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Volumn 1742, Issue 1-3, 2004, Pages 21-36

The mammalian TRPC cation channels

Author keywords

Calcium channel; Capacitative calcium entry; Diacylglycerol; Inositol trisphosphate receptor; Ion channel; Non selective cation channel; Phospholipase C; Second messenger operated channel; Store operated channel; TRP channel; TRPC channel

Indexed keywords

AMINO ACID DERIVATIVE; CATION CHANNEL; MEMBRANE PROTEIN; PROTEIN DERIVATIVE;

EID: 10044259546     PISSN: 01674889     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbamcr.2004.08.015     Document Type: Conference Paper
Times cited : (287)

References (141)
  • 1
    • 0028800096 scopus 로고
    • Molecular cloning of a widely expressed human homologue for the Drosophila trp gene
    • X. Zhu, P.B. Chu, M. Peyton, and L. Birnbaumer Molecular cloning of a widely expressed human homologue for the Drosophila trp gene FEBS Lett. 373 1995 193 198
    • (1995) FEBS Lett. , vol.373 , pp. 193-198
    • Zhu, X.1    Chu, P.B.2    Peyton, M.3    Birnbaumer, L.4
  • 5
    • 0033280228 scopus 로고    scopus 로고
    • Visual transduction in Drosophila
    • C. Montell Visual transduction in Drosophila Annu. Rev. Cell Dev. Biol. 15 1999 231 268
    • (1999) Annu. Rev. Cell Dev. Biol. , vol.15 , pp. 231-268
    • Montell, C.1
  • 8
    • 0036223954 scopus 로고    scopus 로고
    • The TRP family of cation channels: Probing and advancing the concepts on receptor-activated calcium entry
    • C. Zitt, C.R. Halaszovich, and A. Lückhoff The TRP family of cation channels: probing and advancing the concepts on receptor-activated calcium entry Prog. Neurobiol. 66 2002 243 264
    • (2002) Prog. Neurobiol. , vol.66 , pp. 243-264
    • Zitt, C.1    Halaszovich, C.R.2    Lückhoff, A.3
  • 10
    • 0037452884 scopus 로고    scopus 로고
    • Relaxed selective pressure on an essential component of pheromone transduction in primate evolution
    • E.R. Liman, and H. Innan Relaxed selective pressure on an essential component of pheromone transduction in primate evolution Proc. Natl. Acad. Sci. 100 2003 3328 3332
    • (2003) Proc. Natl. Acad. Sci. , vol.100 , pp. 3328-3332
    • Liman, E.R.1    Innan, H.2
  • 11
    • 0032502787 scopus 로고    scopus 로고
    • The membrane topology of human transient receptor potential 3 as inferred from glycosylation-scanning mutagenesis and epitope immunocytochemistry
    • B. Vannier, X. Zhu, D. Brown, and L. Birnbaumer The membrane topology of human transient receptor potential 3 as inferred from glycosylation-scanning mutagenesis and epitope immunocytochemistry J. Biol. Chem. 273 1998 8675 8679
    • (1998) J. Biol. Chem. , vol.273 , pp. 8675-8679
    • Vannier, B.1    Zhu, X.2    Brown, D.3    Birnbaumer, L.4
  • 13
    • 2442706456 scopus 로고    scopus 로고
    • The ankyrin repeat as molecular architecture for protein recognition
    • L.K. Mosavi, T.J. Cammett, D.C. Desrosiers, and Z.y. Peng The ankyrin repeat as molecular architecture for protein recognition Protein Sci. 13 2004 1435 1448
    • (2004) Protein Sci. , vol.13 , pp. 1435-1448
    • Mosavi, L.K.1    Cammett, T.J.2    Desrosiers, D.C.3    Peng, Z.Y.4
  • 14
    • 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
    • B.J. Wedel, G. Vazquez, R.R. McKay, G.St.J. Bird, and 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    Bird, G.St.J.4    Putney Jr., J.W.5
  • 17
    • 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, and 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
  • 19
    • 3142582011 scopus 로고    scopus 로고
    • Caveolins: Structure and function in signal transduction
    • W.M. Krajewska, and I. Maslowska Caveolins: structure and function in signal transduction Cell. Mol. Biol. Lett. 9 2004 195 220
    • (2004) Cell. Mol. Biol. Lett. , vol.9 , pp. 195-220
    • Krajewska, W.M.1    Maslowska, I.2
  • 21
    • 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. Wieland, and 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    Wieland, S.5    Ambudkar, I.S.6
  • 22
    • 0035834716 scopus 로고    scopus 로고
    • 2+ influx without disruption of Trp3-inositol trisphosphate receptor association
    • 2+ influx without disruption of Trp3-inositol trisphosphate receptor association J. Biol. Chem. 276 2001 42401 42408
    • (2001) J. Biol. Chem. , vol.276 , pp. 42401-42408
    • Lockwich, T.1    Singh, B.B.2    Liu, X.3    Ambudkar, I.S.4
  • 23
    • 0030941001 scopus 로고    scopus 로고
    • Identification of peptide and protein ligands for the caveolin-scaffolding domain: Implications for the interaction of caveolin with caveolin-associated proteins
    • J. Couet, S.W. Li, T. Okamoto, T. Ikezu, and M.P. Lisanti Identification of peptide and protein ligands for the caveolin-scaffolding domain: Implications for the interaction of caveolin with caveolin-associated proteins J. Biol. Chem. 272 1997 6525 6533
    • (1997) J. Biol. Chem. , vol.272 , pp. 6525-6533
    • Couet, J.1    Li, S.W.2    Okamoto, T.3    Ikezu, T.4    Lisanti, M.P.5
  • 24
    • 0141755156 scopus 로고    scopus 로고
    • Formation of novel TRPC channels by complex subunit interactions in embryonic brain
    • C. Strubing, G. Krapivinsky, L. Krapivinsky, and 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
  • 25
    • 0037188517 scopus 로고    scopus 로고
    • Subunit composition of mammalian transient receptor potential channels in living cells
    • T. Hofmann, M. Schaefer, G. Schultz, and T. Gudermann Subunit composition of mammalian transient receptor potential channels in living cells Proc. Natl. Acad. Sci. U. S. A. 99 2002 7461 7466
    • (2002) Proc. Natl. Acad. Sci. U. S. A. , vol.99 , pp. 7461-7466
    • Hofmann, T.1    Schaefer, M.2    Schultz, G.3    Gudermann, T.4
  • 26
    • 0037423392 scopus 로고    scopus 로고
    • Lanthanides potentiate TRPC5 currents by an action at extracellular sites close to the pore mouth
    • S. Jung, A. Mühle, M. Schaefer, R. Strotmann, G. Schultz, and 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    Mühle, A.2    Schaefer, M.3    Strotmann, R.4    Schultz, G.5    Plant, T.D.6
  • 27
    • 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
  • 29
    • 4544271500 scopus 로고    scopus 로고
    • Association of immunophilins with mammalian TRPC channels
    • W.G. Sinkins, M. Goel, M. Estacion, and W.P. Schilling Association of immunophilins with mammalian TRPC channels J. Biol. Chem. 279 2004 34521 34529
    • (2004) J. Biol. Chem. , vol.279 , pp. 34521-34529
    • Sinkins, W.G.1    Goel, M.2    Estacion, M.3    Schilling, W.P.4
  • 32
    • 0035808240 scopus 로고    scopus 로고
    • Alternative splice variants of hTrp4 differentially interact with the C-terminal portion of the inositol 1,4,5-trisphosphate receptors
    • L. Mery, F. Magnino, K. Schmidt, and K.-H. Krause Alternative splice variants of hTrp4 differentially interact with the C-terminal portion of the inositol 1,4,5-trisphosphate receptors FEBS Lett. 487 2001 377 383
    • (2001) FEBS Lett. , vol.487 , pp. 377-383
    • Mery, L.1    Magnino, F.2    Schmidt, K.3    Krause, K.-H.4
  • 33
    • 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, and 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
  • 34
    • 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, and 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
  • 35
    • 0036713652 scopus 로고    scopus 로고
    • The PDZ-interacting domain of TRPC4 controls its localization and surface expression in HEK293 cells
    • L. Mery, B. Strauß, J.F. Dufour, K.H. Krause, and M. Hoth The PDZ-interacting domain of TRPC4 controls its localization and surface expression in HEK293 cells J. Cell. Sci. 115 2002 3497 3508
    • (2002) J. Cell. Sci. , vol.115 , pp. 3497-3508
    • Mery, L.1    Strauß, B.2    Dufour, J.F.3    Krause, K.H.4    Hoth, M.5
  • 36
    • 0346850851 scopus 로고    scopus 로고
    • N-linked protein glycosylation is a major determinant for basal TRPC3 and TRPC6 channel activity
    • A. Dietrich, M. Schnitzler, J. Emmel, H. Kalwa, T. Hofmann, and T. Gudermann N-linked protein glycosylation is a major determinant for basal TRPC3 and TRPC6 channel activity J. Biol. Chem. 278 2003 47842 47852
    • (2003) J. Biol. Chem. , vol.278 , pp. 47842-47852
    • Dietrich, A.1    Schnitzler, M.2    Emmel, J.3    Kalwa, H.4    Hofmann, T.5    Gudermann, T.6
  • 38
    • 0035051978 scopus 로고    scopus 로고
    • TRPC1 and TRPC5 form a novel cation channel in mammalian brain
    • C. Strübing, G. Krapivinsky, L. Krapivinsky, and 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
    • Strübing, C.1    Krapivinsky, G.2    Krapivinsky, L.3    Clapham, D.E.4
  • 40
    • 0026594980 scopus 로고
    • Depletion of intracellular calcium stores activates a calcium current in mast cells
    • M. Hoth, and R. Penner Depletion of intracellular calcium stores activates a calcium current in mast cells Nature 355 1992 353 355
    • (1992) Nature , vol.355 , pp. 353-355
    • Hoth, M.1    Penner, R.2
  • 41
    • 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, and 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
  • 43
    • 0031594711 scopus 로고    scopus 로고
    • 2+ influx via human Trp3 stably expressed in human embryonic kidney (HEK)293 cells. Evidence for a non-capacitative calcium entry
    • 2+ influx via human Trp3 stably expressed in human embryonic kidney (HEK)293 cells. Evidence for a non-capacitative calcium entry J. Biol. Chem. 273 1998 133 142
    • (1998) J. Biol. Chem. , vol.273 , pp. 133-142
    • Zhu, X.1    Jiang, M.2    Birnbaumer, L.3
  • 48
    • 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.St.J. Bird, R.R. McKay, and 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.St.J.2    McKay, R.R.3    Putney Jr., J.W.4
  • 49
    • 0034534979 scopus 로고    scopus 로고
    • Inhibition of TRP3 by lanthanides. Block from the cytosolic side of the plasma membrane
    • C.R. Halaszovich, C. Zitt, E. Jüngling, and A. Lückhoff Inhibition of TRP3 by lanthanides. Block from the cytosolic side of the plasma membrane J. Biol. Chem. 275 2000 37423 37428
    • (2000) J. Biol. Chem. , vol.275 , pp. 37423-37428
    • Halaszovich, C.R.1    Zitt, C.2    Jüngling, E.3    Lückhoff, A.4
  • 57
    • 0034714212 scopus 로고    scopus 로고
    • Calcium influx factor (CIF) directly activates store-operated cation channels in vascular smooth muscle cells
    • E.S. Trepakova, P. Csutora, D.L. Hunton, R.B. Marchase, R.A. Cohen, and V.M. Bolotina Calcium influx factor (CIF) directly activates store-operated cation channels in vascular smooth muscle cells J. Biol. Chem. 275 2000 26158 26163
    • (2000) J. Biol. Chem. , vol.275 , pp. 26158-26163
    • Trepakova, E.S.1    Csutora, P.2    Hunton, D.L.3    Marchase, R.B.4    Cohen, R.A.5    Bolotina, V.M.6
  • 58
    • 0036462592 scopus 로고    scopus 로고
    • 2+ stores in single rabbit portal vein myocytes
    • 2+ stores in single rabbit portal vein myocytes J. Physiol. (Lond.) 538 2002 717 728
    • (2002) J. Physiol. (Lond.) , vol.538 , pp. 717-728
    • Albert, A.P.1    Large, W.A.2
  • 61
  • 68
    • 0035910618 scopus 로고    scopus 로고
    • TrpC1 is a membrane-spanning subunit of store-operated Ca(2+) channels in native vascular smooth muscle cells
    • S.Z. Xu, and D.J. Beech TrpC1 is a membrane-spanning subunit of store-operated Ca(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
  • 71
    • 0034306264 scopus 로고    scopus 로고
    • Cloning, expression and subcellular localization of two splice variants of mouse transient receptor potential channel 2
    • T. Hofmann, M. Schaefer, G. Schultz, and T. Gudermann Cloning, expression and subcellular localization of two 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
  • 72
    • 0034872061 scopus 로고    scopus 로고
    • Involvement of trp-2 protein in store-operated influx of calcium in fibroblasts
    • P. Gailly, and 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, S.M.2
  • 75
    • 0030875355 scopus 로고    scopus 로고
    • Expression of TRPC3 in Chinese hamster ovary cells results in calcium-activated cation currents not related to store depletion
    • C. Zitt, A.G. Obukhov, C. Strübing, A. Zobel, F. Kalkbrenner, A. Lückhoff, and G. Schultz Expression of TRPC3 in Chinese hamster ovary cells results in calcium-activated cation currents not related to store depletion J. Cell Biol. 138 1997 1333 1341
    • (1997) J. Cell Biol. , vol.138 , pp. 1333-1341
    • Zitt, C.1    Obukhov, A.G.2    Strübing, C.3    Zobel, A.4    Kalkbrenner, F.5    Lückhoff, A.6    Schultz, G.7
  • 78
    • 0035949497 scopus 로고    scopus 로고
    • Trp3 forms both inositol trisphosphate receptor-dependent and independent store-operated cation channels in DT40 avian B-lymphocytes
    • G. Vazquez, J.-P. Lièvremont, G. St.J. Bird, and J.W. Putney Jr. Trp3 forms both inositol trisphosphate receptor-dependent and independent store-operated cation channels in DT40 avian B-lymphocytes Proc. Natl. Acad. Sci. U. S. A. 98 2001 11777 11782
    • (2001) Proc. Natl. Acad. Sci. U. S. A. , vol.98 , pp. 11777-11782
    • Vazquez, G.1    Lièvremont, J.-P.2    St.j. Bird, G.3    Putney Jr., J.W.4
  • 79
    • 0037484292 scopus 로고    scopus 로고
    • Expression level of TRPC3 channel determines its mechanism of activation
    • G. Vazquez, B.J. Wedel, M. Trebak, G.St.J. Bird, and J.W. Putney Jr. Expression level of TRPC3 channel determines its mechanism of activation J. Biol. Chem. 278 2003 21649 21654
    • (2003) J. Biol. Chem. , vol.278 , pp. 21649-21654
    • Vazquez, G.1    Wedel, B.J.2    Trebak, M.3    Bird, G.St.J.4    Putney Jr., J.W.5
  • 80
    • 0035823479 scopus 로고    scopus 로고
    • Expression of functional receptor-coupled TRPC3 channels in DT40 triple receptor InsP3 knockout cells
    • K. Venkatachalam, H.-T. Ma, D.L. Ford, and D.L. Gill Expression of functional receptor-coupled TRPC3 channels in DT40 triple receptor InsP3 knockout cells J. Biol. Chem. 276 2001 33980 33985
    • (2001) J. Biol. Chem. , vol.276 , pp. 33980-33985
    • Venkatachalam, K.1    Ma, H.-T.2    Ford, D.L.3    Gill, D.L.4
  • 81
    • 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, and 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
  • 82
    • 2942740971 scopus 로고    scopus 로고
    • The enigmatic TRPCs: Multifunctional cation channels
    • J.W. Putney Jr. The enigmatic TRPCs: multifunctional cation channels Trends Cell Biol. 14 2004 282 286
    • (2004) Trends Cell Biol. , vol.14 , pp. 282-286
    • Putney Jr., J.W.1
  • 84
    • 0030725660 scopus 로고    scopus 로고
    • Cloning and expression of a novel mammalian homolog of Drosophila Transient Receptor Potential (Trp) involved in calcium entry secondary to activation of receptors coupled by the Gq class of G protein
    • G. Boulay, X. Zhu, M. Peyton, M. Jiang, R. Hurst, E. Stefani, and L. Birnbaumer Cloning and expression of a novel mammalian homolog of Drosophila Transient Receptor Potential (Trp) involved in calcium entry secondary to activation of receptors coupled by the Gq class of G protein J. Biol. Chem. 272 1997 29672 29680
    • (1997) J. Biol. Chem. , vol.272 , pp. 29672-29680
    • Boulay, G.1    Zhu, X.2    Peyton, M.3    Jiang, M.4    Hurst, R.5    Stefani, E.6    Birnbaumer, L.7
  • 91
    • 0037013309 scopus 로고    scopus 로고
    • 2+ to trigger exocytosis in neuroendocrine cells
    • 2+ to trigger exocytosis in neuroendocrine cells J. Biol. Chem. 277 2002 16172 16178
    • (2002) J. Biol. Chem. , vol.277 , pp. 16172-16178
    • Obukhov, A.G.1    Nowycky, M.C.2
  • 92
    • 0037134510 scopus 로고    scopus 로고
    • The role of endogenous human Trp4 in regulating carbachol-induced calcium oscillations in HEK-293 cells
    • X. Wu, G. Babnigg, T. Zagranichnaya, and M.L. Villereal The role of endogenous human Trp4 in regulating carbachol-induced calcium oscillations in HEK-293 cells J. Biol. Chem. 277 2002 13597 13608
    • (2002) J. Biol. Chem. , vol.277 , pp. 13597-13608
    • Wu, X.1    Babnigg, G.2    Zagranichnaya, T.3    Villereal, M.L.4
  • 93
    • 0034752902 scopus 로고    scopus 로고
    • Activation of inositol 1,4,5-trisphosphate receptor is essential for the opening of mouse TRP5 channel
    • H. Kanki, M. Kinoshita, A. Akaike, M. Satoh, Y. Mori, and S. Kaneko Activation of inositol 1,4,5-trisphosphate receptor is essential for the opening of mouse TRP5 channel Mol. Pharmacol. 60 2001 989 998
    • (2001) Mol. Pharmacol. , vol.60 , pp. 989-998
    • Kanki, H.1    Kinoshita, M.2    Akaike, A.3    Satoh, M.4    Mori, Y.5    Kaneko, S.6
  • 94
    • 0025195367 scopus 로고
    • 2+ entry by inositol phosphates-a possible mechanism
    • 2+ entry by inositol phosphates-a possible mechanism FEBS Lett. 263 1990 5 9
    • (1990) FEBS Lett. , vol.263 , pp. 5-9
    • Irvine, R.F.1
  • 95
    • 0028826727 scopus 로고
    • Capacitative calcium entry
    • M.J. Berridge Capacitative calcium entry Biochem. J. 312 1995 1 11
    • (1995) Biochem. J. , vol.312 , pp. 1-11
    • Berridge, M.J.1
  • 97
    • 0035877761 scopus 로고    scopus 로고
    • Identification of common binding sites for calmodulin and inositol 1,4,5-trisphosphate receptors on the carboxy termini of Trp channels
    • J. Tang, Y. Lin, Z. Zhang, S. Tikunova, L. Birnbaumer, and M.X. Zhu Identification of common binding sites for calmodulin and inositol 1,4,5-trisphosphate receptors on the carboxy termini of Trp channels J. Biol. Chem. 276 2001 21303 21310
    • (2001) J. Biol. Chem. , vol.276 , pp. 21303-21310
    • Tang, J.1    Lin, Y.2    Zhang, Z.3    Tikunova, S.4    Birnbaumer, L.5    Zhu, M.X.6
  • 99
    • 0035874486 scopus 로고    scopus 로고
    • Activation of store-mediated calcium entry by secretion-like coupling between the inositol 1,4,5-trisphosphate receptor type II and human transient receptor potential (hTrp1) channels in human platelets
    • J.A. Rosado, and S.O. Sage Activation of store-mediated calcium entry by secretion-like coupling between the inositol 1,4,5-trisphosphate receptor type II and human transient receptor potential (hTrp1) channels in human platelets Biochem. J. 356 2001 191 198
    • (2001) Biochem. J. , vol.356 , pp. 191-198
    • Rosado, J.A.1    Sage, S.O.2
  • 101
    • 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, and 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
  • 103
    • 18744384645 scopus 로고    scopus 로고
    • Type-specific inositol 1,4,5-trisphosphate receptor localization in the vomeronasal organ and its interaction with a transient receptor potential channel, TRPC2
    • J.H. Brann, J.C. Dennis, E.E. Morrison, and D.A. Fadool Type-specific inositol 1,4,5-trisphosphate receptor localization in the vomeronasal organ and its interaction with a transient receptor potential channel, TRPC2 J. Neurochem. 83 2002 1452 1460
    • (2002) J. Neurochem. , vol.83 , pp. 1452-1460
    • Brann, J.H.1    Dennis, J.C.2    Morrison, E.E.3    Fadool, D.A.4
  • 104
    • 0242391824 scopus 로고    scopus 로고
    • Synergism between inositol phosphates and diacylglycerol on native TRPC6-like channels in rabbit portal vein myocytes
    • A.P. Albert, and 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
  • 105
    • 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, and 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
  • 109
    • 0035847080 scopus 로고    scopus 로고
    • Stable activation of single CRAC-channels in divalent cation-free solutions
    • F.-J. Braun, L.M. Broad, D.L. Armstrong, and J.W. Putney Jr. Stable activation of single CRAC-channels in divalent cation-free solutions J. Biol. Chem. 276 2001 1063 1070
    • (2001) J. Biol. Chem. , vol.276 , pp. 1063-1070
    • Braun, F.-J.1    Broad, L.M.2    Armstrong, D.L.3    Putney Jr., J.W.4
  • 111
    • 0035281595 scopus 로고    scopus 로고
    • 2+ channels in liver cells, and acts through a mechanism which does not involve inositol trisphosphate receptors
    • 2+ channels in liver cells, and acts through a mechanism which does not involve inositol trisphosphate receptors Biochem. J. 354 2001 285 290
    • (2001) Biochem. J. , vol.354 , pp. 285-290
    • Gregory, R.B.1    Rychkov, G.2    Barritt, G.J.3
  • 112
    • 0035476846 scopus 로고    scopus 로고
    • 2+ channels by 2-aminoethyldiphenyl borate (2-APB) occurs independently of IP3 receptors
    • 2+ channels by 2-aminoethyldiphenyl borate (2-APB) occurs independently of IP3 receptors J. Physiol. (Lond.) 536 2001 3 19
    • (2001) J. Physiol. (Lond.) , vol.536 , pp. 3-19
    • Prakriya, M.1    Lewis, R.S.2
  • 113
    • 0034874198 scopus 로고    scopus 로고
    • 2-Aminoethoxydiphenyl borate directly inhibits store-operated calcium entry channels in human platelets
    • Y. Dobrydneva, and P. Blackmore 2-Aminoethoxydiphenyl borate directly inhibits store-operated calcium entry channels in human platelets Mol. Pharmacol. 60 2001 541 552
    • (2001) Mol. Pharmacol. , vol.60 , pp. 541-552
    • Dobrydneva, Y.1    Blackmore, P.2
  • 114
    • 0035669916 scopus 로고    scopus 로고
    • 2-Aminoethoxydiphenyl borate (2-APB) inhibits capacitative calcium entry independently of the function of inositol 1,4,5-trisphosphate receptors
    • H. Iwasaki, Y. Mori, Y. Hara, K. Uchida, H. Zhou, and K. Mikoshiba 2-Aminoethoxydiphenyl borate (2-APB) inhibits capacitative calcium entry independently of the function of inositol 1,4,5-trisphosphate receptors Recept. Channels 7 2001 429 439
    • (2001) Recept. Channels , vol.7 , pp. 429-439
    • Iwasaki, H.1    Mori, Y.2    Hara, Y.3    Uchida, K.4    Zhou, H.5    Mikoshiba, K.6
  • 116
    • 0033200089 scopus 로고    scopus 로고
    • Activation of a TRPC3-dependent cation channel through the neurotrophin BDNF
    • H.-S. Li, X.-Z.S. Xu, and C. Montell Activation of a TRPC3-dependent cation channel through the neurotrophin BDNF Neuron 24 1999 261 273
    • (1999) Neuron , vol.24 , pp. 261-273
    • Li, H.-S.1    Xu, X.-Z.S.2    Montell, C.3
  • 117
    • 0031007450 scopus 로고    scopus 로고
    • Genetic evidence for involvement of type 1, type 2 and type 3 inositol 1,4,5-trisphosphate receptors in signal transduction through the B-cell antigen receptor
    • H. Sugawara, M. Kurosaki, M. Takata, and T. Kurosaki Genetic evidence for involvement of type 1, type 2 and type 3 inositol 1,4,5-trisphosphate receptors in signal transduction through the B-cell antigen receptor EMBO J. 16 1997 3078 3088
    • (1997) EMBO J. , vol.16 , pp. 3078-3088
    • Sugawara, H.1    Kurosaki, M.2    Takata, M.3    Kurosaki, T.4
  • 118
    • 0035844216 scopus 로고    scopus 로고
    • Role of the phospholipase C- inositol 1,4,5-trisphosphate pathway in calcium release-activated calcium current (Icrac) and capacitative calcium entry
    • L.M. Broad, F.-J. Braun, J.-P. Lièvremont, G. St.J. Bird, T. Kurosaki, and J.W. Putney Jr. Role of the phospholipase C- inositol 1,4,5-trisphosphate pathway in calcium release-activated calcium current (Icrac) and capacitative calcium entry J. Biol. Chem. 276 2001 15945 15952
    • (2001) J. Biol. Chem. , vol.276 , pp. 15945-15952
    • Broad, L.M.1    Braun, F.-J.2    Lièvremont, J.-P.3    St.j. Bird, G.4    Kurosaki, T.5    Putney Jr., J.W.6
  • 119
    • 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
  • 120
    • 0042206600 scopus 로고    scopus 로고
    • Regulation of canonical transient receptor potential (TRPC) channel function by diacylglycerol and protein kinase C
    • K. Venkatachalam, F. Zheng, and 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
  • 121
    • 0037061681 scopus 로고    scopus 로고
    • Signaling microdomains define the specificity of receptor-mediated InsP3 pathways in Neurons
    • P. Delmas, N. Wanaverbecq, F.C. Abogadie, M. Mistry, and D.A. Brown Signaling microdomains define the specificity of receptor-mediated InsP3 pathways in Neurons Neuron 34 2002 209 220
    • (2002) Neuron , vol.34 , pp. 209-220
    • Delmas, P.1    Wanaverbecq, N.2    Abogadie, F.C.3    Mistry, M.4    Brown, D.A.5
  • 122
    • 0036199229 scopus 로고    scopus 로고
    • Calmodulin as an ion channel subunit
    • Y. Saimi, and C. Kung Calmodulin as an ion channel subunit Annu. Rev. Physiol. 64 2002 289 311
    • (2002) Annu. Rev. Physiol. , vol.64 , pp. 289-311
    • Saimi, Y.1    Kung, C.2
  • 123
    • 0029800956 scopus 로고    scopus 로고
    • 2+ and calmodulin, and by guanosine 5′[gamma-thio]triphosphate
    • 2+ and calmodulin, and by guanosine 5′[gamma-thio]triphosphate Biochem. J. 316 Pt 3 1996 793 803
    • (1996) Biochem. J. , vol.316 , Issue.3 , pp. 793-803
    • Lan, L.1    Bawden, M.J.2    Auld, A.M.3    Barritt, G.J.4
  • 124
    • 0029866944 scopus 로고    scopus 로고
    • Identification and characterization of two distinct calmodulin-binding sites in the Trpl ion-channel protein of Drosophila melanogaster
    • C.G. Warr, and L.E. Kelly Identification and characterization of two distinct calmodulin-binding sites in the Trpl ion-channel protein of Drosophila melanogaster Biochem. J. 314 Pt 2 1996 497 503
    • (1996) Biochem. J. , vol.314 , Issue.2 , pp. 497-503
    • Warr, C.G.1    Kelly, L.E.2
  • 125
    • 0036028768 scopus 로고    scopus 로고
    • 2+ entry activity of TRPC6 in HEK-293 cells
    • 2+ entry activity of TRPC6 in HEK-293 cells Cell Calcium 320 2002 201 207
    • (2002) Cell Calcium , vol.320 , pp. 201-207
    • Boulay, G.1
  • 130
    • 2442685287 scopus 로고    scopus 로고
    • Protein kinase Calpha phosphorylates the TRPC1 channel and regulates store-operated Ca2+ entry in endothelial cells
    • G.U. Ahmmed, D. Mehta, S. Vogel, M. Holinstat, B.C. Paria, C. Tiruppathi, and A.B. Malik Protein kinase Calpha phosphorylates the TRPC1 channel and regulates store-operated Ca2+ entry in endothelial cells J. Biol. Chem. 279 2004 20941 20949
    • (2004) J. Biol. Chem. , vol.279 , pp. 20941-20949
    • Ahmmed, G.U.1    Mehta, D.2    Vogel, S.3    Holinstat, M.4    Paria, B.C.5    Tiruppathi, C.6    Malik, A.B.7
  • 131
    • 1442330339 scopus 로고    scopus 로고
    • Regulation of canonical transient receptor potential isoform 3 (TRPC3) channel by protein kinase G
    • H.Y. Kwan, Y. Huang, and X. Yao Regulation of canonical transient receptor potential isoform 3 (TRPC3) channel by protein kinase G Proc. Natl. Acad. Sci. U. S. A. 101 2004 2625 2630
    • (2004) Proc. Natl. Acad. Sci. U. S. A. , vol.101 , pp. 2625-2630
    • Kwan, H.Y.1    Huang, Y.2    Yao, X.3
  • 132
    • 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, and 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
  • 134
    • 0034700494 scopus 로고    scopus 로고
    • Induction of vanilloid receptor channel by protein kinase C
    • L.S. Premkumar, and G.P. Ahern Induction of vanilloid receptor channel by protein kinase C Nature 408 2000 985 990
    • (2000) Nature , vol.408 , pp. 985-990
    • Premkumar, L.S.1    Ahern, G.P.2
  • 135
    • 0242322027 scopus 로고    scopus 로고
    • Regulation of a TRPM7-like current in rat brain microglia
    • X. Jiang, E.W. Newell, and L.C. Schlichter Regulation of a TRPM7-like current in rat brain microglia J. Biol. Chem. 278 2003 42867 42876
    • (2003) J. Biol. Chem. , vol.278 , pp. 42867-42876
    • Jiang, X.1    Newell, E.W.2    Schlichter, L.C.3
  • 137
    • 0038175469 scopus 로고    scopus 로고
    • Regulation of a transient receptor potential (TRP) channel by tyrosine phosphorylation
    • H. Xu, H. Zhao, W. Tian, K. Yoshida, J.-B. Roullet, and D.M. Cohen Regulation of a transient receptor potential (TRP) channel by tyrosine phosphorylation J. Biol. Chem. 278 2003 11520 11527
    • (2003) J. Biol. Chem. , vol.278 , pp. 11520-11527
    • Xu, H.1    Zhao, H.2    Tian, W.3    Yoshida, K.4    Roullet, J.-B.5    Cohen, D.M.6
  • 138
    • 0028831997 scopus 로고
    • Calcium signaling
    • D.E. Clapham Calcium signaling Cell 80 1995 259 268
    • (1995) Cell , vol.80 , pp. 259-268
    • Clapham, D.E.1
  • 141
    • 0023375195 scopus 로고
    • The neighbor-joining method: A new method for reconstructing phylogenetic trees
    • N. Saitou, and M. Nei The neighbor-joining method: a new method for reconstructing phylogenetic trees Mol. Biol. Evol. 4 1987 406 425
    • (1987) Mol. Biol. Evol. , vol.4 , pp. 406-425
    • Saitou, N.1    Nei, M.2


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