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Volumn 6, Issue , 2012, Pages 68-107

Biophysics of TRP channels

Author keywords

Allosteric gating mechanism; Chemical Sensing; Drosophila TRP and TRPL channels; Heteromultimerization; Lipid rafts; Mechanosensitivity; Phosphoinositides; Thermosensation; Translocation; TRP channels; TRP modules; Voltage dependence

Indexed keywords


EID: 84870862340     PISSN: None     EISSN: None     Source Type: Book    
DOI: 10.1016/B978-0-12-374920-8.00617-2     Document Type: Chapter
Times cited : (4)

References (401)
  • 1
    • 0014683485 scopus 로고
    • Abnormal electroretinogram from a Drosophila mutant
    • Cosens D.J., Manning A. Abnormal electroretinogram from a Drosophila mutant. Nature 1969, 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 W.L. Induction of photoreceptor voltage noise in the dark in Drosophila mutant. Nature 1975, 258:84-87.
    • (1975) Nature , vol.258 , pp. 84-87
    • Minke, B.1    Wu, C.2    Pak, W.L.3
  • 3
    • 0020086093 scopus 로고
    • Light-induced reduction in excitation efficiency in the trp mutant of Drosophila
    • Minke B. Light-induced reduction in excitation efficiency in the trp mutant of Drosophila. J. Gen. Physiol. 1982, 79:361-385.
    • (1982) J. Gen. Physiol. , vol.79 , pp. 361-385
    • Minke, B.1
  • 4
    • 0024642547 scopus 로고
    • Molecular characterization of the Drosophila trp locus: a putative integral membrane protein required for phototransduction
    • Montell C., Rubin G.M. Molecular characterization of the Drosophila trp locus: a putative integral membrane protein required for phototransduction. Neuron 1989, 2:1313-1323.
    • (1989) Neuron , vol.2 , pp. 1313-1323
    • Montell, C.1    Rubin, G.M.2
  • 5
    • 0026583241 scopus 로고
    • 2+ channel in Drosophila photoreceptors
    • 2+ channel in Drosophila photoreceptors. Neuron 1992, 8:643-651.
    • (1992) Neuron , vol.8 , pp. 643-651
    • Hardie, R.C.1    Minke, B.2
  • 6
    • 0028284467 scopus 로고
    • The light response of Drosophila photoreceptors is accompanied by an increase in cellular calcium: effects of specific mutations
    • Peretz A., Suss-Toby E., Rom-Glas A., Arnon A., Payne R., Minke B. The light response of Drosophila photoreceptors is accompanied by an increase in cellular calcium: effects of specific mutations. Neuron 1994, 12:1257-1267.
    • (1994) Neuron , vol.12 , pp. 1257-1267
    • Peretz, A.1    Suss-Toby, E.2    Rom-Glas, A.3    Arnon, A.4    Payne, R.5    Minke, B.6
  • 10
    • 0024151761 scopus 로고
    • Inositol lipid cascade of vision studied in mutant flies
    • Selinger Z., Minke B. Inositol lipid cascade of vision studied in mutant flies. Cold Spring Harb. Symp. Quant. Biol. 1988, 53(Pt 1):333-341.
    • (1988) Cold Spring Harb. Symp. Quant. Biol. , vol.53 , Issue.PT 1 , pp. 333-341
    • Selinger, Z.1    Minke, B.2
  • 11
    • 0026508664 scopus 로고
    • Identification of a Drosophila gene encoding a calmodulin-binding protein with homology to the trp phototransduction gene
    • Phillips A.M., Bull A., Kelly L.E. Identification of a Drosophila gene encoding a calmodulin-binding protein with homology to the trp phototransduction gene. Neuron 1992, 8:631-642.
    • (1992) Neuron , vol.8 , pp. 631-642
    • Phillips, A.M.1    Bull, A.2    Kelly, L.E.3
  • 14
    • 0028800096 scopus 로고
    • Molecular cloning of a widely expressed human homologue for the Drosophila trp gene
    • Zhu X., Chu P.B., Peyton M., Birnbaumer L. Molecular cloning of a widely expressed human homologue for the Drosophila trp gene. FEBS Lett. 1995, 373:193-198.
    • (1995) FEBS Lett. , vol.373 , pp. 193-198
    • Zhu, X.1    Chu, P.B.2    Peyton, M.3    Birnbaumer, L.4
  • 16
    • 0036080482 scopus 로고    scopus 로고
    • TRP channel proteins and signal transduction
    • Minke B., Cook B. TRP channel proteins and signal transduction. Physiol. Rev. 2002, 82:429-472.
    • (2002) Physiol. Rev. , vol.82 , pp. 429-472
    • Minke, B.1    Cook, B.2
  • 17
    • 0037040395 scopus 로고    scopus 로고
    • The TRP channels, a remarkably functional family
    • Montell C., Birnbaumer L., Flockerzi V. The TRP channels, a remarkably functional family. Cell 2002, 108:595-598.
    • (2002) Cell , vol.108 , pp. 595-598
    • Montell, C.1    Birnbaumer, L.2    Flockerzi, V.3
  • 18
    • 0347504835 scopus 로고    scopus 로고
    • TRP channels as cellular sensors
    • Clapham D.E. TRP channels as cellular sensors. Nature 2003, 426:517-524.
    • (2003) Nature , vol.426 , pp. 517-524
    • Clapham, D.E.1
  • 19
    • 0041520528 scopus 로고    scopus 로고
    • New TRP channels in hearing and mechanosensation
    • Corey D.P. New TRP channels in hearing and mechanosensation. Neuron 2003, 39:585-588.
    • (2003) Neuron , vol.39 , pp. 585-588
    • Corey, D.P.1
  • 20
    • 3242728834 scopus 로고    scopus 로고
    • Polycystins: from mechanosensation to gene regulation
    • Delmas P. Polycystins: from mechanosensation to gene regulation. Cell 2004, 118:145-148.
    • (2004) Cell , vol.118 , pp. 145-148
    • Delmas, P.1
  • 22
    • 26444591482 scopus 로고    scopus 로고
    • TRP channels: a TR(I)P through a world of multifunctional cation channels
    • Nilius B., Voets T. TRP channels: a TR(I)P through a world of multifunctional cation channels. Pflugers Arch. 2005, 451:1-10.
    • (2005) Pflugers Arch. , vol.451 , pp. 1-10
    • Nilius, B.1    Voets, T.2
  • 23
    • 0037710542 scopus 로고    scopus 로고
    • NompC TRP channel required for vertebrate sensory hair cell mechanotransduction
    • Sidi S., Friedrich R.W., Nicolson T. NompC TRP channel required for vertebrate sensory hair cell mechanotransduction. Science 2003, 301:96-99.
    • (2003) Science , vol.301 , pp. 96-99
    • Sidi, S.1    Friedrich, R.W.2    Nicolson, T.3
  • 24
    • 0034708452 scopus 로고    scopus 로고
    • A Drosophila mechanosensory transduction channel
    • Walker R.G., Willingham A.T., ZGBRer C.S. A Drosophila mechanosensory transduction channel. Science 2000, 287:2229-2234.
    • (2000) Science , vol.287 , pp. 2229-2234
    • Walker, R.G.1    Willingham, A.T.2    ZGBRer, C.S.3
  • 26
    • 0141755156 scopus 로고    scopus 로고
    • Formation of novel TRPC channels by complex subunit interactions in embryonic brain
    • Strubing C., Krapivinsky G., Krapivinsky L., Clapham D.E. Formation of novel TRPC channels by complex subunit interactions in embryonic brain. J. Biol. Chem. 2003, 278:39014-39019.
    • (2003) J. Biol. Chem. , vol.278 , pp. 39014-39019
    • Strubing, C.1    Krapivinsky, G.2    Krapivinsky, L.3    Clapham, D.E.4
  • 27
    • 0035051978 scopus 로고    scopus 로고
    • TRPC1 and TRPC5 form a novel cation channel in mammalian brain
    • Strubing C., Krapivinsky G., Krapivinsky L., Clapham D.E. TRPC1 and TRPC5 form a novel cation channel in mammalian brain. Neuron 2001, 29:645-655.
    • (2001) Neuron , vol.29 , pp. 645-655
    • Strubing, C.1    Krapivinsky, G.2    Krapivinsky, L.3    Clapham, D.E.4
  • 29
    • 37549029225 scopus 로고    scopus 로고
    • The role of the N terminus and transmembrane domain of TRPM8 in channel localization and tetramerization
    • Phelps C.B., Gaudet R. The role of the N terminus and transmembrane domain of TRPM8 in channel localization and tetramerization. J. Biol. Chem. 2007, 282:36474-36480.
    • (2007) J. Biol. Chem. , vol.282 , pp. 36474-36480
    • Phelps, C.B.1    Gaudet, R.2
  • 31
    • 29844451971 scopus 로고    scopus 로고
    • International Union of Pharmacology. XLIX. Nomenclature and structure-function relationships of transient receptor potential channels
    • Clapham D.E., Julius D., Montell C., Schultz G. International Union of Pharmacology. XLIX. Nomenclature and structure-function relationships of transient receptor potential channels. Pharmacol. Rev. 2005, 57:427-450.
    • (2005) Pharmacol. Rev. , vol.57 , pp. 427-450
    • Clapham, D.E.1    Julius, D.2    Montell, C.3    Schultz, G.4
  • 32
  • 33
    • 0032792551 scopus 로고    scopus 로고
    • The ankyrin repeat: a diversity of interactions on a common structural framework
    • Sedgwick S.G., Smerdon S.J. The ankyrin repeat: a diversity of interactions on a common structural framework. Trends Biochem. Sci. 1999, 24:311-316.
    • (1999) Trends Biochem. Sci. , vol.24 , pp. 311-316
    • Sedgwick, S.G.1    Smerdon, S.J.2
  • 34
    • 33748748066 scopus 로고    scopus 로고
    • Structure of the N-terminal ankyrin repeat domain of the TRPV2 ion channel
    • Jin X., Touhey J., Gaudet R. Structure of the N-terminal ankyrin repeat domain of the TRPV2 ion channel. J. Biol. Chem. 2006, 281:25006-25010.
    • (2006) J. Biol. Chem. , vol.281 , pp. 25006-25010
    • Jin, X.1    Touhey, J.2    Gaudet, R.3
  • 38
    • 1842535278 scopus 로고    scopus 로고
    • Hypothesis: a helix of ankyrin repeats of the NOMPC-TRP ion channel is the gating spring of mechanoreceptors
    • Howard J., Bechstedt S. Hypothesis: a helix of ankyrin repeats of the NOMPC-TRP ion channel is the gating spring of mechanoreceptors. Curr. Biol. 2004, 14:R224-R226.
    • (2004) Curr. Biol. , vol.14
    • Howard, J.1    Bechstedt, S.2
  • 41
    • 0001105482 scopus 로고
    • Is alpha-keratin a coiled coil?
    • Crick F.H. Is alpha-keratin a coiled coil?. Nature 1952, 170:882-883.
    • (1952) Nature , vol.170 , pp. 882-883
    • Crick, F.H.1
  • 42
    • 0027756896 scopus 로고
    • A switch between two-, three-, and four-stranded coiled coils in GCN4 leucine zipper mutants
    • Harbury P.B., Zhang T., Kim P.S., Alber T. A switch between two-, three-, and four-stranded coiled coils in GCN4 leucine zipper mutants. Science 1993, 262:1401-1407.
    • (1993) Science , vol.262 , pp. 1401-1407
    • Harbury, P.B.1    Zhang, T.2    Kim, P.S.3    Alber, T.4
  • 43
    • 0029911261 scopus 로고    scopus 로고
    • The crystal structure of a five-stranded coiled coil in COMP: a prototype ion channel?
    • Malashkevich V.N., Kammerer R.A., Efimov V.P., Schulthess T., Engel J. The crystal structure of a five-stranded coiled coil in COMP: a prototype ion channel?. Science 1996, 274:761-765.
    • (1996) Science , vol.274 , pp. 761-765
    • Malashkevich, V.N.1    Kammerer, R.A.2    Efimov, V.P.3    Schulthess, T.4    Engel, J.5
  • 44
    • 24644460439 scopus 로고    scopus 로고
    • 2+-binding proteins in the functional regulation of TRP channels
    • 2+-binding proteins in the functional regulation of TRP channels. Pflugers Arch. 2005, 451:105-115.
    • (2005) Pflugers Arch. , vol.451 , pp. 105-115
    • Zhu, M.X.1
  • 45
    • 0033623942 scopus 로고    scopus 로고
    • TRPγ, a Drosophila TRP-related subunit, forms a regulated cation channel with TRPL
    • Xu X.Z., Chien F., Butler A., Salkoff L., Montell C. TRPγ, a Drosophila TRP-related subunit, forms a regulated cation channel with TRPL. Neuron 2000, 26:647-657.
    • (2000) Neuron , vol.26 , pp. 647-657
    • Xu, X.Z.1    Chien, F.2    Butler, A.3    Salkoff, L.4    Montell, C.5
  • 46
    • 0031587878 scopus 로고    scopus 로고
    • Coassembly of TRP and TRPL produces a distinct store-operated conductance
    • Xu X.Z.S., Li H.S., Guggino W.B., Montell C. Coassembly of TRP and TRPL produces a distinct store-operated conductance. Cell 1997, 89:1155-1164.
    • (1997) Cell , vol.89 , pp. 1155-1164
    • Xu, X.Z.S.1    Li, H.S.2    Guggino, W.B.3    Montell, C.4
  • 47
    • 0030841932 scopus 로고    scopus 로고
    • 301 mutant and TRPL cation channels expressed in a stably transfected Drosophila cell line
    • 301 mutant and TRPL cation channels expressed in a stably transfected Drosophila cell line. Cell Calcium 1997, 21:431-440.
    • (1997) Cell Calcium , vol.21 , pp. 431-440
    • Hardie, R.C.1    Reuss, H.2    Lansdell, S.J.3    Millar, N.S.4
  • 48
    • 0031036405 scopus 로고    scopus 로고
    • Properties of single Drosophila Trpl channels expressed in Sf9 insect cells
    • Kunze D.L., Sinkins W.G., Vaca L., Schilling W.P. Properties of single Drosophila Trpl channels expressed in Sf9 insect cells. Am. J. Physiol. 1997, 272:C27-C34.
    • (1997) Am. J. Physiol. , vol.272
    • Kunze, D.L.1    Sinkins, W.G.2    Vaca, L.3    Schilling, W.P.4
  • 49
    • 33845939887 scopus 로고    scopus 로고
    • 2+ underlies the voltage dependence of Drosophila TRPL channel
    • 2+ underlies the voltage dependence of Drosophila TRPL channel. J. Gen. Physiol. 2007, 129:17-28.
    • (2007) J. Gen. Physiol. , vol.129 , pp. 17-28
    • Parnas, M.1    Katz, B.2    Minke, B.3
  • 51
    • 0028294559 scopus 로고
    • Spontaneous activation of light-sensitive channels in Drosophila photoreceptors
    • Hardie R.C., Minke B. Spontaneous activation of light-sensitive channels in Drosophila photoreceptors. J. Gen. Physiol. 1994, 103:389-407.
    • (1994) J. Gen. Physiol. , vol.103 , pp. 389-407
    • Hardie, R.C.1    Minke, B.2
  • 52
    • 33645997388 scopus 로고    scopus 로고
    • Insights on TRP channels from in vivo studies in Drosophila
    • Minke B., Parnas M. Insights on TRP channels from in vivo studies in Drosophila. Annu. Rev. Physiol. 2006, 68:649-684.
    • (2006) Annu. Rev. Physiol. , vol.68 , pp. 649-684
    • Minke, B.1    Parnas, M.2
  • 53
    • 0031459042 scopus 로고    scopus 로고
    • In vivo analysis of the Drosophila light-sensitive channels, TRP and TRPL
    • Reuss H., Mojet M.H., Chyb S., Hardie R.C. In vivo analysis of the Drosophila light-sensitive channels, TRP and TRPL. Neuron 1997, 19:1249-1259.
    • (1997) Neuron , vol.19 , pp. 1249-1259
    • Reuss, H.1    Mojet, M.H.2    Chyb, S.3    Hardie, R.C.4
  • 54
    • 0037073749 scopus 로고    scopus 로고
    • Selective association of TRPC channel subunits in rat brain synaptosomes
    • Goel M., Sinkins W.G., Schilling W.P. Selective association of TRPC channel subunits in rat brain synaptosomes. J. Biol. Chem. 2002, 277:48303-48310.
    • (2002) J. Biol. Chem. , vol.277 , pp. 48303-48310
    • Goel, M.1    Sinkins, W.G.2    Schilling, W.P.3
  • 55
    • 0037188517 scopus 로고    scopus 로고
    • Subunit composition of mammalian transient receptor potential channels in living cells
    • Hofmann T., Schaefer M., Schultz G., Gudermann T. Subunit composition of mammalian transient receptor potential channels in living cells. Proc. Natl. Acad. Sci. USA 2002, 99:7461-7466.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 7461-7466
    • Hofmann, T.1    Schaefer, M.2    Schultz, G.3    Gudermann, T.4
  • 57
    • 24144490391 scopus 로고    scopus 로고
    • Extensive co-localization and heteromultimer formation of the vanilloid receptor-like protein TRPV2 and the capsaicin receptor TRPV1 in the adult rat cerebral cortex
    • Liapi A., Wood J.N. Extensive co-localization and heteromultimer formation of the vanilloid receptor-like protein TRPV2 and the capsaicin receptor TRPV1 in the adult rat cerebral cortex. Eur. J. Neurosci. 2005, 22:825-834.
    • (2005) Eur. J. Neurosci. , vol.22 , pp. 825-834
    • Liapi, A.1    Wood, J.N.2
  • 60
    • 26444598978 scopus 로고    scopus 로고
    • Subcellular localization and trafficking of polycystins
    • Kottgen M., Walz G. Subcellular localization and trafficking of polycystins. Pflugers Arch. 2005, 451:286-293.
    • (2005) Pflugers Arch. , vol.451 , pp. 286-293
    • Kottgen, M.1    Walz, G.2
  • 62
    • 56649092997 scopus 로고    scopus 로고
    • Molecular mechanisms of TRPV4-mediated neural signaling
    • Liedtke W. Molecular mechanisms of TRPV4-mediated neural signaling. Ann. N. Y. Acad. Sci. 2008, 1144:42-52.
    • (2008) Ann. N. Y. Acad. Sci. , vol.1144 , pp. 42-52
    • Liedtke, W.1
  • 64
    • 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 A.C., Kuriyan J. Crystal structure of the atypical protein kinase domain of a TRP channel with phosphotransferase activity. Mol. Cell 2001, 7:1047-1057.
    • (2001) Mol. Cell , vol.7 , pp. 1047-1057
    • Yamaguchi, H.1    Matsushita, M.2    Nairn, A.C.3    Kuriyan, J.4
  • 65
    • 0037415755 scopus 로고    scopus 로고
    • C-terminal domains implicated in the functional surface expression of potassium channels
    • Jenke M., Sanchez A., Monje F., Stuhmer W., Weseloh R.M., Pardo L.A. C-terminal domains implicated in the functional surface expression of potassium channels. EMBO J. 2003, 22:395-403.
    • (2003) EMBO J. , vol.22 , pp. 395-403
    • Jenke, M.1    Sanchez, A.2    Monje, F.3    Stuhmer, W.4    Weseloh, R.M.5    Pardo, L.A.6
  • 66
    • 33644875032 scopus 로고    scopus 로고
    • The TRP superfamily of cation channels
    • Montell C. The TRP superfamily of cation channels. Sci. STKE. 2005, 2005:re3.
    • (2005) Sci. STKE. , vol.2005
    • Montell, C.1
  • 67
    • 17444424974 scopus 로고    scopus 로고
    • The structure of alpha-helical coiled coils
    • Lupas A.N., Gruber M. The structure of alpha-helical coiled coils. Adv. Protein Chem. 2005, 70:37-78.
    • (2005) Adv. Protein Chem. , vol.70 , pp. 37-78
    • Lupas, A.N.1    Gruber, M.2
  • 68
    • 17444433002 scopus 로고    scopus 로고
    • The design of coiled-coil structures and assemblies
    • Woolfson D.N. The design of coiled-coil structures and assemblies. Adv. Protein Chem. 2005, 70:79-112.
    • (2005) Adv. Protein Chem. , vol.70 , pp. 79-112
    • Woolfson, D.N.1
  • 71
    • 33745877323 scopus 로고    scopus 로고
    • Coiled coils direct assembly of a cold-activated TRP channel
    • Tsuruda P.R., Julius D., Minor D.L. Coiled coils direct assembly of a cold-activated TRP channel. Neuron 2006, 51:201-212.
    • (2006) Neuron , vol.51 , pp. 201-212
    • Tsuruda, P.R.1    Julius, D.2    Minor, D.L.3
  • 74
    • 23244441222 scopus 로고    scopus 로고
    • Voltage sensor of Kv1.2: structural basis of electromechanical coupling
    • Long S.B., Campbell E.B., MacKinnon R. Voltage sensor of Kv1.2: structural basis of electromechanical coupling. Science 2005, 309:903-908.
    • (2005) Science , vol.309 , pp. 903-908
    • Long, S.B.1    Campbell, E.B.2    MacKinnon, R.3
  • 75
    • 0035931906 scopus 로고    scopus 로고
    • The voltage-sensitive sodium channel is a bell-shaped molecule with several cavities
    • Sato C., Ueno Y., Asai K., Takahashi K., Sato M., Engel A., Fujiyoshi Y. The voltage-sensitive sodium channel is a bell-shaped molecule with several cavities. Nature 2001, 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
  • 76
    • 48549095714 scopus 로고    scopus 로고
    • TRP channels entering the structural era
    • Gaudet R. TRP channels entering the structural era. J. Physiol. 2008, 586:3565-3575.
    • (2008) J. Physiol. , vol.586 , pp. 3565-3575
    • Gaudet, R.1
  • 78
    • 33644969008 scopus 로고    scopus 로고
    • Human TRPV4 channel splice variants revealed a key role of ankyrin domains in multimerization and trafficking
    • Arniges M., Fernandez-Fernandez J.M., Albrecht N., Schaefer M., Valverde M.A. Human TRPV4 channel splice variants revealed a key role of ankyrin domains in multimerization and trafficking. J. Biol. Chem. 2006, 281:1580-1586.
    • (2006) J. Biol. Chem. , vol.281 , pp. 1580-1586
    • Arniges, M.1    Fernandez-Fernandez, J.M.2    Albrecht, N.3    Schaefer, M.4    Valverde, M.A.5
  • 83
    • 21744438625 scopus 로고    scopus 로고
    • Phosphoinositide phosphatase activity coupled to an intrinsic voltage sensor
    • Murata Y., Iwasaki H., Sasaki M., Inaba K., Okamura Y. Phosphoinositide phosphatase activity coupled to an intrinsic voltage sensor. Nature 2005, 435:1239-1243.
    • (2005) Nature , vol.435 , pp. 1239-1243
    • Murata, Y.1    Iwasaki, H.2    Sasaki, M.3    Inaba, K.4    Okamura, Y.5
  • 84
    • 33646229810 scopus 로고    scopus 로고
    • A voltage sensor-domain protein is a voltage-gated proton channel
    • Sasaki M., Takagi M., Okamura Y. A voltage sensor-domain protein is a voltage-gated proton channel. Science 2006, 312:589-592.
    • (2006) Science , vol.312 , pp. 589-592
    • Sasaki, M.1    Takagi, M.2    Okamura, Y.3
  • 85
    • 0036183319 scopus 로고    scopus 로고
    • Molecular basis for species-specific sensitivity to "hot" chili peppers
    • Jordt S.E., Julius D. Molecular basis for species-specific sensitivity to "hot" chili peppers. Cell 2002, 108:421-430.
    • (2002) Cell , vol.108 , pp. 421-430
    • Jordt, S.E.1    Julius, D.2
  • 86
    • 0033788731 scopus 로고    scopus 로고
    • Low-threshold heat response antagonized by capsazepine in chick sensory neurons, which are capsaicin-insensitive
    • Marin-Burgin A., Reppenhagen S., Klusch A., Wendland J.R., Petersen M. Low-threshold heat response antagonized by capsazepine in chick sensory neurons, which are capsaicin-insensitive. Eur. J. Neurosci. 2000, 12:3560-3566.
    • (2000) Eur. J. Neurosci. , vol.12 , pp. 3560-3566
    • Marin-Burgin, A.1    Reppenhagen, S.2    Klusch, A.3    Wendland, J.R.4    Petersen, M.5
  • 90
    • 0034610391 scopus 로고    scopus 로고
    • The activation mechanism of rat vanilloid receptor 1 by capsaicin involves the pore domain and differs from the activation by either acid or heat
    • Welch J.M., Simon S.A., Reinhart P.H. The activation mechanism of rat vanilloid receptor 1 by capsaicin involves the pore domain and differs from the activation by either acid or heat. Proc. Natl. Acad. Sci. USA 2000, 97:13889-13894.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 13889-13894
    • Welch, J.M.1    Simon, S.A.2    Reinhart, P.H.3
  • 97
    • 0141831003 scopus 로고    scopus 로고
    • Structural basis for modulation and agonist specificity of HCN pacemaker channels
    • Zagotta W.N., Olivier N.B., Black K.D., Young E.C., Olson R., Gouaux E. Structural basis for modulation and agonist specificity of HCN pacemaker channels. Nature 2003, 425:200-205.
    • (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
  • 99
    • 0037799198 scopus 로고    scopus 로고
    • 2 binding site as a determinant of capsaicin receptor sensitivity
    • 2 binding site as a determinant of capsaicin receptor sensitivity. Science 2003, 300:1284-1288.
    • (2003) Science , vol.300 , pp. 1284-1288
    • Prescott, E.D.1    Julius, D.2
  • 100
    • 33646899582 scopus 로고    scopus 로고
    • A hot-sensing cold receptor: C-terminal domain determines thermosensation in transient receptor potential channels
    • Brauchi S., Orta G., Salazar M., Rosenmann E., Latorre R. A hot-sensing cold receptor: C-terminal domain determines thermosensation in transient receptor potential channels. J. Neurosci. 2006, 26:4835-4840.
    • (2006) J. Neurosci. , vol.26 , pp. 4835-4840
    • Brauchi, S.1    Orta, G.2    Salazar, M.3    Rosenmann, E.4    Latorre, R.5
  • 102
    • 33244472133 scopus 로고    scopus 로고
    • Phosphoinositide-derived messengers in endocrine signaling
    • Balla T. Phosphoinositide-derived messengers in endocrine signaling. J. Endocrinol. 2006, 188:135-153.
    • (2006) J. Endocrinol. , vol.188 , pp. 135-153
    • Balla, T.1
  • 103
    • 0038605062 scopus 로고    scopus 로고
    • The M2 muscarinic G-protein-coupled receptor is voltage-sensitive
    • Ben-Chaim Y., Tour O., Dascal N., Parnas I., Parnas H. The M2 muscarinic G-protein-coupled receptor is voltage-sensitive. J. Biol. Chem. 2003, 278:22482-22491.
    • (2003) J. Biol. Chem. , vol.278 , pp. 22482-22491
    • Ben-Chaim, Y.1    Tour, O.2    Dascal, N.3    Parnas, I.4    Parnas, H.5
  • 104
    • 0034017867 scopus 로고    scopus 로고
    • The voltage sensor in voltage-dependent ion channels
    • Bezanilla F. The voltage sensor in voltage-dependent ion channels. Physiol. Rev. 2000, 80:555-592.
    • (2000) Physiol. Rev. , vol.80 , pp. 555-592
    • Bezanilla, F.1
  • 105
    • 0033576580 scopus 로고    scopus 로고
    • Atomic scale movement of the voltage-sensing region in a potassium channel measured via spectroscopy
    • Cha A., Snyder G.E., Selvin P.R., Bezanilla F. Atomic scale movement of the voltage-sensing region in a potassium channel measured via spectroscopy. Nature 1999, 402:809-813.
    • (1999) Nature , vol.402 , pp. 809-813
    • Cha, A.1    Snyder, G.E.2    Selvin, P.R.3    Bezanilla, F.4
  • 106
    • 0029084477 scopus 로고
    • Evidence for voltage-dependent S4 movement in sodium channels
    • Yang N., Horn R. Evidence for voltage-dependent S4 movement in sodium channels. Neuron 1995, 15:213-218.
    • (1995) Neuron , vol.15 , pp. 213-218
    • Yang, N.1    Horn, R.2
  • 107
    • 3142682246 scopus 로고    scopus 로고
    • The screw-helical voltage gating of ion channels
    • Keynes R.D., Elinder F. The screw-helical voltage gating of ion channels. Proc. Biol. Sci. 1999, 266:843-852.
    • (1999) Proc. Biol. Sci. , vol.266 , pp. 843-852
    • Keynes, R.D.1    Elinder, F.2
  • 108
    • 9944226711 scopus 로고    scopus 로고
    • Towards a structural view of gating in potassium channels
    • Swartz K.J. Towards a structural view of gating in potassium channels. Nat. Rev. Neurosci. 2004, 5:905-916.
    • (2004) Nat. Rev. Neurosci. , vol.5 , pp. 905-916
    • Swartz, K.J.1
  • 109
    • 0015970876 scopus 로고
    • Gating currents of the sodium channels: three ways to block them
    • Bezanilla F., Armstrong C.M. Gating currents of the sodium channels: three ways to block them. Science 1974, 183:753-754.
    • (1974) Science , vol.183 , pp. 753-754
    • Bezanilla, F.1    Armstrong, C.M.2
  • 110
    • 0015868742 scopus 로고
    • Currents related to movement of the gating particles of the sodium channels
    • Armstrong C.M., Bezanilla F. Currents related to movement of the gating particles of the sodium channels. Nature 1973, 242:459-461.
    • (1973) Nature , vol.242 , pp. 459-461
    • Armstrong, C.M.1    Bezanilla, F.2
  • 112
    • 0029998701 scopus 로고    scopus 로고
    • Structure and function of cyclic nucleotide-gated channels
    • Zagotta W.N., Siegelbaum S.A. Structure and function of cyclic nucleotide-gated channels. Annu. Rev. Neurosci. 1996, 19:235-263.
    • (1996) Annu. Rev. Neurosci. , vol.19 , pp. 235-263
    • Zagotta, W.N.1    Siegelbaum, S.A.2
  • 113
    • 0036301043 scopus 로고    scopus 로고
    • Cyclic nucleotide-gated ion channels
    • Kaupp U.B., Seifert R. Cyclic nucleotide-gated ion channels. Physiol. Rev. 2002, 82:769-824.
    • (2002) Physiol. Rev. , vol.82 , pp. 769-824
    • Kaupp, U.B.1    Seifert, R.2
  • 114
    • 16544376850 scopus 로고    scopus 로고
    • Role of distinct NMDA receptor subtypes at central synapses
    • 2004, re16.
    • Cull-Candy, S. G.; Leszkiewicz, D. N. Role of distinct NMDA receptor subtypes at central synapses. Sci. STKE. 2004, 2004, re16.
    • (2004) Sci. STKE.
    • Cull-Candy, S.G.1    Leszkiewicz, D.N.2
  • 116
    • 0023929233 scopus 로고
    • The role of divalent cations in the N-methyl-Daspartate responses of mouse central neurones in culture
    • Ascher P., Nowak L. The role of divalent cations in the N-methyl-Daspartate responses of mouse central neurones in culture. J. Physiol. 1988, 399:247-266.
    • (1988) J. Physiol. , vol.399 , pp. 247-266
    • Ascher, P.1    Nowak, L.2
  • 117
    • 0025249158 scopus 로고
    • 2+ of N-methyl-D-aspartate-activated channels
    • 2+ of N-methyl-D-aspartate-activated channels. Biophys. J. 1990, 57:1085-1090.
    • (1990) Biophys. J. , vol.57 , pp. 1085-1090
    • Johnson, J.W.1    Ascher, P.2
  • 119
    • 4043077669 scopus 로고    scopus 로고
    • The principle of temperature-dependent gating in cold- and heat-sensitive TRP channels
    • Voets T., Droogmans G., Wissenbach U., Janssens A., Flockerzi V., Nilius B. The principle of temperature-dependent gating in cold- and heat-sensitive TRP channels. Nature 2004, 430:748-754.
    • (2004) Nature , vol.430 , pp. 748-754
    • Voets, T.1    Droogmans, G.2    Wissenbach, U.3    Janssens, A.4    Flockerzi, V.5    Nilius, B.6
  • 120
    • 33847050898 scopus 로고    scopus 로고
    • TRPM8 voltage sensor mutants reveal a mechanism for integrating thermal and chemical stimuli
    • Voets T., Owsianik G., Janssens A., Talavera K., Nilius B. TRPM8 voltage sensor mutants reveal a mechanism for integrating thermal and chemical stimuli. Nat. Chem. Biol. 2007, 3:174-182.
    • (2007) Nat. Chem. Biol. , vol.3 , pp. 174-182
    • Voets, T.1    Owsianik, G.2    Janssens, A.3    Talavera, K.4    Nilius, B.5
  • 121
    • 34547953765 scopus 로고    scopus 로고
    • ThermoTRP channels as modular proteins with allosteric gating
    • Latorre R., Brauchi S., Orta G., Zaelzer C., Vargas G. ThermoTRP channels as modular proteins with allosteric gating. Cell Calcium 2007, 42:427-438.
    • (2007) Cell Calcium , vol.42 , pp. 427-438
    • Latorre, R.1    Brauchi, S.2    Orta, G.3    Zaelzer, C.4    Vargas, G.5
  • 124
    • 44449102835 scopus 로고    scopus 로고
    • Calcium plays a central role in the sensitization of TRPV3 channel to repetitive stimulations
    • Xiao R., Tang J., Wang C., Colton C.K., Tian J., Zhu M.X. Calcium plays a central role in the sensitization of TRPV3 channel to repetitive stimulations. J. Biol. Chem. 2008, 283:6162-6174.
    • (2008) J. Biol. Chem. , vol.283 , pp. 6162-6174
    • Xiao, R.1    Tang, J.2    Wang, C.3    Colton, C.K.4    Tian, J.5    Zhu, M.X.6
  • 125
    • 13944262457 scopus 로고    scopus 로고
    • 2+ block and regulates inward current amplitude of a transient receptor potential channel
    • 2+ block and regulates inward current amplitude of a transient receptor potential channel. J. Neurosci. 2005, 25:1234-1239.
    • (2005) J. Neurosci. , vol.25 , pp. 1234-1239
    • Obukhov, A.G.1    Nowycky, M.C.2
  • 126
    • 10644283084 scopus 로고    scopus 로고
    • Multiple regulation by calcium of murine homologues of transient receptor potential proteins TRPC6 and TRPC7 expressed in HEK293 cells
    • Shi J., Mori E., Mori Y., Mori M., Li J., Ito Y., Inoue R. Multiple regulation by calcium of murine homologues of transient receptor potential proteins TRPC6 and TRPC7 expressed in HEK293 cells. J. Physiol. 2004, 561:415-432.
    • (2004) J. Physiol. , vol.561 , pp. 415-432
    • Shi, J.1    Mori, E.2    Mori, Y.3    Mori, M.4    Li, J.5    Ito, Y.6    Inoue, R.7
  • 128
    • 20544451564 scopus 로고    scopus 로고
    • Biophysical properties of menthol-activated cold receptor TRPM8 channels
    • Hui K., Guo Y., Feng Z.P. Biophysical properties of menthol-activated cold receptor TRPM8 channels. Biochem. Biophys. Res. Commun. 2005, 333:374-382.
    • (2005) Biochem. Biophys. Res. Commun. , vol.333 , pp. 374-382
    • Hui, K.1    Guo, Y.2    Feng, Z.P.3
  • 130
    • 0029564429 scopus 로고
    • Magnesium-dependent block of the lightactivated and trp- dependent conductance in Drosophila photoreceptors
    • Hardie R.C., Mojet M.H. Magnesium-dependent block of the lightactivated and trp- dependent conductance in Drosophila photoreceptors. J. Neurosci. 1995, 74:2590-2599.
    • (1995) J. Neurosci. , vol.74 , pp. 2590-2599
    • Hardie, R.C.1    Mojet, M.H.2
  • 131
    • 21844468257 scopus 로고    scopus 로고
    • Mechanisms of light adaptation in Drosophila photoreceptors
    • Gu Y., Oberwinkler J., Postma M., Hardie R.C. Mechanisms of light adaptation in Drosophila photoreceptors. Curr. Biol. 2005, 15:1228-1234.
    • (2005) Curr. Biol. , vol.15 , pp. 1228-1234
    • Gu, Y.1    Oberwinkler, J.2    Postma, M.3    Hardie, R.C.4
  • 133
    • 0030665081 scopus 로고    scopus 로고
    • Calmodulin regulation of Drosophila light-activated channels and receptor function mediates termination of the light response
    • Scott K., Sun Y., Beckingham K., ZGBRer C.S. Calmodulin regulation of Drosophila light-activated channels and receptor function mediates termination of the light response. in vivo. Cell 1997, 91:375-383.
    • (1997) in vivo. Cell , vol.91 , pp. 375-383
    • Scott, K.1    Sun, Y.2    Beckingham, K.3    ZGBRer, C.S.4
  • 134
    • 0021185585 scopus 로고
    • Activation of calmodulin by various metal cations as a function of ionic radius
    • Chao S.H., Suzuki Y., Zysk J.R., Cheung W.Y. Activation of calmodulin by various metal cations as a function of ionic radius. Mol. Pharmacol. 1984, 26:75-82.
    • (1984) Mol. Pharmacol. , vol.26 , pp. 75-82
    • Chao, S.H.1    Suzuki, Y.2    Zysk, J.R.3    Cheung, W.Y.4
  • 136
    • 0033521589 scopus 로고    scopus 로고
    • 2+-binding site in the pore of cyclic nucleotidegated channels: S5/S6 segments control affinity of intrapore glutamates
    • 2+-binding site in the pore of cyclic nucleotidegated channels: S5/S6 segments control affinity of intrapore glutamates. EMBO J. 1999, 18:119-130.
    • (1999) EMBO J. , vol.18 , pp. 119-130
    • Seifert, R.1    Eismann, E.2    Ludwig, J.3    Baumann, A.4    Kaupp, U.B.5
  • 137
    • 0345119039 scopus 로고    scopus 로고
    • A diacylglycerol-gated cation channel in vomeronasal neuron dendrites is impaired in TRPC2 mutant mice: mechanism of pheromone transduction
    • Lucas P., GBRhanov K., Leinders-Zufall T., Zufall F. A diacylglycerol-gated cation channel in vomeronasal neuron dendrites is impaired in TRPC2 mutant mice: mechanism of pheromone transduction. Neuron 2003, 40:551-561.
    • (2003) Neuron , vol.40 , pp. 551-561
    • Lucas, P.1    GBRhanov, K.2    Leinders-Zufall, T.3    Zufall, F.4
  • 138
    • 33750802650 scopus 로고    scopus 로고
    • A common mechanism underlies stretch activation and receptor activation of TRPC6 channels
    • Spassova M.A., Hewavitharana T., Xu W., Soboloff J., Gill D.L. A common mechanism underlies stretch activation and receptor activation of TRPC6 channels. Proc. Natl. Acad. Sci. USA 2006, 103:16586-16591.
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , pp. 16586-16591
    • Spassova, M.A.1    Hewavitharana, T.2    Xu, W.3    Soboloff, J.4    Gill, D.L.5
  • 142
    • 0033119629 scopus 로고    scopus 로고
    • A capsaicin-receptor homologue with a high threshold for noxious heat
    • Caterina M.J., Rosen T.A., Tominaga M., Brake A.J., Julius D. A capsaicin-receptor homologue with a high threshold for noxious heat. Nature 1999, 398:436-441.
    • (1999) Nature , vol.398 , pp. 436-441
    • Caterina, M.J.1    Rosen, T.A.2    Tominaga, M.3    Brake, A.J.4    Julius, D.5
  • 144
    • 0037033077 scopus 로고    scopus 로고
    • Heat-evoked activation of TRPV4 channels in a HEK293 cell expression system and in native mouse aorta endothelial cells
    • Watanabe H., Vriens J., Suh S.H., Benham C.D., Droogmans G., Nilius B. Heat-evoked activation of TRPV4 channels in a HEK293 cell expression system and in native mouse aorta endothelial cells. J. Biol. Chem. 2002, 277:47044-47051.
    • (2002) J. Biol. Chem. , vol.277 , pp. 47044-47051
    • Watanabe, H.1    Vriens, J.2    Suh, S.H.3    Benham, C.D.4    Droogmans, G.5    Nilius, B.6
  • 147
    • 33646543034 scopus 로고    scopus 로고
    • TRPM2 activation by cyclic ADP-ribose at body temperature is involved in insulin secretion
    • Togashi K., Hara Y., Tominaga T., Higashi T., Konishi Y., Mori Y., Tominaga M. TRPM2 activation by cyclic ADP-ribose at body temperature is involved in insulin secretion. EMBO J. 2006, 25(9):1804-1815.
    • (2006) EMBO J. , vol.25 , Issue.9 , pp. 1804-1815
    • Togashi, K.1    Hara, Y.2    Tominaga, T.3    Higashi, T.4    Konishi, Y.5    Mori, Y.6    Tominaga, M.7
  • 149
    • 0037034931 scopus 로고    scopus 로고
    • Identification of a cold receptor reveals a general role for TRP channels in thermosensation
    • McKemy D.D., Neuhausser W.M., Julius D. Identification of a cold receptor reveals a general role for TRP channels in thermosensation. Nature 2002, 416:52-58.
    • (2002) Nature , vol.416 , pp. 52-58
    • McKemy, D.D.1    Neuhausser, W.M.2    Julius, D.3
  • 150
    • 7444240741 scopus 로고    scopus 로고
    • Clues to understanding cold sensation: thermodynamics and electrophysiological analysis of the cold receptor TRPM8
    • Brauchi S., Orio P., Latorre R. Clues to understanding cold sensation: thermodynamics and electrophysiological analysis of the cold receptor TRPM8. Proc. Natl. Acad. Sci. USA 2004, 101:15494-15499.
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 15494-15499
    • Brauchi, S.1    Orio, P.2    Latorre, R.3
  • 151
    • 38449084729 scopus 로고    scopus 로고
    • From peppers to peppermints: natural products as probes of the pain pathway
    • Julius D. From peppers to peppermints: natural products as probes of the pain pathway. Harvey Lect. 2005, 101:89-115.
    • (2005) Harvey Lect. , vol.101 , pp. 89-115
    • Julius, D.1
  • 153
    • 38549092780 scopus 로고    scopus 로고
    • Prostaglandin-induced activation of nociceptive neurons via direct interaction with transient receptor potential A1 (TRPA1)
    • Taylor-Clark T.E., Undem B.J., Macglashan D.W., Ghatta S., Carr M.J., McAlexander M.A. Prostaglandin-induced activation of nociceptive neurons via direct interaction with transient receptor potential A1 (TRPA1). Mol. Pharmacol. 2008, 73:274-281.
    • (2008) Mol. Pharmacol. , vol.73 , pp. 274-281
    • Taylor-Clark, T.E.1    Undem, B.J.2    Macglashan, D.W.3    Ghatta, S.4    Carr, M.J.5    McAlexander, M.A.6
  • 154
    • 40449121206 scopus 로고    scopus 로고
    • Transient receptor potential A1 is a sensory receptor for multiple products of oxidative stress
    • Andersson D.A., Gentry C., Moss S., Bevan S. Transient receptor potential A1 is a sensory receptor for multiple products of oxidative stress. J. Neurosci. 2008, 28:2485-2494.
    • (2008) J. Neurosci. , vol.28 , pp. 2485-2494
    • Andersson, D.A.1    Gentry, C.2    Moss, S.3    Bevan, S.4
  • 155
    • 63849101712 scopus 로고    scopus 로고
    • Nitrooleic acid, an endogenous product of nitrative stress, activates nociceptive sensory nerves via the direct activation of TRPA1
    • Taylor-Clark T.E., Ghatta S., Bettner W., Undem B.J. Nitrooleic acid, an endogenous product of nitrative stress, activates nociceptive sensory nerves via the direct activation of TRPA1. Mol. Pharmacol. 2009, 75:820-829.
    • (2009) Mol. Pharmacol. , vol.75 , pp. 820-829
    • Taylor-Clark, T.E.1    Ghatta, S.2    Bettner, W.3    Undem, B.J.4
  • 157
    • 0036117729 scopus 로고    scopus 로고
    • 3 receptor: a model ligand-gated ion channel (review)
    • 3 receptor: a model ligand-gated ion channel (review). Mol. Membr. Biol. 2002, 19:11-26.
    • (2002) Mol. Membr. Biol. , vol.19 , pp. 11-26
    • Reeves, D.C.1    Lummis, S.C.2
  • 161
    • 66249083118 scopus 로고    scopus 로고
    • Emerging roles for lipids in shaping membrane-protein function
    • Phillips R., Ursell T., Wiggins P., Sens P. Emerging roles for lipids in shaping membrane-protein function. Nature 2009, 459:379-385.
    • (2009) Nature , vol.459 , pp. 379-385
    • Phillips, R.1    Ursell, T.2    Wiggins, P.3    Sens, P.4
  • 163
    • 66049158598 scopus 로고    scopus 로고
    • A transient receptor potential-like channel mediates synaptic transmission in rod bipolar cells
    • Shen Y., Heimel J.A., Kamermans M., Peachey N.S., Gregg R.G., Nawy S. A transient receptor potential-like channel mediates synaptic transmission in rod bipolar cells. J. Neurosci. 2009, 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
  • 164
    • 0031830559 scopus 로고    scopus 로고
    • Bactericidal activity of carvacrol towards the food-borne pathogen Bacillus cereus
    • Ultee A., Gorris L.G., Smid E.J. Bactericidal activity of carvacrol towards the food-borne pathogen Bacillus cereus. J. Appl. Microbiol. 1998, 85:211-218.
    • (1998) J. Appl. Microbiol. , vol.85 , pp. 211-218
    • Ultee, A.1    Gorris, L.G.2    Smid, E.J.3
  • 167
  • 169
    • 33749562292 scopus 로고    scopus 로고
    • Bisandrographolide from Andrographis paniculata activates TRPV4 channels
    • Smith P.L., Maloney K.N., Pothen R.G., Clardy J., Clapham D.E. Bisandrographolide from Andrographis paniculata activates TRPV4 channels. J. Biol. Chem. 2006, 281:29897-29904.
    • (2006) J. Biol. Chem. , vol.281 , pp. 29897-29904
    • Smith, P.L.1    Maloney, K.N.2    Pothen, R.G.3    Clardy, J.4    Clapham, D.E.5
  • 175
    • 33846450261 scopus 로고    scopus 로고
    • 2-aminoethoxydiphenyl borate directly inhibits channels composed of connexin26 and/or connexin32
    • Tao L., Harris A.L. 2-aminoethoxydiphenyl borate directly inhibits channels composed of connexin26 and/or connexin32. Mol. Pharmacol. 2007, 71:570-579.
    • (2007) Mol. Pharmacol. , vol.71 , pp. 570-579
    • Tao, L.1    Harris, A.L.2
  • 176
    • 0242385383 scopus 로고    scopus 로고
    • Thermodynamics of heat activation of single capsaicin ion channels VR1
    • Liu B., Hui K., Qin F. Thermodynamics of heat activation of single capsaicin ion channels VR1. Biophys. J. 2003, 85:2988-3006.
    • (2003) Biophys. J. , vol.85 , pp. 2988-3006
    • Liu, B.1    Hui, K.2    Qin, F.3
  • 177
    • 0038502070 scopus 로고    scopus 로고
    • Low pH potentiates both capsaicin binding and channel gating of VR1 receptors
    • Ryu S., Liu B., Qin F. Low pH potentiates both capsaicin binding and channel gating of VR1 receptors. J. Gen. Physiol. 2003, 122:45-61.
    • (2003) J. Gen. Physiol. , vol.122 , pp. 45-61
    • Ryu, S.1    Liu, B.2    Qin, F.3
  • 178
    • 0037547117 scopus 로고    scopus 로고
    • Capsaicin activation of the pain receptor, VR1: multiple open states from both partial and full binding
    • Hui K., Liu B., Qin F. Capsaicin activation of the pain receptor, VR1: multiple open states from both partial and full binding. Biophys. J. 2003, 84:2957-2968.
    • (2003) Biophys. J. , vol.84 , pp. 2957-2968
    • Hui, K.1    Liu, B.2    Qin, F.3
  • 179
    • 0000410893 scopus 로고
    • The principles of the stochastic interpretation of ion-channel mechanisms
    • Plenum Press, New York, pp 397-482, B. Sakmann, E. Neher (Eds.)
    • Colquhoun D., Hawkes A.G. The principles of the stochastic interpretation of ion-channel mechanisms. Single-Channel Recording 1995, Plenum Press, New York, pp 397-482. 2nd ed. B. Sakmann, E. Neher (Eds.).
    • (1995) Single-Channel Recording
    • Colquhoun, D.1    Hawkes, A.G.2
  • 180
    • 0033162068 scopus 로고    scopus 로고
    • Translocation of a calcium-permeable cation channel induced by insulin-like growth factor-I
    • Kanzaki M., Zhang Y.Q., Mashima H., Li L., Shibata H., Kojima I. Translocation of a calcium-permeable cation channel induced by insulin-like growth factor-I. Nat. Cell Biol. 1999, 1:165-170.
    • (1999) Nat. Cell Biol. , vol.1 , pp. 165-170
    • Kanzaki, M.1    Zhang, Y.Q.2    Mashima, H.3    Li, L.4    Shibata, H.5    Kojima, I.6
  • 181
    • 33746032231 scopus 로고    scopus 로고
    • Subcellular translocation of the eGFP-tagged TRPL channel in Drosophila photoreceptors requires activation of the phototransduction cascade
    • Meyer N.E., Joel-Almagor T., Frechter S., Minke B., Huber A. Subcellular translocation of the eGFP-tagged TRPL channel in Drosophila photoreceptors requires activation of the phototransduction cascade. J. Cell Sci. 2006, 119:2592-2603.
    • (2006) J. Cell Sci. , vol.119 , pp. 2592-2603
    • Meyer, N.E.1    Joel-Almagor, T.2    Frechter, S.3    Minke, B.4    Huber, A.5
  • 182
    • 0029927299 scopus 로고    scopus 로고
    • The Drosophila light-activated conductance is composed of the two channels TRP and TRPL
    • Niemeyer B.A., Suzuki E., Scott K., Jalink K., ZGBRer C.S. The Drosophila light-activated conductance is composed of the two channels TRP and TRPL. Cell 1996, 85:651-659.
    • (1996) Cell , vol.85 , pp. 651-659
    • Niemeyer, B.A.1    Suzuki, E.2    Scott, K.3    Jalink, K.4    ZGBRer, C.S.5
  • 183
    • 0037187771 scopus 로고    scopus 로고
    • Light-regulated subcellular translocation of Drosophila TRPL channels induces long-term adaptation and modifies the light-induced current
    • Bähner M., Frechter S., Da Silva N., Minke B., Paulsen R., Huber A. Light-regulated subcellular translocation of Drosophila TRPL channels induces long-term adaptation and modifies the light-induced current. Neuron 2002, 34:83-93.
    • (2002) Neuron , vol.34 , pp. 83-93
    • Bähner, M.1    Frechter, S.2    Da Silva, N.3    Minke, B.4    Paulsen, R.5    Huber, A.6
  • 185
    • 27844586833 scopus 로고    scopus 로고
    • Epidermal growth factor induces tyrosine phosphorylation, membrane insertion, and activation of transient receptor potential channel 4
    • Odell A.F., Scott J.L., Van Helden D.F. Epidermal growth factor induces tyrosine phosphorylation, membrane insertion, and activation of transient receptor potential channel 4. J. Biol. Chem. 2005, 280:37974-37987.
    • (2005) J. Biol. Chem. , vol.280 , pp. 37974-37987
    • Odell, A.F.1    Scott, J.L.2    Van Helden, D.F.3
  • 188
    • 33750515856 scopus 로고    scopus 로고
    • The TRPM7 ion channel functions in cholinergic synaptic vesicles and affects transmitter release
    • Krapivinsky G., Mochida S., Krapivinsky L., Cibulsky S.M., Clapham D.E. The TRPM7 ion channel functions in cholinergic synaptic vesicles and affects transmitter release. Neuron 2006, 52:485-496.
    • (2006) Neuron , vol.52 , pp. 485-496
    • Krapivinsky, G.1    Mochida, S.2    Krapivinsky, L.3    Cibulsky, S.M.4    Clapham, D.E.5
  • 189
    • 33750516096 scopus 로고    scopus 로고
    • An exciting release on TRPM7
    • Montell C. An exciting release on TRPM7. Neuron 2006, 52:395-397.
    • (2006) Neuron , vol.52 , pp. 395-397
    • Montell, C.1
  • 190
    • 33644855566 scopus 로고    scopus 로고
    • Functional TRPM7 channels accumulate at the plasma membrane in response to fluid flow
    • Oancea E., Wolfe J.T., Clapham D.E. Functional TRPM7 channels accumulate at the plasma membrane in response to fluid flow. Circ. Res. 2006, 98:245-253.
    • (2006) Circ. Res. , vol.98 , pp. 245-253
    • Oancea, E.1    Wolfe, J.T.2    Clapham, D.E.3
  • 191
    • 28444477387 scopus 로고    scopus 로고
    • Plasma membrane phosphoinositide organization by protein electrostatics
    • McLaughlin S., Murray D. Plasma membrane phosphoinositide organization by protein electrostatics. Nature 2005, 438:605-611.
    • (2005) Nature , vol.438 , pp. 605-611
    • McLaughlin, S.1    Murray, D.2
  • 193
    • 34547125088 scopus 로고    scopus 로고
    • Target-specific PIP(2) signalling: how might it work?
    • Gamper N., Shapiro M.S. Target-specific PIP(2) signalling: how might it work?. J. Physiol. 2007, 582:967-975.
    • (2007) J. Physiol. , vol.582 , pp. 967-975
    • Gamper, N.1    Shapiro, M.S.2
  • 194
    • 67349183758 scopus 로고    scopus 로고
    • Phosphoinositide regulation of non-canonical transient receptor potential channels
    • Rohacs T. Phosphoinositide regulation of non-canonical transient receptor potential channels. Cell Calcium 2009, 45:554-565.
    • (2009) Cell Calcium , vol.45 , pp. 554-565
    • Rohacs, T.1
  • 195
    • 34548643512 scopus 로고    scopus 로고
    • Phosphoinositide phosphatases in a network of signalling reactions
    • Blero D., Payrastre B., Schurmans S., Erneux C. Phosphoinositide phosphatases in a network of signalling reactions. Pflugers Arch. 2007, 455:31-44.
    • (2007) Pflugers Arch. , vol.455 , pp. 31-44
    • Blero, D.1    Payrastre, B.2    Schurmans, S.3    Erneux, C.4
  • 196
    • 18644381102 scopus 로고    scopus 로고
    • Functional recovery from desensitization of vanilloid receptor TRPV1 requires resynthesis of phosphatidylinositol 4,5-bisphosphate
    • Liu B., Zhang C., Qin F. Functional recovery from desensitization of vanilloid receptor TRPV1 requires resynthesis of phosphatidylinositol 4,5-bisphosphate. J. Neurosci. 2005, 25:4835-4843.
    • (2005) J. Neurosci. , vol.25 , pp. 4835-4843
    • Liu, B.1    Zhang, C.2    Qin, F.3
  • 200
    • 0033590449 scopus 로고    scopus 로고
    • Polyunsaturated fatty acids activate the Drosophila light-sensitive channels TRP and TRPL
    • Chyb S., Raghu P., Hardie R.C. Polyunsaturated fatty acids activate the Drosophila light-sensitive channels TRP and TRPL. Nature 1999, 397:255-259.
    • (1999) Nature , vol.397 , pp. 255-259
    • Chyb, S.1    Raghu, P.2    Hardie, R.C.3
  • 201
    • 33749579981 scopus 로고    scopus 로고
    • Receptorinduced activation of Drosophila TRP gamma by polyunsaturated fatty acids
    • Jors S., Kazanski V., Foik A., Krautwurst D., Harteneck C. Receptorinduced activation of Drosophila TRP gamma by polyunsaturated fatty acids. J. Biol. Chem. 2006, 281:29693-29702.
    • (2006) J. Biol. Chem. , vol.281 , pp. 29693-29702
    • Jors, S.1    Kazanski, V.2    Foik, A.3    Krautwurst, D.4    Harteneck, C.5
  • 202
    • 67649363951 scopus 로고    scopus 로고
    • Linoleic acid inhibits TRP channels with intrinsic voltage sensitivity: Implications on the mechanism of linoleic acid action
    • Parnas M., Peters M., Minke B. Linoleic acid inhibits TRP channels with intrinsic voltage sensitivity: Implications on the mechanism of linoleic acid action. Channels (Austin) 2009, 3:164-166.
    • (2009) Channels (Austin) , vol.3 , pp. 164-166
    • Parnas, M.1    Peters, M.2    Minke, B.3
  • 203
    • 0025982360 scopus 로고
    • Molecular genetic studies of photoreceptor function using Drosophila mutants
    • Wiley-Liss, New York, J. Piatigorsky, T. Shinohara, P.S. Zelenka (Eds.)
    • Pak W.L. Molecular genetic studies of photoreceptor function using Drosophila mutants. Molecular Biology of the Retina: Basic and Clinical Relevant Studies 1991, 1-32. Wiley-Liss, New York. J. Piatigorsky, T. Shinohara, P.S. Zelenka (Eds.).
    • (1991) Molecular Biology of the Retina: Basic and Clinical Relevant Studies , pp. 1-32
    • Pak, W.L.1
  • 204
    • 0028868905 scopus 로고
    • Drosophila in vision research. The Friedenwald Lecture
    • Pak W.L. Drosophila in vision research. The Friedenwald Lecture. Invest. Ophthalmol. Vis. Sci. 1995, 36:2340-2357.
    • (1995) Invest. Ophthalmol. Vis. Sci. , vol.36 , pp. 2340-2357
    • Pak, W.L.1
  • 205
    • 0026317309 scopus 로고
    • Properties of photoreceptor-specific phospholipase C encoded by the norpA gene of Drosophila melanogaster
    • Schneuwly S., Burg M.G., Lending C., Perdew M.H., Pak W.L. Properties of photoreceptor-specific phospholipase C encoded by the norpA gene of Drosophila melanogaster. J. Biol. Chem. 1991, 266:24314-24319.
    • (1991) J. Biol. Chem. , vol.266 , pp. 24314-24319
    • Schneuwly, S.1    Burg, M.G.2    Lending, C.3    Perdew, M.H.4    Pak, W.L.5
  • 206
    • 0014691624 scopus 로고
    • Abnormal electroretinograms in visual mutants of Drosophila
    • Hotta Y., Benzer S. Abnormal electroretinograms in visual mutants of Drosophila. Nature 1969, 222:354-356.
    • (1969) Nature , vol.222 , pp. 354-356
    • Hotta, Y.1    Benzer, S.2
  • 207
    • 0014691611 scopus 로고
    • Nonphototactic mutants in a study of vision of Drosophila
    • Pak W.L., Grossfield J., White N.V. Nonphototactic mutants in a study of vision of Drosophila. Nature 1969, 222:351-354.
    • (1969) Nature , vol.222 , pp. 351-354
    • Pak, W.L.1    Grossfield, J.2    White, N.V.3
  • 208
    • 0001936877 scopus 로고
    • The inositol-lipid pathway is necessary for light excitation in fly photoreceptors
    • The Rockofeller University Press, New York
    • Minke B., Selinger Z. The inositol-lipid pathway is necessary for light excitation in fly photoreceptors. Sensory Transduction 1992, Vol. 47:202-217. The Rockofeller University Press, New York.
    • (1992) Sensory Transduction , vol.47 , pp. 202-217
    • Minke, B.1    Selinger, Z.2
  • 209
    • 0015841595 scopus 로고
    • Reversibly temperature sensitive phototransduction mutant of Drosophila melanogaster. Nat
    • Deland M.C., Pak W.L. Reversibly temperature sensitive phototransduction mutant of Drosophila melanogaster. Nat. New Biol. 1973, 244:184-186.
    • (1973) New Biol. , vol.244 , pp. 184-186
    • Deland, M.C.1    Pak, W.L.2
  • 210
    • 0029926102 scopus 로고    scopus 로고
    • Molecular, biochemical, and electrophysiological characterization of Drosohpila norpA mutannts
    • Pearn M.T., Randall L.L., Shortridge R.D., Burg M.G., Pak W.L. Molecular, biochemical, and electrophysiological characterization of Drosohpila norpA mutannts. J. Biol. Chem. 1996, 271:4937-4945.
    • (1996) J. Biol. Chem. , vol.271 , pp. 4937-4945
    • Pearn, M.T.1    Randall, L.L.2    Shortridge, R.D.3    Burg, M.G.4    Pak, W.L.5
  • 211
    • 84890873409 scopus 로고    scopus 로고
    • Drosophila photoreceptors and signaling mechanisms
    • Katz B., Minke B. Drosophila photoreceptors and signaling mechanisms. Front Cell Neurosci. 2009, 3:2.
    • (2009) Front Cell Neurosci. , vol.3 , pp. 2
    • Katz, B.1    Minke, B.2
  • 212
    • 34447097610 scopus 로고    scopus 로고
    • STIM1 heteromultimerizes TRPC channels to determine their function as store-operated channels
    • Yuan J.P., Zeng W., Huang G.N., Worley P.F., Muallem S. STIM1 heteromultimerizes TRPC channels to determine their function as store-operated channels. Nat. Cell Biol. 2007, 9:636-645.
    • (2007) Nat. Cell Biol. , vol.9 , pp. 636-645
    • Yuan, J.P.1    Zeng, W.2    Huang, G.N.3    Worley, P.F.4    Muallem, S.5
  • 213
    • 34250188666 scopus 로고    scopus 로고
    • Inositol lipids and TRPC channel activation
    • Putney J.W. Inositol lipids and TRPC channel activation. Biochem. Soc. Symp. 2007, 37-45.
    • (2007) Biochem. Soc. Symp. , pp. 37-45
    • Putney, J.W.1
  • 214
    • 0022641027 scopus 로고
    • Pressure injection of calcium both excites and adapts Limulus ventral photoreceptors
    • Payne R., Corson D.W., Fein A. Pressure injection of calcium both excites and adapts Limulus ventral photoreceptors. J. Gen. Physiol. 1986, 88:107-126.
    • (1986) J. Gen. Physiol. , vol.88 , pp. 107-126
    • Payne, R.1    Corson, D.W.2    Fein, A.3
  • 215
    • 0028819281 scopus 로고
    • 2+ facilitates and inactivates but does not directly excite light-sensitive channels in Drosophila photoreceptors
    • 2+ facilitates and inactivates but does not directly excite light-sensitive channels in Drosophila photoreceptors. J. Neurosci. 1995, 15:889-902.
    • (1995) J. Neurosci. , vol.15 , pp. 889-902
    • Hardie, R.C.1
  • 218
    • 0038724276 scopus 로고    scopus 로고
    • Regulation of trp channels via lipid second messengers
    • Hardie R.C. Regulation of trp channels via lipid second messengers. Annu. Rev. Physiol. 2003, 65:735-759.
    • (2003) Annu. Rev. Physiol. , vol.65 , pp. 735-759
    • Hardie, R.C.1
  • 220
    • 0033679832 scopus 로고    scopus 로고
    • Constitutive activity of the light-sensitive channels TRP and TRPL in the Drosophila diacylglycerol kinase mutant
    • Raghu P., Usher K., Jonas S., Chyb S., Polyanovsky A., Hardie R.C. Constitutive activity of the light-sensitive channels TRP and TRPL in the Drosophila diacylglycerol kinase mutant. rdgA, Neuron 2000, 26:169-179.
    • (2000) rdgA, Neuron , vol.26 , pp. 169-179
    • Raghu, P.1    Usher, K.2    Jonas, S.3    Chyb, S.4    Polyanovsky, A.5    Hardie, R.C.6
  • 221
    • 0037628996 scopus 로고    scopus 로고
    • P24, by the diacylglycerol kinase mutant, rdgA, and by metabolic inhibition
    • P24, by the diacylglycerol kinase mutant, rdgA, and by metabolic inhibition. J. Biol. Chem. 2003, 278:18851-18858.
    • (2003) J. Biol. Chem. , vol.278 , pp. 18851-18858
    • Hardie, R.C.1    Martin, F.2    Chyb, S.3    Raghu, P.4
  • 222
    • 65649095597 scopus 로고    scopus 로고
    • Unitary recordings of TRP and TRPL channels from isolated Drosophila retinal photoreceptor rhabdomeres: Activation by light and lipids
    • Delgado R., Bacigalupo J. Unitary recordings of TRP and TRPL channels from isolated Drosophila retinal photoreceptor rhabdomeres: Activation by light and lipids. J. Neurophysiol. 2009, 101:2372-2379.
    • (2009) J. Neurophysiol. , vol.101 , pp. 2372-2379
    • Delgado, R.1    Bacigalupo, J.2
  • 223
    • 0030913352 scopus 로고    scopus 로고
    • Immunolocalization of Drosophila eye-specific diacylgylcerol kinase, rdgA, which is essential for the maintenance of the photoreceptor
    • Masai I., Suzuki E., Yoon C.S., Kohyama A., Hotta Y. Immunolocalization of Drosophila eye-specific diacylgylcerol kinase, rdgA, which is essential for the maintenance of the photoreceptor. J. Neurobiol. 1997, 32:695-706.
    • (1997) J. Neurobiol. , vol.32 , pp. 695-706
    • Masai, I.1    Suzuki, E.2    Yoon, C.S.3    Kohyama, A.4    Hotta, Y.5
  • 225
    • 67349238189 scopus 로고    scopus 로고
    • Regulation of Drosophila TRPC channels by lipid messengers
    • Raghu P., Hardie R.C. Regulation of Drosophila TRPC channels by lipid messengers. Cell Calcium 2009, 45:566-573.
    • (2009) Cell Calcium , vol.45 , pp. 566-573
    • Raghu, P.1    Hardie, R.C.2
  • 226
    • 0034777494 scopus 로고    scopus 로고
    • Regulation of Drosophila transient receptor potential-like (TrpL) channels by phospholipase Cdependent mechanisms
    • Estacion M., Sinkins W.G., Schilling W.P. Regulation of Drosophila transient receptor potential-like (TrpL) channels by phospholipase Cdependent mechanisms. J. Physiol. 2001, 530:1-19.
    • (2001) J. Physiol. , vol.530 , pp. 1-19
    • Estacion, M.1    Sinkins, W.G.2    Schilling, W.P.3
  • 228
    • 33749125215 scopus 로고    scopus 로고
    • Biophysical properties of lipids and dynamic membranes
    • Janmey P.A., Kinnunen P.K. Biophysical properties of lipids and dynamic membranes. Trends Cell Biol. 2006, 16:538-546.
    • (2006) Trends Cell Biol. , vol.16 , pp. 538-546
    • Janmey, P.A.1    Kinnunen, P.K.2
  • 229
    • 2342569734 scopus 로고    scopus 로고
    • Activation, subunit composition and physiological relevance of DAG-sensitive TRPC proteins
    • Gudermann T., Hofmann T., Schnitzler M., Dietrich A. Activation, subunit composition and physiological relevance of DAG-sensitive TRPC proteins. Novartis. Found. Symp. 2004, 258:103-118.
    • (2004) Novartis. Found. Symp. , vol.258 , pp. 103-118
    • Gudermann, T.1    Hofmann, T.2    Schnitzler, M.3    Dietrich, A.4
  • 231
    • 0042206600 scopus 로고    scopus 로고
    • Regulation of canonical transient receptor potential (TRPC) channel function by diacylglycerol and protein kinase C
    • Venkatachalam K., Zheng F., Gill D.L. Regulation of canonical transient receptor potential (TRPC) channel function by diacylglycerol and protein kinase C. J. Biol. Chem. 2003, 278:29031-29040.
    • (2003) J. Biol. Chem. , vol.278 , pp. 29031-29040
    • Venkatachalam, K.1    Zheng, F.2    Gill, D.L.3
  • 232
    • 0035855910 scopus 로고    scopus 로고
    • Visual transduction in Drosophila
    • Hardie R.C., Raghu P. Visual transduction in Drosophila. Nature 2001, 413:186-193.
    • (2001) Nature , vol.413 , pp. 186-193
    • Hardie, R.C.1    Raghu, P.2
  • 233
    • 59649113294 scopus 로고    scopus 로고
    • Physiology and pathophysiology of canonical transient receptor potential channels
    • Abramowitz J., Birnbaumer L. Physiology and pathophysiology of canonical transient receptor potential channels. FASEB J. 2009, 23:297-328.
    • (2009) FASEB J. , vol.23 , pp. 297-328
    • Abramowitz, J.1    Birnbaumer, L.2
  • 234
    • 19244366419 scopus 로고    scopus 로고
    • 2+entry channels: still elusive!
    • 2+entry channels: still elusive!. Sci. STKE. 2004, 2004:e36.
    • (2004) Sci. STKE. , vol.2004
    • Nilius, B.1
  • 235
    • 0037636288 scopus 로고    scopus 로고
    • 2+- permeable nonselective cation channels
    • 2+- permeable nonselective cation channels. Cell Calcium 2003, 33:441-450.
    • (2003) Cell Calcium , vol.33 , pp. 441-450
    • Plant, T.D.1    Schaefer, M.2
  • 236
    • 0037077249 scopus 로고    scopus 로고
    • Comparison of human TRPC3 channels in receptor-activated and store-operated modes. Differential sensitivity to channel blockers suggests fundamental differences in channel composition
    • Trebak M., Bird G.S., McKay R.R., Putney J.W. Comparison of human TRPC3 channels in receptor-activated and store-operated modes. Differential sensitivity to channel blockers suggests fundamental differences in channel composition. J. Biol. Chem. 2002, 277:21617-21623.
    • (2002) J. Biol. Chem. , vol.277 , pp. 21617-21623
    • Trebak, M.1    Bird, G.S.2    McKay, R.R.3    Putney, J.W.4
  • 238
    • 35748985570 scopus 로고    scopus 로고
    • Transient receptor potential channels in mechanosensing and cell volume regulation
    • Pedersen S.F., Nilius B. Transient receptor potential channels in mechanosensing and cell volume regulation. Methods Enzymol. 2007, 428:183-207.
    • (2007) Methods Enzymol. , vol.428 , pp. 183-207
    • Pedersen, S.F.1    Nilius, B.2
  • 239
    • 0022911410 scopus 로고
    • Patch clamp measurements on Xenopus laevis oocytes: currents through endogenous channels and implanted acetylcholine receptor and sodium channels
    • Methfessel C., Witzemann V., Takahashi T., Mishina M., Numa S., Sakmann B. Patch clamp measurements on Xenopus laevis oocytes: currents through endogenous channels and implanted acetylcholine receptor and sodium channels. Pflugers Arch. 1986, 407:577-588.
    • (1986) Pflugers Arch. , vol.407 , pp. 577-588
    • Methfessel, C.1    Witzemann, V.2    Takahashi, T.3    Mishina, M.4    Numa, S.5    Sakmann, B.6
  • 240
    • 0030776196 scopus 로고    scopus 로고
    • OSM-9, a novel protein with structural similarity to channels, is required for olfaction, mechanosensation, and olfactory adaptation in Caenorhabditis elegans
    • Colbert H.A., Smith T.L., Bargmann C.I. OSM-9, a novel protein with structural similarity to channels, is required for olfaction, mechanosensation, and olfactory adaptation in Caenorhabditis elegans. J. Neurosci. 1997, 17:8259-8269.
    • (1997) J. Neurosci. , vol.17 , pp. 8259-8269
    • Colbert, H.A.1    Smith, T.L.2    Bargmann, C.I.3
  • 243
    • 0032899216 scopus 로고    scopus 로고
    • Signaling mechanisms underlying the vascular myogenic response
    • Davis M.J., Hill M.A. Signaling mechanisms underlying the vascular myogenic response. Physiol. Rev. 1999, 79:387-423.
    • (1999) Physiol. Rev. , vol.79 , pp. 387-423
    • Davis, M.J.1    Hill, M.A.2
  • 245
    • 7244239194 scopus 로고    scopus 로고
    • Critical role for transient receptor potential channel TRPM4 in myogenic constriction of cerebral arteries
    • Earley S., Waldron B.J., Brayden J.E. Critical role for transient receptor potential channel TRPM4 in myogenic constriction of cerebral arteries. Circ. Res. 2004, 95:922-929.
    • (2004) Circ. Res. , vol.95 , pp. 922-929
    • Earley, S.1    Waldron, B.J.2    Brayden, J.E.3
  • 247
    • 33847017353 scopus 로고    scopus 로고
    • Direct mechano-stress sensitivity of TRPM7 channel
    • Numata T., Shimizu T., Okada Y. Direct mechano-stress sensitivity of TRPM7 channel. Cell Physiol. Biochem. 2007, 19:1-8.
    • (2007) Cell Physiol. Biochem. , vol.19 , pp. 1-8
    • Numata, T.1    Shimizu, T.2    Okada, Y.3
  • 248
    • 33846312821 scopus 로고    scopus 로고
    • TRPM7 is a stretch- and swellingactivated cation channel involved in volume regulation in human epithelial cells
    • Numata T., Shimizu T., Okada Y. TRPM7 is a stretch- and swellingactivated cation channel involved in volume regulation in human epithelial cells. Am. J. Physiol. Cell Physiol. 2007, 292:C460-C467.
    • (2007) Am. J. Physiol. Cell Physiol. , vol.292
    • Numata, T.1    Shimizu, T.2    Okada, Y.3
  • 249
    • 0038498142 scopus 로고    scopus 로고
    • Molecular and functional characterization of the melastatin-related cation channel TRPM3
    • Grimm C., Kraft R., Sauerbruch S., Schultz G., Harteneck C. Molecular and functional characterization of the melastatin-related cation channel TRPM3. J. Biol. Chem. 2003, 278:21493-21501.
    • (2003) J. Biol. Chem. , vol.278 , pp. 21493-21501
    • Grimm, C.1    Kraft, R.2    Sauerbruch, S.3    Schultz, G.4    Harteneck, C.5
  • 250
    • 34547420154 scopus 로고    scopus 로고
    • TRPs in bladder diseases
    • Birder L.A. TRPs in bladder diseases. Biochim. Biophys. Acta 2007, 1772:879-884.
    • (2007) Biochim. Biophys. Acta , vol.1772 , pp. 879-884
    • Birder, L.A.1
  • 253
    • 15544367400 scopus 로고    scopus 로고
    • A physiological view of the primary cilium
    • Praetorius H.A., Spring K.R. A physiological view of the primary cilium. Annu. Rev. Physiol. 2005, 67:515-529.
    • (2005) Annu. Rev. Physiol. , vol.67 , pp. 515-529
    • Praetorius, H.A.1    Spring, K.R.2
  • 254
    • 0035498717 scopus 로고    scopus 로고
    • Bending the MDCK cell primary cilium increases intracellular calcium
    • Praetorius H.A., Spring K.R. Bending the MDCK cell primary cilium increases intracellular calcium. J. Membr. Biol. 2001, 184:71-79.
    • (2001) J. Membr. Biol. , vol.184 , pp. 71-79
    • Praetorius, H.A.1    Spring, K.R.2
  • 256
    • 20444366051 scopus 로고    scopus 로고
    • Heterologously expressed fungal transient receptor potential channels retain mechanosensitivity in vitro and osmotic response in vivo
    • Zhou X.L., Loukin S.H., Coria R., Kung C., Saimi Y. Heterologously expressed fungal transient receptor potential channels retain mechanosensitivity in vitro and osmotic response in vivo. Eur. Biophys. J. 2005, 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
  • 258
    • 0344630199 scopus 로고    scopus 로고
    • Mammalian TRPV4 (VR-OAC) directs behavioral responses to osmotic and mechanical stimuli in Caenorhabditis elegans
    • Liedtke W., Tobin D.M., Bargmann C.I., Friedman J.M. Mammalian TRPV4 (VR-OAC) directs behavioral responses to osmotic and mechanical stimuli in Caenorhabditis elegans. Proc. Natl. Acad. Sci. USA 2003, 100(Suppl 2):14531-14536.
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , Issue.SUPPL.2 , pp. 14531-14536
    • Liedtke, W.1    Tobin, D.M.2    Bargmann, C.I.3    Friedman, J.M.4
  • 260
    • 33645557094 scopus 로고    scopus 로고
    • A transient receptor potential vanilloid 4-dependent mechanism of hyperalgesia is engaged by concerted action of inflammatory mediators
    • Alessandri-Haber N., Dina O.A., Joseph E.K., Reichling D., Levine J.D. A transient receptor potential vanilloid 4-dependent mechanism of hyperalgesia is engaged by concerted action of inflammatory mediators. J. Neurosci. 2006, 26:3864-3874.
    • (2006) J. Neurosci. , vol.26 , pp. 3864-3874
    • Alessandri-Haber, N.1    Dina, O.A.2    Joseph, E.K.3    Reichling, D.4    Levine, J.D.5
  • 261
    • 21044435352 scopus 로고    scopus 로고
    • TRPV4 exhibits a functional role in cell-volume regulation
    • Becker D., Blase C., Bereiter-Hahn J., Jendrach M. TRPV4 exhibits a functional role in cell-volume regulation. J. Cell Sci. 2005, 118:2435-2440.
    • (2005) J. Cell Sci. , vol.118 , pp. 2435-2440
    • Becker, D.1    Blase, C.2    Bereiter-Hahn, J.3    Jendrach, M.4
  • 262
    • 50249115657 scopus 로고    scopus 로고
    • Dependence of regulatory volume decrease on transient receptor potential vanilloid 4 (TRPV4) expression in human corneal epithelial cells
    • Pan Z., Yang H., Mergler S., Liu H., Tachado S.D., Zhang F., Kao W.W., Koziel H., Pleyer U., Reinach P.S. Dependence of regulatory volume decrease on transient receptor potential vanilloid 4 (TRPV4) expression in human corneal epithelial cells. Cell Calcium 2008, 44:374-385.
    • (2008) Cell Calcium , vol.44 , pp. 374-385
    • Pan, Z.1    Yang, H.2    Mergler, S.3    Liu, H.4    Tachado, S.D.5    Zhang, F.6    Kao, W.W.7    Koziel, H.8    Pleyer, U.9    Reinach, P.S.10
  • 264
    • 33744948236 scopus 로고    scopus 로고
    • A role for AQP5 in activation of TRPV4 by hypotonicity: concerted involvement of AQP5 and TRPV4 in regulation of cell volume recovery
    • Liu X., Bandyopadhyay B.C., Nakamoto T., Singh B., Liedtke W., Melvin J.E., Ambudkar I. A role for AQP5 in activation of TRPV4 by hypotonicity: concerted involvement of AQP5 and TRPV4 in regulation of cell volume recovery. J. Biol. Chem. 2006, 281:15485-15495.
    • (2006) J. Biol. Chem. , vol.281 , pp. 15485-15495
    • Liu, X.1    Bandyopadhyay, B.C.2    Nakamoto, T.3    Singh, B.4    Liedtke, W.5    Melvin, J.E.6    Ambudkar, I.7
  • 266
    • 0034697041 scopus 로고    scopus 로고
    • Assembly of Trp1 in a signaling complex associated with caveolin-scaffolding lipid raft domains
    • Lockwich T.P., Liu X., Singh B.B., Jadlowiec J., Weiland S., Ambudkar I.S. Assembly of Trp1 in a signaling complex associated with caveolin-scaffolding lipid raft domains. J. Biol. Chem. 2000, 275:11934-11942.
    • (2000) J. Biol. Chem. , vol.275 , pp. 11934-11942
    • Lockwich, T.P.1    Liu, X.2    Singh, B.B.3    Jadlowiec, J.4    Weiland, S.5    Ambudkar, I.S.6
  • 268
    • 33745924434 scopus 로고    scopus 로고
    • TRPV1, but not P2X, requires cholesterol for its function and membrane expression in rat nociceptors
    • Liu M., Huang W., Wu D., Priestley J.V. TRPV1, but not P2X, requires cholesterol for its function and membrane expression in rat nociceptors. Eur. J. Neurosci. 2006, 24:1-6.
    • (2006) Eur. J. Neurosci. , vol.24 , pp. 1-6
    • Liu, M.1    Huang, W.2    Wu, D.3    Priestley, J.V.4
  • 269
    • 34548480704 scopus 로고    scopus 로고
    • Light-induced recruitment of INAD-signaling complexes to detergent-resistant lipid rafts in Drosophila photoreceptors
    • Sanxaridis P.D., Cronin M.A., Rawat S.S., Waro G., Acharya U., Tsunoda S. Light-induced recruitment of INAD-signaling complexes to detergent-resistant lipid rafts in Drosophila photoreceptors. Mol. Cell Neurosci. 2007, 36:36-46.
    • (2007) Mol. Cell Neurosci. , vol.36 , pp. 36-46
    • Sanxaridis, P.D.1    Cronin, M.A.2    Rawat, S.S.3    Waro, G.4    Acharya, U.5    Tsunoda, S.6
  • 270
    • 0001718634 scopus 로고
    • Biological membranes as bilayer couples. A molecular mechanism of drug-erythrocyte interactions
    • Sheetz M.P., Singer S.J. Biological membranes as bilayer couples. A molecular mechanism of drug-erythrocyte interactions. Proc. Natl. Acad. Sci. USA 1974, 71:4457-4461.
    • (1974) Proc. Natl. Acad. Sci. USA , vol.71 , pp. 4457-4461
    • Sheetz, M.P.1    Singer, S.J.2
  • 273
    • 4944225045 scopus 로고    scopus 로고
    • Effect of lipids with different spontaneous curvature on the channel activity of colicin E1: evidence in favor of a toroidal pore
    • Sobko A.A., Kotova E.A., Antonenko Y.N., Zakharov S.D., Cramer W.A. Effect of lipids with different spontaneous curvature on the channel activity of colicin E1: evidence in favor of a toroidal pore. FEBS Lett. 2004, 576:205-210.
    • (2004) FEBS Lett. , vol.576 , pp. 205-210
    • Sobko, A.A.1    Kotova, E.A.2    Antonenko, Y.N.3    Zakharov, S.D.4    Cramer, W.A.5
  • 274
    • 33845637597 scopus 로고    scopus 로고
    • Phospholipids and the origin of cationic gating charges in voltage sensors
    • Schmidt D., Jiang Q.X., MacKinnon R. Phospholipids and the origin of cationic gating charges in voltage sensors. Nature 2006, 444:775-779.
    • (2006) Nature , vol.444 , pp. 775-779
    • Schmidt, D.1    Jiang, Q.X.2    MacKinnon, R.3
  • 275
    • 34347262391 scopus 로고    scopus 로고
    • Bilayer thickness and membrane protein function: an energetic perspective
    • Andersen O.S., Koeppe R.E. Bilayer thickness and membrane protein function: an energetic perspective. Annu. Rev. Biophys. Biomol. Struct. 2007, 36:107-130.
    • (2007) Annu. Rev. Biophys. Biomol. Struct. , vol.36 , pp. 107-130
    • Andersen, O.S.1    Koeppe, R.E.2
  • 276
    • 0024586090 scopus 로고
    • Membrane function in mammalian hibernation
    • Aloia R.C., Raison J.K. Membrane function in mammalian hibernation. Biochim. Biophys. Acta 1989, 988:123-146.
    • (1989) Biochim. Biophys. Acta , vol.988 , pp. 123-146
    • Aloia, R.C.1    Raison, J.K.2
  • 278
    • 43049117188 scopus 로고    scopus 로고
    • Formation of a new receptor-operated channel by heteromeric assembly of TRPP2 and TRPC1 subunits
    • Bai C.X., Giamarchi A., Rodat-Despoix L., Padilla F., Downs T., Tsiokas L., Delmas P. Formation of a new receptor-operated channel by heteromeric assembly of TRPP2 and TRPC1 subunits. EMBO Rep. 2008, 9:472-479.
    • (2008) EMBO Rep. , vol.9 , pp. 472-479
    • Bai, C.X.1    Giamarchi, A.2    Rodat-Despoix, L.3    Padilla, F.4    Downs, T.5    Tsiokas, L.6    Delmas, P.7
  • 279
    • 21344464979 scopus 로고    scopus 로고
    • The epithelial calcium channels TRPV5 and TRPV6: regulation and implications for disease
    • van A.M., Hoenderop J.G., Bindels R.J. The epithelial calcium channels TRPV5 and TRPV6: regulation and implications for disease. Naunyn Schmiedebergs Arch. Pharmacol. 2005, 371:295-306.
    • (2005) Naunyn Schmiedebergs Arch. Pharmacol. , vol.371 , pp. 295-306
    • van, A.M.1    Hoenderop, J.G.2    Bindels, R.J.3
  • 280
    • 0035408171 scopus 로고    scopus 로고
    • Trp1-dependent enhancement of salivary gland fluid secretion: role of store-operated calcium entry
    • Singh B.B., Zheng C., Liu X., Lockwich T., Liao D., Zhu M.X., Birnbaumer L., Ambudkar I.S. Trp1-dependent enhancement of salivary gland fluid secretion: role of store-operated calcium entry. FASEB J. 2001, 15:1652-1654.
    • (2001) FASEB J. , vol.15 , pp. 1652-1654
    • Singh, B.B.1    Zheng, C.2    Liu, X.3    Lockwich, T.4    Liao, D.5    Zhu, M.X.6    Birnbaumer, L.7    Ambudkar, I.S.8
  • 282
    • 0041708061 scopus 로고    scopus 로고
    • TRPC5 is a regulator of hippocampal neurite length and growth cone morphology
    • Greka A., Navarro B., Oancea E., Duggan A., Clapham D.E. TRPC5 is a regulator of hippocampal neurite length and growth cone morphology. Nat. Neurosci. 2003, 6:837-845.
    • (2003) Nat. Neurosci. , vol.6 , pp. 837-845
    • Greka, A.1    Navarro, B.2    Oancea, E.3    Duggan, A.4    Clapham, D.E.5
  • 290
    • 20444364145 scopus 로고    scopus 로고
    • Molecular analysis of a store-operated and 2-acetyl-sn-glycerolsensitive non-selective cation channel. Heteromeric assembly of TRPC1-TRPC3
    • Liu X., Bandyopadhyay B.C., Singh B.B., Groschner K., Ambudkar I.S. Molecular analysis of a store-operated and 2-acetyl-sn-glycerolsensitive non-selective cation channel. Heteromeric assembly of TRPC1-TRPC3. J. Biol. Chem. 2005, 280:21600-21606.
    • (2005) J. Biol. Chem. , vol.280 , pp. 21600-21606
    • Liu, X.1    Bandyopadhyay, B.C.2    Singh, B.B.3    Groschner, K.4    Ambudkar, I.S.5
  • 292
    • 33744952751 scopus 로고    scopus 로고
    • TRPC3 and TRPC4 associate to form a redox-sensitive cation channel. Evidence for expression of native TRPC3-TRPC4 heteromeric channels in endothelial cells
    • Poteser M., Graziani A., Rosker C., Eder P., Derler I., Kahr H., Zhu M.X., Romanin C., Groschner K. TRPC3 and TRPC4 associate to form a redox-sensitive cation channel. Evidence for expression of native TRPC3-TRPC4 heteromeric channels in endothelial cells. J. Biol. Chem. 2006, 281:13588-13595.
    • (2006) J. Biol. Chem. , vol.281 , pp. 13588-13595
    • Poteser, M.1    Graziani, A.2    Rosker, C.3    Eder, P.4    Derler, I.5    Kahr, H.6    Zhu, M.X.7    Romanin, C.8    Groschner, K.9
  • 293
  • 296
    • 26444457870 scopus 로고    scopus 로고
    • Homo- and heteromeric assembly of TRP channel subunits
    • Schaefer M. Homo- and heteromeric assembly of TRP channel subunits. Pflugers Arch. 2005, 451:35-42.
    • (2005) Pflugers Arch. , vol.451 , pp. 35-42
    • Schaefer, M.1
  • 297
    • 33847394506 scopus 로고    scopus 로고
    • Thermosensitive TRPV channel subunits coassemble into heteromeric channels with intermediate conductance and gating properties
    • Cheng W., Yang F., Takanishi C.L., Zheng J. Thermosensitive TRPV channel subunits coassemble into heteromeric channels with intermediate conductance and gating properties. J. Gen. Physiol. 2007, 129:191-207.
    • (2007) J. Gen. Physiol. , vol.129 , pp. 191-207
    • Cheng, W.1    Yang, F.2    Takanishi, C.L.3    Zheng, J.4
  • 298
    • 17644426325 scopus 로고    scopus 로고
    • Nociceptor and hair cell transducer properties of TRPA1, a channel for pain and hearing
    • Nagata K., Duggan A., Kumar G., Garcia-Anoveros J. Nociceptor and hair cell transducer properties of TRPA1, a channel for pain and hearing. J. Neurosci. 2005, 25:4052-4061.
    • (2005) J. Neurosci. , vol.25 , pp. 4052-4061
    • Nagata, K.1    Duggan, A.2    Kumar, G.3    Garcia-Anoveros, J.4
  • 300
    • 0032055129 scopus 로고    scopus 로고
    • Functional expression of TrpC1: a human homologue of the Drosophila Trp channel
    • Sinkins W.G., Estacion M., Schilling W.P. Functional expression of TrpC1: a human homologue of the Drosophila Trp channel. Biochem. J. 1998, 331:331-339.
    • (1998) Biochem. J. , vol.331 , pp. 331-339
    • Sinkins, W.G.1    Estacion, M.2    Schilling, W.P.3
  • 304
    • 0346850851 scopus 로고    scopus 로고
    • N-linked protein glycosylation is a major determinant for basal TRPC3 and TRPC6 channel activity
    • Dietrich A., Schnitzler M., Emmel J., Kalwa H., Hofmann T., Gudermann T. N-linked protein glycosylation is a major determinant for basal TRPC3 and TRPC6 channel activity. J. Biol. Chem. 2003, 278:47842-47852.
    • (2003) J. Biol. Chem. , vol.278 , pp. 47842-47852
    • Dietrich, A.1    Schnitzler, M.2    Emmel, J.3    Kalwa, H.4    Hofmann, T.5    Gudermann, T.6
  • 306
    • 33748754387 scopus 로고    scopus 로고
    • Native TRPC7 channel activation by an inositol trisphosphate receptor-dependent mechanism
    • Vazquez G., Bird G.S., Mori Y., Putney J.W. Native TRPC7 channel activation by an inositol trisphosphate receptor-dependent mechanism. J. Biol. Chem. 2006, 281:25250-25258.
    • (2006) J. Biol. Chem. , vol.281 , pp. 25250-25258
    • Vazquez, G.1    Bird, G.S.2    Mori, Y.3    Putney, J.W.4
  • 310
    • 20444491995 scopus 로고    scopus 로고
    • Alternative splicing switches the divalent cation selectivity of TRPM3 channels
    • Oberwinkler J., Lis A., Giehl K.M., Flockerzi V., Philipp S.E. Alternative splicing switches the divalent cation selectivity of TRPM3 channels. J. Biol. Chem. 2005, 280:22540-22548.
    • (2005) J. Biol. Chem. , vol.280 , pp. 22540-22548
    • Oberwinkler, J.1    Lis, A.2    Giehl, K.M.3    Flockerzi, V.4    Philipp, S.E.5
  • 311
    • 14944348415 scopus 로고    scopus 로고
    • Activation of the melastatinrelated cation channel TRPM3 by D-erythro-sphingosine
    • Grimm C., Kraft R., Schultz G., Harteneck C. Activation of the melastatinrelated cation channel TRPM3 by D-erythro-sphingosine. Mol. Pharmacol. 2005, 67:798-805.
    • (2005) Mol. Pharmacol. , vol.67 , pp. 798-805
    • Grimm, C.1    Kraft, R.2    Schultz, G.3    Harteneck, C.4
  • 316
    • 33646140352 scopus 로고    scopus 로고
    • Functional characterization of homo- and heteromeric channel kinases TRPM6 and TRPM7
    • Li M., Jiang J., Yue L. Functional characterization of homo- and heteromeric channel kinases TRPM6 and TRPM7. J. Gen. Physiol. 2006, 127:525-537.
    • (2006) J. Gen. Physiol. , vol.127 , pp. 525-537
    • Li, M.1    Jiang, J.2    Yue, L.3
  • 320
    • 0034306198 scopus 로고    scopus 로고
    • OTRPC4, a nonselective cation channel that confers sensitivity to extracellular osmolarity
    • Strotmann R., Harteneck C., Nunnenmacher K., Schultz G., Plant T.D. OTRPC4, a nonselective cation channel that confers sensitivity to extracellular osmolarity. Nature Cell Biol. 2000, 2:695-702.
    • (2000) Nature Cell Biol. , vol.2 , pp. 695-702
    • Strotmann, R.1    Harteneck, C.2    Nunnenmacher, K.3    Schultz, G.4    Plant, T.D.5
  • 322
    • 0035810243 scopus 로고    scopus 로고
    • CaT1 manifests the pore properties of the calcium-release-activated calcium channel
    • Yue L., Peng J.B., Hediger M.A., Clapham D.E. CaT1 manifests the pore properties of the calcium-release-activated calcium channel. Nature 2001, 410:705-709.
    • (2001) Nature , vol.410 , pp. 705-709
    • Yue, L.1    Peng, J.B.2    Hediger, M.A.3    Clapham, D.E.4
  • 323
    • 84882544325 scopus 로고    scopus 로고
    • Phototransduction in microvillar photoreceptors of Drosophila and other invertebrates
    • Academic Press, New York, I.B. Allan, K. Akimichi, M.S. Gordon, W. Gerald, D.A. Thomas, H.M. Richard, D. Peter, O. Donata, F. Stuart, K.B. Gary, M.C. Bushnell, H.K. Jon, G. Esther (Eds.)
    • Hardie R.C., Postma M. Phototransduction in microvillar photoreceptors of Drosophila and other invertebrates. The Senses: A Comprehensive Reference 2008, 77-130. Academic Press, New York. I.B. Allan, K. Akimichi, M.S. Gordon, W. Gerald, D.A. Thomas, H.M. Richard, D. Peter, O. Donata, F. Stuart, K.B. Gary, M.C. Bushnell, H.K. Jon, G. Esther (Eds.).
    • (2008) The Senses: A Comprehensive Reference , pp. 77-130
    • Hardie, R.C.1    Postma, M.2
  • 325
    • 15944417442 scopus 로고    scopus 로고
    • Cyclic ADP-ribose and hydrogen peroxide synergize with ADP-ribose in the activation of TRPM2 channels
    • Kolisek M., Beck A., Fleig A., Penner R. Cyclic ADP-ribose and hydrogen peroxide synergize with ADP-ribose in the activation of TRPM2 channels. Mol. Cell 2005, 18:61-69.
    • (2005) Mol. Cell , vol.18 , pp. 61-69
    • Kolisek, M.1    Beck, A.2    Fleig, A.3    Penner, R.4
  • 333
    • 17244383526 scopus 로고    scopus 로고
    • Requirement of TRPC channels in netrin-1-induced chemotropic turning of nerve growth cones
    • Wang G.X., Poo M.M. Requirement of TRPC channels in netrin-1-induced chemotropic turning of nerve growth cones. Nature 2005, 434:898-904.
    • (2005) Nature , vol.434 , pp. 898-904
    • Wang, G.X.1    Poo, M.M.2
  • 335
    • 34547134719 scopus 로고    scopus 로고
    • 2+ exchange inhibitor KB-R7943 potently blocks TRPC channels
    • 2+ exchange inhibitor KB-R7943 potently blocks TRPC channels. Biochem. Biophys. Res. Commun. 2007, 361:230-236.
    • (2007) Biochem. Biophys. Res. Commun. , vol.361 , pp. 230-236
    • Kraft, R.1
  • 336
    • 0037423392 scopus 로고    scopus 로고
    • Lanthanides potentiate TRPC5 currents by an action at extracellular sites close to the pore mouth
    • Jung S., Muhle A., Schaefer M., Strotmann R., Schultz G., Plant T.D. Lanthanides potentiate TRPC5 currents by an action at extracellular sites close to the pore mouth. J. Biol. Chem. 2003, 278:3562-3571.
    • (2003) J. Biol. Chem. , vol.278 , pp. 3562-3571
    • Jung, S.1    Muhle, A.2    Schaefer, M.3    Strotmann, R.4    Schultz, G.5    Plant, T.D.6
  • 341
    • 11244343900 scopus 로고    scopus 로고
    • Inhibition of TRPM2 channels by the antifungal agents clotrimazole and econazole
    • Hill K., McNulty S., Randall A.D. Inhibition of TRPM2 channels by the antifungal agents clotrimazole and econazole. Naunyn Schmiedebergs Arch. Pharmacol. 2004, 370:227-237.
    • (2004) Naunyn Schmiedebergs Arch. Pharmacol. , vol.370 , pp. 227-237
    • Hill, K.1    McNulty, S.2    Randall, A.D.3
  • 342
    • 3242736642 scopus 로고    scopus 로고
    • Flufenamic acid is a pH-dependent antagonist of TRPM2 channels
    • Hill K., Benham C.D., McNulty S., Randall A.D. Flufenamic acid is a pH-dependent antagonist of TRPM2 channels. Neuropharmacology 2004, 47:450-460.
    • (2004) Neuropharmacology , vol.47 , pp. 450-460
    • Hill, K.1    Benham, C.D.2    McNulty, S.3    Randall, A.D.4
  • 343
    • 33744483084 scopus 로고    scopus 로고
    • Inhibition of TRPM2 cation channels by N-(p-amylcinnamoyl)anthranilic acid
    • Kraft R., Grimm C., Frenzel H., Harteneck C. Inhibition of TRPM2 cation channels by N-(p-amylcinnamoyl)anthranilic acid. Br. J. Pharmacol. 2006, 148:264-273.
    • (2006) Br. J. Pharmacol. , vol.148 , pp. 264-273
    • Kraft, R.1    Grimm, C.2    Frenzel, H.3    Harteneck, C.4
  • 347
  • 349
    • 20144373342 scopus 로고    scopus 로고
    • 2+-activated cation channel TRPM5 involve residues in the S3-S4 and S5-S6 extracellular domains
    • 2+-activated cation channel TRPM5 involve residues in the S3-S4 and S5-S6 extracellular domains. J. Biol. Chem. 2005, 280:20691-20699.
    • (2005) J. Biol. Chem. , vol.280 , pp. 20691-20699
    • Liu, D.1    Zhang, Z.2    Liman, E.R.3
  • 350
    • 34748877218 scopus 로고    scopus 로고
    • Characterisation of TRPM8 as a pharmacophore receptor
    • Bodding M., Wissenbach U., Flockerzi V. Characterisation of TRPM8 as a pharmacophore receptor. Cell Calcium 2007, 42:618-628.
    • (2007) Cell Calcium , vol.42 , pp. 618-628
    • Bodding, M.1    Wissenbach, U.2    Flockerzi, V.3
  • 351
    • 1842453817 scopus 로고    scopus 로고
    • Characterization of the mouse cold-menthol receptor TRPM8 and vanilloid receptor type-1 VR1 using a fluorometric imaging plate reader (FLIPR) assay
    • Behrendt H.J., Germann T., Gillen C., Hatt H., Jostock R. Characterization of the mouse cold-menthol receptor TRPM8 and vanilloid receptor type-1 VR1 using a fluorometric imaging plate reader (FLIPR) assay. Br. J. Pharmacol. 2004, 141:737-745.
    • (2004) Br. J. Pharmacol. , vol.141 , pp. 737-745
    • Behrendt, H.J.1    Germann, T.2    Gillen, C.3    Hatt, H.4    Jostock, R.5
  • 353
    • 23044500197 scopus 로고    scopus 로고
    • Conservation of functional and pharmacological properties in the distantly related temperature sensors TRVP1 and TRPM8
    • Weil A., Moore S.E., Waite N.J., Randall A., Gunthorpe M.J. Conservation of functional and pharmacological properties in the distantly related temperature sensors TRVP1 and TRPM8. Mol. Pharmacol. 2005, 68:518-527.
    • (2005) Mol. Pharmacol. , vol.68 , pp. 518-527
    • Weil, A.1    Moore, S.E.2    Waite, N.J.3    Randall, A.4    Gunthorpe, M.J.5
  • 356
    • 17144418518 scopus 로고    scopus 로고
    • Effects of piperine, the pungent component of black pepper, at the human vanilloid receptor (TRPV1)
    • McNamara F.N., Randall A., Gunthorpe M.J. Effects of piperine, the pungent component of black pepper, at the human vanilloid receptor (TRPV1). Br. J. Pharmacol. 2005, 144:781-790.
    • (2005) Br. J. Pharmacol. , vol.144 , pp. 781-790
    • McNamara, F.N.1    Randall, A.2    Gunthorpe, M.J.3
  • 358
    • 0035173995 scopus 로고    scopus 로고
    • Iodo-resiniferatoxin, a new potent vanilloid receptor antagonist
    • Wahl P., Foged C., Tullin S., Thomsen C. Iodo-resiniferatoxin, a new potent vanilloid receptor antagonist. Mol. Pharmacol. 2001, 59:9-15.
    • (2001) Mol. Pharmacol. , vol.59 , pp. 9-15
    • Wahl, P.1    Foged, C.2    Tullin, S.3    Thomsen, C.4
  • 359
    • 34447134440 scopus 로고    scopus 로고
    • Activation properties of heterologously expressed mammalian TRPV2: evidence for species dependence
    • Neeper M.P., Liu Y., Hutchinson T.L., Wang Y., Flores C.M., Qin N. Activation properties of heterologously expressed mammalian TRPV2: evidence for species dependence. J. Biol. Chem. 2007, 282:15894-15902.
    • (2007) J. Biol. Chem. , vol.282 , pp. 15894-15902
    • Neeper, M.P.1    Liu, Y.2    Hutchinson, T.L.3    Wang, Y.4    Flores, C.M.5    Qin, N.6
  • 360
    • 46749129338 scopus 로고    scopus 로고
    • TRPV2 is activated by cannabidiol and mediates CGRP release in cultured rat dorsal root ganglion neurons
    • Qin N., Neeper M.P., Liu Y., Hutchinson T.L., Lubin M.L., Flores C.M. TRPV2 is activated by cannabidiol and mediates CGRP release in cultured rat dorsal root ganglion neurons. J. Neurosci. 2008, 28:6231-6238.
    • (2008) J. Neurosci. , vol.28 , pp. 6231-6238
    • Qin, N.1    Neeper, M.P.2    Liu, Y.3    Hutchinson, T.L.4    Lubin, M.L.5    Flores, C.M.6
  • 361
    • 34548637630 scopus 로고    scopus 로고
    • Transient receptor potential V2 expressed in sensory neurons is activated by probenecid
    • Bang S., Kim K.Y., Yoo S., Lee S.H., Hwang S.W. Transient receptor potential V2 expressed in sensory neurons is activated by probenecid. Neurosci. Lett. 2007, 425:120-125.
    • (2007) Neurosci. Lett. , vol.425 , pp. 120-125
    • Bang, S.1    Kim, K.Y.2    Yoo, S.3    Lee, S.H.4    Hwang, S.W.5
  • 362
    • 35548936179 scopus 로고    scopus 로고
    • Pharmacological characterization and molecular determinants of the activation of transient receptor potential V2 channel orthologs by 2- aminoethoxydiphenyl borate
    • Juvin V., Penna A., Chemin J., Lin Y.L., Rassendren F.A. Pharmacological characterization and molecular determinants of the activation of transient receptor potential V2 channel orthologs by 2- aminoethoxydiphenyl borate. Mol. Pharmacol. 2007, 72:1258-1268.
    • (2007) Mol. Pharmacol. , vol.72 , pp. 1258-1268
    • Juvin, V.1    Penna, A.2    Chemin, J.3    Lin, Y.L.4    Rassendren, F.A.5
  • 366
    • 0043267987 scopus 로고    scopus 로고
    • Anandamide and arachidonic acid use epoxyeicosatrienoic acids to activate TRPV4 channels
    • Watanabe H., Vriens J., Prenen J., Droogmans G., Voets T., Nilius B. Anandamide and arachidonic acid use epoxyeicosatrienoic acids to activate TRPV4 channels. Nature 2003, 424:434-438.
    • (2003) Nature , vol.424 , pp. 434-438
    • Watanabe, H.1    Vriens, J.2    Prenen, J.3    Droogmans, G.4    Voets, T.5    Nilius, B.6
  • 369
    • 0037061681 scopus 로고    scopus 로고
    • Signaling microdomains define the specificity of receptor-mediated InsP(3) pathways in neurons
    • Delmas P., Wanaverbecq N., Abogadie F.C., Mistry M., Brown D.A. Signaling microdomains define the specificity of receptor-mediated InsP(3) pathways in neurons. Neuron 2002, 34:209-220.
    • (2002) Neuron , vol.34 , pp. 209-220
    • Delmas, P.1    Wanaverbecq, N.2    Abogadie, F.C.3    Mistry, M.4    Brown, D.A.5
  • 370
    • 23844454223 scopus 로고    scopus 로고
    • Endogenous TRPC1, TRPC3, and TRPC7 proteins combine to form native store-operated channels in HEK-293 cells
    • Zagranichnaya T.K., Wu X., Villereal M.L. Endogenous TRPC1, TRPC3, and TRPC7 proteins combine to form native store-operated channels in HEK-293 cells. J. Biol. Chem. 2005, 280:29559-29569.
    • (2005) J. Biol. Chem. , vol.280 , pp. 29559-29569
    • Zagranichnaya, T.K.1    Wu, X.2    Villereal, M.L.3
  • 371
    • 22044432899 scopus 로고    scopus 로고
    • Block of TRPC5 channels by 2-aminoethoxydiphenyl borate: a differential, extracellular and voltage-dependent effect
    • Xu S.Z., Zeng F., Boulay G., Grimm C., Harteneck C., Beech D.J. Block of TRPC5 channels by 2-aminoethoxydiphenyl borate: a differential, extracellular and voltage-dependent effect. Br. J. Pharmacol. 2005, 145:405-414.
    • (2005) Br. J. Pharmacol. , vol.145 , pp. 405-414
    • Xu, S.Z.1    Zeng, F.2    Boulay, G.3    Grimm, C.4    Harteneck, C.5    Beech, D.J.6
  • 372
    • 33645806495 scopus 로고    scopus 로고
    • Protection of TRPC7 cation channels from calcium inhibition by closely associated SERCA pumps
    • Lemonnier L., Trebak M., Lievremont J.P., Bird G.S., Putney J.W. Protection of TRPC7 cation channels from calcium inhibition by closely associated SERCA pumps. FASEB J. 2006, 20:503-505.
    • (2006) FASEB J. , vol.20 , pp. 503-505
    • Lemonnier, L.1    Trebak, M.2    Lievremont, J.P.3    Bird, G.S.4    Putney, J.W.5
  • 373
    • 40949124783 scopus 로고    scopus 로고
    • Inhibition of the transient receptor potential cation channel TRPM2 by 2-aminoethoxydiphenyl borate (2-APB)
    • Togashi K., Inada H., Tominaga M. Inhibition of the transient receptor potential cation channel TRPM2 by 2-aminoethoxydiphenyl borate (2-APB). Br. J. Pharmacol. 2008, 153:1324-1330.
    • (2008) Br. J. Pharmacol. , vol.153 , pp. 1324-1330
    • Togashi, K.1    Inada, H.2    Tominaga, M.3
  • 374
    • 60849098730 scopus 로고    scopus 로고
    • Two amino acid residues determine 2-APB sensitivity of the ion channels TRPV3 and TRPV4
    • Hu H., Grandl J., Bandell M., Petrus M., Patapoutian A. Two amino acid residues determine 2-APB sensitivity of the ion channels TRPV3 and TRPV4. Proc. Natl. Acad. Sci. USA 2009, 106:1626-1631.
    • (2009) Proc. Natl. Acad. Sci. USA , vol.106 , pp. 1626-1631
    • Hu, H.1    Grandl, J.2    Bandell, M.3    Petrus, M.4    Patapoutian, A.5
  • 376
    • 33744955626 scopus 로고    scopus 로고
    • Dissociation of regulated trafficking of TRPC3 channels to the plasma membrane from their activation by phospholipase C
    • Smyth J.T., Lemonnier L., Vazquez G., Bird G.S., Putney J.W. Dissociation of regulated trafficking of TRPC3 channels to the plasma membrane from their activation by phospholipase C. J. Biol. Chem. 2006, 281:11712-11720.
    • (2006) J. Biol. Chem. , vol.281 , pp. 11712-11720
    • Smyth, J.T.1    Lemonnier, L.2    Vazquez, G.3    Bird, G.S.4    Putney, J.W.5
  • 378
    • 33845956224 scopus 로고    scopus 로고
    • Homer 1 mediates store- and inositol 1,4,5-trisphosphate receptor-dependent translocation and retrieval of TRPC3 to the plasma membrane
    • Kim J.Y., Zeng W., Kiselyov K., Yuan J.P., Dehoff M.H., Mikoshiba K., Worley P.F., Muallem S. Homer 1 mediates store- and inositol 1,4,5-trisphosphate receptor-dependent translocation and retrieval of TRPC3 to the plasma membrane. J. Biol. Chem. 2006, 281:32540-32549.
    • (2006) J. Biol. Chem. , vol.281 , pp. 32540-32549
    • Kim, J.Y.1    Zeng, W.2    Kiselyov, K.3    Yuan, J.P.4    Dehoff, M.H.5    Mikoshiba, K.6    Worley, P.F.7    Muallem, S.8
  • 383
  • 385
    • 65649098394 scopus 로고    scopus 로고
    • The mechanosensitive cell line ND-C does not express functional thermoTRP channels
    • Rugiero F., Wood J.N. The mechanosensitive cell line ND-C does not express functional thermoTRP channels. Neuropharmacology 2009, 56:1138-1146.
    • (2009) Neuropharmacology , vol.56 , pp. 1138-1146
    • Rugiero, F.1    Wood, J.N.2
  • 387
    • 57049153922 scopus 로고    scopus 로고
    • Hypoosmotic- and pressureinduced membrane stretch activate TRPC5 channels
    • Gomis A., Soriano S., Belmonte C., Viana F. Hypoosmotic- and pressureinduced membrane stretch activate TRPC5 channels. J. Physiol. 2008, 586:5633-5649.
    • (2008) J. Physiol. , vol.586 , pp. 5633-5649
    • Gomis, A.1    Soriano, S.2    Belmonte, C.3    Viana, F.4
  • 388
    • 34247372291 scopus 로고    scopus 로고
    • Membrane stretch-induced activation of a TRPM4-like nonselective cation channel in cerebral artery myocytes
    • Morita H., Honda A., Inoue R., Ito Y., Abe K., Nelson M.T., Brayden J.E. Membrane stretch-induced activation of a TRPM4-like nonselective cation channel in cerebral artery myocytes. J. Pharmacol. Sci. 2007, 103:417-426.
    • (2007) J. Pharmacol. Sci. , vol.103 , pp. 417-426
    • Morita, H.1    Honda, A.2    Inoue, R.3    Ito, Y.4    Abe, K.5    Nelson, M.T.6    Brayden, J.E.7
  • 389
    • 34547100281 scopus 로고    scopus 로고
    • TRPM7 channel is sensitive to osmotic gradients in human kidney cells
    • Bessac B.F., Fleig A. TRPM7 channel is sensitive to osmotic gradients in human kidney cells. J. Physiol. 2007, 582:1073-1086.
    • (2007) J. Physiol. , vol.582 , pp. 1073-1086
    • Bessac, B.F.1    Fleig, A.2
  • 390
    • 29444456617 scopus 로고    scopus 로고
    • An N-terminal variant of Trpv1 channel is required for osmosensory transduction
    • Sharif N.R., Witty M.F., Seguela P., Bourque C.W. An N-terminal variant of Trpv1 channel is required for osmosensory transduction. Nat. Neurosci. 2006, 9:93-98.
    • (2006) Nat. Neurosci. , vol.9 , pp. 93-98
    • Sharif, N.R.1    Witty, M.F.2    Seguela, P.3    Bourque, C.W.4
  • 397
    • 33645325125 scopus 로고    scopus 로고
    • TRPM7 channel is regulated by magnesium nucleotides via its kinase domain
    • Demeuse P., Penner R., Fleig A. TRPM7 channel is regulated by magnesium nucleotides via its kinase domain. J. Gen. Physiol. 2006, 127:421-434.
    • (2006) J. Gen. Physiol. , vol.127 , pp. 421-434
    • Demeuse, P.1    Penner, R.2    Fleig, A.3
  • 400
    • 37549038688 scopus 로고    scopus 로고
    • Three-dimensional 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. Three-dimensional reconstruction using transmission electron microscopy reveals a swollen, bell-shaped structure of transient receptor potential melastatin type 2 cation channel. J. Biol. Chem. 2007, 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
  • 401
    • 34250190946 scopus 로고    scopus 로고
    • The ankyrin repeats of TRPV1 bind multiple ligands and modulate channel sensitivity
    • Lishko P.V., Procko E., Jin X., Phelps C.B., Gaudet R. The ankyrin repeats of TRPV1 bind multiple ligands and modulate channel sensitivity. Neuron 2007, 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


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.