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Volumn 141, Issue 4, 2013, Pages 445-465

Construction and validation of a homology model of the human voltage-gated proton channel hHv1

Author keywords

[No Author keywords available]

Indexed keywords

HV1 CHANNEL, HUMAN; ION CHANNEL; PROTON;

EID: 84878666039     PISSN: 00221295     EISSN: 15407748     Source Type: Journal    
DOI: 10.1085/jgp.201210856     Document Type: Article
Times cited : (72)

References (101)
  • 1
    • 36248946187 scopus 로고    scopus 로고
    • Portability of paddle motif function and pharmacology in voltage sensors
    • Alabi, A.A., M.I. Bahamonde, H.J. Jung, J.I. Kim, and K.J. Swartz. 2007. Portability of paddle motif function and pharmacology in voltage sensors. Nature. 450:370-375. http://dx.doi.org/10.1038/ nature06266
    • (2007) Nature. , vol.450 , pp. 370-375
    • Alabi, A.A.1    Bahamonde, M.I.2    Jung, H.J.3    Kim, J.I.4    Swartz, K.J.5
  • 3
    • 0142073070 scopus 로고    scopus 로고
    • A prokaryotic glutamate receptor: homology modelling and molecular dynamics simulations of GluR0
    • Arinaminpathy, Y., P.C. Biggin, I.H. Shrivastava, and M.S.P. Sansom. 2003. A prokaryotic glutamate receptor: homology modelling and molecular dynamics simulations of GluR0. FEBS Lett. 553:321- 327. http://dx.doi.org/10.1016/S0014-5793(03)01036-6
    • (2003) FEBS Lett. , vol.553
    • Arinaminpathy, Y.1    Biggin, P.C.2    Shrivastava, I.H.3    Sansom, M.S.P.4
  • 4
    • 33745907550 scopus 로고    scopus 로고
    • A hydrophobic gate in an ion channel: the closed state of the nicotinic acetylcholine receptor
    • Beckstein, O., and M.S.P. Sansom. 2006. A hydrophobic gate in an ion channel: the closed state of the nicotinic acetylcholine receptor. Phys. Biol. 3:147-159. http://dx.doi.org/10.1088/1478-3975/ 3/2/007
    • (2006) Phys. Biol. , vol.3 , pp. 147-159
    • Beckstein, O.1    Sansom, M.S.P.2
  • 5
    • 84155191394 scopus 로고    scopus 로고
    • The pore of the voltage-gated proton channel
    • Berger, T.K., and E.Y. Isacoff. 2011. The pore of the voltage-gated proton channel. Neuron. 72:991-1000. http://dx.doi.org/10.1016/ j.neuron.2011.11.014
    • (2011) Neuron. , vol.72 , pp. 991-1000
    • Berger, T.K.1    Isacoff, E.Y.2
  • 6
    • 41149095488 scopus 로고    scopus 로고
    • How membrane proteins sense voltage
    • Bezanilla, F. 2008. How membrane proteins sense voltage. Nat. Rev. Mol. Cell Biol. 9:323-332. http://dx.doi.org/10.1038/nrm2376
    • (2008) Nat. Rev. Mol. Cell Biol. , vol.9 , pp. 323-332
    • Bezanilla, F.1
  • 7
  • 9
    • 0037007814 scopus 로고    scopus 로고
    • Molecular dynamics simulations of a K channel model: Sensitivity to changes in ions, waters, and membrane environment
    • Capener, C.E., and M.S.P. Sansom. 2002. Molecular dynamics simulations of a K channel model: Sensitivity to changes in ions, waters, and membrane environment. J. Phys. Chem. B. 106:4543- 4551. http://dx.doi.org/10.1021/jp0129986
    • (2002) J. Phys. Chem. B. , vol.106
    • Capener, C.E.1    Sansom, M.S.P.2
  • 10
    • 4644308725 scopus 로고    scopus 로고
    • Structural determinants of proton blockage in aquaporins
    • Chakrabarti, N., B. Roux, and R. Pomès. 2004. Structural determinants of proton blockage in aquaporins. J. Mol. Biol. 343:493-510. http://dx.doi.org/10.1016/j.jmb.2004.08.036
    • (2004) J. Mol. Biol. , vol.343 , pp. 493-510
    • Chakrabarti, N.1    Roux, B.2    Pomès, R.3
  • 11
    • 77749320417 scopus 로고    scopus 로고
    • An iris-like mechanism of pore dilation in the CorA magnesium transport system
    • Chakrabarti, N., C. Neale, J. Payandeh, E.F. Pai, and R. Pomès. 2010. An iris-like mechanism of pore dilation in the CorA magnesium transport system. Biophys. J. 98:784-792. http://dx.doi.org/ 10.1016/j.bpj.2009.11.009
    • (2010) Biophys. J. , vol.98 , pp. 784-792
    • Chakrabarti, N.1    Neale, C.2    Payandeh, J.3    Pai, E.F.4    Pomès, R.5
  • 12
    • 34248549547 scopus 로고    scopus 로고
    • Can molecular dynamics simulations provide high-resolution refinement of protein structure?
    • Chen, J., and C.L. Brooks III. 2007. Can molecular dynamics simulations provide high-resolution refinement of protein structure? Proteins. 67:922-930. http://dx.doi.org/10.1002/prot.21345
    • (2007) Proteins , vol.67 , pp. 922-930
    • Chen, J.1    Brooks, C.L.2
  • 13
  • 14
    • 0038580629 scopus 로고    scopus 로고
    • Properties of single voltage-gated proton channels in human eosinophils estimated by noise analysis and by direct measurement
    • Cherny, V.V., R. Murphy, V. Sokolov, R.A. Levis, and T.E. DeCoursey. 2003. Properties of single voltage-gated proton channels in human eosinophils estimated by noise analysis and by direct measurement. J. Gen. Physiol. 121:615-628. http://dx.doi.org/10.1085/ jgp.200308813
    • (2003) J. Gen. Physiol. , vol.121 , pp. 615-628
    • Cherny, V.V.1    Murphy, R.2    Sokolov, V.3    Levis, R.A.4    DeCoursey, T.E.5
  • 15
    • 0037379781 scopus 로고    scopus 로고
    • Voltage-gated proton channels and other proton transfer pathways
    • DeCoursey, T.E. 2003. Voltage-gated proton channels and other proton transfer pathways. Physiol. Rev. 83:475-579. http://dx.doi .org/10.1152/physrev.00028.2002
    • (2003) Physiol. Rev. , vol.83 , pp. 475-579
    • DeCoursey, T.E.1
  • 16
    • 76349113357 scopus 로고    scopus 로고
    • Voltage-gated proton channels find their dream job managing the respiratory burst in phagocytes
    • DeCoursey, T.E. 2010. Voltage-gated proton channels find their dream job managing the respiratory burst in phagocytes. Physiology (Bethesda). 25:27-40. http://dx.doi.org/10.1152/physiol.00039.2009
    • (2010) Physiology (Bethesda). , vol.25 , pp. 27-40
    • DeCoursey, T.E.1
  • 17
    • 78649713698 scopus 로고    scopus 로고
    • Physiological roles of voltage- gated proton channels in leukocytes
    • Demaurex, N., and A. El Chemaly. 2010. Physiological roles of voltage- gated proton channels in leukocytes. J. Physiol. 588:4659-4665. http://dx.doi.org/10.1113/jphysiol.2010.194225
    • (2010) J. Physiol. , vol.588 , pp. 4659-4665
    • Demaurex, N.1    Chemaly, A.El.2
  • 18
    • 1842682281 scopus 로고    scopus 로고
    • Electric field-controlled water permeation coupled to ion transport through a nanopore
    • Dzubiella, J., R.J. Allen, and J.P. Hansen. 2004. Electric field-controlled water permeation coupled to ion transport through a nanopore. J. Chem. Phys. 120:5001-5004. http://dx.doi.org/10.1063/ 1.1665656
    • (2004) J. Chem. Phys. , vol.120 , pp. 5001-5004
    • Dzubiella, J.1    Allen, R.J.2    Hansen, J.P.3
  • 19
    • 79953759344 scopus 로고    scopus 로고
    • Role of solvation effects in protein denaturation: from thermodynamics to single molecules and back
    • England, J.L., and G. Haran. 2011. Role of solvation effects in protein denaturation: from thermodynamics to single molecules and back. Annu. Rev. Phys. Chem. 62:257-277. http://dx.doi.org/10 .1146/annurev-physchem-032210-103531
    • (2011) Annu. Rev. Phys. Chem. , vol.62 , pp. 257-277
    • England, J.L.1    Haran, G.2
  • 21
    • 79959931985 scopus 로고    scopus 로고
    • HMMER web server: interactive sequence similarity searching
    • Finn, R.D., J. Clements, and S.R. Eddy. 2011. HMMER web server: interactive sequence similarity searching. Nucleic Acids Res. 39:W29-W37. http://dx.doi.org/10.1093/nar/gkr367
    • (2011) Nucleic Acids Res. , vol.39
    • Finn, R.D.1    Clements, J.2    Eddy, S.R.3
  • 22
    • 84868122687 scopus 로고    scopus 로고
    • Function of proton channels in lung epithelia
    • Fischer, H. 2012. Function of proton channels in lung epithelia. Wiley Interdiscip Rev Membr Transp Signal. 1:247-258. http://dx.doi .org/10.1002/wmts.17
    • (2012) Wiley Interdiscip Rev Membr Transp Signal. , vol.1 , pp. 247-258
    • Fischer, H.1
  • 23
    • 33745714411 scopus 로고    scopus 로고
    • On the accuracy of homology modeling and sequence alignment methods applied to membrane proteins
    • Forrest, L.R., C.L. Tang, and B. Honig. 2006. On the accuracy of homology modeling and sequence alignment methods applied to membrane proteins. Biophys. J. 91:508-517. http://dx.doi.org/ 10.1529/biophysj.106.082313
    • (2006) Biophys. J. , vol.91 , pp. 508-517
    • Forrest, L.R.1    Tang, C.L.2    Honig, B.3
  • 24
    • 33845365529 scopus 로고    scopus 로고
    • A voltage-sensor water pore
    • Freites, J.A., D.J. Tobias, and S.H. White. 2006. A voltage-sensor water pore. Biophys. J. 91:L90-L92. http://dx.doi.org/10.1529/biophysj .106.096065
    • (2006) Biophys. J. , vol.91
    • Freites, J.A.1    Tobias, D.J.2    White, S.H.3
  • 25
    • 77449143196 scopus 로고    scopus 로고
    • Strong cooperativity between subunits in voltage-gated proton channels
    • Gonzalez, C., H.P. Koch, B.M. Drum, and H.P. Larsson. 2010. Strong cooperativity between subunits in voltage-gated proton channels. Nat. Struct. Mol. Biol. 17:51-56. http://dx.doi.org/10.1038/ nsmb.1739
    • (2010) Nat. Struct. Mol. Biol. , vol.17 , pp. 51-56
    • Gonzalez, C.1    Koch, H.P.2    Drum, B.M.3    Larsson, H.P.4
  • 26
    • 84874729303 scopus 로고    scopus 로고
    • Molecular mechanism of voltage sensing in voltage-gated proton channels
    • Gonzalez, C., S. Rebolledo, M.E. Perez, and H.P. Larsson. 2013. Molecular mechanism of voltage sensing in voltage-gated proton channels. J. Gen. Physiol. 141:275-285. http://dx.doi.org/10.1085/ jgp.201310970
    • (2013) J. Gen. Physiol. , vol.141 , pp. 275-285
    • Gonzalez, C.1    Rebolledo, S.2    Perez, M.E.3    Larsson, H.P.4
  • 27
    • 84861664954 scopus 로고    scopus 로고
    • A proton leak current through the cardiac sodium channel is linked to mixed arrhythmia and the dilated cardiomyopathy phenotype
    • Gosselin-Badaroudine, P., D.I. Keller, H. Huang, V. Pouliot, A. Chatelier, S. Osswald, M. Brink, and M. Chahine. 2012. A proton leak current through the cardiac sodium channel is linked to mixed arrhythmia and the dilated cardiomyopathy phenotype. PLoS ONE. 7:e38331. http://dx.doi.org/10.1371/journal .pone.0038331
    • (2012) PLoS ONE. , vol.7
    • Gosselin-Badaroudine, P.1    Keller, D.I.2    Huang, H.3    Pouliot, V.4    Chatelier, A.5    Osswald, S.6    Brink, M.7    Chahine, M.8
  • 28
    • 34948906954 scopus 로고    scopus 로고
    • MaxAlign: maximizing usable data in an alignment
    • Gouveia-Oliveira, R., P.W. Sackett, and A.G. Pedersen. 2007. MaxAlign: maximizing usable data in an alignment. BMC Bioinformatics. 8:312. http://dx.doi.org/10.1186/1471-2105-8-312
    • (2007) BMC Bioinformatics. , vol.8 , pp. 312
    • Gouveia-Oliveira, R.1    Sackett, P.W.2    Pedersen, A.G.3
  • 29
    • 0242578620 scopus 로고    scopus 로고
    • A simple, fast, and accurate algorithm to estimate large phylogenies by maximum likelihood
    • Guindon, S., and O. Gascuel. 2003. A simple, fast, and accurate algorithm to estimate large phylogenies by maximum likelihood. Syst. Biol. 52:696-704. http://dx.doi.org/10.1080/10635150390235520
    • (2003) Syst. Biol. , vol.52 , pp. 696-704
    • Guindon, S.1    Gascuel, O.2
  • 30
    • 0000153689 scopus 로고
    • Complex formation between metallic cations and proteins, peptides and amino acids
    • Gurd, F.R., and P.E. Wilcox. 1956. Complex formation between metallic cations and proteins, peptides and amino acids. Adv. Protein Chem. 11:311-427. http://dx.doi.org/10.1016/S0065-3233(08) 60424-6
    • (1956) Adv. Protein Chem. , vol.11 , pp. 311-427
    • Gurd, F.R.1    Wilcox, P.E.2
  • 31
    • 0023718702 scopus 로고
    • Superoxide generation by the electrogenic NADPH oxidase of human neutrophils is limited by the movement of a compensating charge
    • Henderson, L.M., J.B. Chappell, and O.T.G. Jones. 1988. Superoxide generation by the electrogenic NADPH oxidase of human neutrophils is limited by the movement of a compensating charge. Biochem. J. 255:285-290.
    • (1988) Biochem. J. , vol.255 , pp. 285-290
    • Henderson, L.M.1    Chappell, J.B.2    Jones, O.T.G.3
  • 33
    • 0000388705 scopus 로고    scopus 로고
    • LINCS: A linear constraint solver for molecular simulations
    • Hess, B., H. Bekker, H.J.C. Berendsen, and J. Fraaije. 1997. LINCS: A linear constraint solver for molecular simulations. J. Comput. Chem. 18:1463-1472. http://dx.doi.org/10.1002/ (SICI)1096-987X(199709)18:121463::AID-JCC43.0.CO;2-H
    • (1997) J. Comput. Chem. , vol.18 , pp. 1463-1472
    • Hess, B.1    Bekker, H.2    Berendsen, H.J.C.3    Fraaije, J.4
  • 34
    • 46249092554 scopus 로고    scopus 로고
    • GROMACS 4: Algorithms for highly efficient, load-balanced, and scalable molecular simulation
    • Hess, B., C. Kutzner, D. van der Spoel, and E. Lindahl. 2008. GROMACS 4: Algorithms for highly efficient, load-balanced, and scalable molecular simulation. J. Chem. Theory Comput. 4:435-447. http://dx.doi.org/10.1021/ct700301q
    • (2008) J. Chem. Theory Comput , vol.4 , pp. 435-447
    • Hess, B.1    Kutzner, C.2    van der Spoel, D.3    Lindahl, E.4
  • 36
    • 0029878720 scopus 로고    scopus 로고
    • VMD: visual molecular dynamics
    • Humphrey, W., A. Dalke, and K. Schulten. 1996. VMD: visual molecular dynamics. J. Mol. Graph. 14:33-38. http://dx.doi.org/ 10.1016/0263-7855(96)00018-5
    • (1996) J. Mol. Graph. , vol.14 , pp. 33-38
    • Humphrey, W.1    Dalke, A.2    Schulten, K.3
  • 37
    • 12844260161 scopus 로고    scopus 로고
    • Comparative protein structure modeling and its applications to drug discovery
    • Jacobson, M., and A. Sali. 2004. Comparative protein structure modeling and its applications to drug discovery. Annu. Rep. Med. Chem. 39:259-276. http://dx.doi.org/10.1016/S0065-7743(04) 39020-2
    • (2004) Annu. Rep. Med. Chem. , vol.39 , pp. 259-276
    • Jacobson, M.1    Sali, A.2
  • 40
  • 41
    • 0004016501 scopus 로고
    • Comparison of simple potential functions for simulating liquid water
    • Jorgensen, W.L., J. Chandrasekhar, J.D. Madura, R.W. Impey, and M.L. Klein. 1983. Comparison of simple potential functions for simulating liquid water. J. Chem. Phys. 79:926-935. http://dx.doi .org/10.1063/1.445869
    • (1983) J. Chem. Phys. , vol.79 , pp. 926-935
    • Jorgensen, W.L.1    Chandrasekhar, J.2    Madura, J.D.3    Impey, R.W.4    Klein, M.L.5
  • 42
    • 0029912748 scopus 로고    scopus 로고
    • Development and testing of the OPLS all-atom force field on conformational energetics and properties of organic liquids
    • Jorgensen, W.L., D.S. Maxwell, and J. Tirado-Rives. 1996. Development and testing of the OPLS all-atom force field on conformational energetics and properties of organic liquids. J. Am. Chem. Soc. 118:11225-11236. http://dx.doi.org/10.1021/ja9621760
    • (1996) J. Am. Chem. Soc. , vol.118 , pp. 11225-11236
    • Jorgensen, W.L.1    Maxwell, D.S.2    Tirado-Rives, J.3
  • 43
    • 33947139278 scopus 로고    scopus 로고
    • Setting up and running molecular dynamics simulations of membrane proteins
    • Kandt, C., W.L. Ash, and D.P. Tieleman. 2007. Setting up and running molecular dynamics simulations of membrane proteins. Methods. 41:475-488. http://dx.doi.org/10.1016/j.ymeth.2006.08.006 Koch, H.P., T. Kurokawa, Y. Okochi, M. Sasaki, Y. Okamura, and H.P. Larsson. 2008. Multimeric nature of voltage-gated proton channels. Proc. Natl. Acad. Sci. USA. 105:9111-9116. http:// dx.doi.org/10.1073/pnas.0801553105
    • (2007) Methods. , vol.41 , pp. 475-488
    • Kandt, C.1    Ash, W.L.2    Tieleman, D.P.3
  • 46
    • 5644279114 scopus 로고    scopus 로고
    • Homology modelling and molecular dynamics simulations: comparative studies of human aquaporin- 1
    • Law, R.J., and M.S. Sansom. 2004. Homology modelling and molecular dynamics simulations: comparative studies of human aquaporin- 1. Eur. Biophys. J. 33:477-489. http://dx.doi.org/10.1007/ s00249-004-0398-z
    • (2004) Eur. Biophys. J. , vol.33 , pp. 477-489
    • Law, R.J.1    Sansom, M.S.2
  • 47
    • 45849154166 scopus 로고    scopus 로고
    • An improved general amino acid replacement matrix
    • Le, S.Q., and O. Gascuel. 2008. An improved general amino acid replacement matrix. Mol. Biol. Evol. 25:1307-1320. http://dx.doi .org/10.1093/molbev/msn067
    • (2008) Mol. Biol. Evol. , vol.25 , pp. 1307-1320
    • Le, S.Q.1    Gascuel, O.2
  • 49
    • 45549106075 scopus 로고    scopus 로고
    • Dimeric subunit stoichiometry of the human voltage-dependent proton channel Hv1
    • Lee, S.Y., J.A. Letts, and R. Mackinnon. 2008. Dimeric subunit stoichiometry of the human voltage-dependent proton channel Hv1. Proc. Natl. Acad. Sci. USA. 105:7692-7695. http://dx.doi .org/10.1073/pnas.0803277105
    • (2008) Proc. Natl. Acad. Sci. USA. , vol.105 , pp. 7692-7695
    • Lee, S.Y.1    Letts, J.A.2    Mackinnon, R.3
  • 51
    • 33845873289 scopus 로고    scopus 로고
    • Interactive Tree Of Life (iTOL): an online tool for phylogenetic tree display and annotation
    • Letunic, I., and P. Bork. 2007. Interactive Tree Of Life (iTOL): an online tool for phylogenetic tree display and annotation. Bioinformatics. 23:127-128. http://dx.doi.org/10.1093/bioinformatics/ btl529
    • (2007) Bioinformatics. , vol.23 , pp. 127-128
    • Letunic, I.1    Bork, P.2
  • 52
    • 0018072320 scopus 로고
    • Number of water molecules coupled to the transport of sodium, potassium and hydrogen ions via gramicidin, nonactin or valinomycin
    • Levitt, D.G., S.R. Elias, and J.M. Hautman. 1978. Number of water molecules coupled to the transport of sodium, potassium and hydrogen ions via gramicidin, nonactin or valinomycin. Biochim. Biophys. Acta. 512:436-451. http://dx.doi.org/10.1016/0005-2736 (78)90266-3
    • (1978) Biochim. Biophys. Acta. , vol.512 , pp. 436-451
    • Levitt, D.G.1    Elias, S.R.2    Hautman, J.M.3
  • 53
    • 79961124704 scopus 로고    scopus 로고
    • R1 in the Shaker S4 occupies the gating charge transfer center in the resting state
    • Lin, M.C., J.Y. Hsieh, A.F. Mock, and D.M. Papazian. 2011. R1 in the Shaker S4 occupies the gating charge transfer center in the resting state. J. Gen. Physiol. 138:155-163. http://dx.doi.org/10.1085/jgp.201110642
    • (2011) J. Gen. Physiol. , vol.138 , pp. 155-163
    • Lin, M.C.1    Hsieh, J.Y.2    Mock, A.F.3    Papazian, D.M.4
  • 54
    • 84857463877 scopus 로고    scopus 로고
    • Systematic validation of protein force fields against experimental data
    • LindorffLarsen, K., P. Maragakis, S. Piana, M.P. Eastwood, R.O. Dror, and D.E. Shaw. 2012. Systematic validation of protein force fields against experimental data. PLoS ONE. 7:e32131. http:// dx.doi.org/10.1371/journal.pone.0032131
    • (2012) PLoS ONE. , vol.7
    • LindorffLarsen, K.1    Maragakis, P.2    Piana, S.3    Eastwood, M.P.4    Dror, R.O.5    Shaw, D.E.6
  • 55
    • 75749122696 scopus 로고    scopus 로고
    • Acid extrusion from human spermatozoa is mediated by flagellar voltage-gated proton channel
    • Lishko, P.V., I.L. Botchkina, A. Fedorenko, and Y. Kirichok. 2010. Acid extrusion from human spermatozoa is mediated by flagellar voltage-gated proton channel. Cell. 140:327-337. http://dx.doi .org/10.1016/j.cell.2009.12.053
    • (2010) Cell. , vol.140 , pp. 327-337
    • Lishko, P.V.1    Botchkina, I.L.2    Fedorenko, A.3    Kirichok, Y.4
  • 58
    • 21744438625 scopus 로고    scopus 로고
    • Phosphoinositide phosphatase activity coupled to an intrinsic voltage sensor
    • Murata, Y., H. Iwasaki, M. Sasaki, K. Inaba, and Y. Okamura. 2005. Phosphoinositide phosphatase activity coupled to an intrinsic voltage sensor. Nature. 435:1239-1243. http://dx.doi.org/10.1038/ nature03650
    • (2005) Nature. , vol.435 , pp. 1239-1243
    • Murata, Y.1    Iwasaki, H.2    Sasaki, M.3    Inaba, K.4    Okamura, Y.5
  • 59
    • 43749098079 scopus 로고    scopus 로고
    • Detailed comparison of expressed and native voltage-gated proton channel currents
    • Musset, B., V.V. Cherny, D. Morgan, Y. Okamura, I.S. Ramsey, D.E. Clapham, and T.E. DeCoursey. 2008. Detailed comparison of expressed and native voltage-gated proton channel currents. J. Physiol. 586:2477-2486. http://dx.doi.org/10.1113/jphysiol .2007.149427
    • (2008) J. Physiol. , vol.586 , pp. 2477-2486
    • Musset, B.1    Cherny, V.V.2    Morgan, D.3    Okamura, Y.4    Ramsey, I.S.5    Clapham, D.E.6    DeCoursey, T.E.7
  • 60
    • 77952939105 scopus 로고    scopus 로고
    • Zinc inhibition of monomeric and dimeric proton channels suggests cooperative gating
    • Musset, B., S.M.E. Smith, S. Rajan, V.V. Cherny, S. Sujai, D. Morgan, and T.E. DeCoursey. 2010. Zinc inhibition of monomeric and dimeric proton channels suggests cooperative gating. J. Physiol. 588:1435-1449. http://dx.doi.org/10.1113/jphysiol .2010.188318
    • (2010) J. Physiol. , vol.588 , pp. 1435-1449
    • Musset, B.1    Smith, S.M.E.2    Rajan, S.3    Cherny, V.V.4    Sujai, S.5    Morgan, D.6    DeCoursey, T.E.7
  • 61
    • 83055176497 scopus 로고    scopus 로고
    • Aspartate 112 is the selectivity filter of the human voltage-gated proton channel
    • Musset, B., S.M.E. Smith, S. Rajan, D. Morgan, V.V. Cherny, and T.E. DeCoursey. 2011. Aspartate 112 is the selectivity filter of the human voltage-gated proton channel. Nature. 480:273-277. http://dx.doi.org/10.1038/nature10557
    • (2011) Nature. , vol.480 , pp. 273-277
    • Musset, B.1    Smith, S.M.E.2    Rajan, S.3    Morgan, D.4    Cherny, V.V.5    DeCoursey, T.E.6
  • 62
    • 0033222872 scopus 로고    scopus 로고
    • Modular assembly of voltage-gated channel proteins: a sequence analysis and phylogenetic study
    • Nelson, R.D., G. Kuan, M.H. Saier Jr., and M. Montal. 1999. Modular assembly of voltage-gated channel proteins: a sequence analysis and phylogenetic study. J. Mol. Microbiol. Biotechnol. 1:281-287.
    • (1999) J. Mol. Microbiol. Biotechnol. , vol.1 , pp. 281-287
    • Nelson, R.D.1    Kuan, G.2    Saier Jr, M.H.3    Montal, M.4
  • 64
    • 0031167555 scopus 로고    scopus 로고
    • Atomic radii for continuum electrostatics calculations based on molecular dynamics free energy simulations
    • Nina, M., D. Beglov, and B. Roux. 1997. Atomic radii for continuum electrostatics calculations based on molecular dynamics free energy simulations. J. Phys. Chem. B. 101:5239-5248. http://dx.doi .org/10.1021/jp970736r
    • (1997) J. Phys. Chem. B. , vol.101 , pp. 5239-5248
    • Nina, M.1    Beglov, D.2    Roux, B.3
  • 65
    • 34547809547 scopus 로고
    • A unified formulation of the constant temperature molecular dynamics methods
    • Nosè, S. 1984. A unified formulation of the constant temperature molecular dynamics methods. J. Chem. Phys. 81:511. http:// dx.doi.org/10.1063/1.447334
    • (1984) J. Chem. Phys. , vol.81 , pp. 511
    • Nosè, S.1
  • 66
    • 0034623005 scopus 로고    scopus 로고
    • T-Coffee: A novel method for fast and accurate multiple sequence alignment
    • Notredame, C., D.G. Higgins, and J. Heringa. 2000. T-Coffee: A novel method for fast and accurate multiple sequence alignment. J. Mol. Biol. 302:205-217. http://dx.doi.org/10.1006/jmbi.2000.4042
    • (2000) J. Mol. Biol. , vol.302 , pp. 205-217
    • Notredame, C.1    Higgins, D.G.2    Heringa, J.3
  • 67
    • 59649119224 scopus 로고    scopus 로고
    • Voltage-sensing phosphatase: actions and potentials
    • Okamura, Y., Y. Murata, and H. Iwasaki. 2009. Voltage-sensing phosphatase: actions and potentials. J. Physiol. 587:513-520. http:// dx.doi.org/10.1113/jphysiol.2008.163097
    • (2009) J. Physiol. , vol.587 , pp. 513-520
    • Okamura, Y.1    Murata, Y.2    Iwasaki, H.3
  • 69
    • 26144434487 scopus 로고
    • Crystal structure and pair potentials: A molecular-dynamics study
    • Parrinello, M., and A. Rahman. 1980. Crystal structure and pair potentials: A molecular-dynamics study. Phys. Rev. Lett. 45:1196- 1199. http://dx.doi.org/10.1103/PhysRevLett.45.1196
    • (1980) Phys. Rev. Lett. , vol.45
    • Parrinello, M.1    Rahman, A.2
  • 70
    • 79960621367 scopus 로고    scopus 로고
    • The crystal structure of a voltage-gated sodium channel
    • Payandeh, J., T. Scheuer, N. Zheng, and W.A. Catterall. 2011. The crystal structure of a voltage-gated sodium channel. Nature. 475:353-358. http://dx.doi.org/10.1038/nature10238
    • (2011) Nature. , vol.475 , pp. 353-358
    • Payandeh, J.1    Scheuer, T.2    Zheng, N.3    Catterall, W.A.4
  • 71
    • 84861945912 scopus 로고    scopus 로고
    • Crystal structure of a voltage-gated sodium channel in two potentially inactivated states
    • Payandeh, J., T.M. Gamal El-Din, T. Scheuer, N. Zheng, and W.A. Catterall. 2012. Crystal structure of a voltage-gated sodium channel in two potentially inactivated states. Nature. 486: 135-139.
    • (2012) Nature. , vol.486 , pp. 135-139
    • Payandeh, J.1    Gamal El-Din, T.M.2    Scheuer, T.3    Zheng, N.4    Catterall, W.A.5
  • 72
    • 42449090264 scopus 로고    scopus 로고
    • PROMALS3D: a tool for multiple protein sequence and structure alignments
    • Pei, J., B.H. Kim, and N.V. Grishin. 2008. PROMALS3D: a tool for multiple protein sequence and structure alignments. Nucleic Acids Res. 36:2295-2300. http://dx.doi.org/10.1093/nar/gkn072
    • (2008) Nucleic Acids Res. , vol.36 , pp. 2295-2300
    • Pei, J.1    Kim, B.H.2    Grishin, N.V.3
  • 73
    • 0030011088 scopus 로고    scopus 로고
    • + translocation along the single-file water chain in the gramicidin A channel
    • + translocation along the single-file water chain in the gramicidin A channel. Biophys. J. 71:19-39. http://dx.doi.org/10.1016/S0006-3495(96)79211-1
    • (1996) Biophys. J. , vol.71 , pp. 19-39
    • Pomès, R.1    Roux, B.2
  • 74
    • 0036225143 scopus 로고    scopus 로고
    • + conduction in the single-file water chain of the gramicidin channel
    • + conduction in the single-file water chain of the gramicidin channel. Biophys. J. 82:2304-2316. http://dx.doi.org/10.1016/S0006-3495 (02)75576-8
    • (2002) Biophys. J. , vol.82 , pp. 2304-2316
    • Pomès, R.1    Roux, B.2
  • 75
    • 33646358260 scopus 로고    scopus 로고
    • A voltage-gated proton-selective channel lacking the pore domain
    • Ramsey, I.S., M.M. Moran, J.A. Chong, and D.E. Clapham. 2006. A voltage-gated proton-selective channel lacking the pore domain. Nature. 440:1213-1216. http://dx.doi.org/10.1038/nature04700
    • (2006) Nature. , vol.440 , pp. 1213-1216
    • Ramsey, I.S.1    Moran, M.M.2    Chong, J.A.3    Clapham, D.E.4
  • 77
    • 84863775602 scopus 로고    scopus 로고
    • Refinement of protein structure homology models via long, all-atom molecular dynamics simulations
    • Raval, A., S. Piana, M.P. Eastwood, R.O. Dror, and D.E. Shaw. 2012. Refinement of protein structure homology models via long, all-atom molecular dynamics simulations. Proteins. 80: 2071-2079.
    • (2012) Proteins. , vol.80 , pp. 2071-2079
    • Raval, A.1    Piana, S.2    Eastwood, M.P.3    Dror, R.O.4    Shaw, D.E.5
  • 78
    • 44849140144 scopus 로고    scopus 로고
    • Bubbles, gating, and anesthetics in ion channels
    • Roth, R., D. Gillespie, W. Nonner, and R.E. Eisenberg. 2008. Bubbles, gating, and anesthetics in ion channels. Biophys. J. 94:4282-4298. http://dx.doi.org/10.1529/biophysj.107.120493
    • (2008) Biophys. J. , vol.94 , pp. 4282-4298
    • Roth, R.1    Gillespie, D.2    Nonner, W.3    Eisenberg, R.E.4
  • 80
    • 0027136282 scopus 로고
    • Comparative protein modelling by satisfaction of spatial restraints
    • Sali, A., and T.L. Blundell. 1993. Comparative protein modelling by satisfaction of spatial restraints. J. Mol. Biol. 234:779-815. http:// dx.doi.org/10.1006/jmbi.1993.1626
    • (1993) J. Mol. Biol. , vol.234 , pp. 779-815
    • Sali, A.1    Blundell, T.L.2
  • 81
    • 33846785439 scopus 로고    scopus 로고
    • How does a voltage sensor interact with a lipid bilayer? Simulations of a potassium channel domain
    • Sands, Z.A., and M.S. Sansom. 2007. How does a voltage sensor interact with a lipid bilayer? Simulations of a potassium channel domain. Structure. 15:235-244. http://dx.doi.org/10.1016/j.str.2007 .01.004
    • (2007) Structure. , vol.15 , pp. 235-244
    • Sands, Z.A.1    Sansom, M.S.2
  • 82
    • 33646229810 scopus 로고    scopus 로고
    • A voltage sensor-domain protein is a voltage-gated proton channel
    • Sasaki, M., M. Takagi, and Y. Okamura. 2006. A voltage sensor-domain protein is a voltage-gated proton channel. Science. 312:589- 592. http://dx.doi.org/10.1126/science.1122352
    • (2006) Science. , vol.312
    • Sasaki, M.1    Takagi, M.2    Okamura, Y.3
  • 83
    • 33749578940 scopus 로고    scopus 로고
    • Statistical potential for assessment and prediction of protein structures
    • Shen, M.Y., and A. Sali. 2006. Statistical potential for assessment and prediction of protein structures. Protein Sci. 15:2507-2524. http:// dx.doi.org/10.1110/ps.062416606
    • (2006) Protein Sci. , vol.15 , pp. 2507-2524
    • Shen, M.Y.1    Sali, A.2
  • 86
    • 1142274549 scopus 로고    scopus 로고
    • A proton pore in a potassium channel voltage sensor reveals a focused electric field
    • Starace, D.M., and F. Bezanilla. 2004. A proton pore in a potassium channel voltage sensor reveals a focused electric field. Nature. 427:548-553. http://dx.doi.org/10.1038/nature02270
    • (2004) Nature. , vol.427 , pp. 548-553
    • Starace, D.M.1    Bezanilla, F.2
  • 88
    • 34347211819 scopus 로고    scopus 로고
    • + channel mutation linked to hypokalemic periodic paralysis exposes a proton-selective gating pore
    • + channel mutation linked to hypokalemic periodic paralysis exposes a proton-selective gating pore. J. Gen. Physiol. 130:11-20. http://dx.doi.org/10.1085/ jgp.200709755
    • (2007) J. Gen. Physiol. , vol.130 , pp. 11-20
    • Struyk, A.F.1    Cannon, S.C.2
  • 89
    • 57749196006 scopus 로고    scopus 로고
    • Sensing voltage across lipid membranes
    • Swartz, K.J. 2008. Sensing voltage across lipid membranes. Nature. 456:891-897. http://dx.doi.org/10.1038/nature07620
    • (2008) Nature. , vol.456 , pp. 891-897
    • Swartz, K.J.1
  • 90
    • 77950488909 scopus 로고    scopus 로고
    • A gating charge transfer center in voltage sensors
    • Tao, X., A. Lee, W. Limapichat, D.A. Dougherty, and R. MacKinnon. 2010. A gating charge transfer center in voltage sensors. Science. 328:67-73. http://dx.doi.org/10.1126/science.1185954
    • (2010) Science. , vol.328 , pp. 67-73
    • Tao, X.1    Lee, A.2    Limapichat, W.3    Dougherty, D.A.4    MacKinnon, R.5
  • 91
    • 0032951553 scopus 로고    scopus 로고
    • Alamethicin helices in a bilayer and in solution: molecular dynamics simulations
    • Tieleman, D.P., M.S.P. Sansom, and H.J.C. Berendsen. 1999. Alamethicin helices in a bilayer and in solution: molecular dynamics simulations. Biophys. J. 76:40-49. http://dx.doi.org/10.1016/ S0006-3495(99)77176-6
    • (1999) Biophys. J. , vol.76 , pp. 40-49
    • Tieleman, D.P.1    Sansom, M.S.P.2    Berendsen, H.J.C.3
  • 93
    • 43449139690 scopus 로고    scopus 로고
    • The voltage-gated proton channel Hv1 has two pores, each controlled by one voltage sensor
    • Tombola, F., M.H. Ulbrich, and E.Y. Isacoff. 2008. The voltage-gated proton channel Hv1 has two pores, each controlled by one voltage sensor. Neuron. 58:546-556. http://dx.doi.org/10.1016/j.neuron .2008.03.026
    • (2008) Neuron. , vol.58 , pp. 546-556
    • Tombola, F.1    Ulbrich, M.H.2    Isacoff, E.Y.3
  • 94
    • 77449091709 scopus 로고    scopus 로고
    • The opening of the two pores of the Hv1 voltage-gated proton channel is tuned by cooperativity
    • Tombola, F., M.H. Ulbrich, S.C. Kohout, and E.Y. Isacoff. 2010. The opening of the two pores of the Hv1 voltage-gated proton channel is tuned by cooperativity. Nat. Struct. Mol. Biol. 17:44-50. http:// dx.doi.org/10.1038/nsmb.1738
    • (2010) Nat. Struct. Mol. Biol. , vol.17 , pp. 44-50
    • Tombola, F.1    Ulbrich, M.H.2    Kohout, S.C.3    Isacoff, E.Y.4
  • 95
    • 84859945797 scopus 로고    scopus 로고
    • Clinicopathological and biological significance of human voltage-gated proton channel Hv1 protein overexpression in breast cancer
    • Wang, Y., S.J. Li, X. Wu, Y. Che, and Q. Li. 2012. Clinicopathological and biological significance of human voltage-gated proton channel Hv1 protein overexpression in breast cancer. J. Biol. Chem. 287:13877-13888. http://dx.doi.org/10.1074/jbc.M112.345280
    • (2012) J. Biol. Chem. , vol.287 , pp. 13877-13888
    • Wang, Y.1    Li, S.J.2    Wu, X.3    Che, Y.4    Li, Q.5
  • 98
    • 0030021584 scopus 로고    scopus 로고
    • Molecular basis of charge movement in voltage-gated sodium channels
    • Yang, N., A.L.J. George Jr., and R. Horn. 1996. Molecular basis of charge movement in voltage-gated sodium channels. Neuron. 16:113-122. http://dx.doi.org/10.1016/S0896-6273(00)80028-8
    • (1996) Neuron. , vol.16 , pp. 113-122
    • Yang, N.1    George Jr, A.L.J.2    Horn, R.3
  • 100
    • 15244344363 scopus 로고    scopus 로고
    • The VGL-chanome: a protein superfamily specialized for electrical signaling and ionic homeostasis
    • Yu, F.H., and W.A. Catterall. 2004. The VGL-chanome: a protein superfamily specialized for electrical signaling and ionic homeostasis. Sci. STKE. 2004:re15. http://dx.doi.org/10.1126/stke .2532004re15
    • (2004) Sci. STKE. , vol.2004
    • Yu, F.H.1    Catterall, W.A.2


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