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Volumn 5, Issue NOVEMBER2016, 2016, Pages

Structure and dynamics underlying elementary ligand binding events in human pacemaking channels

Author keywords

[No Author keywords available]

Indexed keywords

CARRIER PROTEINS AND BINDING PROTEINS; CYCLIC AMP; CYCLIC NUCLEOTIDE GATED CHANNEL;

EID: 84996551331     PISSN: None     EISSN: 2050084X     Source Type: Journal    
DOI: 10.7554/eLife.20797     Document Type: Article
Times cited : (42)

References (63)
  • 2
    • 0016355478 scopus 로고
    • A new look at the statistical model identification
    • Akaike H. 1974. A new look at the statistical model identification. IEEE Transactions on Automatic Control 19: 716–723. doi: 10.1109/TAC.1974.1100705
    • (1974) IEEE Transactions on Automatic Control , vol.19 , pp. 716-723
    • Akaike, H.1
  • 4
    • 0032917076 scopus 로고    scopus 로고
    • A minimal peptide substrate in biotin holoenzyme synthetase-catalyzed biotinylation
    • PMID: 10211839
    • Beckett D, Kovaleva E, Schatz PJ. 1999. A minimal peptide substrate in biotin holoenzyme synthetase-catalyzed biotinylation. Protein Science 8:921–929. doi: 10.1110/ps.8.4.921, PMID: 10211839
    • (1999) Protein Science , vol.8 , pp. 921-929
    • Beckett, D.1    Kovaleva, E.2    Schatz, P.J.3
  • 5
    • 84868576729 scopus 로고    scopus 로고
    • Unraveling subunit cooperativity in homotetrameric HCN2 channels
    • PMID: 23199914
    • Benndorf K, Thon S, Schulz E. 2012. Unraveling subunit cooperativity in homotetrameric HCN2 channels. Biophysical Journal 103:1860–1869. doi: 10.1016/j.bpj.2012.09.024, PMID: 23199914
    • (2012) Biophysical Journal , vol.103 , pp. 1860-1869
    • Benndorf, K.1    Thon, S.2    Schulz, E.3
  • 7
    • 84865723813 scopus 로고    scopus 로고
    • Optimization of the additive CHARMM all-atom protein force field targeting improved sampling of the backbone j, y and side-chain c1 and c2 dihedral angles
    • PMID: 23341755
    • Best RB, Zhu X, Shim J, Lopes PE, Mittal J, Feig M, Mackerell AD. 2012. Optimization of the additive CHARMM all-atom protein force field targeting improved sampling of the backbone j, y and side-chain c1 and c2 dihedral angles. Journal of Chemical Theory and Computation 8:3257–3273. doi: 10.1021/ct300400x, PMID: 23341755
    • (2012) Journal of Chemical Theory and Computation , vol.8 , pp. 3257-3273
    • Best, R.B.1    Zhu, X.2    Shim, J.3    Lopes, P.E.4    Mittal, J.5    Feig, M.6    Mackerell, A.D.7
  • 8
    • 73449090455 scopus 로고    scopus 로고
    • Learning rates and states from biophysical time series: A Bayesian approach to model selection and single-molecule FRET data
    • PMID: 20006957
    • Bronson JE, Fei J, Hofman JM, Gonzalez RL, Wiggins CH. 2009. Learning rates and states from biophysical time series: a Bayesian approach to model selection and single-molecule FRET data. Biophysical Journal 97:3196–3205. doi: 10.1016/j.bpj.2009.09.031, PMID: 20006957
    • (2009) Biophysical Journal , vol.97 , pp. 3196-3205
    • Bronson, J.E.1    Fei, J.2    Hofman, J.M.3    Gonzalez, R.L.4    Wiggins, C.H.5
  • 9
    • 33846647992 scopus 로고    scopus 로고
    • Voltage sensor movement and cAMP binding allosterically regulate an inherently voltage-independent closed-open transition in HCN channels
    • PMID: 17261842
    • Chen S, Wang J, Zhou L, George MS, Siegelbaum SA. 2007. Voltage sensor movement and cAMP binding allosterically regulate an inherently voltage-independent closed-open transition in HCN channels. Journal of General Physiology 129:175–188. doi: 10.1085/jgp.200609585, PMID: 17261842
    • (2007) Journal of General Physiology , vol.129 , pp. 175-188
    • Chen, S.1    Wang, J.2    Zhou, L.3    George, M.S.4    Siegelbaum, S.A.5
  • 10
    • 8844263765 scopus 로고    scopus 로고
    • Structural basis of ligand activation in a cyclic nucleotide regulated potassium channel
    • PMID: 15550244
    • Clayton GM, Silverman WR, Heginbotham L, Morais-Cabral JH. 2004. Structural basis of ligand activation in a cyclic nucleotide regulated potassium channel. Cell 119:615–627. doi: 10.1016/j.cell.2004.10.030, PMID: 15550244
    • (2004) Cell , vol.119 , pp. 615-627
    • Clayton, G.M.1    Silverman, W.R.2    Heginbotham, L.3    Morais-Cabral, J.H.4
  • 11
    • 84870979396 scopus 로고    scopus 로고
    • Perspectives on: Conformational coupling in ion channels: Allosteric coupling in ligand-gated ion channels
    • PMID: 23183696
    • Colquhoun D, Lape R. 2012. Perspectives on: conformational coupling in ion channels: allosteric coupling in ligand-gated ion channels. Journal of General Physiology 140:599–612. doi: 10.1085/jgp.201210844, PMID: 23183696
    • (2012) Journal of General Physiology , vol.140 , pp. 599-612
    • Colquhoun, D.1    Lape, R.2
  • 13
    • 77957231785 scopus 로고    scopus 로고
    • Induced fit, conformational selection and independent dynamic segments: An extended view of binding events
    • PMID: 20541943
    • Csermely P, Palotai R, Nussinov R. 2010. Induced fit, conformational selection and independent dynamic segments: an extended view of binding events. Trends in Biochemical Sciences 35:539–546. doi: 10.1016/j.tibs. 2010.04.009, PMID: 20541943
    • (2010) Trends in Biochemical Sciences , vol.35 , pp. 539-546
    • Csermely, P.1    Palotai, R.2    Nussinov, R.3
  • 14
    • 84952889325 scopus 로고    scopus 로고
    • Structure and energetics of Allosteric regulation of HCN2 Ion channels by cyclic nucleotides
    • PMID: 26559974
    • DeBerg HA, Brzovic PS, Flynn GE, Zagotta WN, Stoll S. 2016. Structure and energetics of Allosteric regulation of HCN2 Ion channels by cyclic nucleotides. Journal of Biological Chemistry 291:371–381. doi: 10.1074/jbc.M115. 696450, PMID: 26559974
    • (2016) Journal of Biological Chemistry , vol.291 , pp. 371-381
    • Deberg, H.A.1    Brzovic, P.S.2    Flynn, G.E.3    Zagotta, W.N.4    Stoll, S.5
  • 16
    • 0028945654 scopus 로고
    • Imaging of single fluorescent molecules and individual ATP turnovers by single myosin molecules in aqueous solution
    • PMID: 7700383
    • Funatsu T, Harada Y, Tokunaga M, Saito K, Yanagida T. 1995. Imaging of single fluorescent molecules and individual ATP turnovers by single myosin molecules in aqueous solution. Nature 374:555–559. doi: 10.1038/ 374555a0, PMID: 7700383
    • (1995) Nature , vol.374 , pp. 555-559
    • Funatsu, T.1    Harada, Y.2    Tokunaga, M.3    Saito, K.4    Yanagida, T.5
  • 18
    • 84860195444 scopus 로고    scopus 로고
    • Benzodiazepines modulate GABAA receptors by regulating the preactivation step after GABA binding
    • PMID: 22539833
    • Gielen MC, Lumb MJ, Smart TG. 2012. Benzodiazepines modulate GABAA receptors by regulating the preactivation step after GABA binding. Journal of Neuroscience 32:5707–5715. doi: 10.1523/JNEUROSCI. 5663-11.2012, PMID: 22539833
    • (2012) Journal of Neuroscience , vol.32 , pp. 5707-5715
    • Gielen, M.C.1    Lumb, M.J.2    Smart, T.G.3
  • 19
    • 84978162014 scopus 로고    scopus 로고
    • The DynDom3D webserver for the analysis of domain movements in multimeric proteins
    • PMID: 26540459
    • Girdlestone C, Hayward S. 2016. The DynDom3D webserver for the analysis of domain movements in multimeric proteins. Journal of Computational Biology 23:21–26. doi: 10.1089/cmb.2015.0143, PMID: 26540459
    • (2016) Journal of Computational Biology , vol.23 , pp. 21-26
    • Girdlestone, C.1    Hayward, S.2
  • 20
    • 84903794767 scopus 로고    scopus 로고
    • A nonequilibrium binary elements-based kinetic model for benzodiazepine regulation of GABAA receptors
    • PMID: 24981228
    • Goldschen-Ohm MP, Haroldson A, Jones MV, Pearce RA. 2014. A nonequilibrium binary elements-based kinetic model for benzodiazepine regulation of GABAA receptors. Journal of General Physiology 144:27–39. doi: 10. 1085/jgp.201411183, PMID: 24981228
    • (2014) Journal of General Physiology , vol.144 , pp. 27-39
    • Goldschen-Ohm, M.P.1    Haroldson, A.2    Jones, M.V.3    Pearce, R.A.4
  • 21
    • 84904291286 scopus 로고    scopus 로고
    • Both protein dynamics and ligand concentration can shift the binding mechanism between conformational selection and induced fit
    • PMID: 24982141
    • Greives N, Zhou H-X. 2014. Both protein dynamics and ligand concentration can shift the binding mechanism between conformational selection and induced fit. PNAS 111:10197–10202. doi: 10.1073/pnas.1407545111, PMID: 24982141
    • (2014) PNAS , vol.111 , pp. 10197-10202
    • Greives, N.1    Zhou, H.-X.2
  • 22
    • 84974627299 scopus 로고    scopus 로고
    • Protein Allostery and Conformational Dynamics
    • PMID: 26876046
    • Guo J, Zhou HX. 2016. Protein Allostery and Conformational Dynamics. Chemical Reviews 116:6503–6515. doi: 10.1021/acs.chemrev.5b00590, PMID: 26876046
    • (2016) Chemical Reviews , vol.116 , pp. 6503-6515
    • Guo, J.1    Zhou, H.X.2
  • 23
    • 84855661433 scopus 로고    scopus 로고
    • Optimization of the CHARMM additive force field for DNA: Improved treatment of the BI/BII conformational equilibrium
    • PMID: 22368531
    • Hart K, Foloppe N, Baker CM, Denning EJ, Nilsson L, Mackerell AD. 2012. Optimization of the CHARMM additive force field for DNA: Improved treatment of the BI/BII conformational equilibrium. Journal of Chemical Theory and Computation 8:348–362. doi: 10.1021/ct200723y, PMID: 22368531
    • (2012) Journal of Chemical Theory and Computation , vol.8 , pp. 348-362
    • Hart, K.1    Foloppe, N.2    Baker, C.M.3    Denning, E.J.4    Nilsson, L.5    Mackerell, A.D.6
  • 24
  • 25
    • 50649121477 scopus 로고    scopus 로고
    • Advances in single-molecule fluorescence methods for molecular biology
    • PMID: 18412538
    • Joo C, Balci H, Ishitsuka Y, Buranachai C, Ha T. 2008. Advances in single-molecule fluorescence methods for molecular biology. Annual Review of Biochemistry 77:51–76. doi: 10.1146/annurev.biochem.77.070606.101543, PMID: 18412538
    • (2008) Annual Review of Biochemistry , vol.77 , pp. 51-76
    • Joo, C.1    Balci, H.2    Ishitsuka, Y.3    Buranachai, C.4    Ha, T.5
  • 26
    • 13244291292 scopus 로고    scopus 로고
    • Crystal structure of a complex between the catalytic and regulatory (RIalpha) subunits of PKA
    • PMID: 15692043
    • Kim C, Xuong NH, Taylor SS. 2005. Crystal structure of a complex between the catalytic and regulatory (RIalpha) subunits of PKA. Science 307:690–696. doi: 10.1126/science.1104607, PMID: 15692043
    • (2005) Science , vol.307 , pp. 690-696
    • Kim, C.1    Xuong, N.H.2    Taylor, S.S.3
  • 27
    • 79955977163 scopus 로고    scopus 로고
    • Structure-function analysis of the C-terminal domain of CNM67, a core component of the Saccharomyces cerevisiae spindle pole body
    • PMID: 21454609
    • Klenchin VA, Frye JJ, Jones MH, Winey M, Rayment I. 2011. Structure-function analysis of the C-terminal domain of CNM67, a core component of the Saccharomyces cerevisiae spindle pole body. Journal of Biological Chemistry 286:18240–18250. doi: 10.1074/jbc.M111.227371, PMID: 21454609
    • (2011) Journal of Biological Chemistry , vol.286 , pp. 18240-18250
    • Klenchin, V.A.1    Frye, J.J.2    Jones, M.H.3    Winey, M.4    Rayment, I.5
  • 29
    • 13444307044 scopus 로고    scopus 로고
    • Secondary-structure matching (SSM), a new tool for fast protein structure alignment in three dimensions
    • PMID: 15572779
    • Krissinel E, Henrick K. 2004. Secondary-structure matching (SSM), a new tool for fast protein structure alignment in three dimensions. Acta Crystallographica Section D Biological Crystallography 60:2256–2268. doi: 10.1107/ S0907444904026460, PMID: 15572779
    • (2004) Acta Crystallographica Section D Biological Crystallography , vol.60 , pp. 2256-2268
    • Krissinel, E.1    Henrick, K.2
  • 30
    • 77954483652 scopus 로고    scopus 로고
    • Interdependence of receptor activation and ligand binding in HCN2 pacemaker channels
    • PMID: 20624593
    • Kusch J, Biskup C, Thon S, Schulz E, Nache V, Zimmer T, Schwede F, Benndorf K. 2010. Interdependence of receptor activation and ligand binding in HCN2 pacemaker channels. Neuron 67:75–85. doi: 10.1016/j.neuron. 2010.05.022, PMID: 20624593
    • (2010) Neuron , vol.67 , pp. 75-85
    • Kusch, J.1    Biskup, C.2    Thon, S.3    Schulz, E.4    Nache, V.5    Zimmer, T.6    Schwede, F.7    Benndorf, K.8
  • 32
    • 79951847774 scopus 로고    scopus 로고
    • Structural landscape of isolated agonist- binding domains from single AMPA receptors
    • PMID: 21297640
    • Landes CF, Rambhadran A, Taylor JN, Salatan F, Jayaraman V. 2011. Structural landscape of isolated agonist- binding domains from single AMPA receptors. Nature Chemical Biology 7:168–173. doi: 10.1038/nchembio. 523, PMID: 21297640
    • (2011) Nature Chemical Biology , vol.7 , pp. 168-173
    • Landes, C.F.1    Rambhadran, A.2    Taylor, J.N.3    Salatan, F.4    Jayaraman, V.5
  • 33
    • 49649102025 scopus 로고    scopus 로고
    • On the nature of partial agonism in the nicotinic receptor superfamily
    • PMID: 18633353
    • Lape R, Colquhoun D, Sivilotti LG. 2008. On the nature of partial agonism in the nicotinic receptor superfamily. Nature 454:722–727. doi: 10.1038/nature07139, PMID: 18633353
    • (2008) Nature , vol.454 , pp. 722-727
    • Lape, R.1    Colquhoun, D.2    Sivilotti, L.G.3
  • 34
    • 0037474152 scopus 로고    scopus 로고
    • Zero-mode waveguides for single-molecule analysis at high concentrations
    • PMID: 12560545
    • Levene MJ, Korlach J, Turner SW, Foquet M, Craighead HG, Webb WW. 2003. Zero-mode waveguides for single-molecule analysis at high concentrations. Science 299:682–686. doi: 10.1126/science.1079700, PMID: 12560545
    • (2003) Science , vol.299 , pp. 682-686
    • Levene, M.J.1    Korlach, J.2    Turner, S.W.3    Foquet, M.4    Craighead, H.G.5    Webb, W.W.6
  • 38
    • 0031586385 scopus 로고    scopus 로고
    • Allosteric proteins. Cuddling up to channel activation
    • PMID: 9311770
    • Miller C. 1997. Allosteric proteins. Cuddling up to channel activation. Nature 389:328–329. doi: 10.1038/38599, PMID: 9311770
    • (1997) Nature , vol.389 , pp. 328-329
    • Miller, C.1
  • 39
    • 67349279395 scopus 로고    scopus 로고
    • Detection and trapping of intermediate states priming nicotinic receptor channel opening
    • PMID: 19339970
    • Mukhtasimova N, Lee WY, Wang HL, Sine SM. 2009. Detection and trapping of intermediate states priming nicotinic receptor channel opening. Nature 459:451–454. doi: 10.1038/nature07923, PMID: 19339970
    • (2009) Nature , vol.459 , pp. 451-454
    • Mukhtasimova, N.1    Lee, W.Y.2    Wang, H.L.3    Sine, S.M.4
  • 40
    • 84893051703 scopus 로고    scopus 로고
    • Solving ion channel kinetics with the QuB software
    • Nicolai C, Sachs F. 2013. Solving ion channel kinetics with the QuB software. Biophysical Reviews and Letters 08: 191–211. doi: 10.1142/S1793048013300053
    • (2013) Biophysical Reviews and Letters , vol.8 , pp. 191-211
    • Nicolai, C.1    Sachs, F.2
  • 41
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • PMID: 27799103
    • Otwinowski Z, Minor W. 1997. Processing of X-ray diffraction data collected in oscillation mode. Methods in Enzymology 276:307–326. doi: 10.1016/S0076-6879(97)76066-X, PMID: 27799103
    • (1997) Methods in Enzymology , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 44
    • 84903957215 scopus 로고    scopus 로고
    • Double electron–electron resonance reveals cAMP-induced conformational change in HCN channels
    • Puljung MC, DeBerg HA, Zagotta WN, Stoll S. 2014. Double electron–electron resonance reveals cAMP-induced conformational change in HCN channels. PNAS 111:9816–9821. doi: 10.1073/pnas.1405371111
    • (2014) PNAS , vol.111 , pp. 9816-9821
    • Puljung, M.C.1    Deberg, H.A.2    Zagotta, W.N.3    Stoll, S.4
  • 45
    • 84877132586 scopus 로고    scopus 로고
    • A secondary structural transition in the C-helix promotes gating of cyclic nucleotide-regulated ion channels
    • PMID: 23525108
    • Puljung MC, Zagotta WN. 2013. A secondary structural transition in the C-helix promotes gating of cyclic nucleotide-regulated ion channels. Journal of Biological Chemistry 288:12944–12956. doi: 10.1074/jbc.M113. 464123, PMID: 23525108
    • (2013) Journal of Biological Chemistry , vol.288 , pp. 12944-12956
    • Puljung, M.C.1    Zagotta, W.N.2
  • 46
    • 84903974104 scopus 로고    scopus 로고
    • Catch-and-hold activation of muscle acetylcholine receptors having transmitter binding site mutations
    • PMID: 24988344
    • Purohit P, Bruhova I, Gupta S, Auerbach A. 2014. Catch-and-hold activation of muscle acetylcholine receptors having transmitter binding site mutations. Biophysical Journal 107:88–99. doi: 10.1016/j.bpj.2014.04.057, PMID: 24988344
    • (2014) Biophysical Journal , vol.107 , pp. 88-99
    • Purohit, P.1    Bruhova, I.2    Gupta, S.3    Auerbach, A.4
  • 47
    • 0033808511 scopus 로고    scopus 로고
    • A direct optimization approach to hidden Markov modeling for single channel kinetics
    • PMID: 11023897
    • Qin F, Auerbach A, Sachs F. 2000. A direct optimization approach to hidden Markov modeling for single channel kinetics. Biophysical Journal 79:1915–1927. doi: 10.1016/S0006-3495(00)76441-1, PMID: 11023897
    • (2000) Biophysical Journal , vol.79 , pp. 1915-1927
    • Qin, F.1    Auerbach, A.2    Sachs, F.3
  • 48
    • 0030778914 scopus 로고    scopus 로고
    • Single cyclic nucleotide-gated channels locked in different ligand-bound states
    • PMID: 9311781
    • Ruiz ML, Karpen JW. 1997. Single cyclic nucleotide-gated channels locked in different ligand-bound states. Nature 389:389–392. doi: 10.1038/38744, PMID: 9311781
    • (1997) Nature , vol.389 , pp. 389-392
    • Ruiz, M.L.1    Karpen, J.W.2
  • 49
    • 49349084992 scopus 로고    scopus 로고
    • Red light, green light: Probing single molecules using alternating-laser excitation
    • PMID: 1 8631150
    • Santoso Y, Hwang LC, Le Reste L, Kapanidis AN. 2008. Red light, green light: probing single molecules using alternating-laser excitation. Biochemical Society Transactions 36:738–744. doi: 10.1042/BST0360738, PMID: 1 8631150
    • (2008) Biochemical Society Transactions , vol.36 , pp. 738-744
    • Santoso, Y.1    Hwang, L.C.2    Le Reste, L.3    Kapanidis, A.N.4
  • 51
    • 79955011398 scopus 로고    scopus 로고
    • Structural insights into conformational changes of a cyclic nucleotide-binding domain in solution from Mesorhizobium loti K1 channel
    • Schunke S, Stoldt M, Lecher J, Kaupp UB, Willbold D. 2011. Structural insights into conformational changes of a cyclic nucleotide-binding domain in solution from Mesorhizobium loti K1 channel. PNAS 108:6121–6126. doi: 10.1073/pnas.1015890108
    • (2011) PNAS , vol.108 , pp. 6121-6126
    • Schunke, S.1    Stoldt, M.2    Lecher, J.3    Kaupp, U.B.4    Willbold, D.5
  • 53
    • 14844294424 scopus 로고    scopus 로고
    • Protein production by auto-induction in high density shaking cultures
    • PMID: 15915565
    • Studier FW. 2005. Protein production by auto-induction in high density shaking cultures. Protein Expression and Purification 41:207–234. doi: 10.1016/j.pep.2005.01.016, PMID: 15915565
    • (2005) Protein Expression and Purification , vol.41 , pp. 207-234
    • Studier, F.W.1
  • 54
    • 67649604544 scopus 로고    scopus 로고
    • Mapping the structure and conformational movements of proteins with transition metal ion FRET
    • PMID: 19525958
    • Taraska JW, Puljung MC, Olivier NB, Flynn GE, Zagotta WN. 2009. Mapping the structure and conformational movements of proteins with transition metal ion FRET. Nature Methods 6:532–537. doi: 10.1038/nmeth.1341, PMID: 19525958
    • (2009) Nature Methods , vol.6 , pp. 532-537
    • Taraska, J.W.1    Puljung, M.C.2    Olivier, N.B.3    Flynn, G.E.4    Zagotta, W.N.5
  • 55
    • 84949595852 scopus 로고    scopus 로고
    • Conformational flip of nonactivated HCN2 Channel subunits evoked by cyclic nucleotides
    • PMID: 26636938
    • Thon S, Schulz E, Kusch J, Benndorf K. 2015. Conformational flip of nonactivated HCN2 Channel subunits evoked by cyclic nucleotides. Biophysical Journal 109:2268–2276. doi: 10.1016/j.bpj.2015.08.054, PMID: 26636938
    • (2015) Biophysical Journal , vol.109 , pp. 2268-2276
    • Thon, S.1    Schulz, E.2    Kusch, J.3    Benndorf, K.4
  • 56
    • 77951107295 scopus 로고    scopus 로고
    • Real-time tRNA transit on single translating ribosomes at codon resolution
    • PMID: 20393556
    • Uemura S, Aitken CE, Korlach J, Flusberg BA, Turner SW, Puglisi JD. 2010. Real-time tRNA transit on single translating ribosomes at codon resolution. Nature 464:1012–1017. doi: 10.1038/nature08925, PMID: 20393556
    • (2010) Nature , vol.464 , pp. 1012-1017
    • Uemura, S.1    Aitken, C.E.2    Korlach, J.3    Flusberg, B.A.4    Turner, S.W.5    Puglisi, J.D.6
  • 57
    • 84940478169 scopus 로고    scopus 로고
    • Conformational dynamics of a class C G-protein-coupled receptor
    • PMID: 26258295
    • Vafabakhsh R, Levitz J, Isacoff EY. 2015. Conformational dynamics of a class C G-protein-coupled receptor. Nature 524:497–501. doi: 10.1038/nature14679, PMID: 26258295
    • (2015) Nature , vol.524 , pp. 497-501
    • Vafabakhsh, R.1    Levitz, J.2    Isacoff, E.Y.3
  • 58
    • 84954367060 scopus 로고    scopus 로고
    • Structural dynamics of potassium-channel gating revealed by single-molecule FRET
    • PMID: 26641713
    • Wang S, Vafabakhsh R, Borschel WF, Ha T, Nichols CG. 2016. Structural dynamics of potassium-channel gating revealed by single-molecule FRET. Nature Structural & Molecular Biology 23:31–36. doi: 10.1038/nsmb.3138, PMID: 26641713
    • (2016) Nature Structural & Molecular Biology , vol.23 , pp. 31-36
    • Wang, S.1    Vafabakhsh, R.2    Borschel, W.F.3    Ha, T.4    Nichols, C.G.5
  • 60
    • 78449237959 scopus 로고    scopus 로고
    • Structural basis for the cAMP-dependent gating in the human HCN4 channel
    • PMID: 20829353
    • Xu X, Vysotskaya ZV, Liu Q, Zhou L. 2010. Structural basis for the cAMP-dependent gating in the human HCN4 channel. Journal of Biological Chemistry 285:37082–37091. doi: 10.1074/jbc.M110.152033, PMID: 20829353
    • (2010) Journal of Biological Chemistry , vol.285 , pp. 37082-37091
    • Xu, X.1    Vysotskaya, Z.V.2    Liu, Q.3    Zhou, L.4
  • 61
    • 0141831003 scopus 로고    scopus 로고
    • Structural basis for modulation and agonist specificity of HCN pacemaker channels
    • PMID: 129681 85
    • Zagotta WN, Olivier NB, Black KD, Young EC, Olson R, Gouaux E. 2003. Structural basis for modulation and agonist specificity of HCN pacemaker channels. Nature 425:200–205. doi: 10.1038/nature01922, PMID: 129681 85
    • (2003) Nature , vol.425 , pp. 200-205
    • Zagotta, W.N.1    Olivier, N.B.2    Black, K.D.3    Young, E.C.4    Olson, R.5    Gouaux, E.6
  • 62
    • 84889679137 scopus 로고    scopus 로고
    • Potential-dependent single molecule blinking dynamics for flavin adenine dinucleotide covalently immobilized in zero-mode waveguide array of working electrodes
    • PMID: 24466658
    • Zhao J, Zaino LP, Bohna PW. 2013. Potential-dependent single molecule blinking dynamics for flavin adenine dinucleotide covalently immobilized in zero-mode waveguide array of working electrodes. Faraday Discussions 164:57–69. doi: 10.1039/c3fd00013c, PMID: 24466658
    • (2013) Faraday Discussions , vol.164 , pp. 57-69
    • Zhao, J.1    Zaino, L.P.2    Bohna, P.W.3
  • 63
    • 84861398807 scopus 로고    scopus 로고
    • Zero-mode waveguides for single-molecule analysis
    • PMID: 22577821
    • Zhu P, Craighead HG. 2012. Zero-mode waveguides for single-molecule analysis. Annual Review of Biophysics 41:269–293. doi: 10.1146/annurev-biophys-050511-102338, PMID: 22577821
    • (2012) Annual Review of Biophysics , vol.41 , pp. 269-293
    • Zhu, P.1    Craighead, H.G.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.