":"2015-12-08T06:42:53","slug":"%e8%ab%96%e6%96%87%e7%b4%b9%e4%bb%8b2013","status":"publish","type":"page","link":"https:\/\/www2.tagen.tohoku.ac.jp\/lab\/takahashi-s\/seminar\/%e8%ab%96%e6%96%87%e7%b4%b9%e4%bb%8b2013\/","title":{"rendered":"\u8ad6\u6587\u7d39\u4ecb2013"},"content":{"rendered":"

\"\"\u00a0No.32\u30002014.3.17
\n\u62c5\u5f53\u8005<\/strong>\uff1a \u5409\u7530\u6587
\n\u8ad6\u6587<\/strong>\uff1aEvidence of an Intermediate and Parallel Pathways in Protein Unfolding from Single-Molecule Fluorescence
\nAngel Orte et al.
\nJ. Am. Chem. Soc., 2008,130 (25), pp 7898-7907<\/p>\n

\"\"\u00a0No.31\u30002014.3.10
\n\u62c5\u5f53\u8005<\/strong>\uff1a \u5c0f\u4e95\u5ddd\u6d69\u4e4b
\n\u8ad6\u6587<\/strong>\uff1aContinuous throughput and long-term observation of single-molecule FRET without immobilization
\nSwati Tyagi et al.
\nNature Methods, vol.11, no.3, 2014<\/p>\n

\"\"\u00a0No.30\u30002014.3.3
\n\u62c5\u5f53\u8005<\/strong>\uff1a \u938c\u5f62\u6e05\u4eba
\n\u8ad6\u6587<\/strong>\uff1aFolding of tetrameric p53: oligomerization and tumorigenic mutations induce misfolding and loss of function.
\nLubin DJ et al.
\nJ. Mol. Biol.<\/em> 2010 395(4) : 705-16<\/p>\n

Kinetic partitioning during folding of the p53 DNA binding domain.
\nButler JS et al.
\nJ. Mol. Biol.<\/em> 2005 350 (5) : 9906-18<\/p>\n

\"\"\u00a0No.29\u30002014.2.24
\n\u62c5\u5f53\u8005<\/strong>\uff1a \u9ad8\u6a4b\u8061
\n\u8ad6\u6587<\/strong>\uff1aImpact of reconstituted cytosol on protein stability
\nMohona Sarkar et al.
\nPNAS<\/em> (2013) 110, 19342-19347<\/p>\n

\"\"\u00a0No.28\u30002014.2.17
\n\u62c5\u5f53\u8005<\/strong>\uff1a \u5207\u53e3\u7406\u6075
\n\u8ad6\u6587<\/strong>\uff1aRapid protein-folding assay using green fluorescent protein
\nGeoffrey S. Waldo et al.
\nNat Biotechnol.<\/em> 1999 Jul;17(7):691-5.<\/p>\n

\"\"\u00a0No.27\u30002014.2.10
\n\u62c5\u5f53\u8005<\/strong>\uff1a \u4f0a\u85e4\u512a\u5fd7
\n\u8ad6\u6587<\/strong>\uff1aUltrafast Hydrogen Exchange Reveals Specific Structural Events during the Initial Stages of Folding of Cytochrome
\nc
\n<\/em>Hossein Fazelinia et al.
\nJ. Am. Chem. Soc.,<\/em>2014, 136, 733-740<\/p>\n

\"\"\u00a0No.26\u30002014.2.4
\n\u62c5\u5f53\u8005<\/strong>\uff1a \u963f\u8607\u88d5\u6a39
\n\u8ad6\u6587<\/strong>\uff1aTwo-Color, Laser Excitation Improves Temporal Resolution for Detecting the Dynamic, Plasmonic Coupling between MetallicNanoparticles
\nDiane M. Wiener and Troy A. Lionberger
\nAnal. Chem.<\/em> 2013,85,5095-5102<\/p>\n

\"\"\u00a0No.25\u30002014.1.27
\n\u62c5\u5f53\u8005<\/strong>\uff1a \u5409\u7530\u6587
\n\u8ad6\u6587<\/strong>\uff1aFolding of a large protein at high structural resolution
\nBenjamin T. Walters et al.
\nPNAS<\/em>, vol. 110, no.47 (2013) 18898-18903<\/p>\n

\"\"\u00a0No.24\u30002014.1.6
\n\u62c5\u5f53\u8005<\/strong>\uff1a \u938c\u5f62\u6e05\u4eba
\n\u8ad6\u6587<\/strong>\uff1aEngineering of weak helper interactions fo high-efficiency FRET probes
\nRaik Grunberg et al.
\nNature Methods<\/em> Vol.10 No.10 1021-1027 (2013)<\/p>\n

\"\"\u00a0No.23\u30002013.12.16
\n\u62c5\u5f53\u8005<\/strong>\uff1a \u5c0f\u4e95\u5ddd\u6d69\u4e4b
\n\u8ad6\u6587<\/strong>\uff1aSingle-molecule fluorescence probes dynamics of barrier crossing
\nHoi Sung Chung & William A. Eaton
\nNature<\/em> 502, 685-688 (2013)<\/p>\n

\"\"\u00a0No.22\u30002013.11.25
\n\u62c5\u5f53\u8005<\/strong>\uff1a \u9ad8\u6a4b\u8061
\n\u8ad6\u6587<\/strong>\uff1aProbing the protein-folding mechanism using denaturant and temperature effects on rate vonstants
\nEmily j. Guinn et al.
\nPNAS<\/em>, vol.110, no.42, 16784-16789<\/p>\n

\"\"\u00a0No.21\u30002013.11.18
\n\u62c5\u5f53\u8005<\/strong>\uff1a \u5207\u53e3\u7406\u6075
\n\u8ad6\u6587<\/strong>\uff1aProtein tagging and detection with engineered self-assembling fragments of green fluorescent protein
\nCabantous, S. et al.
\nNature biotechnology<\/em>, 23(1), 102-107<\/p>\n

\"\"\u00a0No.20\u30002013.11.11
\n\u62c5\u5f53\u8005<\/strong>\uff1a \u4f0a\u85e4\u512a\u5fd7
\n\u8ad6\u6587<\/strong>\uff1aFolding and Binding of an Intrinsically Disordered Protein: Fast, but Not ‘Diffusion-Limited’
\nJoseph M. Rogers et al.
\nJ.Am. Chem. Soc. <\/em>2013,135,1415-1422<\/p>\n

\"\"\u00a0No.19\u30002013.10.21
\n\u62c5\u5f53\u8005<\/strong>\uff1a \u6751\u7530\u5d07\u4eba
\n\u8ad6\u6587<\/strong>\uff1aBypass of a protein barrier by a replicative DNA helicase
\nhasan Yardimci et al.
\n13. December, 2012, vol. 492, Nature<\/em><\/p>\n

\"\"\u00a0No.18\u30002013.10.7
\n\u62c5\u5f53\u8005<\/strong>\uff1a \u9f4a\u85e4\u96c5\u5d69
\n\u8ad6\u6587<\/strong>\uff1aPolymer scaling laws of unfolded and intrinsically disordered proteins quantified with single-molecule spectroscopy
\nhagen Hofmann et al.
\nPNAS<\/em>, vol.109, no.40, 16155-16160<\/p>\n

\"\"\u00a0No.17\u30002013.9.9
\n\u62c5\u5f53\u8005<\/strong>\uff1a \u963f\u8607\u88d5\u6a39
\n\u8ad6\u6587<\/strong>\uff1aUbiquitin chain conformation regulates recognitionand \u00a0activity of interacting proteins
\nYu Ye et al.
\nNature<\/em>, vol.492<\/p>\n

\"\"\u00a0No.16\u30002013.9.2
\n\u62c5\u5f53\u8005<\/strong>\uff1a \u4e45\u4fdd\u7530\u4fca\u5f66
\n\u8ad6\u6587<\/strong>\uff1aSingle Molecule Fluorescence under Conditions of Fast Flow
\nMathew H. Horrocks et al.
\nAnal. Chem.<\/em> 2012,84 (1),pp179-185<\/p>\n

\"\"\u00a0No.15\u30002013.8.26
\n\u62c5\u5f53\u8005<\/strong>\uff1a \u5409\u7530\u6587
\n\u8ad6\u6587<\/strong>\uff1aA tightly regulated molecular toggle controls AAA+ disaggregase.
\nYuki Oguchi et al.
\nNature Structural & molecular biology<\/em>, volume 19, number 12, 2012,1338-1346<\/p>\n

\"\"\u00a0No.14\u30002013.8.19
\n\u62c5\u5f53\u8005<\/strong>\uff1a \u4e2d\u91ce\u99ff\u4ecb
\n\u8ad6\u6587<\/strong>\uff1aEngineered nanostructured \u03b2-sheet peptides protect membrane proteins
\nHouchao Tao et al.
\nNature Methods, Vol.10, No.8, 759-761<\/div>\n

\"\"\u00a0No.13\u30002013.8.5
\n\u62c5\u5f53\u8005<\/strong>\uff1a\u938c\u5f62\u6e05\u4eba
\n\u8ad6\u6587<\/strong>\uff1aSingle-molecule imaging of transcription factor binding to DNA in live mammalian cells.
\nGebhardt JC et al.
\nNat. Methods, \u00a02013 May; 10 (5): 421-6<\/p>\n

\"\"\u00a0No.12\u30002013.7.29
\n\u62c5\u5f53\u8005<\/strong>\uff1a\u5c0f\u4e95\u5ddd\u6d69\u4e4b
\n\u8ad6\u6587<\/strong>\uff1aSingle-molecule spectroscopy reveals photosynthetic LH2 complexes switch between emissive states
\nGabriela S. Schlau-Cohen et al.
\nPNAS, vol.110, No.27, 10899-10903<\/p>\n

\"\"\u00a0No.11\u30002013.7.22
\n\u62c5\u5f53\u8005<\/strong>\uff1a\u9ad8\u6a4b\u8061
\n\u8ad6\u6587<\/strong>\uff1aCrystal Structure of a GroEL-ADP complex in the relaxed allosteric state at 2.7 \u00c5 resolution
\nXue Fei et al.
\nPNAS <\/em>\uff082013\uff09<\/p>\n

\"\"\u00a0No.10\u30002013.7.8
\n\u62c5\u5f53\u8005<\/strong>\uff1a\u4e45\u4fdd\u7530\u4fca\u5f66
\n\u8ad6\u6587<\/strong>\uff1aGradual Disordering of the Native State on a Slow Two-State Folding Protein Monitored by Single-Molecule Fluorescence Spectroscopy and NMR
\nLuis Alberto Campos et al.
\nJ. Phys. Chem. B,<\/em> 24 Jun, 2013<\/p>\n

\"\"\u00a0No.9\u30002013.7.1
\n\u62c5\u5f53\u8005<\/strong>\uff1a\u5207\u53e3\u7406\u6075
\n\u8ad6\u6587<\/strong>\uff1aSurveyin Protein Structure and Function Using Bis-Arsenical Small Molecules
\nRebecca A. Scheck & Alanna Schepartz
\nAcc. Chem. Res.,<\/em> 2011,44, (9), pp 654-665<\/p>\n

\"\"\u00a0No.8\u30002013.6.24
\n\u62c5\u5f53\u8005<\/strong>\uff1a\u4f0a\u85e4\u512a\u5fd7
\n\u8ad6\u6587<\/strong>\uff1aIntrinsically Disordered p53 and its Complexes Populate Compact Conformations in the Gas Phase
\nKevin Pagel et al.
\nAngew. Chem. Int. Ed.<\/em> 2013, 52, 361-365<\/p>\n

\"\"\u00a0No.7\u30002013.6.17
\n\u62c5\u5f53\u8005<\/strong>\uff1a\u6751\u7530\u5d07\u4eba
\n\u8ad6\u6587<\/strong>\uff1aFrustration in protein-DNA binding infuences conformational switching and target search kinetics
\nAmir Marcovitz and yaakov Levy
\nPNAS,<\/i> vol.108, no.44, 17957-17962<\/p>\n

\"\"\u00a0No.5\u30002013.6.3
\n\u62c5\u5f53\u8005<\/strong>\uff1a\u5409\u7530\u6587
\n\u8ad6\u6587<\/strong>\uff1aMechanical Properties of \u03b2- Catenin revealed by Single-Molecule Experiments
\nAlejandro Valbuena et al.
\nBiophysical Journal,<\/em> Colume 103, Issue 8, 17 October 2012, pp1744-1752<\/p>\n

\"\"\u00a0No.4\u30002013.5.27
\n\u62c5\u5f53\u8005<\/strong>\uff1a\u963f\u8607\u88d5\u6a39
\n\u8ad6\u6587<\/strong>\uff1aSite-directed nanoparticle labeling of cytochrome c
\nMarie-Eve Aubin-Tam et al.
\nPNAS, January 16, 2009<\/p>\n

\"\"\u00a0No.3\u30002013.5.13
\n\u62c5\u5f53\u8005<\/strong>\uff1a\u9ad8\u6a4b\u8061
\n\u8ad6\u6587<\/strong>\uff1aAtomic-level description of ubiquitin folding
\nStefano Piana et al.
\nPNAS<\/em>, April 9, 2013, vol.110, no.15, 5915-5920<\/p>\n

\"\"\u00a0No.2\u30002013.4.22
\n\u62c5\u5f53\u8005<\/strong>\uff1a\u5c0f\u4e95\u5ddd\u6d69\u4e4b
\n\u8ad6\u6587<\/strong>\uff1aSingle molecule unfolding and atretching of protein domains inside a solid-state nanopore by electric field
\nKevin J. Freedman et al.
\nScientific Reports <\/em>3<\/strong>, Article number: 1638<\/p>\n

\"\"\u00a0No.1\u30002013.4.15
\n\u62c5\u5f53\u8005<\/strong>\uff1a\u938c\u5f62\u6e05\u4eba
\n\u8ad6\u6587<\/strong>\uff1aA single-molecule dissection of ligand binding to a protein with intrinsic dynamics
\nEunkyung Kim et al.
\nNature chemical biology<\/em><\/p>\n","protected":false},"excerpt":{"rendered":"

\u00a0No.32\u30002014.3.17 \u62c5\u5f53\u8005\uff1a \u5409\u7530\u6587 \u8ad6\u6587\uff1aEvidence of an Intermediate and P…<\/p>\n","protected":false},"author":1,"featured_media":0,"parent":151,"menu_order":0,"comment_status":"closed","ping_status":"closed","template":"","meta":{"footnotes":""},"class_list":["post-164","page","type-page","status-publish","hentry"],"_links":{"self":[{"href":"https:\/\/www2.tagen.tohoku.ac.jp\/lab\/takahashi-s\/wp-json\/wp\/v2\/pages\/164","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=164"}],"version-history":[{"count":1,"href":"https:\/\/www2.tagen.tohoku.ac.jp\/lab\/takahashi-s\/wp-json\/wp\/v2\/pages\/164\/revisions"}],"predecessor-version":[{"id":165,"href":"https:\/\/www2.tagen.tohoku.ac.jp\/lab\/takahashi-s\/wp-json\/wp\/v2\/pages\/164\/revisions\/165"}],"up":[{"embeddable":true,"href":"https:\/\/www2.tagen.tohoku.ac.jp\/lab\/takahashi-s\/wp-json\/wp\/v2\/pages\/151"}],"wp:attachment":[{"href":"https:\/\/www2.tagen.tohoku.ac.jp\/lab\/takahashi-s\/wp-json\/wp\/v2\/media?parent=164"}],"curies":[{"name":"wp","href":"https:\/\/api.w.org\/{rel}","templated":true}]}}