{"id":166,"date":"2015-12-08T15:38:48","date_gmt":"2015-12-08T06:38:48","guid":{"rendered":"https:\/\/www2.tagen.tohoku.ac.jp\/lab\/takahashi-s\/?page_id=166"},"modified":"2015-12-08T15:43:04","modified_gmt":"2015-12-08T06:43:04","slug":"%e8%ab%96%e6%96%87%e7%b4%b9%e4%bb%8b2012","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%8b2012\/","title":{"rendered":"\u8ad6\u6587\u7d39\u4ecb2012"},"content":{"rendered":"

\"\"\u00a0No.30\u30002013.3.18
\n\u62c5\u5f53\u8005<\/strong>\uff1a\u9f4a\u85e4\u96c5\u5d69
\n\u8ad6\u6587<\/strong>\uff1aDirect observation of multiple misfolding pathways in a single prion protein molecule
\nhao Yu et al.
\nPNAS vol. 109 (2012) 5283-5288\u00a0<\/em>
\n<\/em>
\n\"\"\u00a0No.29\u30002013.2.25
\n\u62c5\u5f53\u8005<\/strong>\uff1a\u6751\u7530\u5d07\u4eba
\n\u8ad6\u6587<\/strong>\uff1aDynamics of DNA Supercoils
\nM.T.J. van Loenhout \u00a0et al.
\nScience (2012) 94-7<\/em>
\n<\/em><\/p>\n

 <\/p>\n

\"\"\u00a0No.28\u30002013.2.12
\n\u62c5\u5f53\u8005<\/strong>\uff1a\u4e45\u4fdd\u7530\u4fca\u5f66
\n\u8ad6\u6587<\/strong>\uff1aNanochannel-Based Single Molecule recycling
\nJohn F. Lesoine et al.
\nNano Lett. (2012) 3273-3278<\/em><\/p>\n

\"\"\u00a0No.27\u30002013.2.4
\n\u62c5\u5f53\u8005<\/strong>\uff1a\u4e2d\u91ce\u99ff\u4ecb
\n\u8ad6\u6587<\/strong>\uff1aCytoplasmic ATP Hydrolysis Powers Transport of Lipopolysaccharide Across the Periplasm in E.coli
\nSuguru Okuda et al.
\nScience 30 (2012) 1214-1217<\/em><\/p>\n

\"\"\u00a0No.26\u30002013.1.21
\n\u62c5\u5f53\u8005<\/strong>\uff1a\u5c0f\u4e95\u5ddd\u6d69\u4e4b
\n\u8ad6\u6587<\/strong>\uff1aEnergy landscape analysis of native folding of the prion protein yields the diffusion constant, transition path time, and rates
\nHau Yu et al.
\nPNAS, 2012, vol109,no.36, 14452-14457<\/em><\/div>\n

\"\"\u00a0No.25\u30002013.1.15
\n\u62c5\u5f53\u8005<\/strong>\uff1a\u938c\u5f62\u6e05\u4eba
\n\u8ad6\u6587<\/strong>\uff1aTetramer of p53 in the Absence of DNA Forms a Relaxed Quaternary State.
\nPham N et al.
\nBiochemistry 2012, 51, 8053-8055<\/em><\/p>\n

\"\"\u00a0No.24\u30002012.12.3
\n\u62c5\u5f53\u8005<\/strong>\uff1a\u9ad8\u6a4b\u8061
\n\u8ad6\u6587<\/strong>\uff1aLocalizing internal friction along the reaction coordinate of protein folding by combining ensemble and single-molecule fluorescence spectroscopy
\nAlessandro Borgia et al.
\nNat. Comm. 3, 1195 \uff082012\uff09<\/i><\/p>\n

\"\"\u00a0No.23\u30002012.11.12
\n\u62c5\u5f53\u8005<\/strong>\uff1a\u4e2d\u91ce\u99ff\u4ecb
\n\u8ad6\u6587<\/strong>\uff1aDynamics of a bacterial multidrug ABC transporter in the inward- and outward-facing conformations
\nShahid Mehmood et al.
\nPNAS\u00a0<\/em>(2012) 109(27):10832-6<\/p>\n

\"\"\u00a0No.22\u30002012.11.5
\n\u62c5\u5f53\u8005<\/strong>\uff1a\u6751\u7530\u5d07\u4eba
\n\u8ad6\u6587<\/strong>\uff1aSequence-dependent sliding kinetics of p53
\njason S Leith et al.
\nPNAS <\/em>(2012)16552-16557<\/p>\n

\"\"\u00a0No.21\u30002012.10.29
\n\u62c5\u5f53\u8005<\/strong>\uff1a\u9f4a\u85e4\u96c5\u5d69
\n\u8ad6\u6587<\/strong>\uff1aObservation of protein Folding\/unfolding dynamics of ubiquitin trapped in agarose gel by single-molecule FRET
\nLi-Ling Yang et al.
\nEur Biophys J<\/em> (2012) 41:189-198<\/p>\n

\"\"\u00a0No.20\u30002012.10.22
\n\u62c5\u5f53\u8005<\/strong>\uff1a\u6589\u85e4\u7fd4
\n\u8ad6\u6587<\/strong>\uff1aConstruction of Gene Screening System Using Giant Unilamellar Liposomes and a Fluorescence-Activated Cell sorter
\nTakehiro NIshikawa et al.
\nAnalytical chemistry<\/em><\/p>\n

\"\"\u00a0No.19\u30002012.10.15
\n\u62c5\u5f53\u8005<\/strong>\uff1a\u4e45\u4fdd\u7530\u4fca\u5f66
\n\u8ad6\u6587<\/strong>\uff1aInertial lift enhanced phase partitioning for continuous microfluidic surface energy based sorting of particles
\nVahidreza Parichehreh and Palaniappan Sethu
\nLab Chip<\/em>, 2012, 12<\/strong>,1296-1301<\/p>\n

\"\"\u00a0No.18\u30002012.10.9
\n\u62c5\u5f53\u8005<\/strong>\uff1a\u6e21\u8fba\u512a
\n\u8ad6\u6587<\/strong>\uff1aSensing cooperativity in ATP hydrolysis for single multisubunit enzymes in solution
\nYan Jiang et al.
\nPNAS<\/em> vol.108 (2011) 41<\/strong>, 16962-16967<\/div>\n

\"\"\u00a0No.17\u30002012.10.1
\n\u62c5\u5f53\u8005<\/strong>\uff1a\u9ad8\u6a4b\u8056\u5f25
\n\u8ad6\u6587<\/strong>\uff1aInteraction of the p53 DNA-Binding Domein with Its N-Terminal Extension Modulates the Stability of the p53 Tetramer
\nJ. Mol. Biol.<\/em> (2011) 409<\/strong>, 358-368<\/p>\n

\"\"\u00a0No.16\u30002012.9.28
\n\u62c5\u5f53\u8005<\/strong>\uff1a\u5c0f\u4e95\u5ddd\u6d69\u4e4b
\n\u8ad6\u6587<\/strong>\uff1aSlow Unfolded-State Structuring in Acyl-CoA Binding Protein Folding Revealed by Simulation and Experiment
\nVincent A.Voelz et al.
\nJ. Am. Chem. Soc<\/em> 2012,<\/strong> 134\uff0c12565-12577<\/p>\n

\"\"\u00a0No.15\u30002012.9.14
\n\u62c5\u5f53\u8005<\/strong>\uff1a\ufffd\u6a4b\u8061
\n\u8ad6\u6587<\/strong>\uff1aRevisiting the contribution of negative charges on the chaperonin cage wall to the acceleration of protein folding
\nFumihiro Motojima et al.
\nPNAS<\/em>, (2012), early edition.<\/p>\n

\"\"\u00a0No.14\u30002012.8.24
\n\u62c5\u5f53\u8005<\/strong>\uff1a\u938c\u5f62\u6e05\u4eba
\n\u8ad6\u6587<\/strong>\uff1aStructural rearrangements underlying ligand-gating in Kir channels
\nShizhen Wang et al.
\nNature Communications <\/em>(2012)<\/div>\n

\"\"\u00a0No.13\u30002012.8.3
\n\u62c5\u5f53\u8005<\/strong>\uff1a\u4e2d\u91ce\u99ff\u4ecb
\n\u8ad6\u6587<\/strong>\uff1aDissociation of ATP-binding Cassette Nubleotide-binding Domain Dimers into Monomers during the Hydrolysis Cycle
\nMaria E. Zoghbi et al.
\nJournal of Biological Chemistry <\/em>(2012) 287(18): 14994-15000.<\/p>\n

\"\"\u00a0No.12\u30002012.7.27
\n\u62c5\u5f53\u8005<\/strong>\uff1a\u6751\u7530\u5d07\u4eba
\n\u8ad6\u6587<\/strong>\uff1aLarge conformational changes in MutS during DNA scanning, mismatch recognition and repair signalling
\nRuoyi Qiu et al.
\nThe EMBO Journal<\/em> (2012) 31<\/strong>, 2528-2540<\/p>\n

\"\"\u00a0No.11\u30002012.7.20
\n\u62c5\u5f53\u8005<\/strong>\uff1a\u9f4a\u85e4\u96c5\u5d69
\n\u8ad6\u6587<\/strong>\uff1aEfficient Single-Molecule Fluorescence Resonance Energy Transfer Analysis by Site-Specific Dual-Labeling of Protein Using an Unnatural Amino Acid
\nMoon-Hyeong Seo et al.
\nAnal. Chem. 2011, 83, 8849- 8854<\/p>\n

\"\"\u00a0No.10\u30002012.7.13
\n\u62c5\u5f53\u8005<\/strong>\uff1a\u4e45\u4fdd\u7530\u4fca\u5f66
\n\u8ad6\u6587<\/strong>\uff1aMicrofluidic sorting of arbitrary cells with dynamic optical tweezers
\nBenjamin Landenberger et al.
\nLab Chip<\/em>, 2012<\/div>\n

\"\"\u00a0No.9\u30002012.7.6
\n\u62c5\u5f53\u8005<\/strong>\uff1a\u963f\u8607\u88d5\u6a39
\n\u8ad6\u6587<\/strong>\uff1aA molecular ruler based on plasmon coupling of single gold and silver nanoparticles
\nCarsten Sonnichsen et al.
\nNature biotechnology<\/em> volume23 number 6 (2005) 741-745<\/p>\n

\"\"No.8\u30002012.6.29
\n\u62c5\u5f53\u8005<\/strong>\uff1a\u6e21\u8fba\u512a
\n\u8ad6\u6587<\/strong>\uff1aATP-Triggered Conformational Changes Delineate Substrate-Biding and -Folding Mechanics of the GroEL Chaperonin
\nDaniel K. Clare et al.
\nCell <\/em>149,113-123 (2012)<\/p>\n

\"\"\u00a0No.7\u30002012.6.15
\n\u62c5\u5f53\u8005<\/strong>\uff1a\u6589\u85e4\u7fd4
\n\u8ad6\u6587<\/strong>\uff1aHigh-Throughput Fluorescence-Activated Nanoscale Subcellular Sorter with Single-Molecule Sensitivity
\nPerry G. Schiro et al.
\nJ. Phys. Chem<\/em> (2012)<\/p>\n

\"\"\u00a0No.6\u30002012.6.1
\n\u62c5\u5f53\u8005<\/strong>\uff1a\u9ad8\u6a4b\u8056\u5f25
\n\u8ad6\u6587<\/strong>\uff1aQuanternary structure of the specific p53-DNA complex reveals the mechanism of p53 mutant dominance
\nRicardo Aramayo et al.
\nNucleic Acids Research <\/em>(2011)<\/p>\n

\"\"\u00a0No.5\u30002012.5.25
\n\u62c5\u5f53\u8005<\/strong>\uff1a\ufffd\u6a4b\u8061
\n\u8ad6\u6587<\/strong>\uff1aReal-time analysis and selection of methylated DNA by fluorescence-activated single molecule sorting in a nanofluidic channel
\nBenjamin R. Cipriany et al.
\nPNAS<\/em>, \uff082012\uff09<\/p>\n

\"\"\u00a0No.4\u30002012.5.18
\n\u62c5\u5f53\u8005<\/strong>\uff1a\u5c0f\u4e95\u5ddd\u6d69\u4e4b
\n\u8ad6\u6587<\/strong>\uff1aSingle-Molecule Fluorescence Experiments Determine Protein Folding Transition Path Times
\nHoi Sung Chung et al.
\nScience Vol335 981-984<\/i>\u00a0(2012)<\/div>\n

\"\"\u00a0No.3\u30002012.5.11
\n\u62c5\u5f53\u8005<\/strong>\uff1a\u938c\u5f62\u6e05\u4eba
\n\u8ad6\u6587<\/strong>\uff1aA Close Look at Proteins: Submolecular Resolution of Two- and Three-Dimensionally Folded Cytochrome c at Surfaces
\nZhitao Deng et al.
\nNano letters<\/em> (2012)<\/p>\n

\"\"\u00a0No.2\u30002012.4.20
\n\u62c5\u5f53\u8005<\/strong>\uff1a\u9f4a\u85e4\u7fd4
\n\u8ad6\u6587<\/strong>\uff1aPulsed laser triggered high speed microfluidic fluorescence activated cell sorter
\nTing-Hsiang Wu et al.
\nLab on a Chip<\/em> (2012) \u00a01378-1383<\/p>\n

\"\"\u00a0No.1\u30002012.4.13
\n\u62c5\u5f53\u8005<\/strong>\uff1a\ufffd\u6a4b\u8061
\n\u8ad6\u6587<\/strong>\uff1aFolding without charges
\nMartin Kurnik et al.
\nPNAS<\/em>, April 10, 2012\/ vol.109<\/strong>\/ no.15\/ 5705-5710<\/p>\n","protected":false},"excerpt":{"rendered":"

\u00a0No.30\u30002013.3.18 \u62c5\u5f53\u8005\uff1a\u9f4a\u85e4\u96c5\u5d69 \u8ad6\u6587\uff1aDirect observation of multiple mi…<\/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-166","page","type-page","status-publish","hentry"],"_links":{"self":[{"href":"https:\/\/www2.tagen.tohoku.ac.jp\/lab\/takahashi-s\/wp-json\/wp\/v2\/pages\/166","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=166"}],"version-history":[{"count":1,"href":"https:\/\/www2.tagen.tohoku.ac.jp\/lab\/takahashi-s\/wp-json\/wp\/v2\/pages\/166\/revisions"}],"predecessor-version":[{"id":167,"href":"https:\/\/www2.tagen.tohoku.ac.jp\/lab\/takahashi-s\/wp-json\/wp\/v2\/pages\/166\/revisions\/167"}],"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=166"}],"curies":[{"name":"wp","href":"https:\/\/api.w.org\/{rel}","templated":true}]}}