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Volumn 25, Issue 12, 2004, Pages 633-639

The TRPM ion channel subfamily: Molecular, biophysical and functional features

Author keywords

[No Author keywords available]

Indexed keywords

CLUSTERIN; PROTEIN; PROTEIN TRPM1; PROTEIN TRPM3; PROTEIN TRPM4; PROTEIN TRPM5; PROTEIN TRPM6; PROTEIN TRPM7; PROTEIN TRPM8; UNCLASSIFIED DRUG;

EID: 7644238945     PISSN: 01656147     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.tips.2004.10.004     Document Type: Review
Times cited : (240)

References (65)
  • 1
    • 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
  • 2
    • 0037636295 scopus 로고    scopus 로고
    • The venerable inveterate invertebrate TRP channels
    • C. Montell The venerable inveterate invertebrate TRP channels Cell Calcium 33 2003 409 417
    • (2003) Cell Calcium , vol.33 , pp. 409-417
    • Montell, C.1
  • 3
    • 2342484509 scopus 로고    scopus 로고
    • Emerging roles of TRPM channels
    • A. Fleig, and R. Penner Emerging roles of TRPM channels Novartis Found. Symp. 258 2004 248 258
    • (2004) Novartis Found. Symp. , vol.258 , pp. 248-258
    • Fleig, A.1    Penner, R.2
  • 4
    • 2342613631 scopus 로고    scopus 로고
    • Diversity of TRP channel activation
    • B. Nilius, and T. Voets Diversity of TRP channel activation Novartis Found. Symp. 258 2004 140 149
    • (2004) Novartis Found. Symp. , vol.258 , pp. 140-149
    • Nilius, B.1    Voets, T.2
  • 5
    • 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 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
  • 6
    • 0032533315 scopus 로고    scopus 로고
    • 2+ channel protein (TRPC7) highly expressed in brain
    • 2+ channel protein (TRPC7) highly expressed in brain Genomics 54 1998 124 131
    • (1998) Genomics , vol.54 , pp. 124-131
    • Nagamine, K.1
  • 7
    • 0035978751 scopus 로고    scopus 로고
    • ADP-ribose gating of the calcium-permeable LTRPC2 channel revealed by Nudix motif homology
    • A.L. Perraud ADP-ribose gating of the calcium-permeable LTRPC2 channel revealed by Nudix motif homology Nature 411 2001 595 599
    • (2001) Nature , vol.411 , pp. 595-599
    • Perraud, A.L.1
  • 8
    • 0035902767 scopus 로고    scopus 로고
    • 2+ influx system mediated by LTRPC2
    • 2+ influx system mediated by LTRPC2 Science 293 2001 1327 1330
    • (2001) Science , vol.293 , pp. 1327-1330
    • Sano, Y.1
  • 9
    • 18244391511 scopus 로고    scopus 로고
    • 2+-permeable channel activated by changes in redox status confers susceptibility to cell death
    • 2+-permeable channel activated by changes in redox status confers susceptibility to cell death Mol. Cell 9 2002 163 173
    • (2002) Mol. Cell , vol.9 , pp. 163-173
    • Hara, Y.1
  • 10
    • 0037449761 scopus 로고    scopus 로고
    • NUDT9, a member of the Nudix hydrolase family, is an evolutionarily conserved mitochondrial ADP-ribose pyrophosphatase
    • A.L. Perraud NUDT9, a member of the Nudix hydrolase family, is an evolutionarily conserved mitochondrial ADP-ribose pyrophosphatase J. Biol. Chem. 278 2003 1794 1801
    • (2003) J. Biol. Chem. , vol.278 , pp. 1794-1801
    • Perraud, A.L.1
  • 11
    • 0035978239 scopus 로고    scopus 로고
    • LTRPC7 is a Mg·ATP-regulated divalent cation channel required for cell viability
    • M.J. Nadler LTRPC7 is a Mg·ATP-regulated divalent cation channel required for cell viability Nature 411 2001 590 595
    • (2001) Nature , vol.411 , pp. 590-595
    • Nadler, M.J.1
  • 12
    • 0035131504 scopus 로고    scopus 로고
    • TRP-PLIK, a bifunctional protein with kinase and ion channel activities
    • L.W. Runnels 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
  • 13
    • 0035947077 scopus 로고    scopus 로고
    • Crystal structure of the atypical protein kinase domain of a TRP channel with phosphotransferase activity
    • H. Yamaguchi Crystal structure of the atypical protein kinase domain of a TRP channel with phosphotransferase activity Mol. Cell 7 2001 1047 1057
    • (2001) Mol. Cell , vol.7 , pp. 1047-1057
    • Yamaguchi, H.1
  • 14
    • 1842536165 scopus 로고    scopus 로고
    • Alpha-kinases: Analysis of the family and comparison with conventional protein kinases
    • D. Drennan, and 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
  • 15
    • 0942265537 scopus 로고    scopus 로고
    • Characterization of the protein kinase activity of TRPM7/ChaK1, a protein kinase fused to the transient receptor potential ion channel
    • L.V. Ryazanova Characterization of the protein kinase activity of TRPM7/ChaK1, a protein kinase fused to the transient receptor potential ion channel J. Biol. Chem. 279 2004 3708 3716
    • (2004) J. Biol. Chem. , vol.279 , pp. 3708-3716
    • Ryazanova, L.V.1
  • 16
    • 1542297755 scopus 로고    scopus 로고
    • Disruption of TRPM6/TRPM7 complex formation by a mutation in the TRPM6 gene causes hypomagnesemia with secondary hypocalcemia
    • V. Chubanov Disruption of TRPM6/TRPM7 complex formation by a mutation in the TRPM6 gene causes hypomagnesemia with secondary hypocalcemia Proc. Natl. Acad. Sci. U. S. A. 101 2004 2894 2899
    • (2004) Proc. Natl. Acad. Sci. U. S. A. , vol.101 , pp. 2894-2899
    • Chubanov, V.1
  • 17
    • 0032054272 scopus 로고    scopus 로고
    • Down-regulation of the novel gene melastatin correlates with potential for melanoma metastasis
    • L.M. Duncan Down-regulation of the novel gene melastatin correlates with potential for melanoma metastasis Cancer Res. 58 1998 1515 1520
    • (1998) Cancer Res. , vol.58 , pp. 1515-1520
    • Duncan, L.M.1
  • 18
    • 0034627233 scopus 로고    scopus 로고
    • Expression and Up-regulation of alternatively spliced transcripts of melastatin, a melanoma metastasis-related gene, in human melanoma cells
    • D. Fang, and V. Setaluri Expression and Up-regulation of alternatively spliced transcripts of melastatin, a melanoma metastasis-related gene, in human melanoma cells Biochem. Biophys. Res. Commun. 279 2000 53 61
    • (2000) Biochem. Biophys. Res. Commun. , vol.279 , pp. 53-61
    • Fang, D.1    Setaluri, V.2
  • 19
    • 0035863283 scopus 로고    scopus 로고
    • Melastatin expression and prognosis in cutaneous malignant melanoma
    • L.M. Duncan Melastatin expression and prognosis in cutaneous malignant melanoma J. Clin. Oncol. 19 2001 568 576
    • (2001) J. Clin. Oncol. , vol.19 , pp. 568-576
    • Duncan, L.M.1
  • 20
    • 0035845566 scopus 로고    scopus 로고
    • Regulation of melastatin, a TRP-related protein, through interaction with a cytoplasmic isoform
    • X.Z. Xu Regulation of melastatin, a TRP-related protein, through interaction with a cytoplasmic isoform Proc. Natl. Acad. Sci. U. S. A. 98 2001 10692 10697
    • (2001) Proc. Natl. Acad. Sci. U. S. A. , vol.98 , pp. 10692-10697
    • Xu, X.Z.1
  • 21
    • 0037974386 scopus 로고    scopus 로고
    • Role and regulation of TRP channels in neutrophil granulocytes
    • I. Heiner Role and regulation of TRP channels in neutrophil granulocytes Cell Calcium 33 2003 533 540
    • (2003) Cell Calcium , vol.33 , pp. 533-540
    • Heiner, I.1
  • 22
    • 0346727508 scopus 로고    scopus 로고
    • Hydrogen peroxide and ADP-ribose induce TRPM2-mediated calcium influx and cation currents in microglia
    • R. Kraft Hydrogen peroxide and ADP-ribose induce TRPM2-mediated calcium influx and cation currents in microglia Am. J. Physiol. Cell Physiol. 286 2004 C129 C137
    • (2004) Am. J. Physiol. Cell Physiol. , vol.286
    • Kraft, R.1
  • 23
    • 0042930997 scopus 로고    scopus 로고
    • Response to ADP-ribose by activation of TRPM2 in the CRI-G1 insulinoma cell line
    • K. Inamura Response to ADP-ribose by activation of TRPM2 in the CRI-G1 insulinoma cell line J. Membr. Biol. 191 2003 201 207
    • (2003) J. Membr. Biol. , vol.191 , pp. 201-207
    • Inamura, K.1
  • 24
    • 0037189484 scopus 로고    scopus 로고
    • Activation of the cation channel long transient receptor potential channel 2 (LTRPC2) by hydrogen peroxide. A splice variant reveals a mode of activation independent of ADP-ribose
    • E. Wehage Activation of the cation channel long transient receptor potential channel 2 (LTRPC2) by hydrogen peroxide. A splice variant reveals a mode of activation independent of ADP-ribose J. Biol. Chem. 277 2002 23150 23156
    • (2002) J. Biol. Chem. , vol.277 , pp. 23150-23156
    • Wehage, E.1
  • 25
    • 0038237529 scopus 로고    scopus 로고
    • 2+ dependence of transient receptor potential melastatin 2 (TRPM2) cation channel activation
    • 2+ dependence of transient receptor potential melastatin 2 (TRPM2) cation channel activation J. Biol. Chem. 278 2003 11002 11006
    • (2003) J. Biol. Chem. , vol.278 , pp. 11002-11006
    • McHugh, D.1
  • 26
    • 0033303239 scopus 로고    scopus 로고
    • Human CD38, a surface receptor, an enzyme, an adhesion molecule and not a simple marker
    • A. Funaro, and F. Malavasi Human CD38, a surface receptor, an enzyme, an adhesion molecule and not a simple marker J. Biol. Regul. Homeost. Agents 13 1999 54 61
    • (1999) J. Biol. Regul. Homeost. Agents , vol.13 , pp. 54-61
    • Funaro, A.1    Malavasi, F.2
  • 27
    • 0033961770 scopus 로고    scopus 로고
    • Enzymatic functions and structures of CD38 and homologs
    • H.C. Lee Enzymatic functions and structures of CD38 and homologs Chem. Immunol. 75 2000 39 59
    • (2000) Chem. Immunol. , vol.75 , pp. 39-59
    • Lee, H.C.1
  • 28
    • 1942485497 scopus 로고    scopus 로고
    • Structure and enzymology of ADP-ribosyl cyclases: Conserved enzymes that produce multiple calcium mobilizing metabolites
    • F. Schuber, and F.E. Lund Structure and enzymology of ADP-ribosyl cyclases: conserved enzymes that produce multiple calcium mobilizing metabolites Curr. Mol. Med. 4 2004 249 261
    • (2004) Curr. Mol. Med. , vol.4 , pp. 249-261
    • Schuber, F.1    Lund, F.E.2
  • 29
    • 0035425899 scopus 로고    scopus 로고
    • Importance of poly(ADP-ribose) glycohydrolase in the control of poly(ADP-ribose) metabolism
    • L. Davidovic Importance of poly(ADP-ribose) glycohydrolase in the control of poly(ADP-ribose) metabolism Exp. Cell Res. 268 2001 7 13
    • (2001) Exp. Cell Res. , vol.268 , pp. 7-13
    • Davidovic, L.1
  • 30
    • 0036022402 scopus 로고    scopus 로고
    • Poly(ADP-ribose) polymerase-1 cleavage during apoptosis: An update
    • C. Soldani, and A.I. Scovassi Poly(ADP-ribose) polymerase-1 cleavage during apoptosis: an update Apoptosis 7 2002 321 328
    • (2002) Apoptosis , vol.7 , pp. 321-328
    • Soldani, C.1    Scovassi, A.I.2
  • 31
    • 0038498142 scopus 로고    scopus 로고
    • Molecular and functional characterization of the melastatin-related cation channel TRPM3
    • C. Grimm 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
  • 32
    • 0038080920 scopus 로고    scopus 로고
    • Expression and characterization of human transient receptor potential melastatin 3 (hTRPM3)
    • N. Lee Expression and characterization of human transient receptor potential melastatin 3 (hTRPM3) J. Biol. Chem. 278 2003 20890 20897
    • (2003) J. Biol. Chem. , vol.278 , pp. 20890-20897
    • Lee, N.1
  • 33
    • 0037012649 scopus 로고    scopus 로고
    • 2+-activated nonselective cation channel mediating cell membrane depolarization
    • 2+-activated nonselective cation channel mediating cell membrane depolarization Cell 109 2002 397 407
    • (2002) Cell , vol.109 , pp. 397-407
    • Launay, P.1
  • 34
    • 0037672155 scopus 로고    scopus 로고
    • 2+-activated monovalent selective cation channel
    • 2+-activated monovalent selective cation channel Curr. Biol. 13 2003 1153 1158
    • (2003) Curr. Biol. , vol.13 , pp. 1153-1158
    • Hofmann, T.1
  • 35
    • 0043234534 scopus 로고    scopus 로고
    • 2+-activated cation channel TRPM4
    • 2+-activated cation channel TRPM4 J. Biol. Chem. 278 2003 30813 30820
    • (2003) J. Biol. Chem. , vol.278 , pp. 30813-30820
    • Nilius, B.1
  • 36
    • 0027741870 scopus 로고
    • Nonselective cation channels
    • D. Siemen Nonselective cation channels EXS 66 1993 3 25
    • (1993) EXS , vol.66 , pp. 3-25
    • Siemen, D.1
  • 37
    • 0028068572 scopus 로고
    • Calcium-activated non-selective channels in the nervous system
    • L.D. Partridge Calcium-activated non-selective channels in the nervous system Brain Res. Brain Res. Rev. 19 1994 319 325
    • (1994) Brain Res. Brain Res. Rev. , vol.19 , pp. 319-325
    • Partridge, L.D.1
  • 38
    • 0037031319 scopus 로고    scopus 로고
    • Cation channels: Homing in on the elusive CAN channels
    • O.H. Petersen Cation channels: homing in on the elusive CAN channels Curr. Biol. 12 2002 R520 R522
    • (2002) Curr. Biol. , vol.12
    • Petersen, O.H.1
  • 39
    • 7244250645 scopus 로고    scopus 로고
    • Decavanadate modulates gating of TRPM4 cation channels
    • B. Nilius Decavanadate modulates gating of TRPM4 cation channels J. Physiol. 2004
    • (2004) J. Physiol.
    • Nilius, B.1
  • 40
    • 2442653881 scopus 로고    scopus 로고
    • 2+-activated cation channel TRPM4b
    • 2+-activated cation channel TRPM4b Pflugers Arch. 448 2004 70 75
    • (2004) Pflugers Arch. , vol.448 , pp. 70-75
    • Nilius, B.1
  • 41
    • 0033958493 scopus 로고    scopus 로고
    • Identification and characterization of MTR1, a novel gene with homology to melastatin (MLSN1) and the trp gene family located in the BWS-WT2 critical region on chromosome 11p15.5 and showing allele-specific expression
    • D. Prawitt Identification and characterization of MTR1, a novel gene with homology to melastatin (MLSN1) and the trp gene family located in the BWS-WT2 critical region on chromosome 11p15.5 and showing allele-specific expression Hum. Mol. Genet. 9 2000 203 216
    • (2000) Hum. Mol. Genet. , vol.9 , pp. 203-216
    • Prawitt, D.1
  • 42
    • 0036830145 scopus 로고    scopus 로고
    • A transient receptor potential channel expressed in taste receptor cells
    • C.A. Perez A transient receptor potential channel expressed in taste receptor cells Nat. Neurosci. 5 2002 1169 1176
    • (2002) Nat. Neurosci. , vol.5 , pp. 1169-1176
    • Perez, C.A.1
  • 43
    • 0037423367 scopus 로고    scopus 로고
    • Coding of sweet, bitter, and umami tastes: Different receptor cells sharing similar signaling pathways
    • Y. Zhang 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
  • 44
    • 0344149569 scopus 로고    scopus 로고
    • 2 regulate the taste transduction ion channel TRPM5
    • 2 regulate the taste transduction ion channel TRPM5 Proc. Natl. Acad. Sci. U. S. A. 100 2003 15160 15165
    • (2003) Proc. Natl. Acad. Sci. U. S. A. , vol.100 , pp. 15160-15165
    • Liu, D.1    Liman, E.R.2
  • 46
    • 0034786750 scopus 로고    scopus 로고
    • Mechanisms and physiological significance of the cholinergic control of pancreatic beta-cell function
    • P. Gilon, and J.C. Henquin Mechanisms and physiological significance of the cholinergic control of pancreatic beta-cell function Endocr. Rev. 22 2001 565 604
    • (2001) Endocr. Rev. , vol.22 , pp. 565-604
    • Gilon, P.1    Henquin, J.C.2
  • 47
    • 0347683487 scopus 로고    scopus 로고
    • 2+ absorption
    • 2+ absorption J. Biol. Chem. 279 2004 19 25
    • (2004) J. Biol. Chem. , vol.279 , pp. 19-25
    • Voets, T.1
  • 48
    • 18544369466 scopus 로고    scopus 로고
    • Hypomagnesemia with secondary hypocalcemia is caused by mutations in TRPM6, a new member of the TRPM gene family
    • K.P. Schlingmann Hypomagnesemia with secondary hypocalcemia is caused by mutations in TRPM6, a new member of the TRPM gene family Nat. Genet. 31 2002 166 170
    • (2002) Nat. Genet. , vol.31 , pp. 166-170
    • Schlingmann, K.P.1
  • 49
    • 0036592004 scopus 로고    scopus 로고
    • Mutation of TRPM6 causes familial hypomagnesemia with secondary hypocalcemia
    • R.Y. Walder Mutation of TRPM6 causes familial hypomagnesemia with secondary hypocalcemia Nat. Genet. 31 2002 171 174
    • (2002) Nat. Genet. , vol.31 , pp. 171-174
    • Walder, R.Y.1
  • 50
    • 0037252056 scopus 로고    scopus 로고
    • TRPM7 provides an ion channel mechanism for cellular entry of trace metal ions
    • M.K. Monteilh-Zoller TRPM7 provides an ion channel mechanism for cellular entry of trace metal ions J. Gen. Physiol. 121 2003 49 60
    • (2003) J. Gen. Physiol. , vol.121 , pp. 49-60
    • Monteilh-Zoller, M.K.1
  • 51
    • 0036521977 scopus 로고    scopus 로고
    • CRAC and the Mg-nucleotide-regulated metal ion current MagNuM
    • CRAC and the Mg-nucleotide-regulated metal ion current MagNuM J. Physiol. 539 2002 445 458
    • (2002) J. Physiol. , vol.539 , pp. 445-458
    • Hermosura, M.C.1
  • 52
    • 0036023404 scopus 로고    scopus 로고
    • Distinct properties of CRAC and MIC channels in RBL cells
    • J.A. Kozak Distinct properties of CRAC and MIC channels in RBL cells J. Gen. Physiol. 120 2002 221 235
    • (2002) J. Gen. Physiol. , vol.120 , pp. 221-235
    • Kozak, J.A.1
  • 55
    • 1942437482 scopus 로고    scopus 로고
    • Receptor-mediated regulation of the TRPM7 channel through its endogenous protein kinase domain
    • R. Takezawa Receptor-mediated regulation of the TRPM7 channel through its endogenous protein kinase domain Proc. Natl. Acad. Sci. U. S. A. 101 2004 6009 6014
    • (2004) Proc. Natl. Acad. Sci. U. S. A. , vol.101 , pp. 6009-6014
    • Takezawa, R.1
  • 56
    • 0042197392 scopus 로고    scopus 로고
    • 2+ homeostasis by TRPM7
    • 2+ homeostasis by TRPM7 Cell 114 2003 191 200
    • (2003) Cell , vol.114 , pp. 191-200
    • Schmitz, C.1
  • 57
    • 0346186100 scopus 로고    scopus 로고
    • A key role for TRPM7 channels in anoxic neuronal death
    • M. Aarts A key role for TRPM7 channels in anoxic neuronal death Cell 115 2003 863 877
    • (2003) Cell , vol.115 , pp. 863-877
    • Aarts, M.1
  • 58
    • 4644278854 scopus 로고    scopus 로고
    • Magnesium-inhibited, TRPM6/7-like channel in cardiac myocytes: Permeation of divalent cations and pH-mediated regulation
    • A. Gwanyana Magnesium-inhibited, TRPM6/7-like channel in cardiac myocytes: permeation of divalent cations and pH-mediated regulation J. Physiol. 15 2004 761 776
    • (2004) J. Physiol. , vol.15 , pp. 761-776
    • Gwanyana, A.1
  • 59
    • 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 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
  • 60
    • 0037034931 scopus 로고    scopus 로고
    • Identification of a cold receptor reveals a general role for TRP channels in thermosensation
    • D.D. McKemy Identification of a cold receptor reveals a general role for TRP channels in thermosensation Nature 416 2002 52 58
    • (2002) Nature , vol.416 , pp. 52-58
    • McKemy, D.D.1
  • 61
    • 18344386202 scopus 로고    scopus 로고
    • A TRP channel that senses cold stimuli and menthol
    • A.M. Peier A TRP channel that senses cold stimuli and menthol Cell 108 2002 705 715
    • (2002) Cell , vol.108 , pp. 705-715
    • Peier, A.M.1
  • 62
    • 0026516973 scopus 로고
    • The role of nociceptors of cutaneous veins in the mediation of cold pain in man
    • W. Klement, and J.O. Arndt The role of nociceptors of cutaneous veins in the mediation of cold pain in man J. Physiol. 449 1992 73 83
    • (1992) J. Physiol. , vol.449 , pp. 73-83
    • Klement, W.1    Arndt, J.O.2
  • 63
    • 0037824388 scopus 로고    scopus 로고
    • TRPM8 mRNA is expressed in a subset of cold-responsive trigeminal neurons from rat
    • M.L. Nealen TRPM8 mRNA is expressed in a subset of cold-responsive trigeminal neurons from rat J. Neurophysiol. 90 2003 515 520
    • (2003) J. Neurophysiol. , vol.90 , pp. 515-520
    • Nealen, M.L.1
  • 64
    • 2942536048 scopus 로고    scopus 로고
    • TRPM8 activation by menthol, icilin, and cold is differentially modulated by intracellular pH
    • D.A. Andersson 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
  • 65
    • 4043077669 scopus 로고    scopus 로고
    • The principle of temperature-dependent gating in cold- and heat-sensitive TRP channels
    • T. Voets 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


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