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Volumn 12, Issue 3, 2011, Pages

The transient receptor potential family of ion channels

Author keywords

[No Author keywords available]

Indexed keywords

ION CHANNEL; POLYCYSTIN; TRANSIENT RECEPTOR POTENTIAL CHANNEL; TRANSIENT RECEPTOR POTENTIAL CHANNEL 1; TRANSIENT RECEPTOR POTENTIAL CHANNEL 2; TRANSIENT RECEPTOR POTENTIAL CHANNEL 3; TRANSIENT RECEPTOR POTENTIAL CHANNEL 4; TRANSIENT RECEPTOR POTENTIAL CHANNEL 5; TRANSIENT RECEPTOR POTENTIAL CHANNEL 6; TRANSIENT RECEPTOR POTENTIAL CHANNEL 7; TRANSIENT RECEPTOR POTENTIAL CHANNEL A1; TRANSIENT RECEPTOR POTENTIAL CHANNEL C; TRANSIENT RECEPTOR POTENTIAL CHANNEL M; TRANSIENT RECEPTOR POTENTIAL CHANNEL M1; TRANSIENT RECEPTOR POTENTIAL CHANNEL M2; TRANSIENT RECEPTOR POTENTIAL CHANNEL M3; TRANSIENT RECEPTOR POTENTIAL CHANNEL M4; TRANSIENT RECEPTOR POTENTIAL CHANNEL M5; TRANSIENT RECEPTOR POTENTIAL CHANNEL M6; TRANSIENT RECEPTOR POTENTIAL CHANNEL M7; TRANSIENT RECEPTOR POTENTIAL CHANNEL M8; UNINDEXED DRUG; VANILLOID RECEPTOR; VANILLOID RECEPTOR 1; VANILLOID RECEPTOR 2; VANILLOID RECEPTOR 3; VANILLOID RECEPTOR 4; VANILLOID RECEPTOR 5; VANILLOID RECEPTOR 6; VOLTAGE DEPENDENT ANION CHANNEL;

EID: 79952683619     PISSN: 14747596     EISSN: 1474760X     Source Type: Journal    
DOI: 10.1186/gb-2011-12-3-218     Document Type: Review
Times cited : (689)

References (106)
  • 1
    • 0014683485 scopus 로고
    • Abnormal electroretinogram from a Drosophila mutant.
    • 10.1038/224285a0, 5344615
    • Cosens DJ, Manning A. Abnormal electroretinogram from a Drosophila mutant. Nature 1969, 224:285-287. 10.1038/224285a0, 5344615.
    • (1969) Nature , vol.224 , pp. 285-287
    • Cosens, D.J.1    Manning, A.2
  • 2
    • 0024642547 scopus 로고
    • Molecular characterization of the Drosophila trp locus: a putative integral membrane protein required for phototransduction.
    • 10.1016/0896-6273(89)90069-X, 2516726
    • Montell C, Rubin GM. Molecular characterization of the Drosophila trp locus: a putative integral membrane protein required for phototransduction. Neuron 1989, 2:1313-1323. 10.1016/0896-6273(89)90069-X, 2516726.
    • (1989) Neuron , vol.2 , pp. 1313-1323
    • Montell, C.1    Rubin, G.M.2
  • 3
    • 0026583241 scopus 로고
    • The trp gene is essential for a light-activated Ca2+ channel in Drosophila photoreceptors.
    • 10.1016/0896-6273(92)90086-S, 1314617
    • Hardie RC, Minke B. The trp gene is essential for a light-activated Ca2+ channel in Drosophila photoreceptors. Neuron 1992, 8:643-651. 10.1016/0896-6273(92)90086-S, 1314617.
    • (1992) Neuron , vol.8 , pp. 643-651
    • Hardie, R.C.1    Minke, B.2
  • 4
    • 77956272001 scopus 로고    scopus 로고
    • International Union of Basic and Clinical Pharmacology. LXXVI. Current progress in the mammalian TRP ion channel family.
    • 10.1124/pr.110.002725, 20716668
    • Wu LJ, Sweet TB, Clapham DE. International Union of Basic and Clinical Pharmacology. LXXVI. Current progress in the mammalian TRP ion channel family. Pharmacol Rev 2010, 62:381-404. 10.1124/pr.110.002725, 20716668.
    • (2010) Pharmacol Rev , vol.62 , pp. 381-404
    • Wu, L.J.1    Sweet, T.B.2    Clapham, D.E.3
  • 5
    • 0037710542 scopus 로고    scopus 로고
    • NompC TRP channel required for vertebrate sensory hair cell mechanotransduction.
    • 10.1126/science.1084370, 12805553
    • Sidi S, Friedrich RW, Nicolson T. NompC TRP channel required for vertebrate sensory hair cell mechanotransduction. Science 2003, 301:96-99. 10.1126/science.1084370, 12805553.
    • (2003) Science , vol.301 , pp. 96-99
    • Sidi, S.1    Friedrich, R.W.2    Nicolson, T.3
  • 6
    • 2942741365 scopus 로고    scopus 로고
    • Only six kingdoms of life.
    • 10.1098/rspb.2004.2705, 1691724, 15306349
    • Cavalier-Smith T. Only six kingdoms of life. Proc Biol Sci 2004, 271:1251-1262. 10.1098/rspb.2004.2705, 1691724, 15306349.
    • (2004) Proc Biol Sci , vol.271 , pp. 1251-1262
    • Cavalier-Smith, T.1
  • 7
    • 50349089617 scopus 로고    scopus 로고
    • Ca(2+) signalling in plants and green algae - changing channels.
    • 10.1016/j.tplants.2008.06.004, 18703378
    • Wheeler GL, Brownlee C. Ca(2+) signalling in plants and green algae - changing channels. Trends Plant Sci 2008, 13:506-514. 10.1016/j.tplants.2008.06.004, 18703378.
    • (2008) Trends Plant Sci , vol.13 , pp. 506-514
    • Wheeler, G.L.1    Brownlee, C.2
  • 8
    • 34848839244 scopus 로고    scopus 로고
    • Yeast screens show aromatic residues at the end of the sixth helix anchor transient receptor potential channel gate.
    • 10.1073/pnas.0704039104, 2000494, 17878311
    • Zhou X, Su Z, Anishkin A, Haynes WJ, Friske EM, Loukin SH, Kung C, Saimi Y. Yeast screens show aromatic residues at the end of the sixth helix anchor transient receptor potential channel gate. Proc Natl Acad Sci USA 2007, 104:15555-15559. 10.1073/pnas.0704039104, 2000494, 17878311.
    • (2007) Proc Natl Acad Sci USA , vol.104 , pp. 15555-15559
    • Zhou, X.1    Su, Z.2    Anishkin, A.3    Haynes, W.J.4    Friske, E.M.5    Loukin, S.H.6    Kung, C.7    Saimi, Y.8
  • 9
    • 37649002371 scopus 로고    scopus 로고
    • Yeast gain-of-function mutations reveal structure-function relationships conserved among different subfamilies of transient receptor potential channels.
    • 10.1073/pnas.0708584104, 2148336, 18042709
    • Su Z, Zhou X, Haynes WJ, Loukin SH, Anishkin A, Saimi Y, Kung C. Yeast gain-of-function mutations reveal structure-function relationships conserved among different subfamilies of transient receptor potential channels. Proc Natl Acad Sci USA 2007, 104:19607-19612. 10.1073/pnas.0708584104, 2148336, 18042709.
    • (2007) Proc Natl Acad Sci USA , vol.104 , pp. 19607-19612
    • Su, Z.1    Zhou, X.2    Haynes, W.J.3    Loukin, S.H.4    Anishkin, A.5    Saimi, Y.6    Kung, C.7
  • 10
    • 42949117400 scopus 로고    scopus 로고
    • A yeast genetic screen reveals a critical role for the pore helix domain in TRP channel gating.
    • 10.1016/j.neuron.2008.04.012, 2422846, 18466747
    • Myers BR, Bohlen CJ, Julius D. A yeast genetic screen reveals a critical role for the pore helix domain in TRP channel gating. Neuron 2008, 58:362-373. 10.1016/j.neuron.2008.04.012, 2422846, 18466747.
    • (2008) Neuron , vol.58 , pp. 362-373
    • Myers, B.R.1    Bohlen, C.J.2    Julius, D.3
  • 11
    • 77952668567 scopus 로고    scopus 로고
    • Properties of the intracellular transient receptor potential (TRP) channel in yeast, Yvc1.
    • 10.1016/j.febslet.2009.12.035, 20035756
    • Chang Y, Schlenstedt G, Flockerzi V, Beck A. Properties of the intracellular transient receptor potential (TRP) channel in yeast, Yvc1. FEBS Lett 2010, 584:2028-2032. 10.1016/j.febslet.2009.12.035, 20035756.
    • (2010) FEBS Lett , vol.584 , pp. 2028-2032
    • Chang, Y.1    Schlenstedt, G.2    Flockerzi, V.3    Beck, A.4
  • 12
    • 68149126541 scopus 로고    scopus 로고
    • The use of yeast to understand TRP-channel mechanosensitivity.
    • 10.1007/s00424-009-0680-0, 19462180
    • Su Z, Zhou X, Loukin SH, Haynes WJ, Saimi Y, Kung C. The use of yeast to understand TRP-channel mechanosensitivity. Pflugers Arch 2009, 458:861-867. 10.1007/s00424-009-0680-0, 19462180.
    • (2009) Pflugers Arch , vol.458 , pp. 861-867
    • Su, Z.1    Zhou, X.2    Loukin, S.H.3    Haynes, W.J.4    Saimi, Y.5    Kung, C.6
  • 13
    • 60849091022 scopus 로고    scopus 로고
    • Mechanical force and cytoplasmic Ca(2+) activate yeast TRPY1 in parallel.
    • 10.1007/s00232-009-9153-9, 19219385
    • Su Z, Zhou X, Loukin SH, Saimi Y, Kung C. Mechanical force and cytoplasmic Ca(2+) activate yeast TRPY1 in parallel. J Membr Biol 2009, 227:141-150. 10.1007/s00232-009-9153-9, 19219385.
    • (2009) J Membr Biol , vol.227 , pp. 141-150
    • Su, Z.1    Zhou, X.2    Loukin, S.H.3    Saimi, Y.4    Kung, C.5
  • 14
    • 0034934074 scopus 로고    scopus 로고
    • A TRP homolog in Saccharomyces cerevisiae forms an intracellular Ca2+- permeable channel in the yeast vacuolar membrane.
    • 10.1073/pnas.141036198, 35422, 11427713
    • Palmer CP, Zhou XL, Lin J, Loukin SH, Kung C, Saimi Y. A TRP homolog in Saccharomyces cerevisiae forms an intracellular Ca2+- permeable channel in the yeast vacuolar membrane. Proc Natl Acad Sci USA 2001, 98:7801-7805. 10.1073/pnas.141036198, 35422, 11427713.
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 7801-7805
    • Palmer, C.P.1    Zhou, X.L.2    Lin, J.3    Loukin, S.H.4    Kung, C.5    Saimi, Y.6
  • 15
    • 0037033784 scopus 로고    scopus 로고
    • Internal Ca2+ release in yeast is triggered by hypertonic shock and mediated by a TRP channel homologue.
    • 10.1083/jcb.200111004, 2173594, 11781332
    • Denis V, Cyert MS. Internal Ca2+ release in yeast is triggered by hypertonic shock and mediated by a TRP channel homologue. J Cell Biol 2002, 156:29-34. 10.1083/jcb.200111004, 2173594, 11781332.
    • (2002) J Cell Biol , vol.156 , pp. 29-34
    • Denis, V.1    Cyert, M.S.2
  • 16
    • 45849109876 scopus 로고    scopus 로고
    • Unicellular Ca2+ signaling 'toolkit' at the origin of metazoa.
    • 10.1093/molbev/msn077, 18385221
    • Cai X. Unicellular Ca2+ signaling 'toolkit' at the origin of metazoa. Mol Biol Evol 2008, 25:1357-1361. 10.1093/molbev/msn077, 18385221.
    • (2008) Mol Biol Evol , vol.25 , pp. 1357-1361
    • Cai, X.1
  • 17
    • 0037188517 scopus 로고    scopus 로고
    • Subunit composition of mammalian transient receptor potential channels in living cells.
    • 10.1073/pnas.102596199, 124253, 12032305
    • 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. 10.1073/pnas.102596199, 124253, 12032305.
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 7461-7466
    • Hofmann, T.1    Schaefer, M.2    Schultz, G.3    Gudermann, T.4
  • 18
    • 33646842722 scopus 로고    scopus 로고
    • Structure-function relationship of the TRP channel superfamily.
    • full_text, 16634147
    • Owsianik G, D'Hoedt D, Voets T, Nilius B. Structure-function relationship of the TRP channel superfamily. Rev Physiol Biochem Pharmacol 2006, 156:61-90. full_text, 16634147.
    • (2006) Rev Physiol Biochem Pharmacol , vol.156 , pp. 61-90
    • Owsianik, G.1    D'Hoedt, D.2    Voets, T.3    Nilius, B.4
  • 19
    • 48549095714 scopus 로고    scopus 로고
    • TRP channels entering the structural era.
    • 10.1113/jphysiol.2008.155812, 2538826, 18535090
    • Gaudet R. TRP channels entering the structural era. J Physiol 2008, 586:3565-3575. 10.1113/jphysiol.2008.155812, 2538826, 18535090.
    • (2008) J Physiol , vol.586 , pp. 3565-3575
    • Gaudet, R.1
  • 20
    • 33847157855 scopus 로고    scopus 로고
    • The TRPC3 channel has a large internal chamber surrounded by signal sensing antennas.
    • 10.1016/j.jmb.2006.12.043, 17258231
    • Mio K, Ogura T, Kiyonaka S, Hiroaki Y, Tanimura Y, Fujiyoshi Y, Mori Y, Sato C. The TRPC3 channel has a large internal chamber surrounded by signal sensing antennas. J Mol Biol 2007, 367:373-383. 10.1016/j.jmb.2006.12.043, 17258231.
    • (2007) J Mol Biol , vol.367 , pp. 373-383
    • Mio, K.1    Ogura, T.2    Kiyonaka, S.3    Hiroaki, Y.4    Tanimura, Y.5    Fujiyoshi, Y.6    Mori, Y.7    Sato, C.8
  • 22
    • 0035131504 scopus 로고    scopus 로고
    • TRP-PLIK, a bifunctional protein with kinase and ion channel activities.
    • 10.1126/science.1058519, 11161216
    • Runnels LW, Yue L, Clapham DE. TRP-PLIK, a bifunctional protein with kinase and ion channel activities. Science 2001, 291:1043-1047. 10.1126/science.1058519, 11161216.
    • (2001) Science , vol.291 , pp. 1043-1047
    • Runnels, L.W.1    Yue, L.2    Clapham, D.E.3
  • 24
    • 42349109026 scopus 로고    scopus 로고
    • A primer on ankyrin repeat function in TRP channels and beyond.
    • 10.1039/b801481g, 3006086, 18414734
    • Gaudet R. A primer on ankyrin repeat function in TRP channels and beyond. Mol Biosyst 2008, 4:372-379. 10.1039/b801481g, 3006086, 18414734.
    • (2008) Mol Biosyst , vol.4 , pp. 372-379
    • Gaudet, R.1
  • 25
    • 33748748066 scopus 로고    scopus 로고
    • Structure of the N-terminal ankyrin repeat domain of the TRPV2 ion channel.
    • 10.1074/jbc.C600153200, 16809337
    • 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. 10.1074/jbc.C600153200, 16809337.
    • (2006) J Biol Chem , vol.281 , pp. 25006-25010
    • Jin, X.1    Touhey, J.2    Gaudet, R.3
  • 26
    • 64549108500 scopus 로고    scopus 로고
    • Divide and conquer: high resolution structural information on TRP channel fragments.
    • 10.1085/jgp.200810137, 2654082, 19237587
    • Gaudet R. Divide and conquer: high resolution structural information on TRP channel fragments. J Gen Physiol 2009, 133:231-237. 10.1085/jgp.200810137, 2654082, 19237587.
    • (2009) J Gen Physiol , vol.133 , pp. 231-237
    • Gaudet, R.1
  • 27
  • 29
    • 78751470131 scopus 로고    scopus 로고
    • The role of transient receptor potential cation channels in Ca2+ signaling.
    • 10.1101/cshperspect.a003962, 20861159
    • Gees M, Colsoul B, Nilius B. The role of transient receptor potential cation channels in Ca2+ signaling. Cold Spring Harb Perspect Biol 2010, 2:a003962. 10.1101/cshperspect.a003962, 20861159.
    • (2010) Cold Spring Harb Perspect Biol , vol.2
    • Gees, M.1    Colsoul, B.2    Nilius, B.3
  • 30
    • 33846807748 scopus 로고    scopus 로고
    • Transient receptor potential cation channels in disease.
    • 10.1152/physrev.00021.2006, 17237345
    • Nilius B, Owsianik G, Voets T, Peters JA. Transient receptor potential cation channels in disease. Physiol Rev 2007, 87:165-217. 10.1152/physrev.00021.2006, 17237345.
    • (2007) Physiol Rev , vol.87 , pp. 165-217
    • Nilius, B.1    Owsianik, G.2    Voets, T.3    Peters, J.A.4
  • 31
    • 77955569436 scopus 로고    scopus 로고
    • Transient receptor potential channelopathies.
    • 10.1007/s00424-010-0788-2, 20127491
    • Nilius B, Owsianik G. Transient receptor potential channelopathies. Pflugers Arch 2010, 460:437-450. 10.1007/s00424-010-0788-2, 20127491.
    • (2010) Pflugers Arch , vol.460 , pp. 437-450
    • Nilius, B.1    Owsianik, G.2
  • 32
    • 28244495051 scopus 로고    scopus 로고
    • TRPC6 - a new podocyte gene involved in focal segmental glomerulosclerosis.
    • 10.1016/j.molmed.2005.10.001, 16290061
    • Kriz W. TRPC6 - a new podocyte gene involved in focal segmental glomerulosclerosis. Trends Mol Med 2005, 11:527-530. 10.1016/j.molmed.2005.10.001, 16290061.
    • (2005) Trends Mol Med , vol.11 , pp. 527-530
    • Kriz, W.1
  • 38
    • 75749129058 scopus 로고    scopus 로고
    • Channelopathies converge on TRPV4.
    • 10.1038/ng0210-98, 20104247
    • Nilius B, Owsianik G. Channelopathies converge on TRPV4. Nat Genet 2010, 42:98-100. 10.1038/ng0210-98, 20104247.
    • (2010) Nat Genet , vol.42 , pp. 98-100
    • Nilius, B.1    Owsianik, G.2
  • 40
    • 1642515793 scopus 로고    scopus 로고
    • Transcriptional regulation of the melanoma prognostic marker melastatin (TRPM1) by MITF in melanocytes and melanoma.
    • 10.1158/0008-5472.CAN-03-2440, 14744763
    • Miller AJ, Du J, Rowan S, Hershey CL, Widlund HR, Fisher DE. Transcriptional regulation of the melanoma prognostic marker melastatin (TRPM1) by MITF in melanocytes and melanoma. Cancer Res 2004, 64:509-516. 10.1158/0008-5472.CAN-03-2440, 14744763.
    • (2004) Cancer Res , vol.64 , pp. 509-516
    • Miller, A.J.1    Du, J.2    Rowan, S.3    Hershey, C.L.4    Widlund, H.R.5    Fisher, D.E.6
  • 44
    • 55749100524 scopus 로고    scopus 로고
    • Differential gene expression of TRPM1, the potential cause of congenital stationary night blindness and coat spotting patterns (LP) in the Appaloosa horse (Equus caballus).
    • 10.1534/genetics.108.088807, 2516064, 18660533
    • Bellone RR, Brooks SA, Sandmeyer L, Murphy BA, Forsyth G, Archer S, Bailey E, Grahn B. Differential gene expression of TRPM1, the potential cause of congenital stationary night blindness and coat spotting patterns (LP) in the Appaloosa horse (Equus caballus). Genetics 2008, 179:1861-1870. 10.1534/genetics.108.088807, 2516064, 18660533.
    • (2008) Genetics , vol.179 , pp. 1861-1870
    • Bellone, R.R.1    Brooks, S.A.2    Sandmeyer, L.3    Murphy, B.A.4    Forsyth, G.5    Archer, S.6    Bailey, E.7    Grahn, B.8
  • 45
    • 67651146417 scopus 로고    scopus 로고
    • Isolation of ON bipolar cell genes via hrGFP-coupled cell enrichment using the mGluR6 promoter.
    • 10.1093/jb/mvp038, 19270057
    • Nakajima Y, Moriyama M, Hattori M, Minato N, Nakanishi S. Isolation of ON bipolar cell genes via hrGFP-coupled cell enrichment using the mGluR6 promoter. J Biochem 2009, 145:811-818. 10.1093/jb/mvp038, 19270057.
    • (2009) J Biochem , vol.145 , pp. 811-818
    • Nakajima, Y.1    Moriyama, M.2    Hattori, M.3    Minato, N.4    Nakanishi, S.5
  • 47
    • 71849089234 scopus 로고    scopus 로고
    • Recessive mutations of the gene TRPM1 abrogate ON bipolar cell function and cause complete congenital stationary night blindness in humans.
    • 10.1016/j.ajhg.2009.10.003, 2775833, 19878917
    • Li Z, Sergouniotis PI, Michaelides M, Mackay DS, Wright GA, Devery S, Moore AT, Holder GE, Robson AG, Webster AR. Recessive mutations of the gene TRPM1 abrogate ON bipolar cell function and cause complete congenital stationary night blindness in humans. Am J Hum Genet 2009, 85:711-719. 10.1016/j.ajhg.2009.10.003, 2775833, 19878917.
    • (2009) Am J Hum Genet , vol.85 , pp. 711-719
    • Li, Z.1    Sergouniotis, P.I.2    Michaelides, M.3    Mackay, D.S.4    Wright, G.A.5    Devery, S.6    Moore, A.T.7    Holder, G.E.8    Robson, A.G.9    Webster, A.R.10
  • 48
    • 70349215874 scopus 로고    scopus 로고
    • Impaired endocytosis of the ion channel TRPM4 is associated with human progressive familial heart block type I.
    • 10.1172/JCI38292, 2735920, 19726882
    • Kruse M, Schulze-Bahr E, Corfield V, Beckmann A, Stallmeyer B, Kurtbay G, Ohmert I, Brink P, Pongs O. Impaired endocytosis of the ion channel TRPM4 is associated with human progressive familial heart block type I. J Clin Invest 2009, 119:2737-2744. 10.1172/JCI38292, 2735920, 19726882.
    • (2009) J Clin Invest , vol.119 , pp. 2737-2744
    • Kruse, M.1    Schulze-Bahr, E.2    Corfield, V.3    Beckmann, A.4    Stallmeyer, B.5    Kurtbay, G.6    Ohmert, I.7    Brink, P.8    Pongs, O.9
  • 51
    • 0347683487 scopus 로고    scopus 로고
    • TRPM6 forms the Mg2+ influx channel involved in intestinal and renal Mg2+ absorption.
    • 10.1074/jbc.M311201200, 14576148
    • Voets T, Nilius B, Hoefs S, van der Kemp AW, Droogmans G, Bindels RJ, Hoenderop JG. TRPM6 forms the Mg2+ influx channel involved in intestinal and renal Mg2+ absorption. J Biol Chem 2004, 279:19-25. 10.1074/jbc.M311201200, 14576148.
    • (2004) J Biol Chem , vol.279 , pp. 19-25
    • Voets, T.1    Nilius, B.2    Hoefs, S.3    van der Kemp, A.W.4    Droogmans, G.5    Bindels, R.J.6    Hoenderop, J.G.7
  • 53
    • 26444446487 scopus 로고    scopus 로고
    • Mucolipin 1: endocytosis and cation channel-a review.
    • 10.1007/s00424-004-1361-7, 15570434
    • Bach G. Mucolipin 1: endocytosis and cation channel-a review. Pflugers Arch 2005, 451:313-317. 10.1007/s00424-004-1361-7, 15570434.
    • (2005) Pflugers Arch , vol.451 , pp. 313-317
    • Bach, G.1
  • 54
    • 77949696020 scopus 로고    scopus 로고
    • Mucolipins: intracellular TRPML1-3 channels.
    • 10.1016/j.febslet.2009.12.056, 20074572
    • Cheng X, Shen D, Samie M, Xu H. Mucolipins: intracellular TRPML1-3 channels. FEBS Lett 2010, 584:2013-2021. 10.1016/j.febslet.2009.12.056, 20074572.
    • (2010) FEBS Lett , vol.584 , pp. 2013-2021
    • Cheng, X.1    Shen, D.2    Samie, M.3    Xu, H.4
  • 55
    • 66449121620 scopus 로고    scopus 로고
    • TRPMLs: in sickness and in health.
    • 10.1152/ajprenal.90522.2008, 2692446, 19158345
    • Puertollano R, Kiselyov K. TRPMLs: in sickness and in health. Am J Physiol Renal Physiol 2009, 296:F1245-1254. 10.1152/ajprenal.90522.2008, 2692446, 19158345.
    • (2009) Am J Physiol Renal Physiol , vol.296
    • Puertollano, R.1    Kiselyov, K.2
  • 56
    • 0027354899 scopus 로고
    • Polycystic kidney disease: hereditary and acquired.
    • Grantham JJ. Polycystic kidney disease: hereditary and acquired. Adv Intern Med 1993, 38:409-420.
    • (1993) Adv Intern Med , vol.38 , pp. 409-420
    • Grantham, J.J.1
  • 59
    • 4043077669 scopus 로고    scopus 로고
    • The principle of temperature-dependent gating in cold- and heat-sensitive TRP channels.
    • 10.1038/nature02732, 15306801
    • 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. 10.1038/nature02732, 15306801.
    • (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
  • 61
    • 33847050898 scopus 로고    scopus 로고
    • TRPM8 voltage sensor mutants reveal a mechanism for integrating thermal and chemical stimuli.
    • 10.1038/nchembio862, 17293875
    • 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. 10.1038/nchembio862, 17293875.
    • (2007) Nat Chem Biol , vol.3 , pp. 174-182
    • Voets, T.1    Owsianik, G.2    Janssens, A.3    Talavera, K.4    Nilius, B.5
  • 62
    • 43249120882 scopus 로고    scopus 로고
    • The taste transduction channel TRPM5 is a locus for bitter-sweet taste interactions.
    • 10.1096/fj.07-9591com, 18070821
    • Talavera K, Yasumatsu K, Yoshida R, Margolskee RF, Voets T, Ninomiya Y, Nilius B. The taste transduction channel TRPM5 is a locus for bitter-sweet taste interactions. FASEB J 2008, 22:1343-1355. 10.1096/fj.07-9591com, 18070821.
    • (2008) FASEB J , vol.22 , pp. 1343-1355
    • Talavera, K.1    Yasumatsu, K.2    Yoshida, R.3    Margolskee, R.F.4    Voets, T.5    Ninomiya, Y.6    Nilius, B.7
  • 63
    • 52549112698 scopus 로고    scopus 로고
    • Modulation of the transient receptor potential channel TRPA1 by phosphatidylinositol 4,5-biphosphate manipulators.
    • 10.1007/s00424-008-0493-6, 18461353
    • Karashima Y, Prenen J, Meseguer V, Owsianik G, Voets T, Nilius B. Modulation of the transient receptor potential channel TRPA1 by phosphatidylinositol 4,5-biphosphate manipulators. Pflugers Arch 2008, 457:77-89. 10.1007/s00424-008-0493-6, 18461353.
    • (2008) Pflugers Arch , vol.457 , pp. 77-89
    • Karashima, Y.1    Prenen, J.2    Meseguer, V.3    Owsianik, G.4    Voets, T.5    Nilius, B.6
  • 64
    • 42949125051 scopus 로고    scopus 로고
    • Pirt, a phosphoinositide-binding protein, functions as a regulatory subunit of TRPV1.
    • 10.1016/j.cell.2008.02.053, 2605970, 18455988
    • Kim AY, Tang Z, Liu Q, Patel KN, Maag D, Geng Y, Dong X. Pirt, a phosphoinositide-binding protein, functions as a regulatory subunit of TRPV1. Cell 2008, 133:475-485. 10.1016/j.cell.2008.02.053, 2605970, 18455988.
    • (2008) Cell , vol.133 , pp. 475-485
    • Kim, A.Y.1    Tang, Z.2    Liu, Q.3    Patel, K.N.4    Maag, D.5    Geng, Y.6    Dong, X.7
  • 65
    • 33750524257 scopus 로고    scopus 로고
    • Phosphoinositide 3-kinase binds to TRPV1 and mediates NGF-stimulated TRPV1 trafficking to the plasma membrane.
    • 10.1085/jgp.200609576, 2151588, 17074976
    • Stein AT, Ufret-Vincenty CA, Hua L, Santana LF, Gordon SE. Phosphoinositide 3-kinase binds to TRPV1 and mediates NGF-stimulated TRPV1 trafficking to the plasma membrane. J Gen Physiol 2006, 128:509-522. 10.1085/jgp.200609576, 2151588, 17074976.
    • (2006) J Gen Physiol , vol.128 , pp. 509-522
    • Stein, A.T.1    Ufret-Vincenty, C.A.2    Hua, L.3    Santana, L.F.4    Gordon, S.E.5
  • 66
    • 55549104701 scopus 로고    scopus 로고
    • Transient receptor potential channels meet phosphoinositides.
    • 10.1038/emboj.2008.217, 2570475, 18923420
    • Nilius B, Owsianik G, Voets T. Transient receptor potential channels meet phosphoinositides. EMBO J 2008, 27:2809-2816. 10.1038/emboj.2008.217, 2570475, 18923420.
    • (2008) EMBO J , vol.27 , pp. 2809-2816
    • Nilius, B.1    Owsianik, G.2    Voets, T.3
  • 67
    • 34548658196 scopus 로고    scopus 로고
    • Regulation of transient receptor potential (trp) channels by phosphoinositides.
    • 10.1007/s00424-007-0275-6, 17479281
    • Rohacs T, Nilius B. Regulation of transient receptor potential (trp) channels by phosphoinositides. Pflugers Arch 2007, 455:157-168. 10.1007/s00424-007-0275-6, 17479281.
    • (2007) Pflugers Arch , vol.455 , pp. 157-168
    • Rohacs, T.1    Nilius, B.2
  • 68
    • 34547116182 scopus 로고    scopus 로고
    • Modulation of TRPs by PIPs.
    • 10.1113/jphysiol.2007.132522, 2075259, 17395625
    • Voets T, Nilius B. Modulation of TRPs by PIPs. J Physiol 2007, 582:939-944. 10.1113/jphysiol.2007.132522, 2075259, 17395625.
    • (2007) J Physiol , vol.582 , pp. 939-944
    • Voets, T.1    Nilius, B.2
  • 69
    • 14044261739 scopus 로고    scopus 로고
    • Functional control of cold- and menthol-sensitive TRPM8 ion channels by phosphatidylinositol 4,5-bisphosphate.
    • 10.1523/JNEUROSCI.3632-04.2005, 15716403
    • Liu B, Qin F. Functional control of cold- and menthol-sensitive TRPM8 ion channels by phosphatidylinositol 4,5-bisphosphate. J Neurosci 2005, 25:1674-1681. 10.1523/JNEUROSCI.3632-04.2005, 15716403.
    • (2005) J Neurosci , vol.25 , pp. 1674-1681
    • Liu, B.1    Qin, F.2
  • 70
    • 17844373771 scopus 로고    scopus 로고
    • PI(4,5)P(2) regulates the activation and desensitization of TRPM8 channels through the TRP domain.
    • 10.1038/nn1451, 15852009
    • Rohacs T, Lopes CM, Michailidis I, Logothetis DE. PI(4,5)P(2) regulates the activation and desensitization of TRPM8 channels through the TRP domain. Nat Neurosci 2005, 8:626-634. 10.1038/nn1451, 15852009.
    • (2005) Nat Neurosci , vol.8 , pp. 626-634
    • Rohacs, T.1    Lopes, C.M.2    Michailidis, I.3    Logothetis, D.E.4
  • 71
    • 32544442208 scopus 로고    scopus 로고
    • The Ca2+-activated cation channel TRPM4 is regulated by phosphatidylinositol 4,5-biphosphate.
    • 10.1038/sj.emboj.7600963, 1383543, 16424899
    • Nilius B, Mahieu F, Prenen J, Janssens A, Owsianik G, Vennekens R, Voets T. The Ca2+-activated cation channel TRPM4 is regulated by phosphatidylinositol 4,5-biphosphate. EMBO J 2006, 25:467-478. 10.1038/sj.emboj.7600963, 1383543, 16424899.
    • (2006) EMBO J , vol.25 , pp. 467-478
    • Nilius, B.1    Mahieu, F.2    Prenen, J.3    Janssens, A.4    Owsianik, G.5    Vennekens, R.6    Voets, T.7
  • 73
    • 0034700494 scopus 로고    scopus 로고
    • Induction of vanilloid receptor channel activity by protein kinase C.
    • 10.1038/35050121, 11140687
    • Premkumar LS, Ahern GP. Induction of vanilloid receptor channel activity by protein kinase C. Nature 2000, 408:985-990. 10.1038/35050121, 11140687.
    • (2000) Nature , vol.408 , pp. 985-990
    • Premkumar, L.S.1    Ahern, G.P.2
  • 74
    • 0142059776 scopus 로고    scopus 로고
    • Protein kinase C phosphorylation sensitizes but does not activate the capsaicin receptor transient receptor potential vanilloid 1 (TRPV1).
    • 10.1073/pnas.2032100100, 218783, 14523239
    • Bhave G, Hu HJ, Glauner KS, Zhu W, Wang H, Brasier DJ, Oxford GS, Gereau R. Protein kinase C phosphorylation sensitizes but does not activate the capsaicin receptor transient receptor potential vanilloid 1 (TRPV1). Proc Natl Acad Sci USA 2003, 100:12480-12485. 10.1073/pnas.2032100100, 218783, 14523239.
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 12480-12485
    • Bhave, G.1    Hu, H.J.2    Glauner, K.S.3    Zhu, W.4    Wang, H.5    Brasier, D.J.6    Oxford, G.S.7    Gereau, R.8
  • 75
    • 30544438062 scopus 로고    scopus 로고
    • Downregulation of transient receptor potential melastatin 8 by protein kinase C-mediated dephosphorylation.
    • 10.1523/JNEUROSCI.3006-05.2005, 16339027
    • Premkumar LS, Raisinghani M, Pingle SC, Long C, Pimentel F. Downregulation of transient receptor potential melastatin 8 by protein kinase C-mediated dephosphorylation. J Neurosci 2005, 25:11322-11329. 10.1523/JNEUROSCI.3006-05.2005, 16339027.
    • (2005) J Neurosci , vol.25 , pp. 11322-11329
    • Premkumar, L.S.1    Raisinghani, M.2    Pingle, S.C.3    Long, C.4    Pimentel, F.5
  • 76
    • 50249119619 scopus 로고    scopus 로고
    • A-kinase anchoring protein mediates TRPV1 thermal hyperalgesia through PKA phosphorylation of TRPV1.
    • 10.1016/j.pain.2008.02.022, 18381233
    • Jeske NA, Diogenes A, Ruparel NB, Fehrenbacher JC, Henry M, Akopian AN, Hargreaves KM. A-kinase anchoring protein mediates TRPV1 thermal hyperalgesia through PKA phosphorylation of TRPV1. Pain 2008, 38:604-616. 10.1016/j.pain.2008.02.022, 18381233 .
    • (2008) Pain , vol.38 , pp. 604-616
    • Jeske, N.A.1    Diogenes, A.2    Ruparel, N.B.3    Fehrenbacher, J.C.4    Henry, M.5    Akopian, A.N.6    Hargreaves, K.M.7
  • 77
    • 34247523747 scopus 로고    scopus 로고
    • Regulation of transient receptor potential channel of melastatin type 8 (TRPM8): effect of CAMP, cannabinoid and endovailloids.
    • 10.1016/j.yexcr.2007.01.008, 17428469
    • De Petrocellis L, Starowicz K, Moriello AS, Vivese M, Orlando P, Di Marzo V. Regulation of transient receptor potential channel of melastatin type 8 (TRPM8): effect of CAMP, cannabinoid and endovailloids. Exp Cell Res 2007, 313:1911-1920. 10.1016/j.yexcr.2007.01.008, 17428469.
    • (2007) Exp Cell Res , vol.313 , pp. 1911-1920
    • De Petrocellis, L.1    Starowicz, K.2    Moriello, A.S.3    Vivese, M.4    Orlando, P.5    Di Marzo, V.6
  • 78
    • 0030777012 scopus 로고    scopus 로고
    • The capsaicin receptor: a heat-activated ion channel in the pain pathway.
    • 10.1038/39807, 9349813
    • Caterina MJ, Schumacher MA, Tominaga M, Rosen TA, Levine JD, Julius D. The capsaicin receptor: a heat-activated ion channel in the pain pathway. Nature 1997, 389:816-824. 10.1038/39807, 9349813.
    • (1997) Nature , vol.389 , pp. 816-824
    • Caterina, M.J.1    Schumacher, M.A.2    Tominaga, M.3    Rosen, T.A.4    Levine, J.D.5    Julius, D.6
  • 79
    • 0032881344 scopus 로고    scopus 로고
    • Resiniferatoxin-type phorboid vanilloids display capsaicin-like selectivity at native vanilloid receptors on rat DRG neurons and at the cloned vanilloid receptor VR1.
    • 10.1038/sj.bjp.0702810, 1571651, 10510454
    • Szallasi A, Szabo T, Biro T, Modarres S, Blumberg PM, Krause JE, Cortright DN, Appendino G. Resiniferatoxin-type phorboid vanilloids display capsaicin-like selectivity at native vanilloid receptors on rat DRG neurons and at the cloned vanilloid receptor VR1. Br J Pharmacol 1999, 128:428-434. 10.1038/sj.bjp.0702810, 1571651, 10510454.
    • (1999) Br J Pharmacol , vol.128 , pp. 428-434
    • Szallasi, A.1    Szabo, T.2    Biro, T.3    Modarres, S.4    Blumberg, P.M.5    Krause, J.E.6    Cortright, D.N.7    Appendino, G.8
  • 80
    • 17144418518 scopus 로고    scopus 로고
    • Effects of piperine, the pungent component of black pepper, at the human vanilloid receptor (TRPV1).
    • 10.1038/sj.bjp.0706040, 1576058, 15685214
    • McNamara FN, Randall A, Gunthorpe MJ. Effects of piperine, the pungent component of black pepper, at the human vanilloid receptor (TRPV1). Br J Pharmacol 2005, 144:781-790. 10.1038/sj.bjp.0706040, 1576058, 15685214.
    • (2005) Br J Pharmacol , vol.144 , pp. 781-790
    • McNamara, F.N.1    Randall, A.2    Gunthorpe, M.J.3
  • 81
    • 25644433563 scopus 로고    scopus 로고
    • Camphor activates and strongly desensitizes the transient receptor potential vanilloid subtype 1 channel in a vanilloid-independent mechanism.
    • 10.1523/JNEUROSCI.2574-05.2005, 16192383
    • Xu H, Blair NT, Clapham DE. Camphor activates and strongly desensitizes the transient receptor potential vanilloid subtype 1 channel in a vanilloid-independent mechanism. J Neurosci 2005, 25:8924-8937. 10.1523/JNEUROSCI.2574-05.2005, 16192383.
    • (2005) J Neurosci , vol.25 , pp. 8924-8937
    • Xu, H.1    Blair, N.T.2    Clapham, D.E.3
  • 83
    • 0037034931 scopus 로고    scopus 로고
    • Identification of a cold receptor reveals a general role for TRP channels in thermosensation.
    • 10.1038/nature719, 11882888
    • McKemy DD, Neuhausser WM, Julius D. Identification of a cold receptor reveals a general role for TRP channels in thermosensation. Nature 2002, 416:52-58. 10.1038/nature719, 11882888.
    • (2002) Nature , vol.416 , pp. 52-58
    • McKemy, D.D.1    Neuhausser, W.M.2    Julius, D.3
  • 85
    • 33749562292 scopus 로고    scopus 로고
    • Bisandrographolide from Andrographis paniculata activates TRPV4 channels.
    • 10.1074/jbc.M605394200, 16899456
    • Smith PL, Maloney KN, Pothen RG, Clardy J, Clapham DE. Bisandrographolide from Andrographis paniculata activates TRPV4 channels. J Biol Chem 2006, 281:29897-29904. 10.1074/jbc.M605394200, 16899456.
    • (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
  • 86
    • 2642568616 scopus 로고    scopus 로고
    • 2-aminoethoxydiphenyl borate activates and sensitizes the heat-gated ion channel TRPV3.
    • 10.1523/JNEUROSCI.0934-04.2004, 15175387
    • Chung MK, Lee H, Mizuno A, Suzuki M, Caterina MJ. 2-aminoethoxydiphenyl borate activates and sensitizes the heat-gated ion channel TRPV3. J Neurosci 2004, 24:5177-5182. 10.1523/JNEUROSCI.0934-04.2004, 15175387.
    • (2004) J Neurosci , vol.24 , pp. 5177-5182
    • Chung, M.K.1    Lee, H.2    Mizuno, A.3    Suzuki, M.4    Caterina, M.J.5
  • 87
  • 93
    • 63849292300 scopus 로고    scopus 로고
    • The integrative function of TRPC channels.
    • 10.2741/3230, 19273053
    • Kiselyov K, Patterson RL. The integrative function of TRPC channels. Front Biosci 2009, 14:45-58. 10.2741/3230, 19273053.
    • (2009) Front Biosci , vol.14 , pp. 45-58
    • Kiselyov, K.1    Patterson, R.L.2
  • 95
    • 0043267987 scopus 로고    scopus 로고
    • Anandamide and arachidonic acid use epoxyeicosatrienoic acids to activate TRPV4 channels.
    • 10.1038/nature01807, 12879072
    • 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. 10.1038/nature01807, 12879072.
    • (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
  • 96
    • 14944348415 scopus 로고    scopus 로고
    • Activation of the melastatin-related cation channel TRPM3 by D-erythro-sphingosine [corrected].
    • 10.1124/mol.104.006734, 15550678
    • Grimm C, Kraft R, Schultz G, Harteneck C. Activation of the melastatin-related cation channel TRPM3 by D-erythro-sphingosine [corrected]. Mol Pharmacol 2005, 67:798-805. 10.1124/mol.104.006734, 15550678.
    • (2005) Mol Pharmacol , vol.67 , pp. 798-805
    • Grimm, C.1    Kraft, R.2    Schultz, G.3    Harteneck, C.4
  • 97
    • 67349241526 scopus 로고    scopus 로고
    • Analgesic potential of TRPV1 antagonists.
    • 10.1016/j.bcp.2009.02.014, 19481638
    • Kym PR, Kort ME, Hutchins CW. Analgesic potential of TRPV1 antagonists. Biochem Pharmacol 2009, 78:211-216. 10.1016/j.bcp.2009.02.014, 19481638.
    • (2009) Biochem Pharmacol , vol.78 , pp. 211-216
    • Kym, P.R.1    Kort, M.E.2    Hutchins, C.W.3
  • 100
    • 4544271500 scopus 로고    scopus 로고
    • Association of immunophilins with mammalian TRPC channels.
    • 10.1074/jbc.M401156200, 15199065
    • Sinkins WG, Goel M, Estacion M, Schilling WP. Association of immunophilins with mammalian TRPC channels. J Biol Chem 2004, 279:34521-34529. 10.1074/jbc.M401156200, 15199065.
    • (2004) J Biol Chem , vol.279 , pp. 34521-34529
    • Sinkins, W.G.1    Goel, M.2    Estacion, M.3    Schilling, W.P.4
  • 102
    • 0029853148 scopus 로고    scopus 로고
    • WWW-query: an on-line retrieval system for biological sequence banks.
    • 10.1016/0300-9084(96)84768-7, 8905155
    • Perriere G, Gouy M. WWW-query: an on-line retrieval system for biological sequence banks. Biochimie 1996, 78:364-369. 10.1016/0300-9084(96)84768-7, 8905155.
    • (1996) Biochimie , vol.78 , pp. 364-369
    • Perriere, G.1    Gouy, M.2
  • 103
    • 84904594866 scopus 로고    scopus 로고
    • Transient Receptor Potential Channels. IUPHAR database
    • Clapham DI, Nilius B, Owsianik G. Transient Receptor Potential Channels. IUPHAR database. , http://www.iuphar-db.org/DATABASE/FamilyMenuForward?familyId=78
    • Clapham, D.I.1    Nilius, B.2    Owsianik, G.3
  • 104
    • 23844490723 scopus 로고    scopus 로고
    • TRP channels in Drosophila photoreceptor cells.
    • 10.1113/jphysiol.2005.092551, 1474165, 15961416
    • Montell C. TRP channels in Drosophila photoreceptor cells. J Physiol 2005, 567:45-51. 10.1113/jphysiol.2005.092551, 1474165, 15961416.
    • (2005) J Physiol , vol.567 , pp. 45-51
    • Montell, C.1
  • 105
    • 34548632601 scopus 로고    scopus 로고
    • TRP channels.
    • 10.1146/annurev.biochem.75.103004.142819, 17579562
    • Venkatachalam K, Montell C. TRP channels. Annu Rev Biochem 2007, 76:387-417. 10.1146/annurev.biochem.75.103004.142819, 17579562.
    • (2007) Annu Rev Biochem , vol.76 , pp. 387-417
    • Venkatachalam, K.1    Montell, C.2
  • 106
    • 34250878976 scopus 로고    scopus 로고
    • TRP channels in mechanosensation: direct or indirect activation?
    • 10.1038/nrn2149, 17585304
    • Christensen AP, Corey DP. TRP channels in mechanosensation: direct or indirect activation?. Nat Rev Neurosci 2007, 8:510-521. 10.1038/nrn2149, 17585304.
    • (2007) Nat Rev Neurosci , vol.8 , pp. 510-521
    • Christensen, A.P.1    Corey, D.P.2


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