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Volumn 38, Issue 3-4 SPEC. ISS., 2005, Pages 233-252

TRP channels: An overview

Author keywords

Ca2+ entry channels; Ca2+ homeostasis; Cation channels; Mg2+ homeostasis; TRP channels

Indexed keywords

ANKYRIN; CALCIUM ION; CATION CHANNEL; MAGNESIUM ION; MELASTATIN; MEMBRANE PROTEIN; MUCOLIPIN; POLYCYSTIN; TRANSIENT RECEPTOR POTENTIAL CHANNEL; UNCLASSIFIED DRUG; VANILLIN DERIVATIVE; VANILLOID RECEPTOR 1;

EID: 24644445646     PISSN: 01434160     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.ceca.2005.06.028     Document Type: Article
Times cited : (656)

References (264)
  • 2
    • 0037040395 scopus 로고    scopus 로고
    • The TRP channels, a remarkable functional family
    • C. Montell L. Birnbaumer V. Flockerzi The TRP channels, a remarkable functional family Cell 108 2002 595-598
    • (2002) Cell , vol.108 , pp. 595-598
    • Montell, C.1    Birnbaumer, L.2    Flockerzi, V.3
  • 4
    • 0041520528 scopus 로고    scopus 로고
    • New TRP channels in hearing and mechanosensation
    • D.P. Corey New TRP channels in hearing and mechanosensation Neuron 39 2003 585-588
    • (2003) Neuron , vol.39 , pp. 585-588
    • Corey, D.P.1
  • 5
    • 0347504835 scopus 로고    scopus 로고
    • TRP channels as cellular sensors
    • D.E. Clapham TRP channels as cellular sensors Nature 426 2003 517-524
    • (2003) Nature , vol.426 , pp. 517-524
    • Clapham, D.E.1
  • 6
    • 3242728834 scopus 로고    scopus 로고
    • Polycystins: From mechanosensation to gene regulation
    • P. Delmas Polycystins: From mechanosensation to gene regulation Cell 118 2004 145-148
    • (2004) Cell , vol.118 , pp. 145-148
    • Delmas, P.1
  • 8
    • 0038414614 scopus 로고    scopus 로고
    • Discrimination of intracellular calcium store subcompartments using TRPV1 (transient receptor potential channel, vanilloid subfamily member 1) release channel activity
    • H. Turner A. Fleig A. Stokes J.P. Kinet R. Penner Discrimination of intracellular calcium store subcompartments using TRPV1 (transient receptor potential channel, vanilloid subfamily member 1) release channel activity Biochem. J. 371 2003 341-350
    • (2003) Biochem. J. , vol.371 , pp. 341-350
    • Turner, H.1    Fleig, A.2    Stokes, A.3    Kinet, J.P.4    Penner, R.5
  • 9
    • 8544233547 scopus 로고    scopus 로고
    • 2+ channel required for the survival of prostate cancer cells
    • 2+ channel required for the survival of prostate cancer cells Cancer Res. 64 2004 8365-8373
    • (2004) Cancer Res. , vol.64 , pp. 8365-8373
    • Zhang, L.1    Barritt, G.J.2
  • 13
    • 0033162068 scopus 로고    scopus 로고
    • Translocation of a calcium-permeable cation channel induced by insulin-like growth factor-I
    • M. Kanzaki Y.Q. Zhang H. Mashima L. Li H. Shibata I. Kojima Translocation of a calcium-permeable cation channel induced by insulin-like growth factor-I Nat. Cell Biol. 1 1999 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
  • 14
    • 0034759617 scopus 로고    scopus 로고
    • The neuropeptide head activator induces activation and translocation of the growth-factor-regulated Ca(2+)-permeable channel GRC
    • K. Boels G. Glassmeier D. Herrmann I.B. Riedel W. Hampe I. Kojima J.R. Schwarz H.C. Schaller The neuropeptide head activator induces activation and translocation of the growth-factor-regulated Ca(2+)-permeable channel GRC J. Cell Sci. 114 2001 3599-3606
    • (2001) J. Cell Sci. , vol.114 , pp. 3599-3606
    • Boels, K.1    Glassmeier, G.2    Herrmann, D.3    Riedel, I.B.4    Hampe, W.5    Kojima, I.6    Schwarz, J.R.7    Schaller, H.C.8
  • 16
    • 0014683485 scopus 로고
    • Abnormal electroretinogram from a Drosophila mutant
    • D.J. Cosens A. Manning Abnormal electroretinogram from a Drosophila mutant Nature 224 1969 285-287
    • (1969) Nature , vol.224 , pp. 285-287
    • Cosens, D.J.1    Manning, A.2
  • 17
    • 0024642547 scopus 로고
    • Molecular characterization of the Drosophila trp locus: A putative integral membrane protein required for phototransduction
    • C. Montell G.M. Rubin Molecular characterization of the Drosophila trp locus: A putative integral membrane protein required for phototransduction Neuron 2 1989 1313-1323
    • (1989) Neuron , vol.2 , pp. 1313-1323
    • Montell, C.1    Rubin, G.M.2
  • 18
    • 0035746086 scopus 로고    scopus 로고
    • Phototransduction in Drosophila melanogaster
    • R.C. Hardie Phototransduction in Drosophila melanogaster J. Exp. Biol. 204 2001 3403-3409
    • (2001) J. Exp. Biol. , vol.204 , pp. 3403-3409
    • Hardie, R.C.1
  • 19
    • 0033679832 scopus 로고    scopus 로고
    • Constitutive activity of the light-sensitive channels TRP and TRPL in the Drosophila diacylglycerol kinase mutant, rdgA
    • P. Raghu K. Usher S. Jonas S. Chyb A. Polyanovsky R.C. Hardie Constitutive activity of the light-sensitive channels TRP and TRPL in the Drosophila diacylglycerol kinase mutant, rdgA Neuron 26 2000 169-179
    • (2000) 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
  • 20
    • 0033462127 scopus 로고    scopus 로고
    • The organization of INAD-signaling complexes by a multivalent PDZ domain protein in Drosophila photoreceptor cells ensures sensitivity and speed of signalling
    • S. Tsunoda C.S. Zuker The organization of INAD-signaling complexes by a multivalent PDZ domain protein in Drosophila photoreceptor cells ensures sensitivity and speed of signalling Cell Calcium 26 1999 165-171
    • (1999) Cell Calcium , vol.26 , pp. 165-171
    • Tsunoda, S.1    Zuker, C.S.2
  • 22
    • 0029094168 scopus 로고
    • Putative capacitative calcium entry channels: Expression of Drosophila trp and evidence for the existence of vertebrate homologues
    • C.C.H. Petersen M.J. Berridge M.F. Borgese D.L. Bennett Putative capacitative calcium entry channels: Expression of Drosophila trp and evidence for the existence of vertebrate homologues Biochem. J. 311 1995 41-44
    • (1995) Biochem. J. , vol.311 , pp. 41-44
    • Petersen, C.C.H.1    Berridge, M.J.2    Borgese, M.F.3    Bennett, D.L.4
  • 23
    • 0001966533 scopus 로고    scopus 로고
    • Molecular biology of calcium channels
    • J.W.J. Putney (Ed.) CRC Press Boca Raton, USA
    • S. Philipp U. Wissenbach V. Flockerzi Molecular biology of calcium channels in: J.W.J. Putney (Ed.) Calcium Signaling 2000 CRC Press Boca Raton, USA 321-342
    • (2000) Calcium Signaling , pp. 321-342
    • Philipp, S.1    Wissenbach, U.2    Flockerzi, V.3
  • 24
    • 33644875032 scopus 로고    scopus 로고
    • The TRP superfamily of cation channels
    • re3
    • C. Montell The TRP superfamily of cation channels Sci. STKE re3 2005
    • (2005) Sci. STKE
    • Montell, C.1
  • 25
    • 0037188517 scopus 로고    scopus 로고
    • Subunit composition of mammalian transient receptor potential channels in living cells
    • T. Hofmann M. Schaefer G. Schultz T. Gudermann Subunit composition of mammalian transient receptor potential channels in living cells Proc. Natl. Acad. Sci. USA 99 2002 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
  • 26
    • 0035051978 scopus 로고    scopus 로고
    • TRPC1 and TRPC5 form a novel cation channel in mammalian brain
    • C. Strubing G. Krapivinsky L. Krapivinsky D.E. Clapham TRPC1 and TRPC5 form a novel cation channel in mammalian brain Neuron 29 2001 645-655
    • (2001) Neuron , vol.29 , pp. 645-655
    • Strubing, C.1    Krapivinsky, G.2    Krapivinsky, L.3    Clapham, D.E.4
  • 27
    • 0141755156 scopus 로고    scopus 로고
    • Formation of novel TRPC channels by complex subunit interactions in embryonic brain
    • C. Strubing G. Krapivinsky L. Krapivinsky D.E. Clapham Formation of novel TRPC channels by complex subunit interactions in embryonic brain J. Biol. Chem. 278 2003 39014-39019
    • (2003) J. Biol. Chem. , vol.278 , pp. 39014-39019
    • Strubing, C.1    Krapivinsky, G.2    Krapivinsky, L.3    Clapham, D.E.4
  • 28
    • 2342650881 scopus 로고    scopus 로고
    • Mammalian TRPC channel subunit assembly
    • W.P. Schilling M. Goel Mammalian TRPC channel subunit assembly Novartis Found. Symp. 258 2004 18-30
    • (2004) Novartis Found. Symp. , vol.258 , pp. 18-30
    • Schilling, W.P.1    Goel, M.2
  • 29
    • 0037073749 scopus 로고    scopus 로고
    • Selective association of TRPC channel subunits in rat brain synaptosomes
    • M. Goel W.G. Sinkins W.P. Schilling Selective association of TRPC channel subunits in rat brain synaptosomes J. Biol. Chem. 277 2002 48303-48310
    • (2002) J. Biol. Chem. , vol.277 , pp. 48303-48310
    • Goel, M.1    Sinkins, W.G.2    Schilling, W.P.3
  • 33
    • 0036510383 scopus 로고    scopus 로고
    • Modification of store-operated channel coupling and inositol trisphosphate receptor function by 2-aminoethoxydiphenyl borate in DT40 lymphocytes
    • H.-T. Ma K. Venkatachalam J.B. Parys D.L. Gill Modification of store-operated channel coupling and inositol trisphosphate receptor function by 2-aminoethoxydiphenyl borate in DT40 lymphocytes J. Biol. Chem. 277 2002 6915-6922
    • (2002) J. Biol. Chem. , vol.277 , pp. 6915-6922
    • Ma, H.-T.1    Venkatachalam, K.2    Parys, J.B.3    Gill, D.L.4
  • 34
    • 0042206600 scopus 로고    scopus 로고
    • Regulation of canonical transient receptor potential (TRPC) channel function by diacylglycerol and protein kinase C
    • K. Venkatachalam F. Zheng D.L. Gill Regulation of canonical transient receptor potential (TRPC) channel function by diacylglycerol and protein kinase C J. Biol. Chem. 278 2003 29031-29040
    • (2003) J. Biol. Chem. , vol.278 , pp. 29031-29040
    • Venkatachalam, K.1    Zheng, F.2    Gill, D.L.3
  • 36
    • 19244366419 scopus 로고    scopus 로고
    • 2+ entry channels: Still elusive!
    • pe36
    • 2+ entry channels: Still elusive! Sci. STKE pe36 2004
    • (2004) Sci. STKE
    • Nilius, B.1
  • 37
    • 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
    • M. Trebak G.S. Bird R.R. McKay J.W. Putney Jr. 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. 277 2002 21617-21623
    • (2002) J. Biol. Chem. , vol.277 , pp. 21617-21623
    • Trebak, M.1    Bird, G.S.2    McKay, R.R.3    Putney Jr., J.W.4
  • 38
    • 0037636288 scopus 로고    scopus 로고
    • 2+-permeable nonselective cation channels
    • 2+ -permeable nonselective cation channels Cell Calcium 33 2003 441-450
    • (2003) Cell Calcium , vol.33 , pp. 441-450
    • Plant, T.D.1    Schaefer, M.2
  • 40
    • 18844404413 scopus 로고    scopus 로고
    • Capacitative calcium entry: Sensing the calcium stores
    • J.W. Putney Jr. Capacitative calcium entry: Sensing the calcium stores J. Cell Biol. 169 2005 381-382
    • (2005) J. Cell Biol. , vol.169 , pp. 381-382
    • Putney Jr., J.W.1
  • 41
    • 0035341063 scopus 로고    scopus 로고
    • The transient receptor potential, TRP4, cation channel is a novel member of the family of calmodulin binding proteins
    • C. Trost C. Bergs N. Himmerkus V. Flockerzi The transient receptor potential, TRP4, cation channel is a novel member of the family of calmodulin binding proteins Biochem. J. 355 2001 663-670
    • (2001) Biochem. J. , vol.355 , pp. 663-670
    • Trost, C.1    Bergs, C.2    Himmerkus, N.3    Flockerzi, V.4
  • 42
    • 24644460439 scopus 로고    scopus 로고
    • 2+ binding proteins in the functional regulation of TRP channels
    • edited by B. Nilius Functional Role of TRP Channels
    • 2+ binding proteins in the functional regulation of TRP channels. Pflügers Arch. Europ. J. Physiol., Special Issue, Functional role of TRP channels, edited by B. Nilius.
    • (2005) Pflügers Arch. Europ. J. Physiol. , Issue.SPEC. ISSUE
    • Zhu, M.X.1
  • 43
    • 2342577576 scopus 로고    scopus 로고
    • TRPC channel interactions with calmodulin and IP3 receptors
    • M.X. Zhu J. Tang TRPC channel interactions with calmodulin and IP3 receptors Novartis Found. Symp. 258 2004 44-58
    • (2004) Novartis Found. Symp. , vol.258 , pp. 44-58
    • Zhu, M.X.1    Tang, J.2
  • 44
    • 2042449911 scopus 로고    scopus 로고
    • The N-terminal domain of the IP3 receptor gates store-operated hTrp3 channels
    • K. Kiselyov G.A. Mignery M.X. Zhu S. Muallem The N-terminal domain of the IP3 receptor gates store-operated hTrp3 channels Mol. Cell 4 1999 423-429
    • (1999) Mol. Cell , vol.4 , pp. 423-429
    • Kiselyov, K.1    Mignery, G.A.2    Zhu, M.X.3    Muallem, S.4
  • 46
    • 0033635186 scopus 로고    scopus 로고
    • Gating of store-operated channels by conformational coupling to ryanodine receptors
    • K.I. Kiselyov D.M. Shin Y. Wang I.N. Pessah P.D. Allen S. Muallem Gating of store-operated channels by conformational coupling to ryanodine receptors Mol. Cell 6 2000 421-431
    • (2000) Mol. Cell , vol.6 , pp. 421-431
    • Kiselyov, K.I.1    Shin, D.M.2    Wang, Y.3    Pessah, I.N.4    Allen, P.D.5    Muallem, S.6
  • 48
    • 0034697041 scopus 로고    scopus 로고
    • Assembly of Trp1 in a signaling complex associated with caveolin-scaffolding lipid raft domains
    • T.P. Lockwich X. Liu B.B. Singh J. Jadlowiec S. Weiland I.S. Ambudkar Assembly of Trp1 in a signaling complex associated with caveolin-scaffolding lipid raft domains J. Biol. Chem. 275 2000 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
  • 49
    • 0034535348 scopus 로고    scopus 로고
    • Association of mammalian trp4 and phospholipase C isozymes with a PDZ domain-containing protein, NHERF
    • Y. Tang J. Tang Z. Chen C. Trost V. Flockerzi M. Li V. Ramesh M.X. Zhu Association of mammalian trp4 and phospholipase C isozymes with a PDZ domain-containing protein, NHERF J. Biol. Chem. 275 2000 37559-37564
    • (2000) J. Biol. Chem. , vol.275 , pp. 37559-37564
    • Tang, Y.1    Tang, J.2    Chen, Z.3    Trost, C.4    Flockerzi, V.5    Li, M.6    Ramesh, V.7    Zhu, M.X.8
  • 51
    • 0038311985 scopus 로고    scopus 로고
    • Proteins modulating TRP channel function
    • C. Harteneck Proteins modulating TRP channel function Cell Calcium 33 2003 303-310
    • (2003) Cell Calcium , vol.33 , pp. 303-310
    • Harteneck, C.1
  • 52
    • 4644297280 scopus 로고    scopus 로고
    • TRPC5 activation kinetics are modulated by the scaffolding protein ezrin/ radixin/moesin-binding phosphoprotein-50 (EBP50)
    • A.G. Obukhov M.C. Nowycky TRPC5 activation kinetics are modulated by the scaffolding protein ezrin/radixin/moesin-binding phosphoprotein-50 (EBP50) J. Cell Physiol. 201 2004 227-235
    • (2004) J. Cell Physiol. , vol.201 , pp. 227-235
    • Obukhov, A.G.1    Nowycky, M.C.2
  • 57
    • 0034063461 scopus 로고    scopus 로고
    • Transient receptor potential channels as molecular substrates of receptor-mediated cation entry
    • T. Hofmann M. Schaefer G. Schultz T. Gudermann Transient receptor potential channels as molecular substrates of receptor-mediated cation entry J. Mol. Med. 78 2000 14-25
    • (2000) J. Mol. Med. , vol.78 , pp. 14-25
    • Hofmann, T.1    Schaefer, M.2    Schultz, G.3    Gudermann, T.4
  • 60
    • 0037648508 scopus 로고    scopus 로고
    • 2+ channels. Role of acidic amino acid residues in the S5-S6 region
    • 2+ channels. Role of acidic amino acid residues in the S5-S6 region J. Biol. Chem. 278 2003 11337-11343
    • (2003) J. Biol. Chem. , vol.278 , pp. 11337-11343
    • Liu, X.1    Singh, B.B.2    Ambudkar, I.S.3
  • 61
    • 0035910618 scopus 로고    scopus 로고
    • 2+ channels in native vascular smooth muscle cells
    • 2+ channels in native vascular smooth muscle cells Circ. Res. 88 2001 84-87
    • (2001) Circ. Res. , vol.88 , pp. 84-87
    • Xu, S.Z.1    Beech, D.J.2
  • 63
    • 0037116581 scopus 로고    scopus 로고
    • Expression and functional role of bTRPC1 channels in native endothelial cells
    • S. Antoniotti D. Lovisolo A.F. Pla L. Munaron Expression and functional role of bTRPC1 channels in native endothelial cells FEBS Lett. 510 2002 189-195
    • (2002) FEBS Lett. , vol.510 , pp. 189-195
    • Antoniotti, S.1    Lovisolo, D.2    Pla, A.F.3    Munaron, L.4
  • 66
    • 4644239523 scopus 로고    scopus 로고
    • Non-selective cationic channels of smooth muscle and the mammalian homologues of Drosophila TRP
    • D.J. Beech K. Muraki R. Flemming Non-selective cationic channels of smooth muscle and the mammalian homologues of Drosophila TRP J. Physiol. 559 2004 685-706
    • (2004) J. Physiol. , vol.559 , pp. 685-706
    • Beech, D.J.1    Muraki, K.2    Flemming, R.3
  • 67
    • 0344443184 scopus 로고    scopus 로고
    • Activation of the TRPC1 cation channel by metabotropic glutamate receptor mGluR1
    • S.J. Kim Y.S. Kim J.P. Yuan R.S. Petralia P.F. Worley D.J. Linden Activation of the TRPC1 cation channel by metabotropic glutamate receptor mGluR1 Nature 426 2003 285-291
    • (2003) Nature , vol.426 , pp. 285-291
    • Kim, S.J.1    Kim, Y.S.2    Yuan, J.P.3    Petralia, R.S.4    Worley, P.F.5    Linden, D.J.6
  • 68
    • 17244383526 scopus 로고    scopus 로고
    • Requirement of TRPC channels in netrin-1-induced chemotropic turning of nerve growth cones
    • G.X. Wang M.M. Poo Requirement of TRPC channels in netrin-1-induced chemotropic turning of nerve growth cones Nature 434 2005 898-904
    • (2005) Nature , vol.434 , pp. 898-904
    • Wang, G.X.1    Poo, M.M.2
  • 70
    • 0034789020 scopus 로고    scopus 로고
    • Ion channels and their functional role in vascular endothelium
    • B. Nilius G. Droogmans Ion channels and their functional role in vascular endothelium Physiol. Rev. 81 2001 1415-1459
    • (2001) Physiol. Rev. , vol.81 , pp. 1415-1459
    • Nilius, B.1    Droogmans, G.2
  • 73
    • 85071428127 scopus 로고    scopus 로고
    • TRP channels and calcium entry in human platelets
    • S.O. Sage S.L. Brownlow J.A. Rosado TRP channels and calcium entry in human platelets Blood 100 2002 4245-4246
    • (2002) Blood , vol.100 , pp. 4245-4246
    • Sage, S.O.1    Brownlow, S.L.2    Rosado, J.A.3
  • 74
    • 0242552248 scopus 로고    scopus 로고
    • Rapid agonist-evoked coupling of type II Ins(1,4,5)P3 receptor with human transient receptor potential (hTRPC1) channels in human platelets
    • S.L. Brownlow S.O. Sage Rapid agonist-evoked coupling of type II Ins(1,4,5)P3 receptor with human transient receptor potential (hTRPC1) channels in human platelets Biochem. J. 375 2003 697-704
    • (2003) Biochem. J. , vol.375 , pp. 697-704
    • Brownlow, S.L.1    Sage, S.O.2
  • 76
    • 0037700605 scopus 로고    scopus 로고
    • Pharmacological profile of store-operated channels in cerebral arteriolar smooth muscle cells
    • R. Flemming S.Z. Xu D.J. Beech Pharmacological profile of store-operated channels in cerebral arteriolar smooth muscle cells Br. J. Pharmacol. 139 2003 955-965
    • (2003) Br. J. Pharmacol. , vol.139 , pp. 955-965
    • Flemming, R.1    Xu, S.Z.2    Beech, D.J.3
  • 78
    • 18144370824 scopus 로고    scopus 로고
    • Difference in obesity phenotype between orexin-knockout mice and orexin neuron-deficient mice with same genetic background and environmental conditions
    • J. Hara M. Yanagisawa T. Sakurai Difference in obesity phenotype between orexin-knockout mice and orexin neuron-deficient mice with same genetic background and environmental conditions Neurosci. Lett. 380 2005 239-242
    • (2005) Neurosci. Lett. , vol.380 , pp. 239-242
    • Hara, J.1    Yanagisawa, M.2    Sakurai, T.3
  • 80
    • 0345119039 scopus 로고    scopus 로고
    • A diacylglycerol-gated cation channel in vomeronasal neuron dendrites is impaired in TRPC2 mutant mice: Mechanism of pheromone transduction
    • P. Lucas K. Ukhanov T. Leinders-Zufall F. Zufall A diacylglycerol-gated cation channel in vomeronasal neuron dendrites is impaired in TRPC2 mutant mice: Mechanism of pheromone transduction Neuron 40 2003 551-561
    • (2003) Neuron , vol.40 , pp. 551-561
    • Lucas, P.1    Ukhanov, K.2    Leinders-Zufall, T.3    Zufall, F.4
  • 82
    • 85013704592 scopus 로고    scopus 로고
    • Neurobiology of TRPC2: From gene to behaviour
    • edited by B. Nilius Functional Role of TRP Channels
    • F. Zufall, K. Ukhanov, P. Lucas, T. Leinders-Zufall, Neurobiology of TRPC2: From gene to behaviour. Pflügers Arch. Europ. J. Physiol., Special Issue, Functional role of TRP channels, edited by B. Nilius.
    • Pflügers Arch. Europ. J. Physiol. , Issue.SPEC. ISSUE
    • Zufall, F.1    Ukhanov, K.2    Lucas, P.3    Leinders-Zufall, T.4
  • 84
    • 0034872061 scopus 로고    scopus 로고
    • Involvement of trp-2 protein in store-operated influx of calcium in fibroblasts
    • P. Gailly M. Colson-Van Schoor Involvement of trp-2 protein in store-operated influx of calcium in fibroblasts Cell Calcium 30 2001 157-165
    • (2001) Cell Calcium , vol.30 , pp. 157-165
    • Gailly, P.1    Colson-Van Schoor, M.2
  • 85
    • 0037020667 scopus 로고    scopus 로고
    • New aspects of calcium signaling in skeletal muscle cells: Implications in Duchenne muscular dystrophy
    • P. Gailly New aspects of calcium signaling in skeletal muscle cells: implications in Duchenne muscular dystrophy Biochim. Biophys. Acta 1600 2002 38-44
    • (2002) Biochim. Biophys. Acta , vol.1600 , pp. 38-44
    • Gailly, P.1
  • 86
    • 0034306264 scopus 로고    scopus 로고
    • Cloning, expression and subcellular localization of two novel splice variants of mouse transient receptor potential channel 2
    • T. Hofmann M. Schaefer G. Schultz T. Gudermann Cloning, expression and subcellular localization of two novel splice variants of mouse transient receptor potential channel 2 Biochem. J. 351 2000 115-122
    • (2000) Biochem. J. , vol.351 , pp. 115-122
    • Hofmann, T.1    Schaefer, M.2    Schultz, G.3    Gudermann, T.4
  • 87
    • 4644314868 scopus 로고    scopus 로고
    • Obligatory role of Src kinase in the signaling mechanism for TRPC3 cation channels
    • G. Vazquez B.J. Wedel B.T. Kawasaki G.S. Bird J.W. Putney Jr. Obligatory role of Src kinase in the signaling mechanism for TRPC3 cation channels J. Biol. Chem. 279 2004 40521-40528
    • (2004) J. Biol. Chem. , vol.279 , pp. 40521-40528
    • Vazquez, G.1    Wedel, B.J.2    Kawasaki, B.T.3    Bird, G.S.4    Putney Jr., J.W.5
  • 89
    • 0037477379 scopus 로고    scopus 로고
    • A calmodulin/inositol 1,4,5-trisphosphate (IP3) receptor-binding region targets TRPC3 to the plasma membrane in a calmodulin/IP3 receptor-independent process
    • St J.B.G.
    • B.J. Wedel G. Vazquez R.R. McKay J.B.G. St J.W. Putney Jr. A calmodulin/ inositol 1,4,5-trisphosphate (IP3) receptor-binding region targets TRPC3 to the plasma membrane in a calmodulin/IP3 receptor-independent process J. Biol. Chem. 278 2003 25758-25765
    • (2003) J. Biol. Chem. , vol.278 , pp. 25758-25765
    • Wedel, B.J.1    Vazquez, G.2    McKay, R.R.3    Putney Jr., J.W.4
  • 90
    • 0036028768 scopus 로고    scopus 로고
    • Ca(2+)-calmodulin regulates receptor-operated Ca(2+) entry activity of TRPC6 in HEK-293 cells
    • G. Boulay Ca(2+)-calmodulin regulates receptor-operated Ca(2+) entry activity of TRPC6 in HEK-293 cells Cell Calcium 32 2002 201-207
    • (2002) Cell Calcium , vol.32 , pp. 201-207
    • Boulay, G.1
  • 91
    • 17244377058 scopus 로고    scopus 로고
    • Essential role of TRPC channels in the guidance of nerve growth cones by brain-derived neurotrophic factor
    • Y. Li Y.C. Jia K. Cui N. Li Z.Y. Zheng Y.Z. Wang X.B. Yuan Essential role of TRPC channels in the guidance of nerve growth cones by brain-derived neurotrophic factor Nature 434 2005 894-898
    • (2005) Nature , vol.434 , pp. 894-898
    • Li, Y.1    Jia, Y.C.2    Cui, K.3    Li, N.4    Zheng, Z.Y.5    Wang, Y.Z.6    Yuan, X.B.7
  • 92
    • 0033200089 scopus 로고    scopus 로고
    • Activation of a TRPC3-dependent cation current through the neurotrophin BDNF
    • H.S. Li X.Z. Xu C. Montell Activation of a TRPC3-dependent cation current through the neurotrophin BDNF Neuron 24 1999 261-273
    • (1999) Neuron , vol.24 , pp. 261-273
    • Li, H.S.1    Xu, X.Z.2    Montell, C.3
  • 95
    • 0034984762 scopus 로고    scopus 로고
    • Mechanisms of coronary artery depolarization by uridine triphosphate
    • D.G. Welsh J.E. Brayden Mechanisms of coronary artery depolarization by uridine triphosphate Am J. Physiol. Heart Circ. Physiol. 280 2001 H2545-H2553
    • (2001) Am J. Physiol. Heart Circ. Physiol. , vol.280
    • Welsh, D.G.1    Brayden, J.E.2
  • 96
    • 1442330339 scopus 로고    scopus 로고
    • Regulation of canonical transient receptor potential isoform 3 (TRPC3) channel by protein kinase G
    • H.Y. Kwan Y. Huang X. Yao Regulation of canonical transient receptor potential isoform 3 (TRPC3) channel by protein kinase G Proc. Natl. Acad. Sci. USA 101 2004 2625-2630
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 2625-2630
    • Kwan, H.Y.1    Huang, Y.2    Yao, X.3
  • 99
    • 1842640185 scopus 로고    scopus 로고
    • Ca(2+) signaling by TRPC3 involves Na(+) entry and local coupling to the Na(+)/Ca(2+) exchanger
    • C. Rosker A. Graziani M. Lukas P. Eder M.X. Zhu C. Romanin K. Groschner Ca(2+) signaling by TRPC3 involves Na(+) entry and local coupling to the Na(+)/Ca(2+) exchanger J. Biol. Chem. 279 2004 13696-13704
    • (2004) J. Biol. Chem. , vol.279 , pp. 13696-13704
    • Rosker, C.1    Graziani, A.2    Lukas, M.3    Eder, P.4    Zhu, M.X.5    Romanin, C.6    Groschner, K.7
  • 103
    • 0037166343 scopus 로고    scopus 로고
    • Calcium oscillation linked to pacemaking of interstitial cells of Cajal: Requirement of calcium influx and localization of TRP4 in caveolae
    • S. Torihashi T. Fujimoto C. Trost S. Nakayama Calcium oscillation linked to pacemaking of interstitial cells of Cajal: Requirement of calcium influx and localization of TRP4 in caveolae J. Biol. Chem. 277 2002 19191-19197
    • (2002) J. Biol. Chem. , vol.277 , pp. 19191-19197
    • Torihashi, S.1    Fujimoto, T.2    Trost, C.3    Nakayama, S.4
  • 104
    • 0347364627 scopus 로고    scopus 로고
    • Contribution of transient receptor potential channels to the control of GABA release from dendrites
    • T. Munsch M. Freichel V. Flockerzi H.C. Pape Contribution of transient receptor potential channels to the control of GABA release from dendrites Proc. Natl. Acad. Sci. USA 100 2003 16065-16070
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 16065-16070
    • Munsch, T.1    Freichel, M.2    Flockerzi, V.3    Pape, H.C.4
  • 106
    • 13544276570 scopus 로고    scopus 로고
    • Canonical transient receptor potential channel 4 (TRPC4) co-localizes with the scaffolding protein ZO-1 in human fetal astrocytes in culture
    • X. Song Y. Zhao L. Narcisse H. Duffy Y. Kress S. Lee C.F. Brosnan Canonical transient receptor potential channel 4 (TRPC4) co-localizes with the scaffolding protein ZO-1 in human fetal astrocytes in culture GLIA 49 2005 418-429
    • (2005) GLIA , vol.49 , pp. 418-429
    • Song, X.1    Zhao, Y.2    Narcisse, L.3    Duffy, H.4    Kress, Y.5    Lee, S.6    Brosnan, C.F.7
  • 108
    • 0037423392 scopus 로고    scopus 로고
    • Lanthanides potentiate TRPC5 currents by an action at extracellular sites close to the pore mouth
    • S. Jung A. Muhle M. Schaefer R. Strotmann G. Schultz T.D. Plant Lanthanides potentiate TRPC5 currents by an action at extracellular sites close to the pore mouth J. Biol. Chem. 278 2003 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
  • 110
    • 0041708061 scopus 로고    scopus 로고
    • TRPC5 is a regulator of hippocampal neurite length and growth cone morphology
    • A. Greka B. Navarro E. Oancea A. Duggan D.E. Clapham TRPC5 is a regulator of hippocampal neurite length and growth cone morphology Nat. Neurosci. 6 2003 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
  • 113
    • 0036086490 scopus 로고    scopus 로고
    • TRPC6 is a candidate channel involved in receptor-stimulated cation currents in A7r5 smooth muscle cells
    • S. Jung R. Strotmann G. Schultz T.D. Plant TRPC6 is a candidate channel involved in receptor-stimulated cation currents in A7r5 smooth muscle cells Am. J. Physiol. 282 2002 C347-C359
    • (2002) Am. J. Physiol. , vol.282
    • Jung, S.1    Strotmann, R.2    Schultz, G.3    Plant, T.D.4
  • 114
    • 0037108297 scopus 로고    scopus 로고
    • Expression and role of TRPC proteins in human platelets: Evidence that TRPC6 forms the store-independent calcium entry channel
    • S.R. Hassock M.X. Zhu C. Trost V. Flockerzi K.S. Authi Expression and role of TRPC proteins in human platelets: Evidence that TRPC6 forms the store-independent calcium entry channel Blood 100 2002 2801-2811
    • (2002) Blood , vol.100 , pp. 2801-2811
    • Hassock, S.R.1    Zhu, M.X.2    Trost, C.3    Flockerzi, V.4    Authi, K.S.5
  • 117
    • 0242391824 scopus 로고    scopus 로고
    • Synergism between inositol phosphates and diacylglycerol on native TRPC6-like channels in rabbit portal vein myocytes
    • A.P. Albert W.A. Large Synergism between inositol phosphates and diacylglycerol on native TRPC6-like channels in rabbit portal vein myocytes J. Physiol. 552 2003 789-795
    • (2003) J. Physiol. , vol.552 , pp. 789-795
    • Albert, A.P.1    Large, W.A.2
  • 118
    • 0041856188 scopus 로고    scopus 로고
    • 20-hydroxyeicosatetraenoic acid (20-HETE) activates mouse TRPC6 channels expressed in HEK293 cells
    • N. Basora G. Boulay L. Bilodeau E. Rousseau M.D. Payet 20-hydroxyeicosatetraenoic acid (20-HETE) activates mouse TRPC6 channels expressed in HEK293 cells J. Biol. Chem. 278 2003 31709-31716
    • (2003) J. Biol. Chem. , vol.278 , pp. 31709-31716
    • Basora, N.1    Boulay, G.2    Bilodeau, L.3    Rousseau, E.4    Payet, M.D.5
  • 119
    • 10644283084 scopus 로고    scopus 로고
    • Multiple regulation by calcium of murine homologues of transient receptor potential proteins TRPC6 and TRPC7 expressed in HEK293 cells
    • J. Shi E. Mori Y. Mori M. Mori J. Li Y. Ito R. Inoue Multiple regulation by calcium of murine homologues of transient receptor potential proteins TRPC6 and TRPC7 expressed in HEK293 cells J. Physiol. 561 2004 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
  • 120
    • 10644272681 scopus 로고    scopus 로고
    • Activation of TRPC6 channel proteins: Evidence for an essential role of phosphorylation
    • A.P. Albert Activation of TRPC6 channel proteins: Evidence for an essential role of phosphorylation J. Physiol. 561 2004 354
    • (2004) J. Physiol. , vol.561 , pp. 354
    • Albert, A.P.1
  • 122
    • 1342304080 scopus 로고    scopus 로고
    • Exocytotic insertion of TRPC6 channel into the plasma membrane upon Gq protein-coupled receptor activation
    • S. Cayouette M.P. Lussier E.L. Mathieu S.M. Bousquet G. Boulay Exocytotic insertion of TRPC6 channel into the plasma membrane upon Gq protein-coupled receptor activation J. Biol. Chem. 279 2004 7241-7246
    • (2004) J. Biol. Chem. , vol.279 , pp. 7241-7246
    • Cayouette, S.1    Lussier, M.P.2    Mathieu, E.L.3    Bousquet, S.M.4    Boulay, G.5
  • 124
    • 0036277884 scopus 로고    scopus 로고
    • Vanilloid and TRP channels: A family of lipid-gated cation channels
    • C.D. Benham J.B. Davis A.D. Randall Vanilloid and TRP channels: A family of lipid-gated cation channels Neuropharmacology 42 2002 873-888
    • (2002) Neuropharmacology , vol.42 , pp. 873-888
    • Benham, C.D.1    Davis, J.B.2    Randall, A.D.3
  • 125
    • 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
    • H.A. Colbert T.L. Smith C.I. Bargmann OSM-9, a novel protein with structural similarity to channels, is required for olfaction, mechanosensation, and olfactory adaptation in Caenorhabditis elegans J. Neurosci. 17 1997 8259-8269
    • (1997) J. Neurosci. , vol.17 , pp. 8259-8269
    • Colbert, H.A.1    Smith, T.L.2    Bargmann, C.I.3
  • 132
    • 0038049930 scopus 로고    scopus 로고
    • The TRPV4 channel: Structure-function relationship and promiscuous gating behaviour
    • B. Nilius H. Watanabe J. Vriens The TRPV4 channel: Structure-function relationship and promiscuous gating behaviour Pflügers Arch. 446 2003 298-303
    • (2003) Pflügers Arch. , vol.446 , pp. 298-303
    • Nilius, B.1    Watanabe, H.2    Vriens, J.3
  • 135
    • 2642568616 scopus 로고    scopus 로고
    • 2-aminoethoxydiphenyl borate activates and sensitizes the heat-gated ion channel TRPV3
    • M.K. Chung H. Lee A. Mizuno M. Suzuki M.J. Caterina 2-aminoethoxydiphenyl borate activates and sensitizes the heat-gated ion channel TRPV3 J. Neurosci. 24 2004 5177-5182
    • (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
  • 136
    • 24644470357 scopus 로고    scopus 로고
    • Functional aspects and mechanisms of TRPV1 involvement in neurogenic inflammation that leads to thermal hyperalgesia
    • edited by B. Nilius Functional Role of TRP Channels
    • R. Planells-Cases, N. Garcia-Sanz, C. Morenilla-Paloa, A. Ferrer-Montiel, 2005. Functional aspects and mechanisms of TRPV1 involvement in neurogenic inflammation that leads to thermal hyperalgesia. Pflügers Arch. Europ. J. Physiol., Special Issue, Functional role of TRP channels, edited by B. Nilius.
    • (2005) Pflügers Arch. Europ. J. Physiol. , Issue.SPEC. ISSUE
    • Planells-Cases, R.1    Garcia-Sanz, N.2    Morenilla-Paloa, C.3    Ferrer-Montiel, A.4
  • 139
    • 0034926291 scopus 로고    scopus 로고
    • The vanilloid receptor: A molecular gateway to the pain pathway
    • M.J. Caterina D. Julius The vanilloid receptor: A molecular gateway to the pain pathway Annu. Rev. Neurosci. 24 2001 487-517
    • (2001) Annu. Rev. Neurosci. , vol.24 , pp. 487-517
    • Caterina, M.J.1    Julius, D.2
  • 141
    • 2442636258 scopus 로고    scopus 로고
    • Endovanilloids. Putative endogenous ligands of transient receptor potential vanilloid 1 channels
    • M. Van Der Stelt V. Di Marzo Endovanilloids. Putative endogenous ligands of transient receptor potential vanilloid 1 channels Eur. J. Biochem. 271 2004 1827-1834
    • (2004) Eur. J. Biochem. , vol.271 , pp. 1827-1834
    • Van Der Stelt, M.1    Di Marzo, V.2
  • 143
    • 0036183319 scopus 로고    scopus 로고
    • Molecular basis for species-specific sensitivity to "hot" chili peppers
    • S.E. Jordt D. Julius Molecular basis for species-specific sensitivity to "hot" chili peppers Cell 108 2002 421-430
    • (2002) Cell , vol.108 , pp. 421-430
    • Jordt, S.E.1    Julius, D.2
  • 144
    • 4043077669 scopus 로고    scopus 로고
    • The principle of temperature-dependent gating in cold- and heat-sensitive TRP channels
    • T. Voets G. Droogmans U. Wissenbach A. Janssens V. Flockerzi B. Nilius The principle of temperature-dependent gating in cold- and heat-sensitive TRP channels Nature 430 2004 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
  • 146
    • 0036291431 scopus 로고    scopus 로고
    • Activation of protein kinase C sensitizes human VR1 to capsaicin and to moderate decreases in pH at physiological temperatures in Xenopus oocytes
    • M. Crandall J. Kwash W. Yu G. White Activation of protein kinase C sensitizes human VR1 to capsaicin and to moderate decreases in pH at physiological temperatures in Xenopus oocytes Pain 98 2002 109-117
    • (2002) Pain , vol.98 , pp. 109-117
    • Crandall, M.1    Kwash, J.2    Yu, W.3    White, G.4
  • 147
    • 0037799198 scopus 로고    scopus 로고
    • A modular PIP2 binding site as a determinant of capsaicin receptor sensitivity
    • E.D. Prescott D. Julius A modular PIP2 binding site as a determinant of capsaicin receptor sensitivity Science 300 2003 1284-1288
    • (2003) Science , vol.300 , pp. 1284-1288
    • Prescott, E.D.1    Julius, D.2
  • 148
    • 0038712568 scopus 로고    scopus 로고
    • 2+-dependent potentiation of the nonselective cation channel TRPV4 is mediated by a carboxy terminal calmodulin binding site
    • 2+-dependent potentiation of the nonselective cation channel TRPV4 is mediated by a carboxy terminal calmodulin binding site J. Biol. Chem. 278 2003 26541-26549
    • (2003) J. Biol. Chem. , vol.278 , pp. 26541-26549
    • Strotmann, R.1    Schultz, G.2    Plant, T.D.3
  • 150
    • 19444363418 scopus 로고    scopus 로고
    • Extracellular cations sensitize and gate capsaicin receptor TRPV1 modulating pain signaling
    • G.P. Ahern I.M. Brooks R.L. Miyares X.B. Wang Extracellular cations sensitize and gate capsaicin receptor TRPV1 modulating pain signaling J. Neurosci. 25 2005 5109-5116
    • (2005) J. Neurosci. , vol.25 , pp. 5109-5116
    • Ahern, G.P.1    Brooks, I.M.2    Miyares, R.L.3    Wang, X.B.4
  • 151
    • 0042734414 scopus 로고    scopus 로고
    • Activation of TRPV1 by the satiety factor oleoylethanolamide
    • G.P. Ahern Activation of TRPV1 by the satiety factor oleoylethanolamide J. Biol. Chem. 278 2003 30429-30434
    • (2003) J. Biol. Chem. , vol.278 , pp. 30429-30434
    • Ahern, G.P.1
  • 152
    • 17844392649 scopus 로고    scopus 로고
    • Oleoylethanolamide excites vagal sensory neurons, induces visceral pain and reduces short-term food intake in mice via TRPV1
    • X. Wang R.L. Miyares G.P. Ahern Oleoylethanolamide excites vagal sensory neurons, induces visceral pain and reduces short-term food intake in mice via TRPV1 J. Physiol. 564 2005 541-547
    • (2005) J. Physiol. , vol.564 , pp. 541-547
    • Wang, X.1    Miyares, R.L.2    Ahern, G.P.3
  • 155
    • 0033119629 scopus 로고    scopus 로고
    • A capsaicin-receptor homologue with a high threshold for noxious heat
    • M.J. Caterina T.A. Rosen M. Tominaga A.J. Brake D. Julius A capsaicin-receptor homologue with a high threshold for noxious heat Nature 398 1999 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
  • 156
    • 0033529578 scopus 로고    scopus 로고
    • Molecular identification of a eukaryotic, stretch-activated nonselective cation channel
    • M. Kanzaki M. Nagasawa I. Kojima C. Sato K. Naruse M. Sokabe H. Iida Molecular identification of a eukaryotic, stretch-activated nonselective cation channel Science 285 1999 882-886
    • (1999) Science , vol.285 , pp. 882-886
    • Kanzaki, M.1    Nagasawa, M.2    Kojima, I.3    Sato, C.4    Naruse, K.5    Sokabe, M.6    Iida, H.7
  • 158
  • 160
    • 0035918311 scopus 로고    scopus 로고
    • The activity of anandamide at vanilloid VR1 receptors requires facilitated transport across the cell membrane and is limited by intracellular metabolism
    • L. De Petrocellis T. Bisogno M. Maccarrone J.B. Davis A. Finazzi-Agro V. Di Marzo The activity of anandamide at vanilloid VR1 receptors requires facilitated transport across the cell membrane and is limited by intracellular metabolism J. Biol. Chem. 276 2001 12856-12863
    • (2001) J. Biol. Chem. , vol.276 , pp. 12856-12863
    • De Petrocellis, L.1    Bisogno, T.2    Maccarrone, M.3    Davis, J.B.4    Finazzi-Agro, A.5    Di Marzo, V.6
  • 163
    • 0041355261 scopus 로고    scopus 로고
    • Warm temperatures activate TRPV4 in mouse 308 keratinocytes
    • M.-K. Chung H. Lee M.J. Caterina Warm temperatures activate TRPV4 in mouse 308 keratinocytes J Biol Chem. 278 2003 32037-32046
    • (2003) J Biol Chem. , vol.278 , pp. 32037-32046
    • Chung, M.-K.1    Lee, H.2    Caterina, M.J.3
  • 166
    • 0037033077 scopus 로고    scopus 로고
    • Heat-evoked activation of TRPV4 channels in a HEK293 cell expression system and in native mouse aorta endothelial cells
    • H. Watanabe J. Vriens S.H. Suh C.D. Benham G. Droogmans B. Nilius Heat-evoked activation of TRPV4 channels in a HEK293 cell expression system and in native mouse aorta endothelial cells J. Biol. Chem. 277 2002 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
  • 168
    • 0043267987 scopus 로고    scopus 로고
    • Anandamide and arachidonic acid use epoxyeicosatrienoic acids to activate TRPV4 channels
    • H. Watanabe J. Vriens J. Prenen G. Droogmans T. Voets B. Nilius Anandamide and arachidonic acid use epoxyeicosatrienoic acids to activate TRPV4 channels Nature 424 2003 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
  • 170
    • 0347719316 scopus 로고    scopus 로고
    • Cell swelling, heat, and chemical agonists use distinct pathways for the activation of the cation channel TRPV4
    • J. Vriens H. Watanabe A. Janssens G. Droogmans T. Voets B. Nilius Cell swelling, heat, and chemical agonists use distinct pathways for the activation of the cation channel TRPV4 Proc. Natl. Acad. Sci. USA 101 2004 396-401
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 396-401
    • Vriens, J.1    Watanabe, H.2    Janssens, A.3    Droogmans, G.4    Voets, T.5    Nilius, B.6
  • 171
    • 0037697228 scopus 로고    scopus 로고
    • Temperature-modulated diversity of TRPV4 channel gating: Activation by physical stresses and phorbol ester derivatives through protein kinase C-dependent and -independent pathways
    • X. Gao L. Wu R.G. O'Neil Temperature-modulated diversity of TRPV4 channel gating: Activation by physical stresses and phorbol ester derivatives through protein kinase C-dependent and -independent pathways J. Biol. Chem. 278 2003 27129-27137
    • (2003) J. Biol. Chem. , vol.278 , pp. 27129-27137
    • Gao, X.1    Wu, L.2    O'Neil, R.G.3
  • 172
    • 0346435090 scopus 로고    scopus 로고
    • Microfilament-associated protein 7 increases the membrane expression of transient receptor potential vanilloid 4 (TRPV4)
    • M. Suzuki A. Hirao A. Mizuno Microfilament-associated protein 7 increases the membrane expression of transient receptor potential vanilloid 4 (TRPV4) J. Biol. Chem. 278 2003 51448-51453
    • (2003) J. Biol. Chem. , vol.278 , pp. 51448-51453
    • Suzuki, M.1    Hirao, A.2    Mizuno, A.3
  • 175
    • 0037974416 scopus 로고    scopus 로고
    • The epithelial calcium channels, TRPV5 & TRPV6: From identification towards regulation
    • E. Den Dekker J.G. Hoenderop B. Nilius R.J.T. Bindels The epithelial calcium channels, TRPV5 & TRPV6: From identification towards regulation Cell Calcium 33 2003 497-507
    • (2003) Cell Calcium , vol.33 , pp. 497-507
    • Den Dekker, E.1    Hoenderop, J.G.2    Nilius, B.3    Bindels, R.J.T.4
  • 176
    • 0035810243 scopus 로고    scopus 로고
    • CaT1 manifests the pore properties of the calcium-release-activated calcium channel
    • L. Yue J.B. Peng M.A. Hediger D.E. Clapham CaT1 manifests the pore properties of the calcium-release-activated calcium channel Nature 410 2001 705-709
    • (2001) Nature , vol.410 , pp. 705-709
    • Yue, L.1    Peng, J.B.2    Hediger, M.A.3    Clapham, D.E.4
  • 178
    • 0038312015 scopus 로고    scopus 로고
    • From TRPs to SOCs, CCEs, and CRACs: Consensus and controversies
    • B. Nilius From TRPs to SOCs, CCEs, and CRACs: Consensus and controversies Cell Calcium 33 2003 293-298
    • (2003) Cell Calcium , vol.33 , pp. 293-298
    • Nilius, B.1
  • 182
    • 3142704668 scopus 로고    scopus 로고
    • Regulation of the mouse epithelial Ca2(+) channel TRPV6 by the Ca(2+)-sensor calmodulin
    • T.T. Lambers A.F. Weidema B. Nilius J.G. Hoenderop R.J. Bindels Regulation of the mouse epithelial Ca2(+) channel TRPV6 by the Ca(2+)-sensor calmodulin J. Biol. Chem. 279 2004 28855-28861
    • (2004) J. Biol. Chem. , vol.279 , pp. 28855-28861
    • Lambers, T.T.1    Weidema, A.F.2    Nilius, B.3    Hoenderop, J.G.4    Bindels, R.J.5
  • 188
    • 1642515793 scopus 로고    scopus 로고
    • Transcriptional regulation of the melanoma prognostic marker melastatin (TRPM1) by MITF in melanocytes and melanoma
    • A.J. Miller J. Du S. Rowan C.L. Hershey H.R. Widlund D.E. Fisher Transcriptional regulation of the melanoma prognostic marker melastatin (TRPM1) by MITF in melanocytes and melanoma Cancer Res. 64 2004 509-516
    • (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
  • 189
    • 0035845566 scopus 로고    scopus 로고
    • Regulation of melastatin, a TRP-related protein, through interaction with a cytoplasmic isoform
    • X.Z. Xu F. Moebius D.L. Gill C. Montell Regulation of melastatin, a TRP-related protein, through interaction with a cytoplasmic isoform Proc. Natl. Acad. Sci. USA 4 2001 4
    • (2001) Proc. Natl. Acad. Sci. USA , vol.4 , pp. 4
    • Xu, X.Z.1    Moebius, F.2    Gill, D.L.3    Montell, C.4
  • 190
    • 24644505615 scopus 로고    scopus 로고
    • The mammalian melastatin-related transient receptor potential cation channels: An overview
    • edited by B. Nilius Functional Role of TRP Channels
    • R. Kraft, C. Harteneck, 2005, The mammalian melastatin-related transient receptor potential cation channels: An overview, Pflügers Arch. Europ. J. Physiol., Special Issue, Functional role of TRP channels, edited by B. Nilius.
    • (2005) Pflügers Arch. Europ. J. Physiol. , Issue.SPEC. ISSUE
    • Kraft, R.1    Harteneck, C.2
  • 195
    • 3042515434 scopus 로고    scopus 로고
    • Novel aspects of signaling and ion-homeostasis regulation in immunocytes. The TRPM ion channels and their potential role in modulating the immune response
    • A.L. Perraud H.M. Knowles C. Schmitz Novel aspects of signaling and ion-homeostasis regulation in immunocytes. The TRPM ion channels and their potential role in modulating the immune response Mol. Immunol. 41 2004 657-673
    • (2004) Mol. Immunol. , vol.41 , pp. 657-673
    • Perraud, A.L.1    Knowles, H.M.2    Schmitz, C.3
  • 198
    • 0038498142 scopus 로고    scopus 로고
    • Molecular and functional characterization of the melastatin-related cation channel TRPM3
    • C. Grimm R. Kraft S. Sauerbruch G. Schultz C. Harteneck Molecular and functional characterization of the melastatin-related cation channel TRPM3 J. Biol. Chem. 278 2003 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
  • 200
    • 14944348415 scopus 로고    scopus 로고
    • Activation of the melastatin-related cation channel TRMP3 by d-erythro-Sphingosine
    • C. Grimm R. Kraft G. Schultz C. Harteneck Activation of the melastatin-related cation channel TRMP3 by d-erythro-Sphingosine Mol. Pharmacol. 67 2005 798-805
    • (2005) Mol. Pharmacol. , vol.67 , pp. 798-805
    • Grimm, C.1    Kraft, R.2    Schultz, G.3    Harteneck, C.4
  • 203
    • 0037672155 scopus 로고    scopus 로고
    • TRPM5 is a voltage-modulated and Ca(2+)-activated monovalent selective cation channel
    • T. Hofmann V. Chubanov T. Gudermann C. Montell TRPM5 is a voltage-modulated and Ca(2+)-activated monovalent selective cation channel Curr. Biol. 13 2003 1153-1158
    • (2003) Curr. Biol. , vol.13 , pp. 1153-1158
    • Hofmann, T.1    Chubanov, V.2    Gudermann, T.3    Montell, C.4
  • 205
    • 0037423367 scopus 로고    scopus 로고
    • Coding of sweet, bitter, and umami tastes: Different receptor cells sharing similar signaling pathways
    • Y. Zhang M.A. Hoon J. Chandrashekar K.L. Mueller B. Cook D. Wu C.S. Zuker N.J. Ryba Coding of sweet, bitter, and umami tastes: Different receptor cells sharing similar signaling pathways Cell 112 2003 293-301
    • (2003) Cell , vol.112 , pp. 293-301
    • Zhang, Y.1    Hoon, M.A.2    Chandrashekar, J.3    Mueller, K.L.4    Cook, B.5    Wu, D.6    Zuker, C.S.7    Ryba, N.J.8
  • 209
    • 0344149569 scopus 로고    scopus 로고
    • 2+ and the phospholipid PIP2 regulate the taste transduction ion channel TRPM5
    • 2+ and the phospholipid PIP2 regulate the taste transduction ion channel TRPM5 Proc. Natl. Acad. Sci. USA 100 2003 15160-15165
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 15160-15165
    • Liu, D.1    Liman, E.R.2
  • 210
    • 17844373771 scopus 로고    scopus 로고
    • PI(4,5)P(2) regulates the activation and desensitization of TRPM8 channels through the TRP domain
    • T. Rohacs C.M. Lopes I. Michailidis D.E. Logothetis PI(4,5)P(2) regulates the activation and desensitization of TRPM8 channels through the TRP domain Nat. Neurosci. 8 2005 626-634
    • (2005) Nat. Neurosci. , vol.8 , pp. 626-634
    • Rohacs, T.1    Lopes, C.M.2    Michailidis, I.3    Logothetis, D.E.4
  • 212
    • 0035131504 scopus 로고    scopus 로고
    • TRP-PLIK, a bifunctional protein with kinase and ion channel activities
    • L.W. Runnels L. Yue D.E. Clapham TRP-PLIK, a bifunctional protein with kinase and ion channel activities Science 291 2001 1043-1047
    • (2001) Science , vol.291 , pp. 1043-1047
    • Runnels, L.W.1    Yue, L.2    Clapham, D.E.3
  • 213
    • 0036521977 scopus 로고    scopus 로고
    • Dissociation of the store-operated calcium current ICRAC and the Mg-nucleotide-regulated metal ion current MagNuM
    • M.C. Hermosura M.K. Monteilh-Zoller A.M. Scharenberg R. Penner A. Fleig Dissociation of the store-operated calcium current ICRAC and the Mg-nucleotide-regulated metal ion current MagNuM J. Physiol. Lond. 539 2002 445-458
    • (2002) J. Physiol. Lond. , vol.539 , pp. 445-458
    • Hermosura, M.C.1    Monteilh-Zoller, M.K.2    Scharenberg, A.M.3    Penner, R.4    Fleig, A.5
  • 219
    • 0035902925 scopus 로고    scopus 로고
    • Biochemistry. TRP ion channels-two proteins in one
    • I.B. Levitan S.M. Cibulsky Biochemistry. TRP ion channels-two proteins in one Science 293 2001 1270-1271
    • (2001) Science , vol.293 , pp. 1270-1271
    • Levitan, I.B.1    Cibulsky, S.M.2
  • 220
    • 1842536165 scopus 로고    scopus 로고
    • Alpha-kinases: Analysis of the family and comparison with conventional protein kinases
    • D. Drennan A.G. Ryazanov Alpha-kinases: Analysis of the family and comparison with conventional protein kinases Prog. Biophys. Mol. Biol. 85. 2004 1-32
    • (2004) Prog. Biophys. Mol. Biol. , vol.85 , pp. 1-32
    • Drennan, D.1    Ryazanov, A.G.2
  • 222
    • 0036092076 scopus 로고    scopus 로고
    • The TRPM7 channel is inactivated by PIP(2) hydrolysis
    • L.W. Runnels L. Yue D.E. Clapham The TRPM7 channel is inactivated by PIP(2) hydrolysis Nat. Cell Biol. 4 2002 329-336
    • (2002) Nat. Cell Biol. , vol.4 , pp. 329-336
    • Runnels, L.W.1    Yue, L.2    Clapham, D.E.3
  • 224
    • 15244362816 scopus 로고    scopus 로고
    • TRPM7 and ischemic CNS injury
    • M.M. Aarts M. Tymianski TRPM7 and ischemic CNS injury Neuroscientist 11 2005 116-123
    • (2005) Neuroscientist , vol.11 , pp. 116-123
    • Aarts, M.M.1    Tymianski, M.2
  • 225
    • 0033174726 scopus 로고    scopus 로고
    • Magnesium in cell proliferation and differentiation
    • F.I. Wolf A. Cittadini Magnesium in cell proliferation and differentiation Front Biosci. 4 1999 D607-D617
    • (1999) Front Biosci. , vol.4
    • Wolf, F.I.1    Cittadini, A.2
  • 227
    • 0035328671 scopus 로고    scopus 로고
    • Trp-p8, a novel prostate-specific gene, is up-regulated in prostate cancer and other malignancies and shares high homology with transient receptor potential calcium channel proteins
    • L. Tsavaler M.H. Shapero S. Morkowski R. Laus Trp-p8, a novel prostate-specific gene, is up-regulated in prostate cancer and other malignancies and shares high homology with transient receptor potential calcium channel proteins Cancer Res. 61 2001 3760-3769
    • (2001) Cancer Res. , vol.61 , pp. 3760-3769
    • Tsavaler, L.1    Shapero, M.H.2    Morkowski, S.3    Laus, R.4
  • 230
    • 18144421118 scopus 로고    scopus 로고
    • Biphasic currents evoked by chemical or thermal activation of TRPV3
    • M.-K. Chung A.D. Güler M.J. Caterina Biphasic currents evoked by chemical or thermal activation of TRPV3 J. Biol. Chem. 280 2005 15928-15941
    • (2005) J. Biol. Chem. , vol.280 , pp. 15928-15941
    • Chung, M.-K.1    Güler, A.D.2    Caterina, M.J.3
  • 231
    • 2942536048 scopus 로고    scopus 로고
    • TRPM8 activation by menthol, icilin, and cold is differentially modulated by intracellular pH
    • D.A. Andersson H.W. Chase S. Bevan TRPM8 activation by menthol, icilin, and cold is differentially modulated by intracellular pH J. Neurosci. 24 2004 5364-5369
    • (2004) J. Neurosci. , vol.24 , pp. 5364-5369
    • Andersson, D.A.1    Chase, H.W.2    Bevan, S.3
  • 232
    • 4544368241 scopus 로고    scopus 로고
    • The super-cooling agent icilin reveals a mechanism of coincidence detection by a temperature-sensitive TRP channel
    • H.H. Chuang W.M. Neuhausser D. Julius The super-cooling agent icilin reveals a mechanism of coincidence detection by a temperature-sensitive TRP channel Neuron 43 2004 859-869
    • (2004) Neuron , vol.43 , pp. 859-869
    • Chuang, H.H.1    Neuhausser, W.M.2    Julius, D.3
  • 234
    • 0034894817 scopus 로고    scopus 로고
    • Mucolipidosis type IV
    • G. Bach Mucolipidosis type IV Mol. Genet. Metab. 73 2001 197-203
    • (2001) Mol. Genet. Metab. , vol.73 , pp. 197-203
    • Bach, G.1
  • 235
    • 85029465493 scopus 로고    scopus 로고
    • Mucolipin 1: Endocytosis and cation channel - A review
    • edited by B. Nilius Functional Role of TRP Channels
    • G. Bach, 2004, Mucolipin 1: Endocytosis and cation channel - a review. Pflugers Arch. Eur. J. Physiol., Special Issue, Functional role of TRP channels, edited by B. Nilius.
    • (2004) Pflugers Arch. Eur. J. Physiol. , Issue.SPEC. ISSUE
    • Bach, G.1
  • 236
    • 18744363612 scopus 로고    scopus 로고
    • Identification and characterization of the single channel function of human mucolipin-1 implicated in mucolipidosis type IV, a disorder affecting the lysosomal pathway
    • J.M. LaPlante J. Falardeau M. Sun M. Kanazirska E.M. Brown S.A. Slaugenhaupt P.M. Vassilev Identification and characterization of the single channel function of human mucolipin-1 implicated in mucolipidosis type IV, a disorder affecting the lysosomal pathway FEBS Lett. 532 2002 183-187
    • (2002) FEBS Lett. , vol.532 , pp. 183-187
    • LaPlante, J.M.1    Falardeau, J.2    Sun, M.3    Kanazirska, M.4    Brown, E.M.5    Slaugenhaupt, S.A.6    Vassilev, P.M.7
  • 238
    • 4444271489 scopus 로고    scopus 로고
    • CUPpling calcium to lysosomal biogenesis
    • R.C. Piper J.P. Luzio CUPpling calcium to lysosomal biogenesis Trends Cell Biol. 14 2004 471-473
    • (2004) Trends Cell Biol. , vol.14 , pp. 471-473
    • Piper, R.C.1    Luzio, J.P.2
  • 243
    • 24644485135 scopus 로고    scopus 로고
    • Polycystins (TRPP): Polymodal receptor-ion channel cellular sensors
    • edited by B. Nilius Functional Role of TRP Channels
    • P. Delmas, 2005, Polycystins (TRPP): Polymodal receptor-ion channel cellular sensors, Pflügers Arch. Eur. J. Physiol., Special Issue, Functional role of TRP channels, edited by B. Nilius.
    • (2005) Pflügers Arch. Eur. J. Physiol. , Issue.SPEC. ISSUE
    • Delmas, P.1
  • 244
  • 247
    • 0036123997 scopus 로고    scopus 로고
    • The ins and outs of polycystin-2 as a calcium release channel
    • M.D. Cahalan The ins and outs of polycystin-2 as a calcium release channel Nat. Cell Biol. 4 2002 E56-E57
    • (2002) Nat. Cell Biol. , vol.4
    • Cahalan, M.D.1
  • 250
    • 0343619383 scopus 로고    scopus 로고
    • Identification and characterization of a novel polycystin family member, polycystin-L2, in mouse and human: Sequence, expression, alternative splicing, and chromosomal localization
    • L. Guo T.H. Schreiber S. Weremowicz C.C. Morton C. Lee J. Zhou Identification and characterization of a novel polycystin family member, polycystin-L2, in mouse and human: Sequence, expression, alternative splicing, and chromosomal localization Genomics 64 2000 241-251
    • (2000) Genomics , vol.64 , pp. 241-251
    • Guo, L.1    Schreiber, T.H.2    Weremowicz, S.3    Morton, C.C.4    Lee, C.5    Zhou, J.6
  • 251
    • 0033972998 scopus 로고    scopus 로고
    • Molecular genetics and mechanism of autosomal dominant polycystic kidney disease
    • G. Wu S. Somlo Molecular genetics and mechanism of autosomal dominant polycystic kidney disease Mol. Genet. Metab. 69 2000 1-15
    • (2000) Mol. Genet. Metab. , vol.69 , pp. 1-15
    • Wu, G.1    Somlo, S.2
  • 256
    • 0037401071 scopus 로고    scopus 로고
    • A polycystin-2-like large conductance cation channel in rat left ventricular myocytes
    • T. Volk A.P. Schwoerer S. Thiessen J.H. Schultz H. Ehmke A polycystin-2-like large conductance cation channel in rat left ventricular myocytes Cardiovasc. Res. 58 2003 76-88
    • (2003) Cardiovasc. Res. , vol.58 , pp. 76-88
    • Volk, T.1    Schwoerer, A.P.2    Thiessen, S.3    Schultz, J.H.4    Ehmke, H.5
  • 260
    • 33845222371 scopus 로고    scopus 로고
    • How cold is it? TRPM8 and TRPA1 in the molecular logic of cold sensation
    • D.D. McKemy How cold is it? TRPM8 and TRPA1 in the molecular logic of cold sensation Mol. Pain 1 2005 16
    • (2005) Mol. Pain , vol.1 , pp. 16
    • McKemy, D.D.1
  • 262
    • 17644426325 scopus 로고    scopus 로고
    • Nociceptor and hair cell transducer properties of TRPA1, a channel for pain and hearing
    • K. Nagata A. Duggan G. Kumar J. Garcia-Anoveros Nociceptor and hair cell transducer properties of TRPA1, a channel for pain and hearing J. Neurosci. 25 2005 4052-4061
    • (2005) J. Neurosci. , vol.25 , pp. 4052-4061
    • Nagata, K.1    Duggan, A.2    Kumar, G.3    Garcia-Anoveros, J.4
  • 263
    • 0034708452 scopus 로고    scopus 로고
    • A Drosophila mechanosensory transduction channel
    • R.G. Walker A.T. Willingham C.S. Zuker A Drosophila mechanosensory transduction channel Science 287 2000 2229-2234
    • (2000) Science , vol.287 , pp. 2229-2234
    • Walker, R.G.1    Willingham, A.T.2    Zuker, C.S.3
  • 264
    • 0037710542 scopus 로고    scopus 로고
    • NompC TRP channel required for vertebrate sensory hair cell mechanotransduction
    • S. Sidi R.W. Friedrich T. Nicolson NompC TRP channel required for vertebrate sensory hair cell mechanotransduction Science 301 2003 96-99
    • (2003) Science , vol.301 , pp. 96-99
    • Sidi, S.1    Friedrich, R.W.2    Nicolson, T.3


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