메뉴 건너뛰기




Volumn 704, Issue , 2011, Pages 25-40

Functional and structural studies of TRP channels heterologously expressed in budding yeast

Author keywords

Cryo electron microscopy; Protein expression; TRP channel; X ray crystallography

Indexed keywords

ANKYRIN; POLYCYSTIN; PROTEIN TRPML; TRANSIENT RECEPTOR POTENTIAL CHANNEL; TRANSIENT RECEPTOR POTENTIAL CHANNEL C; TRANSIENT RECEPTOR POTENTIAL CHANNEL M; UNCLASSIFIED DRUG; VANILLOID RECEPTOR; RECOMBINANT PROTEIN;

EID: 79959788691     PISSN: 00652598     EISSN: None     Source Type: Book Series    
DOI: 10.1007/978-94-007-0265-3_2     Document Type: Conference Paper
Times cited : (16)

References (100)
  • 1
    • 0014683485 scopus 로고
    • Abnormal electroretinogram from a Drosophila mutant
    • Cosens DJ, Manning A (1969) Abnormal electroretinogram from a Drosophila mutant. Nature 224:285-287
    • (1969) Nature , vol.224 , pp. 285-287
    • Cosens, D.J.1    Manning, A.2
  • 2
    • 0016743642 scopus 로고
    • Induction of photoreceptor voltage noise in the dark in Drosophila mutant
    • Minke B, Wu C, Pak WL (1975) Induction of photoreceptor voltage noise in the dark in Drosophila mutant. Nature 258:84-87
    • (1975) Nature , vol.258 , pp. 84-87
    • Minke, B.1    Wu, C.2    Pak, W.L.3
  • 3
    • 0024642547 scopus 로고
    • Molecular characterization of the Drosophila trp locus: A putative integral membrane protein required for phototransduction
    • Montell C, Rubin GM (1989) Molecular characterization of the Drosophila trp locus: A putative integral membrane protein required for phototransduction. Neuron 2: 1313-1323
    • (1989) Neuron , vol.2 , pp. 1313-1323
    • Montell, C.1    Rubin, G.M.2
  • 4
    • 0345059360 scopus 로고    scopus 로고
    • International Union of Pharmacology. XLIII. Compendium of voltage-gated ion channels: Transient receptor potential channels
    • Clapham DE, Montell C, Schultz G, Julius D (2003) International Union of Pharmacology. XLIII. Compendium of voltage-gated ion channels: Transient receptor potential channels. Pharmacol Rev 55:591-596
    • (2003) Pharmacol Rev , vol.55 , pp. 591-596
    • Clapham, D.E.1    Montell, C.2    Schultz, G.3    Julius, D.4
  • 5
    • 0034708452 scopus 로고    scopus 로고
    • Drosophila mechanosensory transduction channel
    • Walker RG, Willingham AT, Zuker CS:A (2000) Drosophila mechanosensory transduction channel. Science 287:2229-2234
    • (2000) Science , vol.287 , pp. 2229-2234
    • Walker, R.G.1    Willingham, A.T.2    Zuker, C.S.A.3
  • 7
    • 0037710542 scopus 로고    scopus 로고
    • TRP channel required for vertebrate sensory hair cell mechanotransduction
    • Sidi S, Friedrich RW, Nicolson T, Nomp C (2003) TRP channel required for vertebrate sensory hair cell mechanotransduction. Science 301:96-99
    • (2003) Science , vol.301 , pp. 96-99
    • Sidi, S.1    Friedrich, R.W.2    Nicolson, T.3    Nomp, C.4
  • 8
    • 0034934074 scopus 로고    scopus 로고
    • A TRP homolog in Saccharomyces cerevisiae forms an intracellular Ca(2+)-permeable channel in the yeast vacuolar membrane
    • Palmer CP, Zhou XL, Lin J, Loukin SH, Kung C, Saimi Y (2001) A TRP homolog in Saccharomyces cerevisiae forms an intracellular Ca(2+)-permeable channel in the yeast vacuolar membrane. Proc Natl Acad Sci USA 98:7801-7805
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 7801-7805
    • Palmer, C.P.1    Zhou, X.L.2    Lin, J.3    Loukin, S.H.4    Kung, C.5    Saimi, Y.6
  • 9
    • 20444366051 scopus 로고    scopus 로고
    • Heterologously expressed fungal transient receptor potential channels retain mechanosensitivity in vitro and osmotic response in vivo
    • Zhou XL, Loukin SH, Coria R, Kung C, Saimi Y (2005) Heterologously expressed fungal transient receptor potential channels retain mechanosensitivity in vitro and osmotic response in vivo. Eur Biophys J 34:413-422
    • (2005) Eur Biophys J , vol.34 , pp. 413-422
    • Zhou, X.L.1    Loukin, S.H.2    Coria, R.3    Kung, C.4    Saimi, Y.5
  • 10
    • 0347504835 scopus 로고    scopus 로고
    • TRP channels as cellular sensors
    • Clapham DE (2003) TRP channels as cellular sensors. Nature 426:517-524
    • (2003) Nature , vol.426 , pp. 517-524
    • Clapham, D.E.1
  • 11
    • 33644875032 scopus 로고    scopus 로고
    • The TRP superfamily of cation channels
    • re3
    • Montell C (2005) The TRP superfamily of cation channels. Sci STKE 2005:re3
    • (2005) Sci STKE , vol.2005
    • Montell, C.1
  • 12
    • 42349109026 scopus 로고    scopus 로고
    • A primer on ankyrin repeat function in TRP channels and beyond
    • Gaudet R (2008) A primer on ankyrin repeat function in TRP channels and beyond. Mol Biosyst 4:372-379
    • (2008) Mol Biosyst , vol.4 , pp. 372-379
    • Gaudet, R.1
  • 13
    • 61449222945 scopus 로고    scopus 로고
    • The self-association of two N-terminal interaction domains plays an important role in the tetramerization of TRPC4
    • Lepage PK, Lussier MP, McDuff FO, Lavigne P, Boulay G (2009) The self-association of two N-terminal interaction domains plays an important role in the tetramerization of TRPC4. Cell Calcium 45:251-259
    • (2009) Cell Calcium , vol.45 , pp. 251-259
    • Lepage, P.K.1    Lussier, M.P.2    McDuff, F.O.3    Lavigne, P.4    Boulay, G.5
  • 18
    • 0037163111 scopus 로고    scopus 로고
    • Fast and slow inactivation kinetics of the Ca2+ channels ECaC1 and ECaC2 (TRPV5 and TRPV6). Role of the intracellular loop located between transmembrane segments 2 and 3
    • Nilius B, Prenen J, Hoenderop JG, Vennekens R, Hoefs S, Weidema AF, Droogmans G, Bindels RJ (2002) Fast and slow inactivation kinetics of the Ca2+ channels ECaC1 and ECaC2 (TRPV5 and TRPV6). Role of the intracellular loop located between transmembrane segments 2 and 3. J Biol Chem 277:30852-30858
    • (2002) J Biol Chem , vol.277 , pp. 30852-30858
    • Nilius, B.1    Prenen, J.2    Hoenderop, J.G.3    Vennekens, R.4    Hoefs, S.5    Weidema, A.F.6    Droogmans, G.7    Bindels, R.J.8
  • 21
    • 70349161542 scopus 로고    scopus 로고
    • On the putative role of transient receptor potential cation channels in asthma
    • Colsoul B, Nilius B, Vennekens R (2009) On the putative role of transient receptor potential cation channels in asthma. Clin Exp Allergy 39:1456-1466
    • (2009) Clin Exp Allergy , vol.39 , pp. 1456-1466
    • Colsoul, B.1    Nilius, B.2    Vennekens, R.3
  • 23
    • 67849101004 scopus 로고    scopus 로고
    • Mechanosensitive TRP channels in cardiovascular pathophysiology
    • Inoue R, Jian Z, Kawarabayashi Y (2009) Mechanosensitive TRP channels in cardiovascular pathophysiology. Pharmacol Ther 123:371-385
    • (2009) Pharmacol Ther , vol.123 , pp. 371-385
    • Inoue, R.1    Jian, Z.2    Kawarabayashi, Y.3
  • 25
    • 65749107679 scopus 로고    scopus 로고
    • Role of TRPV1 in inflammation-induced airway hypersensitivity
    • Lee LY, Gu Q (2009) Role of TRPV1 in inflammation-induced airway hypersensitivity. Curr Opin Pharmacol 9:243-249
    • (2009) Curr Opin Pharmacol , vol.9 , pp. 243-249
    • Lee, L.Y.1    Gu, Q.2
  • 26
    • 62649117270 scopus 로고    scopus 로고
    • The pathological role of transient receptor potential channels in heart disease
    • Watanabe H, Murakami M, Ohba T, Ono K, Ito H (2009) The pathological role of transient receptor potential channels in heart disease. Circ J 73:419-427
    • (2009) Circ J , vol.73 , pp. 419-427
    • Watanabe, H.1    Murakami, M.2    Ohba, T.3    Ono, K.4    Ito, H.5
  • 27
    • 77249103612 scopus 로고    scopus 로고
    • Molecular advances in autosomal dominant polycystic kidney disease
    • Gallagher AR, Germino GG, Somlo S (2010) Molecular advances in autosomal dominant polycystic kidney disease. Adv Chronic Kidney Dis 17:118-130
    • (2010) Adv Chronic Kidney Dis , vol.17 , pp. 118-130
    • Gallagher, A.R.1    Germino, G.G.2    Somlo, S.3
  • 30
    • 66049158598 scopus 로고    scopus 로고
    • A transient receptor potential-like channel mediates synaptic transmission in rod bipolar cells
    • Shen Y, Heimel JA, Kamermans M, Peachey NS, Gregg RG, Nawy S (2009) A transient receptor potential-like channel mediates synaptic transmission in rod bipolar cells. J Neurosci 29:6088-6093
    • (2009) J Neurosci , vol.29 , pp. 6088-6093
    • Shen, Y.1    Heimel, J.A.2    Kamermans, M.3    Peachey, N.S.4    Gregg, R.G.5    Nawy, S.6
  • 35
    • 47049130668 scopus 로고    scopus 로고
    • Crystal structure of the ligand-free G-protein-coupled receptor opsin
    • Park JH, Scheerer P, Hofmann KP, Choe HW, Ernst OP (2008) Crystal structure of the ligand-free G-protein-coupled receptor opsin. Nature 454:183-187
    • (2008) Nature , vol.454 , pp. 183-187
    • Park, J.H.1    Scheerer, P.2    Hofmann, K.P.3    Choe, H.W.4    Ernst, O.P.5
  • 38
    • 66249147196 scopus 로고    scopus 로고
    • Crystal structure of the sodiumpotassium pump at 2.4 A resolution
    • Shinoda T, Ogawa H, Cornelius F, Toyoshima C (2009) Crystal structure of the sodiumpotassium pump at 2.4 A resolution. Nature 459:446-450
    • (2009) Nature , vol.459 , pp. 446-450
    • Shinoda, T.1    Ogawa, H.2    Cornelius, F.3    Toyoshima, C.4
  • 39
    • 23244456428 scopus 로고    scopus 로고
    • Crystal structure of a mammalian voltagedependent Shaker family K+ channel
    • Long SB, Campbell EB, Mackinnon R (2005) Crystal structure of a mammalian voltagedependent Shaker family K+ channel. Science 309:897-903
    • (2005) Science , vol.309 , pp. 897-903
    • Long, S.B.1    Campbell, E.B.2    Mackinnon, R.3
  • 40
    • 23244441222 scopus 로고    scopus 로고
    • Voltage sensor of Kv1.2: Structural basis of electromechanical coupling
    • Long SB, Campbell EB, Mackinnon R (2005) Voltage sensor of Kv1.2: Structural basis of electromechanical coupling. Science 309:903-908
    • (2005) Science , vol.309 , pp. 903-908
    • Long, S.B.1    Campbell, E.B.2    Mackinnon, R.3
  • 41
    • 36248982122 scopus 로고    scopus 로고
    • Atomic structure of a voltagedependent K+ channel in a lipid membrane-like environment
    • Long SB, Tao X, Campbell EB, MacKinnon R (2007) Atomic structure of a voltagedependent K+ channel in a lipid membrane-like environment. Nature 450:376-382
    • (2007) Nature , vol.450 , pp. 376-382
    • Long, S.B.1    Tao, X.2    Campbell, E.B.3    MacKinnon, R.4
  • 42
    • 67949092829 scopus 로고    scopus 로고
    • Pore architecture and ion sites in acid-sensing ion channels and P2X receptors
    • Gonzales EB, Kawate T, Gouaux E (2009) Pore architecture and ion sites in acid-sensing ion channels and P2X receptors. Nature 460:599-604
    • (2009) Nature , vol.460 , pp. 599-604
    • Gonzales, E.B.1    Kawate, T.2    Gouaux, E.3
  • 43
    • 72949091450 scopus 로고    scopus 로고
    • Crystal structure of the eukaryotic strong inward-rectifier K+ channel Kir2.2 at 3.1 A resolution
    • Tao X, Avalos JL, Chen J, MacKinnon R (2009) Crystal structure of the eukaryotic strong inward-rectifier K+ channel Kir2.2 at 3.1 A resolution. Science 326:1668-1674
    • (2009) Science , vol.326 , pp. 1668-1674
    • Tao, X.1    Avalos, J.L.2    Chen, J.3    MacKinnon, R.4
  • 44
    • 72049124287 scopus 로고    scopus 로고
    • X-ray structure, symmetry and mechanism of an AMPA-subtype glutamate receptor
    • Sobolevsky AI, Rosconi MP, Gouaux E (2009) X-ray structure, symmetry and mechanism of an AMPA-subtype glutamate receptor. Nature 462:745-756
    • (2009) Nature , vol.462 , pp. 745-756
    • Sobolevsky, A.I.1    Rosconi, M.P.2    Gouaux, E.3
  • 45
    • 67949117176 scopus 로고    scopus 로고
    • Crystal structure of the ATP-gated P2X(4) ion channel in the closed state
    • Kawate T, Michel JC, Birdsong WT, Gouaux E (2009) Crystal structure of the ATP-gated P2X(4) ion channel in the closed state. Nature 460:592-598
    • (2009) Nature , vol.460 , pp. 592-598
    • Kawate, T.1    Michel, J.C.2    Birdsong, W.T.3    Gouaux, E.4
  • 46
    • 33748748066 scopus 로고    scopus 로고
    • Structure of the N-terminal ankyrin repeat domain of the TRPV2 ion channel
    • Jin X, Touhey J, Gaudet R (2006) Structure of the N-terminal ankyrin repeat domain of the TRPV2 ion channel. J Biol Chem 281:25006-25010
    • (2006) J Biol Chem , vol.281 , pp. 25006-25010
    • Jin, X.1    Touhey, J.2    Gaudet, R.3
  • 48
    • 34250190946 scopus 로고    scopus 로고
    • The ankyrin repeats of TRPV1 bind multiple ligands and modulate channel sensitivity
    • Lishko PV, Procko E, Jin X, Phelps CB, Gaudet R (2007) The ankyrin repeats of TRPV1 bind multiple ligands and modulate channel sensitivity. Neuron 54:905-918
    • (2007) Neuron , vol.54 , pp. 905-918
    • Lishko, P.V.1    Procko, E.2    Jin, X.3    Phelps, C.B.4    Gaudet, R.5
  • 49
    • 39749115631 scopus 로고    scopus 로고
    • Structural analyses of the ankyrin repeat domain of TRPV6 and related TRPV ion channels
    • Phelps CB, Huang RJ, Lishko PV, Wang RR, Gaudet R (2008) Structural analyses of the ankyrin repeat domain of TRPV6 and related TRPV ion channels. Biochemistry 47: 2476-2484
    • (2008) Biochemistry , vol.47 , pp. 2476-2484
    • Phelps, C.B.1    Huang, R.J.2    Lishko, P.V.3    Wang, R.R.4    Gaudet, R.5
  • 50
    • 73649104785 scopus 로고    scopus 로고
    • Differential regulation of TRPV1, TRPV3, and TRPV4 sensitivity through a conserved binding site on the ankyrin repeat domain
    • Phelps CB,Wang RR, Choo SS, Gaudet R (2010) Differential regulation of TRPV1, TRPV3, and TRPV4 sensitivity through a conserved binding site on the ankyrin repeat domain. J Biol Chem 285:731-740
    • (2010) J Biol Chem , vol.285 , pp. 731-740
    • Phelps, C.B.1    Wang, R.R.2    Choo, S.S.3    Gaudet, R.4
  • 51
    • 53149103958 scopus 로고    scopus 로고
    • X-ray crystal structure of a TRPM assembly domain reveals an antiparallel four-stranded coiled-coil
    • Fujiwara Y,Minor DL Jr (2008) X-ray crystal structure of a TRPM assembly domain reveals an antiparallel four-stranded coiled-coil. J Mol Biol 383:854-870
    • (2008) J Mol Biol , vol.383 , pp. 854-870
    • Fujiwara, Y.1    Minor Jr., D.L.2
  • 52
    • 0035947077 scopus 로고    scopus 로고
    • Crystal structure of the atypical protein kinase domain of a TRP channel with phosphotransferase activity
    • Yamaguchi H, Matsushita M, Nairn AC, Kuriyan J (2001) Crystal structure of the atypical protein kinase domain of a TRP channel with phosphotransferase activity. Mol Cell 7: 1047-1057
    • (2001) Mol Cell , vol.7 , pp. 1047-1057
    • Yamaguchi, H.1    Matsushita, M.2    Nairn, A.C.3    Kuriyan, J.4
  • 54
    • 71549157111 scopus 로고    scopus 로고
    • Selecting an appropriate method for expressing a recombinant protein
    • Brondyk WH (2009) Selecting an appropriate method for expressing a recombinant protein. Methods Enzymol 463:131-147
    • (2009) Methods Enzymol , vol.463 , pp. 131-147
    • Brondyk, W.H.1
  • 56
    • 77951248588 scopus 로고    scopus 로고
    • 3.5-nm structure of rat TRPV4 cation channel revealed by Zernike phase-contrast cryoelectron microscopy
    • Shigematsu H, Sokabe T, Danev R, Tominaga M, Nagayama K:A (2010) 3.5-nm structure of rat TRPV4 cation channel revealed by Zernike phase-contrast cryoelectron microscopy. J Biol Chem 285:11210-11218
    • (2010) J Biol Chem , vol.285 , pp. 11210-11218
    • Shigematsu, H.1    Sokabe, T.2    Danev, R.3    Tominaga, M.4    Nagayama, K.A.5
  • 58
    • 20744449020 scopus 로고    scopus 로고
    • The non-selective cation-permeable channel TRPC3 is a tetrahedron with a cap on the large cytoplasmic end
    • Mio K, Ogura T, Hara Y, Mori Y, Sato C (2005) The non-selective cation-permeable channel TRPC3 is a tetrahedron with a cap on the large cytoplasmic end. Biochem Biophys Res Commun 333:768-777
    • (2005) Biochem Biophys Res Commun , vol.333 , pp. 768-777
    • Mio, K.1    Ogura, T.2    Hara, Y.3    Mori, Y.4    Sato, C.5
  • 60
    • 37549038688 scopus 로고    scopus 로고
    • Threedimensional reconstruction using transmission electron microscopy reveals a swollen, bell-shaped structure of transient receptor potential melastatin type 2 cation channel
    • Maruyama Y, Ogura T, Mio K, Kiyonaka S, Kato K, Mori Y, Sato C (2007) Threedimensional reconstruction using transmission electron microscopy reveals a swollen, bell-shaped structure of transient receptor potential melastatin type 2 cation channel. J Biol Chem 282:36961-36970
    • (2007) J Biol Chem , vol.282 , pp. 36961-36970
    • Maruyama, Y.1    Ogura, T.2    Mio, K.3    Kiyonaka, S.4    Kato, K.5    Mori, Y.6    Sato, C.7
  • 61
    • 0141457531 scopus 로고    scopus 로고
    • Structural characterisation of neuronal voltagesensitive K+ channels heterologously expressed in Pichia pastoris
    • Parcej DN, Eckhardt-Strelau L (2003) Structural characterisation of neuronal voltagesensitive K+ channels heterologously expressed in Pichia pastoris. J Mol Biol 333:103-116
    • (2003) J Mol Biol , vol.333 , pp. 103-116
    • Parcej, D.N.1    Eckhardt-Strelau, L.2
  • 64
    • 49349111148 scopus 로고    scopus 로고
    • Functional analysis of Kv1.2 and paddle chimera Kv channels in planar lipid bilayers
    • Tao X, Mackinnon R (2008) Functional analysis of Kv1.2 and paddle chimera Kv channels in planar lipid bilayers. J Mol Biol 382(1):24-33
    • (2008) J Mol Biol , vol.382 , Issue.1 , pp. 24-33
    • Tao, X.1    Mackinnon, R.2
  • 65
    • 0034176255 scopus 로고    scopus 로고
    • Use of chemical chaperones in the yeast Saccharomyces cerevisiae to enhance heterologous membrane protein expression: High-yield expression and purification of human P-glycoprotein
    • Figler RA, Omote H, Nakamoto RK, Al-Shawi MK (2000) Use of chemical chaperones in the yeast Saccharomyces cerevisiae to enhance heterologous membrane protein expression: High-yield expression and purification of human P-glycoprotein. Arch Biochem Biophys 376:34-46
    • (2000) Arch Biochem Biophys , vol.376 , pp. 34-46
    • Figler, R.A.1    Omote, H.2    Nakamoto, R.K.3    Al-Shawi, M.K.4
  • 67
    • 0037033784 scopus 로고    scopus 로고
    • Internal Ca(2+) release in yeast is triggered by hypertonic shock and mediated by a TRP channel homologue
    • Denis V, Cyert MS (2002) Internal Ca(2+) release in yeast is triggered by hypertonic shock and mediated by a TRP channel homologue. J Cell Biol 156:29-34
    • (2002) J Cell Biol , vol.156 , pp. 29-34
    • Denis, V.1    Cyert, M.S.2
  • 68
    • 0141849083 scopus 로고    scopus 로고
    • Overexpression and purification of the vanilloid receptor in yeast (Saccharomyces cerevisiae)
    • Moiseenkova VY, Hellmich HL, Christensen BN (2003) Overexpression and purification of the vanilloid receptor in yeast (Saccharomyces cerevisiae). Biochem Biophys Res Commun 310:196-201
    • (2003) Biochem Biophys Res Commun , vol.310 , pp. 196-201
    • Moiseenkova, V.Y.1    Hellmich, H.L.2    Christensen, B.N.3
  • 69
    • 0001354986 scopus 로고
    • Expression of opsin genes in COS cells
    • Oprian DD (1993) Expression of opsin genes in COS cells. Methods Neuro. 15:301-306
    • (1993) Methods Neuro , vol.15 , pp. 301-306
    • Oprian, D.D.1
  • 72
    • 0020713543 scopus 로고
    • Monoclonal antibodies to rhodopsin: Characterization, cross-reactivity, and application as structural probes
    • Molday RS, MacKenzie D (1983) Monoclonal antibodies to rhodopsin: Characterization, cross-reactivity, and application as structural probes. Biochemistry 22:653-660
    • (1983) Biochemistry , vol.22 , pp. 653-660
    • Molday, R.S.1    MacKenzie, D.2
  • 73
    • 14844325731 scopus 로고    scopus 로고
    • Electron cryomicroscopy of biological machines at subnanometer resolution
    • ChiuW, Baker ML, JiangW, Dougherty M, Schmid MF (2005) Electron cryomicroscopy of biological machines at subnanometer resolution. Structure (Camb) 13:363-372
    • (2005) Structure (Camb , vol.13 , pp. 363-372
    • Chiu, W.1    Baker, M.L.2    Jiang, W.3    Dougherty, M.4    Schmid, M.F.5
  • 74
    • 67650716743 scopus 로고    scopus 로고
    • The advent of near-atomic resolution in single-particle electron microscopy
    • Cheng Y, Walz T (2009) The advent of near-atomic resolution in single-particle electron microscopy. Annu Rev Biochem 78:723-742
    • (2009) Annu Rev Biochem , vol.78 , pp. 723-742
    • Cheng, Y.1    Walz, T.2
  • 75
    • 0026521233 scopus 로고
    • Three-dimensional reconstruction of single particles embedded in ice
    • Penczek P, Radermacher M, Frank J (1992) Three-dimensional reconstruction of single particles embedded in ice. Ultramicroscopy 40:33-53
    • (1992) Ultramicroscopy , vol.40 , pp. 33-53
    • Penczek, P.1    Radermacher, M.2    Frank, J.3
  • 79
    • 0029975088 scopus 로고    scopus 로고
    • WEB: Processing and visualization of images in 3D electron microscopy and related fields
    • SPIDER
    • Frank J, Radermacher M, Penczek P, Zhu J, Li Y, Ladjadj M, Leith A:SPIDER (1996) WEB: Processing and visualization of images in 3D electron microscopy and related fields. J Struct Biol 116:190-199
    • (1996) J Struct Biol , vol.116 , pp. 190-199
    • Frank, J.1    Radermacher, M.2    Penczek, P.3    Zhu, J.4    Li, Y.5    Ladjadj, M.6    Leith, A.7
  • 80
    • 0035931906 scopus 로고    scopus 로고
    • The voltagesensitive sodium channel is a bell-shaped molecule with several cavities
    • Sato C, Ueno Y, Asai K, Takahashi K, Sato M, Engel A, Fujiyoshi Y (2001) The voltagesensitive sodium channel is a bell-shaped molecule with several cavities. Nature 409: 1047-1051
    • (2001) Nature , vol.409 , pp. 1047-1051
    • Sato, C.1    Ueno, Y.2    Asai, K.3    Takahashi, K.4    Sato, M.5    Engel, A.6    Fujiyoshi, Y.7
  • 81
    • 0037677206 scopus 로고    scopus 로고
    • Structure of the type 1 inositol 1,4,5-trisphosphate receptor revealed by electron cryomicroscopy
    • Serysheva II, Bare DJ, Ludtke SJ, Kettlun CS, Chiu W, Mignery GA (2003) Structure of the type 1 inositol 1,4,5-trisphosphate receptor revealed by electron cryomicroscopy. J Biol Chem 278:21319-21322
    • (2003) J Biol Chem , vol.278 , pp. 21319-21322
    • Serysheva, I.I.1    Bare, D.J.2    Ludtke, S.J.3    Kettlun, C.S.4    Chiu, W.5    Mignery, G.A.6
  • 83
    • 0042235365 scopus 로고    scopus 로고
    • Visualization of the domain structure of an L-type Ca2+ channel using electron cryo-microscopy
    • Wolf M, Eberhart A, Glossmann H, Striessnig J, Grigorieff N (2003) Visualization of the domain structure of an L-type Ca2+ channel using electron cryo-microscopy. J Mol Biol 332:171-182
    • (2003) J Mol Biol , vol.332 , pp. 171-182
    • Wolf, M.1    Eberhart, A.2    Glossmann, H.3    Striessnig, J.4    Grigorieff, N.5
  • 85
    • 0034737734 scopus 로고    scopus 로고
    • Three-dimensional structure of ryanodine receptor isoform three in two conformational states as visualized by cryo-electron microscopy
    • Sharma MR, Jeyakumar LH, Fleischer S, Wagenknecht T (2000) Three-dimensional structure of ryanodine receptor isoform three in two conformational states as visualized by cryo-electron microscopy. J Biol Chem 275:9485-9491
    • (2000) J Biol Chem , vol.275 , pp. 9485-9491
    • Sharma, M.R.1    Jeyakumar, L.H.2    Fleischer, S.3    Wagenknecht, T.4
  • 86
    • 0036617107 scopus 로고    scopus 로고
    • Three-dimensional reconstruction of ryanodine receptors
    • Wagenknecht T, Samso M (2002) Three-dimensional reconstruction of ryanodine receptors. Front Biosci 7:d1464-d1474
    • (2002) Front Biosci , vol.7
    • Wagenknecht, T.1    Samso, M.2
  • 89
    • 4043151338 scopus 로고    scopus 로고
    • Electron microscopic analysis of KvAP voltagedependent K+ channels in an open conformation
    • Jiang QX,Wang DN, MacKinnon R (2004) Electron microscopic analysis of KvAP voltagedependent K+ channels in an open conformation. Nature 430:806-810
    • (2004) Nature , vol.430 , pp. 806-810
    • Jiang, Q.X.1    Wang, D.N.2    MacKinnon, R.3
  • 90
    • 70249124205 scopus 로고    scopus 로고
    • Structure of the BK potassium channel in a lipid membrane from electron cryomicroscopy
    • Wang L, Sigworth FJ (2009) Structure of the BK potassium channel in a lipid membrane from electron cryomicroscopy. Nature 461:292-295
    • (2009) Nature , vol.461 , pp. 292-295
    • Wang, L.1    Sigworth, F.J.2
  • 91
    • 64549113013 scopus 로고    scopus 로고
    • Hot on the trail of TRP channel structure
    • Moiseenkova-Bell VY, Wensel TG (2009) Hot on the trail of TRP channel structure. J Gen Physiol 133:239-244
    • (2009) J Gen Physiol , vol.133 , pp. 239-244
    • Moiseenkova-Bell, V.Y.1    Wensel, T.G.2
  • 92
    • 77449108419 scopus 로고    scopus 로고
    • Single-particle reconstruction of biological macromolecules in electron microscopy - 30 years
    • Frank J (2009) Single-particle reconstruction of biological macromolecules in electron microscopy - 30 years. Q Rev Biophys 42:139-158
    • (2009) Q Rev Biophys , vol.42 , pp. 139-158
    • Frank, J.1
  • 94
    • 77951912692 scopus 로고    scopus 로고
    • 3.3 a cryo-EM structure of a nonenveloped virus reveals a priming mechanism for cell entry
    • Zhang X, Jin L, Fang Q, Hui WH, Zhou ZH (2010) 3.3 a cryo-EM structure of a nonenveloped virus reveals a priming mechanism for cell entry. Cell 141:472-482
    • (2010) Cell , vol.141 , pp. 472-482
    • Zhang, X.1    Jin, L.2    Fang, Q.3    Hui, W.H.4    Zhou, Z.H.5
  • 96
    • 25844445494 scopus 로고    scopus 로고
    • Electron cryomicroscopy of single particles at subnanometer resolution
    • Jiang W, Ludtke SJ (2005) Electron cryomicroscopy of single particles at subnanometer resolution. Curr Opin Struct Biol 15:571-577
    • (2005) Curr Opin Struct Biol , vol.15 , pp. 571-577
    • Jiang, W.1    Ludtke, S.J.2
  • 97
    • 34848839244 scopus 로고    scopus 로고
    • Yeast screens show aromatic residues at the end of the sixth helix anchor transient receptor potential channel gate
    • Zhou X, Su Z, Anishkin A, Haynes WJ, Friske EM, Loukin SH, Kung C, Saimi Y (2007) Yeast screens show aromatic residues at the end of the sixth helix anchor transient receptor potential channel gate. Proc Natl Acad Sci USA 104:15555-15559
    • (2007) Proc Natl Acad Sci USA , vol.104 , pp. 15555-15559
    • Zhou, X.1    Su, Z.2    Anishkin, A.3    Haynes, W.J.4    Friske, E.M.5    Loukin, S.H.6    Kung, C.7    Saimi, Y.8
  • 98
    • 37649002371 scopus 로고    scopus 로고
    • Yeast gain-of-function mutations reveal structure-function relationships conserved among different subfamilies of transient receptor potential channels
    • Su Z, Zhou X, Haynes WJ, Loukin SH, Anishkin A, Saimi Y, Kung C (2007) Yeast gain-of-function mutations reveal structure-function relationships conserved among different subfamilies of transient receptor potential channels. Proc Natl Acad Sci USA 104:19607-19612
    • (2007) Proc Natl Acad Sci USA , vol.104 , pp. 19607-19612
    • Su, Z.1    Zhou, X.2    Haynes, W.J.3    Loukin, S.H.4    Anishkin, A.5    Saimi, Y.6    Kung, C.7
  • 99
    • 77953752223 scopus 로고    scopus 로고
    • Forward-genetic analysis reveals multiple gating mechanisms of Trpv4
    • Loukin S, Su Z, Zhou X, Kung C (2010) Forward-genetic analysis reveals multiple gating mechanisms of Trpv4. J Biol Chem 285(26):19884-19890
    • (2010) J Biol Chem , vol.285 , Issue.26 , pp. 19884-19890
    • Loukin, S.1    Su, Z.2    Zhou, X.3    Kung, C.4
  • 100
    • 42949117400 scopus 로고    scopus 로고
    • A yeast genetic screen reveals a critical role for the pore helix domain in TRP channel gating
    • Myers BR, Bohlen CJ, Julius D (2008) A yeast genetic screen reveals a critical role for the pore helix domain in TRP channel gating. Neuron 58:362-373
    • (2008) Neuron , vol.58 , pp. 362-373
    • Myers, B.R.1    Bohlen, C.J.2    Julius, D.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.