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Volumn 5 MAY, Issue , 2014, Pages

A structural view of ligand-dependent activation in thermoTRP channels

Author keywords

Capsaicin; Menthol; Structure; TRP channels; TRPM8; TRPV1

Indexed keywords

TRANSIENT RECEPTOR POTENTIAL CHANNEL; TRANSIENT RECEPTOR POTENTIAL CHANNEL 1; TRANSIENT RECEPTOR POTENTIAL CHANNEL 5; TRANSIENT RECEPTOR POTENTIAL CHANNEL M2; TRANSIENT RECEPTOR POTENTIAL CHANNEL M4; TRANSIENT RECEPTOR POTENTIAL CHANNEL M5; TRANSIENT RECEPTOR POTENTIAL CHANNEL M8; VANILLOID RECEPTOR 1; VANILLOID RECEPTOR 2; VANILLOID RECEPTOR 3; VANILLOID RECEPTOR 4;

EID: 84904332088     PISSN: None     EISSN: 1664042X     Source Type: Journal    
DOI: 10.3389/fphys.2014.00171     Document Type: Review
Times cited : (48)

References (123)
  • 1
    • 77249125805 scopus 로고    scopus 로고
    • The paradoxical role of the transient receptor potential vanilloid 1 receptor in inflammation
    • doi: 10.1016/j.pharmthera.2009.10.005
    • Alawi, K., and Keeble, J. (2010). The paradoxical role of the transient receptor potential vanilloid 1 receptor in inflammation. Pharmacol. Ther. 125, 181-195. doi: 10.1016/j.pharmthera.2009.10.005.
    • (2010) Pharmacol. Ther. , vol.125 , pp. 181-195
    • Alawi, K.1    Keeble, J.2
  • 2
    • 0038650819 scopus 로고    scopus 로고
    • FRET-based analysis of TRPC subunit stoichiometry
    • doi: 10.1016/S0143-4160(03)00061-7
    • Amiri, H., Schultz, G., and Schaefer, M. (2003). FRET-based analysis of TRPC subunit stoichiometry. Cell Calcium 33, 463-470. doi: 10.1016/S0143-4160(03)00061-7.
    • (2003) Cell Calcium , vol.33 , pp. 463-470
    • Amiri, H.1    Schultz, G.2    Schaefer, M.3
  • 3
    • 33645352477 scopus 로고    scopus 로고
    • High-throughput random mutagenesis screen reveals TRPM8 residues specifically required for activation by menthol
    • doi: 10.1038/nn1665
    • Bandell, M., Dubin, A. E., Petrus, M. J., Orth, A., Mathur, J., Hwang, S. W., et al. (2006). High-throughput random mutagenesis screen reveals TRPM8 residues specifically required for activation by menthol. Nat. Neurosci. 9, 493-500. doi: 10.1038/nn1665.
    • (2006) Nat. Neurosci. , vol.9 , pp. 493-500
    • Bandell, M.1    Dubin, A.E.2    Petrus, M.J.3    Orth, A.4    Mathur, J.5    Hwang, S.W.6
  • 4
    • 84871895296 scopus 로고    scopus 로고
    • Protons stabilize the closed conformation of gain-of-function mutants of the TRPV1 channel
    • doi: 10.1016/j.bbamcr.2012.11.017
    • Boukalova, S., Teisinger, J., and Vlachova, V. (2013). Protons stabilize the closed conformation of gain-of-function mutants of the TRPV1 channel. Biochim. Biophys. Acta 1833, 520-528. doi: 10.1016/j.bbamcr.2012.11.017.
    • (2013) Biochim. Biophys. Acta , vol.1833 , pp. 520-528
    • Boukalova, S.1    Teisinger, J.2    Vlachova, V.3
  • 5
    • 34547200183 scopus 로고    scopus 로고
    • Dissection of the components for PIP2 activation and thermosensation in TRP channels
    • doi: 10.1073/pnas.0703420104
    • Brauchi, S., Orta, G., Mascayano, C., Salazar, M., Raddatz, N., Urbina, H., et al. (2007). Dissection of the components for PIP2 activation and thermosensation in TRP channels. Proc. Natl. Acad. Sci. U.S.A. 104, 10246-10251. doi: 10.1073/pnas.0703420104.
    • (2007) Proc. Natl. Acad. Sci. U.S.A. , vol.104 , pp. 10246-10251
    • Brauchi, S.1    Orta, G.2    Mascayano, C.3    Salazar, M.4    Raddatz, N.5    Urbina, H.6
  • 6
    • 84874229704 scopus 로고    scopus 로고
    • TRPV1 channels are intrinsically heat sensitive and negatively regulated by phosphoinositide lipids
    • doi: 10.1016/j.neuron.2012.12.016
    • Cao, E., Cordero-Morales, J. F., Liu, B., Qin, F., and Julius, D. (2013a). TRPV1 channels are intrinsically heat sensitive and negatively regulated by phosphoinositide lipids. Neuron 77, 667-679. doi: 10.1016/j.neuron.2012.12.016.
    • (2013) Neuron , vol.77 , pp. 667-679
    • Cao, E.1    Cordero-Morales, J.F.2    Liu, B.3    Qin, F.4    Julius, D.5
  • 7
    • 84889594608 scopus 로고    scopus 로고
    • TRPV1 structures in distinct conformations reveal activation mechanisms
    • doi: 10.1038/nature12823
    • Cao, E., Liao, M., Cheng, Y., and Julius, D. (2013b). TRPV1 structures in distinct conformations reveal activation mechanisms. Nature 504, 113-118. doi: 10.1038/nature12823.
    • (2013) Nature , vol.504 , pp. 113-118
    • Cao, E.1    Liao, M.2    Cheng, Y.3    Julius, D.4
  • 8
    • 0032825018 scopus 로고    scopus 로고
    • Sense and specificity: a molecular identity for nociceptors
    • doi: 10.1016/S0959-4388(99)00009-4
    • Caterina, M. J., and Julius, D. (1999). Sense and specificity: a molecular identity for nociceptors. Curr. Opin. Neurobiol. 9, 525-530. doi: 10.1016/S0959-4388(99)00009-4.
    • (1999) Curr. Opin. Neurobiol. , vol.9 , pp. 525-530
    • Caterina, M.J.1    Julius, D.2
  • 9
    • 0030777012 scopus 로고    scopus 로고
    • The capsaicin receptor: a heat-activated ion channel in the pain pathway
    • doi: 10.1038/39807
    • Caterina, M. J., Schumacher, M. A., Tominaga, M., Rosen, T. A., Levine, J. D., and Julius, D. (1997). The capsaicin receptor: a heat-activated ion channel in the pain pathway. Nature 389, 816-824. doi: 10.1038/39807.
    • (1997) Nature , vol.389 , pp. 816-824
    • Caterina, M.J.1    Schumacher, M.A.2    Tominaga, M.3    Rosen, T.A.4    Levine, J.D.5    Julius, D.6
  • 10
    • 0030446311 scopus 로고    scopus 로고
    • A novel heat-activated current in nociceptive neurons and its sensitization by bradykinin
    • doi: 10.1073/pnas.93.26.15435
    • Cesare, P., and McNaughton, P. (1996). A novel heat-activated current in nociceptive neurons and its sensitization by bradykinin. Proc. Natl. Acad. Sci. U.S.A. 93, 15435-15439. doi: 10.1073/pnas.93.26.15435.
    • (1996) Proc. Natl. Acad. Sci. U.S.A. , vol.93 , pp. 15435-15439
    • Cesare, P.1    McNaughton, P.2
  • 11
    • 77954895219 scopus 로고    scopus 로고
    • Structure of the full-length Shaker potassium channel Kv1.2 by normal-mode-based X-ray crystallographic refinement
    • doi: 10.1073/pnas.1000142107
    • Chen, X., Wang, Q., Ni, F., and Ma, J. (2010). Structure of the full-length Shaker potassium channel Kv1.2 by normal-mode-based X-ray crystallographic refinement. Proc. Natl. Acad. Sci. U.S.A. 107, 11352-11357. doi: 10.1073/pnas.1000142107.
    • (2010) Proc. Natl. Acad. Sci. U.S.A. , vol.107 , pp. 11352-11357
    • Chen, X.1    Wang, Q.2    Ni, F.3    Ma, J.4
  • 12
    • 84870045413 scopus 로고    scopus 로고
    • Leucettamols, bifunctionalized marine sphingoids, act as modulators of TRPA1 and TRPM8 channels
    • doi: 10.3390/md10112435
    • Chianese, G., Fattorusso, E., Putra, M. Y., Calcinai, B., Bavestrello, G., Moriello, A. S., et al. (2012). Leucettamols, bifunctionalized marine sphingoids, act as modulators of TRPA1 and TRPM8 channels. Mar. Drugs 10, 2435-2447. doi: 10.3390/md10112435.
    • (2012) Mar. Drugs , vol.10 , pp. 2435-2447
    • Chianese, G.1    Fattorusso, E.2    Putra, M.Y.3    Calcinai, B.4    Bavestrello, G.5    Moriello, A.S.6
  • 13
    • 4544368241 scopus 로고    scopus 로고
    • The super-cooling agent icilin reveals a mechanism of coincidence detection by a temperature-sensitive TRP channel
    • doi: 10.1016/j.neuron.2004.08.038
    • Chuang, H., Neuhausser, W. M., and Julius, D. (2004). The super-cooling agent icilin reveals a mechanism of coincidence detection by a temperature-sensitive TRP channel. Neuron 43, 859-869. doi: 10.1016/j.neuron.2004.08.038.
    • (2004) Neuron , vol.43 , pp. 859-869
    • Chuang, H.1    Neuhausser, W.M.2    Julius, D.3
  • 14
    • 42649095142 scopus 로고    scopus 로고
    • TRPV1 shows dynamic ionic selectivity during agonist stimulation
    • doi: 10.1038/nn.2102
    • Chung, M.-K., Güler, A. D., and Caterina, M. J. (2008). TRPV1 shows dynamic ionic selectivity during agonist stimulation. Nat. Neurosci. 11, 555-564. doi: 10.1038/nn.2102.
    • (2008) Nat. Neurosci. , vol.11 , pp. 555-564
    • Chung, M.-K.1    Güler, A.D.2    Caterina, M.J.3
  • 15
    • 0347504835 scopus 로고    scopus 로고
    • TRP channels as cellular sensors
    • doi: 10.1038/nature02196
    • Clapham, D. E. (2003). TRP channels as cellular sensors. Nature 426, 517-524. doi: 10.1038/nature02196.
    • (2003) Nature , vol.426 , pp. 517-524
    • Clapham, D.E.1
  • 16
    • 81255135460 scopus 로고    scopus 로고
    • 'Transient receptor potential (TRP) channels'
    • ed L. R. Squire
    • Clapham, D. E. (2009). "Transient receptor potential (TRP) channels," in Encyclopedia of Neuroscience, ed L. R. Squire. Available online at: http://clapham.tch.harvard.edu/publications/pdf/01634.pdf.
    • (2009) Encyclopedia of Neuroscience
    • Clapham, D.E.1
  • 17
    • 40349085541 scopus 로고    scopus 로고
    • Structure of the transmembrane regions of a bacterial cyclic nucleotide-regulated channel
    • doi: 10.1073/pnas.0711533105
    • Clayton, G. M., Altieri, S., Heginbotham, L., Unger, V. M., and Morais-Cabral, J. H. (2008). Structure of the transmembrane regions of a bacterial cyclic nucleotide-regulated channel. Proc. Natl. Acad. Sci. U.S.A. 105, 1511-1515. doi: 10.1073/pnas.0711533105.
    • (2008) Proc. Natl. Acad. Sci. U.S.A. , vol.105 , pp. 1511-1515
    • Clayton, G.M.1    Altieri, S.2    Heginbotham, L.3    Unger, V.M.4    Morais-Cabral, J.H.5
  • 18
    • 84885615091 scopus 로고    scopus 로고
    • Coarse Architecture of the Transient Receptor Potential Vanilloid 1 (TRPV1) ion channel determined by fluorescence resonance energy transfer
    • doi: 10.1074/jbc.M113.479618
    • De-la-Rosa, V., Rangel-Yescas, G. E., Ladron-de-Guevara, E., Rosenbaum, T., and Islas, L. D. (2013). Coarse Architecture of the Transient Receptor Potential Vanilloid 1 (TRPV1) ion channel determined by fluorescence resonance energy transfer. J. Biol. Chem. 288, 29506-29517. doi: 10.1074/jbc.M113.479618.
    • (2013) J. Biol. Chem. , vol.288 , pp. 29506-29517
    • De-la-Rosa, V.1    Rangel-Yescas, G.E.2    Ladron-de-Guevara, E.3    Rosenbaum, T.4    Islas, L.D.5
  • 19
    • 44249117614 scopus 로고    scopus 로고
    • Plant-derived cannabinoids modulate the activity of transient receptor potential channels of Ankyrin Type-1 and Melastatin Type-8
    • doi: 10.1124/jpet.107.134809
    • De Petrocellis, L., Vellani, V., Schiano-Moriello, A., Marini, P., Magherini, P. C., Orlando, P., et al. (2008). Plant-derived cannabinoids modulate the activity of transient receptor potential channels of Ankyrin Type-1 and Melastatin Type-8. J. Pharmacol. Exp. Ther. 325, 1007-1015. doi: 10.1124/jpet.107.134809.
    • (2008) J. Pharmacol. Exp. Ther. , vol.325 , pp. 1007-1015
    • De Petrocellis, L.1    Vellani, V.2    Schiano-Moriello, A.3    Marini, P.4    Magherini, P.C.5    Orlando, P.6
  • 20
    • 0036685486 scopus 로고    scopus 로고
    • Endovanilloid signaling in pain
    • doi: 10.1016/S0959-4388(02)00340-9
    • Di Marzo, V., Blumberg, P. M., and Szallasi, A. (2002). Endovanilloid signaling in pain. Curr. Opin. Neurobiol. 12, 372-379. doi: 10.1016/S0959-4388(02)00340-9.
    • (2002) Curr. Opin. Neurobiol. , vol.12 , pp. 372-379
    • Di Marzo, V.1    Blumberg, P.M.2    Szallasi, A.3
  • 22
    • 79952148112 scopus 로고    scopus 로고
    • Voltage-and temperature-dependent activation of TRPV3 channels is potentiated by receptor-mediated PI(4,5)P2 hydrolysis
    • doi: 10.1085/jgp.200910388
    • Doerner, J. F., Hatt, H., and Ramsey, I. S. (2011). Voltage-and temperature-dependent activation of TRPV3 channels is potentiated by receptor-mediated PI(4,5)P2 hydrolysis. J. Gen. Physiol. 137, 271-288. doi: 10.1085/jgp.200910388.
    • (2011) J. Gen. Physiol. , vol.137 , pp. 271-288
    • Doerner, J.F.1    Hatt, H.2    Ramsey, I.S.3
  • 23
    • 0030043489 scopus 로고    scopus 로고
    • Cation-pi interactions in chemistry and biology: a new view of benzene, Phe, Tyr, and Trp
    • doi: 10.1126/science.271.5246.163
    • Dougherty, D. A. (1996). Cation-pi interactions in chemistry and biology: a new view of benzene, Phe, Tyr, and Trp. Science 271, 163-168. doi: 10.1126/science.271.5246.163.
    • (1996) Science , vol.271 , pp. 163-168
    • Dougherty, D.A.1
  • 24
    • 33646766400 scopus 로고    scopus 로고
    • Structure-activity studies of a novel series of 5,6-fused heteroaromatic ureas as TRPV1 antagonists
    • doi: 10.1016/j.bmc.2006.03.027
    • Drizin, I., Gomtsyan, A., Bayburt, E. K., Schmidt, R. G., Zheng, G. Z., Perner, R. J., et al. (2006). Structure-activity studies of a novel series of 5,6-fused heteroaromatic ureas as TRPV1 antagonists. Bioorg. Med. Chem. 14, 4740-4749. doi: 10.1016/j.bmc.2006.03.027.
    • (2006) Bioorg. Med. Chem. , vol.14 , pp. 4740-4749
    • Drizin, I.1    Gomtsyan, A.2    Bayburt, E.K.3    Schmidt, R.G.4    Zheng, G.Z.5    Perner, R.J.6
  • 25
    • 84866734930 scopus 로고    scopus 로고
    • The role of chemosensitive afferent nerves and TRP ion channels in the pathomechanism of headaches
    • doi: 10.1007/s00424-012-1142-7
    • Dux, M., Sántha, P., and Jancsó, G. (2012). The role of chemosensitive afferent nerves and TRP ion channels in the pathomechanism of headaches. Pflüg. Arch. Eur. J. Physiol. 464, 239-248. doi: 10.1007/s00424-012-1142-7.
    • (2012) Pflüg. Arch. Eur. J. Physiol. , vol.464 , pp. 239-248
    • Dux, M.1    Sántha, P.2    Jancsó, G.3
  • 26
    • 53849108437 scopus 로고    scopus 로고
    • Molecular modeling of the full-length human TRPV1 channel in closed and desensitized states
    • doi: 10.1007/s00232-008-9123-7
    • Fernández-Ballester, G., and Ferrer-Montiel, A. (2008). Molecular modeling of the full-length human TRPV1 channel in closed and desensitized states. J. Membr. Biol. 223, 161-172. doi: 10.1007/s00232-008-9123-7.
    • (2008) J. Membr. Biol. , vol.223 , pp. 161-172
    • Fernández-Ballester, G.1    Ferrer-Montiel, A.2
  • 28
    • 84875998693 scopus 로고    scopus 로고
    • Ambient temperature affects the temperature threshold for TRPM8 activation through interaction of Phosphatidylinositol 4,5-Bisphosphate
    • doi: 10.1523/JNEUROSCI.5672-12.2013
    • Fujita, F., Uchida, K., Takaishi, M., Sokabe, T., and Tominaga, M. (2013). Ambient temperature affects the temperature threshold for TRPM8 activation through interaction of Phosphatidylinositol 4,5-Bisphosphate. J. Neurosci. 33, 6154-6159. doi: 10.1523/JNEUROSCI.5672-12.2013.
    • (2013) J. Neurosci. , vol.33 , pp. 6154-6159
    • Fujita, F.1    Uchida, K.2    Takaishi, M.3    Sokabe, T.4    Tominaga, M.5
  • 29
    • 84878677214 scopus 로고    scopus 로고
    • Phosphatidylinositol-4,5-biphosphate-dependent rearrangement of TRPV4 cytosolic tails enables channel activation by physiological stimuli
    • doi: 10.1073/pnas.1220231110
    • Garcia-Elias, A., Mrkonjic, S., Pardo-Pastor, C., Inada, H., Hellmich, U. A., Rubio-Moscardó, F., et al. (2013). Phosphatidylinositol-4,5-biphosphate-dependent rearrangement of TRPV4 cytosolic tails enables channel activation by physiological stimuli. Proc. Natl. Acad. Sci. U.S.A. 110, 9553-9558. doi: 10.1073/pnas.1220231110.
    • (2013) Proc. Natl. Acad. Sci. U.S.A. , vol.110 , pp. 9553-9558
    • Garcia-Elias, A.1    Mrkonjic, S.2    Pardo-Pastor, C.3    Inada, H.4    Hellmich, U.A.5    Rubio-Moscardó, F.6
  • 30
    • 35549010723 scopus 로고    scopus 로고
    • A role of the transient receptor potential domain of vanilloid receptor I in channel gating
    • doi: 10.1523/JNEUROSCI.2457-07.2007
    • Garcia-Sanz, N., Valente, P., Gomis, A., Fernandez-Carvajal, A., Fernandez-Ballester, G., Viana, F., et al. (2007). A role of the transient receptor potential domain of vanilloid receptor I in channel gating. J. Neurosci. 27, 11641-11650. doi: 10.1523/JNEUROSCI.2457-07.2007.
    • (2007) J. Neurosci. , vol.27 , pp. 11641-11650
    • Garcia-Sanz, N.1    Valente, P.2    Gomis, A.3    Fernandez-Carvajal, A.4    Fernandez-Ballester, G.5    Viana, F.6
  • 31
    • 2442498381 scopus 로고    scopus 로고
    • Molecular determinants of vanilloid sensitivity in TRPV1
    • doi: 10.1074/jbc.M312577200
    • Gavva, N. R., Klionsky, L., Qu, Y., Shi, L., Tamir, R., Edenson, S., et al. (2004). Molecular determinants of vanilloid sensitivity in TRPV1. J. Biol. Chem. 279, 20283-20295. doi: 10.1074/jbc.M312577200.
    • (2004) J. Biol. Chem. , vol.279 , pp. 20283-20295
    • Gavva, N.R.1    Klionsky, L.2    Qu, Y.3    Shi, L.4    Tamir, R.5    Edenson, S.6
  • 32
    • 34548858716 scopus 로고    scopus 로고
    • Structure-activity relationship (SAR) investigations of substituted imidazole analogs as TRPV1 antagonists
    • doi: 10.1016/j.bmcl.2007.08.044
    • Gore, V. K., Ma, V. V., Tamir, R., Gavva, N. R., Treanor, J. J. S., and Norman, M. H. (2007). Structure-activity relationship (SAR) investigations of substituted imidazole analogs as TRPV1 antagonists. Bioorg. Med. Chem. Lett. 17, 5825-5830. doi: 10.1016/j.bmcl.2007.08.044.
    • (2007) Bioorg. Med. Chem. Lett. , vol.17 , pp. 5825-5830
    • Gore, V.K.1    Ma, V.V.2    Tamir, R.3    Gavva, N.R.4    Treanor, J.J.S.5    Norman, M.H.6
  • 33
    • 84894485922 scopus 로고    scopus 로고
    • Mutation of I696 and W697 in the TRP box of vanilloid receptor subtype I modulates allosteric channel activation
    • doi: 10.1085/jgp.201311070
    • Gregorio-Teruel, L., Valente, P., González-Ros, J. M., Fernández-Ballester, G., and Ferrer-Montiel, A. (2014). Mutation of I696 and W697 in the TRP box of vanilloid receptor subtype I modulates allosteric channel activation. J. Gen. Physiol. 143, 361-375. doi: 10.1085/jgp.201311070.
    • (2014) J. Gen. Physiol. , vol.143 , pp. 361-375
    • Gregorio-Teruel, L.1    Valente, P.2    González-Ros, J.M.3    Fernández-Ballester, G.4    Ferrer-Montiel, A.5
  • 34
  • 35
    • 0034177642 scopus 로고    scopus 로고
    • From worm to man: three subfamilies of TRP channels
    • doi: 10.1016/S0166-2236(99)01532-5
    • Harteneck, C., Plant, T. D., and Schultz, G. (2000). From worm to man: three subfamilies of TRP channels. Trends Neurosci. 23, 159-166. doi: 10.1016/S0166-2236(99)01532-5.
    • (2000) Trends Neurosci. , vol.23 , pp. 159-166
    • Harteneck, C.1    Plant, T.D.2    Schultz, G.3
  • 36
    • 78149284010 scopus 로고    scopus 로고
    • Discovery and synthesis of 6,7,8,9-tetrahydro-5H-pyrimido-[4,5-d]azepines as novel TRPV1 antagonists
    • doi: 10.1016/j.bmcl.2010.09.023
    • Hawryluk, N. A., Merit, J. E., Lebsack, A. D., Branstetter, B. J., Hack, M. D., Swanson, N., et al. (2010). Discovery and synthesis of 6,7,8,9-tetrahydro-5H-pyrimido-[4,5-d]azepines as novel TRPV1 antagonists. Bioorg. Med. Chem. Lett. 20, 7137-7141. doi: 10.1016/j.bmcl.2010.09.023.
    • (2010) Bioorg. Med. Chem. Lett. , vol.20 , pp. 7137-7141
    • Hawryluk, N.A.1    Merit, J.E.2    Lebsack, A.D.3    Branstetter, B.J.4    Hack, M.D.5    Swanson, N.6
  • 37
    • 0004906771 scopus 로고    scopus 로고
    • Direct activation of capsaicin receptors by products of lipoxygenases: endogenous capsaicin-like substances
    • doi: 10.1073/pnas.97.11.6155
    • Hwang, S. W., Cho, H., Kwak, J., Lee, S. Y., Kang, C. J., Jung, J., et al. (2000). Direct activation of capsaicin receptors by products of lipoxygenases: endogenous capsaicin-like substances. Proc. Natl. Acad. Sci. U.S.A. 97, 6155-6160. doi: 10.1073/pnas.97.11.6155.
    • (2000) Proc. Natl. Acad. Sci. U.S.A. , vol.97 , pp. 6155-6160
    • Hwang, S.W.1    Cho, H.2    Kwak, J.3    Lee, S.Y.4    Kang, C.J.5    Jung, J.6
  • 38
    • 33847792875 scopus 로고    scopus 로고
    • The TRPV1 receptor and nociception
    • doi: 10.1016/j.semcdb.2006.09.004
    • Immke, D. C., and Gavva, N. R. (2006). The TRPV1 receptor and nociception. Semin. Cell Dev. Biol. 17, 582-591. doi: 10.1016/j.semcdb.2006.09.004.
    • (2006) Semin. Cell Dev. Biol. , vol.17 , pp. 582-591
    • Immke, D.C.1    Gavva, N.R.2
  • 39
    • 0035721695 scopus 로고    scopus 로고
    • Biochemical characterization of the vanilloid receptor 1 expressed in a dorsal root ganglia derived cell line
    • doi: 10.1046/j.1432-1033.2001.02500.x
    • Jahnel, R., Dreger, M., Gillen, C., Bender, O., Kurreck, J., and Hucho, F. (2001). Biochemical characterization of the vanilloid receptor 1 expressed in a dorsal root ganglia derived cell line. Eur. J. Biochem. 268, 5489-5496. doi: 10.1046/j.1432-1033.2001.02500.x.
    • (2001) Eur. J. Biochem. , vol.268 , pp. 5489-5496
    • Jahnel, R.1    Dreger, M.2    Gillen, C.3    Bender, O.4    Kurreck, J.5    Hucho, F.6
  • 40
    • 41849142683 scopus 로고    scopus 로고
    • N-pyridin-3-yl-and N-quinolin-3-yl-benzamides: modulators of human vanilloid receptor 1 (TRPV1)
    • doi: 10.1016/j.bmcl.2008.02.075
    • Jetter, M. C., McNally, J. J., Youngman, M. A., McDonnell, M. E., Dubin, A. E., Nasser, N., et al. (2008). N-pyridin-3-yl-and N-quinolin-3-yl-benzamides: modulators of human vanilloid receptor 1 (TRPV1). Bioorg. Med. Chem. Lett. 18, 2730-2734. doi: 10.1016/j.bmcl.2008.02.075.
    • (2008) Bioorg. Med. Chem. Lett. , vol.18 , pp. 2730-2734
    • Jetter, M.C.1    McNally, J.J.2    Youngman, M.A.3    McDonnell, M.E.4    Dubin, A.E.5    Nasser, N.6
  • 41
    • 0036183319 scopus 로고    scopus 로고
    • Molecular basis for species-specific sensitivity to "hot" chili peppers
    • doi: 10.1016/S0092-8674(02)00637-2
    • Jordt, S.-E., and Julius, D. (2002). Molecular basis for species-specific sensitivity to "hot" chili peppers. Cell 108, 421-430. doi: 10.1016/S0092-8674(02)00637-2.
    • (2002) Cell , vol.108 , pp. 421-430
    • Jordt, S.-E.1    Julius, D.2
  • 42
    • 84874650819 scopus 로고    scopus 로고
    • TRPM8 ion channel ligands for new therapeutic applications and as probes to study menthol pharmacology
    • doi: 10.1016/j.lfs.2012.10.032
    • Journigan, V. B., and Zaveri, N. T. (2013). TRPM8 ion channel ligands for new therapeutic applications and as probes to study menthol pharmacology. Life Sci. 92, 425-437. doi: 10.1016/j.lfs.2012.10.032.
    • (2013) Life Sci. , vol.92 , pp. 425-437
    • Journigan, V.B.1    Zaveri, N.T.2
  • 43
    • 84885827972 scopus 로고    scopus 로고
    • TRP channels and pain
    • doi: 10.1146/annurev-cellbio-101011-155833
    • Julius, D. (2013). TRP channels and pain. Annu. Rev. Cell Dev. Biol. 29, 355-384. doi: 10.1146/annurev-cellbio-101011-155833.
    • (2013) Annu. Rev. Cell Dev. Biol. , vol.29 , pp. 355-384
    • Julius, D.1
  • 44
    • 84875762865 scopus 로고    scopus 로고
    • Exploring structure-function relationships between TRP and Kv channels
    • doi: 10.1038/srep01523
    • Kalia, J., and Swartz, K. J. (2013). Exploring structure-function relationships between TRP and Kv channels. Sci. Rep. 3:1523. doi: 10.1038/srep01523.
    • (2013) Sci. Rep. , vol.3 , pp. 1523
    • Kalia, J.1    Swartz, K.J.2
  • 45
    • 34548610605 scopus 로고    scopus 로고
    • Bimodal action of menthol on the transient receptor potential channel TRPA1
    • doi: 10.1523/JNEUROSCI.2221-07.2007
    • Karashima, Y., Damann, N., Prenen, J., Talavera, K., Segal, A., Voets, T., et al. (2007). Bimodal action of menthol on the transient receptor potential channel TRPA1. J. Neurosci. 27, 9874-9884. doi: 10.1523/JNEUROSCI.2221-07.2007.
    • (2007) J. Neurosci. , vol.27 , pp. 9874-9884
    • Karashima, Y.1    Damann, N.2    Prenen, J.3    Talavera, K.4    Segal, A.5    Voets, T.6
  • 46
    • 0035958884 scopus 로고    scopus 로고
    • Analysis of the native quaternary structure of vanilloid receptor 1
    • doi: 10.1074/jbc.M103272200
    • Kedei, N. (2001). Analysis of the native quaternary structure of vanilloid receptor 1. J. Biol. Chem. 276, 28613-28619. doi: 10.1074/jbc.M103272200.
    • (2001) J. Biol. Chem. , vol.276 , pp. 28613-28619
    • Kedei, N.1
  • 47
    • 84866146025 scopus 로고    scopus 로고
    • Regulation of voltage-gated potassium channels by PI(4,5)P2
    • doi: 10.1085/jgp.201210806
    • Kruse, M., Hammond, G. R. V., and Hille, B. (2012). Regulation of voltage-gated potassium channels by PI(4,5)P2. J. Gen. Physiol. 140, 189-205. doi: 10.1085/jgp.201210806.
    • (2012) J. Gen. Physiol. , vol.140 , pp. 189-205
    • Kruse, M.1    Hammond, G.R.V.2    Hille, B.3
  • 48
    • 67349241526 scopus 로고    scopus 로고
    • Analgesic potential of TRPV1 antagonists
    • doi: 10.1016/j.bcp.2009.02.014
    • Kym, P. R., Kort, M. E., and Hutchins, C. W. (2009). Analgesic potential of TRPV1 antagonists. Biochem. Pharmacol. 78, 211-216. doi: 10.1016/j.bcp.2009.02.014.
    • (2009) Biochem. Pharmacol. , vol.78 , pp. 211-216
    • Kym, P.R.1    Kort, M.E.2    Hutchins, C.W.3
  • 49
    • 34547953765 scopus 로고    scopus 로고
    • ThermoTRP channels as modular proteins with allosteric gating
    • doi: 10.1016/j.ceca.2007.04.004
    • Latorre, R., Brauchi, S., Orta, G., Zaelzer, C., and Vargas, G. (2007). ThermoTRP channels as modular proteins with allosteric gating. Cell Calcium 42, 427-438. doi: 10.1016/j.ceca.2007.04.004.
    • (2007) Cell Calcium , vol.42 , pp. 427-438
    • Latorre, R.1    Brauchi, S.2    Orta, G.3    Zaelzer, C.4    Vargas, G.5
  • 50
    • 77449112680 scopus 로고    scopus 로고
    • Structure-functional intimacies of transient receptor potential channels
    • doi: 10.1017/S0033583509990072
    • Latorre, R., Zaelzer, C., and Brauchi, S. (2009). Structure-functional intimacies of transient receptor potential channels. Q. Rev. Biophys. 42, 201. doi: 10.1017/S0033583509990072.
    • (2009) Q. Rev. Biophys. , vol.42 , pp. 201
    • Latorre, R.1    Zaelzer, C.2    Brauchi, S.3
  • 51
    • 42149169961 scopus 로고    scopus 로고
    • Thymol and related alkyl phenols activate the hTRPA1 channel
    • doi: 10.1038/bjp.2008.85
    • Lee, S. P., Buber, M. T., Yang, Q., Cerne, R., Cortés, R. Y., Sprous, D. G., et al. (2008). Thymol and related alkyl phenols activate the hTRPA1 channel. Br. J. Pharmacol. 153, 1739-1749. doi: 10.1038/bjp.2008.85.
    • (2008) Br. J. Pharmacol. , vol.153 , pp. 1739-1749
    • Lee, S.P.1    Buber, M.T.2    Yang, Q.3    Cerne, R.4    Cortés, R.Y.5    Sprous, D.G.6
  • 52
    • 13444263549 scopus 로고    scopus 로고
    • Clathrin-and non-clathrin-mediated endocytic regulation of cell signalling
    • doi: 10.1038/nrm1571
    • Le Roy, C., and Wrana, J. L. (2005). Clathrin-and non-clathrin-mediated endocytic regulation of cell signalling. Nat. Rev. Mol. Cell Biol. 6, 112-126. doi: 10.1038/nrm1571.
    • (2005) Nat. Rev. Mol. Cell Biol. , vol.6 , pp. 112-126
    • Le Roy, C.1    Wrana, J.L.2
  • 53
    • 79959794812 scopus 로고    scopus 로고
    • 'Structural biology of TRP channels'
    • ed M. S. Islam (Dordrecht: Springer Netherlands), (Accessed March 10, 2014).
    • Li, M., Yu, Y., and Yang, J. (2011). "Structural biology of TRP channels," in Transient Receptor Potential Channels, ed M. S. Islam (Dordrecht: Springer Netherlands), 1-23. Available online at: http://link.springer.com/10.1007/978-94-007-0265-3_1 (Accessed March 10, 2014).
    • (2011) Transient Receptor Potential Channels , pp. 1-23
    • Li, M.1    Yu, Y.2    Yang, J.3
  • 54
    • 84889607320 scopus 로고    scopus 로고
    • Structure of the TRPV1 ion channel determined by electron cryo-microscopy
    • doi: 10.1038/nature12822
    • Liao, M., Cao, E., Julius, D., and Cheng, Y. (2013). Structure of the TRPV1 ion channel determined by electron cryo-microscopy. Nature 504, 107-112. doi: 10.1038/nature12822.
    • (2013) Nature , vol.504 , pp. 107-112
    • Liao, M.1    Cao, E.2    Julius, D.3    Cheng, Y.4
  • 55
    • 77952289412 scopus 로고    scopus 로고
    • NPPB structure-specifically activates TRPA1 channels
    • doi: 10.1016/j.bcp.2010.03.005
    • Liu, K., Samuel, M., Ho, M., Harrison, R. K., and Paslay, J. W. (2010). NPPB structure-specifically activates TRPA1 channels. Biochem. Pharmacol. 80, 113-121. doi: 10.1016/j.bcp.2010.03.005.
    • (2010) Biochem. Pharmacol. , vol.80 , pp. 113-121
    • Liu, K.1    Samuel, M.2    Ho, M.3    Harrison, R.K.4    Paslay, J.W.5
  • 57
    • 84890289989 scopus 로고    scopus 로고
    • Promiscuous Activation of Transient Receptor Potential Vanilloid 1 (TRPV1) channels by negatively charged intracellular lipids: the key role of endogenous phosphoinositides in maintaining channel activity
    • doi: 10.1074/jbc.M113.520288
    • Lukacs, V., Rives, J.-M., Sun, X., Zakharian, E., and Rohacs, T. (2013). Promiscuous Activation of Transient Receptor Potential Vanilloid 1 (TRPV1) channels by negatively charged intracellular lipids: the key role of endogenous phosphoinositides in maintaining channel activity. J. Biol. Chem. 288, 35003-35013. doi: 10.1074/jbc.M113.520288.
    • (2013) J. Biol. Chem. , vol.288 , pp. 35003-35013
    • Lukacs, V.1    Rives, J.-M.2    Sun, X.3    Zakharian, E.4    Rohacs, T.5
  • 58
    • 33846692923 scopus 로고    scopus 로고
    • Noxious compounds activate TRPA1 ion channels through covalent modification of cysteines
    • doi: 10.1038/nature05544
    • Macpherson, L. J., Dubin, A. E., Evans, M. J., Marr, F., Schultz, P. G., Cravatt, B. F., et al. (2007). Noxious compounds activate TRPA1 ion channels through covalent modification of cysteines. Nature 445, 541-545. doi: 10.1038/nature05544.
    • (2007) Nature , vol.445 , pp. 541-545
    • Macpherson, L.J.1    Dubin, A.E.2    Evans, M.J.3    Marr, F.4    Schultz, P.G.5    Cravatt, B.F.6
  • 59
    • 20144371097 scopus 로고    scopus 로고
    • The pungency of garlic: activation of TRPA1 and TRPV1 in response to allicin
    • doi: 10.1016/j.cub.2005.04.018
    • Macpherson, L. J., Geierstanger, B. H., Viswanath, V., Bandell, M., Eid, S. R., Hwang, S., et al. (2005). The pungency of garlic: activation of TRPA1 and TRPV1 in response to allicin. Curr. Biol. 15, 929-934. doi: 10.1016/j.cub.2005.04.018.
    • (2005) Curr. Biol. , vol.15 , pp. 929-934
    • Macpherson, L.J.1    Geierstanger, B.H.2    Viswanath, V.3    Bandell, M.4    Eid, S.R.5    Hwang, S.6
  • 60
    • 41149168740 scopus 로고    scopus 로고
    • Activation of TRPA1 by farnesyl thiosalicylic acid
    • doi: 10.1124/mol.107.042663
    • Maher, M., Ao, H., Banke, T., Nasser, N., Wu, N.-T., Breitenbucher, J. G., et al. (2008). Activation of TRPA1 by farnesyl thiosalicylic acid. Mol. Pharmacol. 73, 1225-1234. doi: 10.1124/mol.107.042663.
    • (2008) Mol. Pharmacol. , vol.73 , pp. 1225-1234
    • Maher, M.1    Ao, H.2    Banke, T.3    Nasser, N.4    Wu, N.-T.5    Breitenbucher, J.G.6
  • 61
    • 41949127906 scopus 로고    scopus 로고
    • ThermoTRP channels in nociceptors: taking a lead from capsaicin receptor TRPV1
    • doi: 10.2174/157015908783769680
    • Mandadi, S., and Roufogalis, B. D. (2008). ThermoTRP channels in nociceptors: taking a lead from capsaicin receptor TRPV1. Curr. Neuropharmacol. 6, 21-38. doi: 10.2174/157015908783769680.
    • (2008) Curr. Neuropharmacol. , vol.6 , pp. 21-38
    • Mandadi, S.1    Roufogalis, B.D.2
  • 62
    • 37549038688 scopus 로고    scopus 로고
    • Three-dimensional reconstruction using transmission electron microscopy reveals a swollen, bell-shaped structure of transient receptor potential melastatin type 2 cation channel
    • doi: 10.1074/jbc.M705694200
    • Maruyama, Y., Ogura, T., Mio, K., Kiyonaka, S., Kato, K., Mori, Y., et al. (2007). Three-dimensional reconstruction using transmission electron microscopy reveals a swollen, bell-shaped structure of transient receptor potential melastatin type 2 cation channel. J. Biol. Chem. 282, 36961-36970. doi: 10.1074/jbc.M705694200.
    • (2007) J. Biol. Chem. , vol.282 , pp. 36961-36970
    • Maruyama, Y.1    Ogura, T.2    Mio, K.3    Kiyonaka, S.4    Kato, K.5    Mori, Y.6
  • 63
    • 33846230027 scopus 로고    scopus 로고
    • TRPV1 is a novel target for omega-3 polyunsaturated fatty acids
    • doi: 10.1113/jphysiol.2006.121988
    • Matta, J. A., Miyares, R. L., and Ahern, G. P. (2007). TRPV1 is a novel target for omega-3 polyunsaturated fatty acids. J. Physiol. 578, 397-411. doi: 10.1113/jphysiol.2006.121988.
    • (2007) J. Physiol. , vol.578 , pp. 397-411
    • Matta, J.A.1    Miyares, R.L.2    Ahern, G.P.3
  • 64
    • 0037034931 scopus 로고    scopus 로고
    • Identification of a cold receptor reveals a general role for TRP channels in thermosensation
    • doi: 10.1038/nature719
    • McKemy, D. D., Neuhausser, W. M., and Julius, D. (2002). Identification of a cold receptor reveals a general role for TRP channels in thermosensation. Nature 416, 52-58. doi: 10.1038/nature719.
    • (2002) Nature , vol.416 , pp. 52-58
    • McKemy, D.D.1    Neuhausser, W.M.2    Julius, D.3
  • 65
    • 33646024354 scopus 로고    scopus 로고
    • Physiology and pharmacology of the vanilloid receptor
    • doi: 10.2174/157015906775202995
    • Messeguer, A., Planells-Cases, R., and Ferrer-Montiel, A. (2006). Physiology and pharmacology of the vanilloid receptor. Curr. Neuropharmacol. 4, 1-15. doi: 10.2174/157015906775202995.
    • (2006) Curr. Neuropharmacol. , vol.4 , pp. 1-15
    • Messeguer, A.1    Planells-Cases, R.2    Ferrer-Montiel, A.3
  • 66
    • 33847157855 scopus 로고    scopus 로고
    • The TRPC3 channel has a large internal chamber surrounded by signal sensing antennas
    • doi: 10.1016/j.jmb.2006.12.043
    • Mio, K., Ogura, T., Kiyonaka, S., Hiroaki, Y., Tanimura, Y., Fujiyoshi, Y., et al. (2007). The TRPC3 channel has a large internal chamber surrounded by signal sensing antennas. J. Mol. Biol. 367, 373-383. doi: 10.1016/j.jmb.2006.12.043.
    • (2007) J. Mol. Biol. , vol.367 , pp. 373-383
    • Mio, K.1    Ogura, T.2    Kiyonaka, S.3    Hiroaki, Y.4    Tanimura, Y.5    Fujiyoshi, Y.6
  • 68
    • 33644875032 scopus 로고    scopus 로고
    • The TRP superfamily of cation channels
    • doi: 10.1126/stke.2722005re3
    • Montell, C. (2005). The TRP superfamily of cation channels. Sci. STKE 2005, re3. doi: 10.1126/stke.2722005re3.
    • (2005) Sci. STKE , vol.2005
    • Montell, C.1
  • 69
    • 84879845514 scopus 로고    scopus 로고
    • The role of endogenous molecules in modulating pain through transient receptor potential vanilloid 1 (TRPV1)
    • doi: 10.1113/jphysiol.2013.251751
    • Morales-Lázaro, S. L., Simon, S. A., and Rosenbaum, T. (2013). The role of endogenous molecules in modulating pain through transient receptor potential vanilloid 1 (TRPV1). J. Physiol. 591, 3109-3121. doi: 10.1113/jphysiol.2013.251751.
    • (2013) J. Physiol. , vol.591 , pp. 3109-3121
    • Morales-Lázaro, S.L.1    Simon, S.A.2    Rosenbaum, T.3
  • 70
    • 71749101672 scopus 로고    scopus 로고
    • Synthesis and biological evaluation of piperazinyl carbamates and ureas as fatty acid amide hydrolase (FAAH) and transient receptor potential (TRP) channel dual ligands
    • doi: 10.1016/j.bmcl.2009.09.033
    • Morera, E., De Petrocellis, L., Morera, L., Moriello, A. S., Ligresti, A., Nalli, M., et al. (2009). Synthesis and biological evaluation of piperazinyl carbamates and ureas as fatty acid amide hydrolase (FAAH) and transient receptor potential (TRP) channel dual ligands. Bioorg. Med. Chem. Lett. 19, 6806-6809. doi: 10.1016/j.bmcl.2009.09.033.
    • (2009) Bioorg. Med. Chem. Lett. , vol.19 , pp. 6806-6809
    • Morera, E.1    De Petrocellis, L.2    Morera, L.3    Moriello, A.S.4    Ligresti, A.5    Nalli, M.6
  • 71
    • 84862534272 scopus 로고    scopus 로고
    • TRPA1 is a polyunsaturated fatty acid sensor in mammals
    • e38439. doi: 10.1371/journal.pone.0038439
    • Motter, A. L., and Ahern, G. P. (2012). TRPA1 is a polyunsaturated fatty acid sensor in mammals. PLoS ONE 7:e38439. doi: 10.1371/journal.pone.0038439.
    • (2012) PLoS ONE , vol.7
    • Motter, A.L.1    Ahern, G.P.2
  • 72
    • 34547521545 scopus 로고    scopus 로고
    • TRP channels in disease
    • doi: 10.1016/j.bbadis.2007.02.002
    • Nilius, B. (2007). TRP channels in disease. Biochim. Biophys. Acta 1772, 805-812. doi: 10.1016/j.bbadis.2007.02.002.
    • (2007) Biochim. Biophys. Acta , vol.1772 , pp. 805-812
    • Nilius, B.1
  • 73
    • 55549104701 scopus 로고    scopus 로고
    • Transient receptor potential channels meet phosphoinositides
    • doi: 10.1038/emboj.2008.217
    • Nilius, B., Owsianik, G., and Voets, T. (2008). Transient receptor potential channels meet phosphoinositides. EMBO J. 27, 2809-2816. doi: 10.1038/emboj.2008.217.
    • (2008) EMBO J. , vol.27 , pp. 2809-2816
    • Nilius, B.1    Owsianik, G.2    Voets, T.3
  • 74
    • 77950865335 scopus 로고    scopus 로고
    • (-)-Menthylamine derivatives as potent and selective antagonists of transient receptor potential melastatin type-8 (TRPM8) channels
    • doi: 10.1016/j.bmcl.2010.03.076
    • Ortar, G., De Petrocellis, L., Morera, L., Moriello, A. S., Orlando, P., Morera, E., et al. (2010). (-)-Menthylamine derivatives as potent and selective antagonists of transient receptor potential melastatin type-8 (TRPM8) channels. Bioorg. Med. Chem. Lett. 20, 2729-2732. doi: 10.1016/j.bmcl.2010.03.076.
    • (2010) Bioorg. Med. Chem. Lett. , vol.20 , pp. 2729-2732
    • Ortar, G.1    De Petrocellis, L.2    Morera, L.3    Moriello, A.S.4    Orlando, P.5    Morera, E.6
  • 75
    • 33646842722 scopus 로고    scopus 로고
    • Structure-function relationship of the TRP channel superfamily
    • doi: 10.1007/s10254-005-0006-0
    • Owsianik, G., D'hoedt, D., Voets, T., and Nilius, B. (2006). Structure-function relationship of the TRP channel superfamily. Rev. Physiol. Biochem. Pharmacol. 156, 61-90. doi: 10.1007/s10254-005-0006-0.
    • (2006) Rev. Physiol. Biochem. Pharmacol. , vol.156 , pp. 61-90
    • Owsianik, G.1    D'hoedt, D.2    Voets, T.3    Nilius, B.4
  • 76
    • 84876733546 scopus 로고    scopus 로고
    • Endogenous modulators of TRP channels
    • doi: 10.2174/1568026611313030014
    • Palazzo, E., Rossi, F., de Novellis, V., and Maione, S. (2013). Endogenous modulators of TRP channels. Curr. Top. Med. Chem. 13, 398-407. doi: 10.2174/1568026611313030014.
    • (2013) Curr. Top. Med. Chem. , vol.13 , pp. 398-407
    • Palazzo, E.1    Rossi, F.2    de Novellis, V.3    Maione, S.4
  • 77
    • 29344461269 scopus 로고    scopus 로고
    • TRP channels and thermosensation
    • doi: 10.1093/chemse/bjh180
    • Patapoutian, A. (2005). TRP channels and thermosensation. Chem. Senses 30(Suppl. 1), i193-194. doi: 10.1093/chemse/bjh180.
    • (2005) Chem. Senses , vol.30 , Issue.SUPPL. 1
    • Patapoutian, A.1
  • 79
    • 65249111686 scopus 로고    scopus 로고
    • Comparative modeling of the quaternary structure for the human TRPM8 channel and analysis of its binding features
    • doi: 10.1016/j.bbamem.2009.02.007
    • Pedretti, A., Marconi, C., Bettinelli, I., and Vistoli, G. (2009). Comparative modeling of the quaternary structure for the human TRPM8 channel and analysis of its binding features. Biochim. Biophys. Acta 1788, 973-982. doi: 10.1016/j.bbamem.2009.02.007.
    • (2009) Biochim. Biophys. Acta , vol.1788 , pp. 973-982
    • Pedretti, A.1    Marconi, C.2    Bettinelli, I.3    Vistoli, G.4
  • 80
    • 77954219697 scopus 로고    scopus 로고
    • Synthesis and biological evaluation of 5-substituted and 4,5-disubstituted-2-arylamino oxazole TRPV1 antagonists
    • doi: 10.1016/j.bmc.2010.04.099
    • Perner, R. J., Koenig, J. R., Didomenico, S., Gomtsyan, A., Schmidt, R. G., Lee, C.-H., et al. (2010). Synthesis and biological evaluation of 5-substituted and 4,5-disubstituted-2-arylamino oxazole TRPV1 antagonists. Bioorg. Med. Chem. 18, 4821-4829. doi: 10.1016/j.bmc.2010.04.099.
    • (2010) Bioorg. Med. Chem. , vol.18 , pp. 4821-4829
    • Perner, R.J.1    Koenig, J.R.2    Didomenico, S.3    Gomtsyan, A.4    Schmidt, R.G.5    Lee, C.-H.6
  • 81
    • 84923066343 scopus 로고    scopus 로고
    • 'Mutagenesis and temperature-sensitive little machines'
    • ed R. Mishra (InTech). (Accessed January 18, 2014).
    • Pertusa, M., Moldenhauer, H., Brauchi, S., Latorre, R., Madrid, R., and Orio, P. (2012). "Mutagenesis and temperature-sensitive little machines," in Mutagenesis, ed R. Mishra (InTech). Available online at: http://www.intechopen.com/books/mutagenesis/mutagenesis-and-temperature-sensitive-little-machines (Accessed January 18, 2014).
    • (2012) Mutagenesis
    • Pertusa, M.1    Moldenhauer, H.2    Brauchi, S.3    Latorre, R.4    Madrid, R.5    Orio, P.6
  • 82
    • 0026508664 scopus 로고
    • Identification of a Drosophila gene encoding a calmodulin-binding protein with homology to the trp phototransduction gene
    • doi: 10.1016/0896-6273(92)90085-R
    • Phillips, A. M., Bull, A., and Kelly, L. E. (1992). Identification of a Drosophila gene encoding a calmodulin-binding protein with homology to the trp phototransduction gene. Neuron 8, 631-642. doi: 10.1016/0896-6273(92)90085-R.
    • (1992) Neuron , vol.8 , pp. 631-642
    • Phillips, A.M.1    Bull, A.2    Kelly, L.E.3
  • 83
    • 2342439775 scopus 로고    scopus 로고
    • Identification of species-specific determinants of the action of the antagonist capsazepine and the agonist PPAHV on TRPV1
    • doi: 10.1074/jbc.M313328200
    • Phillips, E. (2004). Identification of species-specific determinants of the action of the antagonist capsazepine and the agonist PPAHV on TRPV1. J. Biol. Chem. 279, 17165-17172. doi: 10.1074/jbc.M313328200.
    • (2004) J. Biol. Chem. , vol.279 , pp. 17165-17172
    • Phillips, E.1
  • 84
    • 0242386586 scopus 로고    scopus 로고
    • Small molecules targeting the vanilloid receptor complex as drugs for inflammatory pain
    • doi: 10.1358/dof.2003.028.08.747395
    • Planells-Cases, R., Garcia-Martinez, C., Royo, M., Perez-Pay, E., Carreño, C., Albericio, F., et al. (2003). Small molecules targeting the vanilloid receptor complex as drugs for inflammatory pain. Drugs Future 28, 787. doi: 10.1358/dof.2003.028.08.747395.
    • (2003) Drugs Future , vol.28 , pp. 787
    • Planells-Cases, R.1    Garcia-Martinez, C.2    Royo, M.3    Perez-Pay, E.4    Carreño, C.5    Albericio, F.6
  • 86
    • 0037799198 scopus 로고    scopus 로고
    • A modular PIP2 binding site as a determinant of capsaicin receptor sensitivity
    • doi: 10.1126/science.1083646
    • Prescott, E. D., and Julius, D. (2003). A modular PIP2 binding site as a determinant of capsaicin receptor sensitivity. Science 300, 1284-1288. doi: 10.1126/science.1083646.
    • (2003) Science , vol.300 , pp. 1284-1288
    • Prescott, E.D.1    Julius, D.2
  • 87
    • 84876908893 scopus 로고    scopus 로고
    • TRPM8 activation attenuates inflammatory responses in mouse models of colitis
    • doi: 10.1073/pnas.1217431110
    • Ramachandran, R., Hyun, E., Zhao, L., Lapointe, T. K., Chapman, K., Hirota, C. L., et al. (2013). TRPM8 activation attenuates inflammatory responses in mouse models of colitis. Proc. Natl. Acad. Sci. U.S.A. 110, 7476-7481. doi: 10.1073/pnas.1217431110.
    • (2013) Proc. Natl. Acad. Sci. U.S.A. , vol.110 , pp. 7476-7481
    • Ramachandran, R.1    Hyun, E.2    Zhao, L.3    Lapointe, T.K.4    Chapman, K.5    Hirota, C.L.6
  • 88
    • 33645297168 scopus 로고    scopus 로고
    • An introduction to TRP channels
    • doi: 10.1146/annurev.physiol.68.040204.100431
    • Ramsey, I. S., Delling, M., and Clapham, D. E. (2006). An introduction to TRP channels. Annu. Rev. Physiol. 68, 619-647. doi: 10.1146/annurev.physiol.68.040204.100431.
    • (2006) Annu. Rev. Physiol. , vol.68 , pp. 619-647
    • Ramsey, I.S.1    Delling, M.2    Clapham, D.E.3
  • 89
    • 67349183758 scopus 로고    scopus 로고
    • Phosphoinositide regulation of non-canonical transient receptor potential channels
    • doi: 10.1016/j.ceca.2009.03.011
    • Rohacs, T. (2009). Phosphoinositide regulation of non-canonical transient receptor potential channels. Cell Calcium 45, 554-565. doi: 10.1016/j.ceca.2009.03.011.
    • (2009) Cell Calcium , vol.45 , pp. 554-565
    • Rohacs, T.1
  • 90
    • 17844373771 scopus 로고    scopus 로고
    • PI(4,5)P2 regulates the activation and desensitization of TRPM8 channels through the TRP domain
    • doi: 10.1038/nn1451
    • Rohács, T., Lopes, C. M. B., Michailidis, I., and Logothetis, D. E. (2005). PI(4,5)P2 regulates the activation and desensitization of TRPM8 channels through the TRP domain. Nat. Neurosci. 8, 626-634. doi: 10.1038/nn1451.
    • (2005) Nat. Neurosci. , vol.8 , pp. 626-634
    • Rohács, T.1    Lopes, C.M.B.2    Michailidis, I.3    Logothetis, D.E.4
  • 91
    • 53749084409 scopus 로고    scopus 로고
    • Phospholipase C mediated modulation of TRPV1 channels
    • doi: 10.1007/s12035-008-8027-y
    • Rohacs, T., Thyagarajan, B., and Lukacs, V. (2008). Phospholipase C mediated modulation of TRPV1 channels. Mol. Neurobiol. 37, 153-163. doi: 10.1007/s12035-008-8027-y.
    • (2008) Mol. Neurobiol. , vol.37 , pp. 153-163
    • Rohacs, T.1    Thyagarajan, B.2    Lukacs, V.3
  • 94
    • 63449123063 scopus 로고    scopus 로고
    • Peripheral mechanisms of pain and analgesia
    • doi: 10.1016/j.brainresrev.2008.12.017
    • Stein, C., Clark, J. D., Oh, U., Vasko, M. R., Wilcox, G. L., Overland, A. C., et al. (2009). Peripheral mechanisms of pain and analgesia. Brain Res. Rev. 60, 90-113. doi: 10.1016/j.brainresrev.2008.12.017.
    • (2009) Brain Res. Rev. , vol.60 , pp. 90-113
    • Stein, C.1    Clark, J.D.2    Oh, U.3    Vasko, M.R.4    Wilcox, G.L.5    Overland, A.C.6
  • 95
    • 0032721391 scopus 로고    scopus 로고
    • Novel natural vanilloid receptor agonists: new therapeutic targets for drug development
    • doi: 10.1016/S0165-6147(99)01393-0
    • Sterner, O., and Szallasi, A. (1999). Novel natural vanilloid receptor agonists: new therapeutic targets for drug development. Trends Pharmacol. Sci. 20, 459-465. doi: 10.1016/S0165-6147(99)01393-0.
    • (1999) Trends Pharmacol. Sci. , vol.20 , pp. 459-465
    • Sterner, O.1    Szallasi, A.2
  • 96
    • 0345616438 scopus 로고    scopus 로고
    • ANKTM1, a TRP-like channel expressed in nociceptive neurons, is activated by cold temperatures
    • doi: 10.1016/S0092-8674(03)00158-2
    • Story, G. M., Peier, A. M., Reeve, A. J., Eid, S. R., Mosbacher, J., Hricik, T. R., et al. (2003). ANKTM1, a TRP-like channel expressed in nociceptive neurons, is activated by cold temperatures. Cell 112, 819-829. doi: 10.1016/S0092-8674(03)00158-2.
    • (2003) Cell , vol.112 , pp. 819-829
    • Story, G.M.1    Peier, A.M.2    Reeve, A.J.3    Eid, S.R.4    Mosbacher, J.5    Hricik, T.R.6
  • 97
    • 84886001653 scopus 로고    scopus 로고
    • Flavanones that selectively inhibit TRPM3 attenuate thermal nociception in vivo
    • doi: 10.1124/mol.113.086843
    • Straub, I., Krügel, U., Mohr, F., Teichert, J., Rizun, O., Konrad, M., et al. (2013). Flavanones that selectively inhibit TRPM3 attenuate thermal nociception in vivo. Mol. Pharmacol. 84, 736-750. doi: 10.1124/mol.113.086843.
    • (2013) Mol. Pharmacol. , vol.84 , pp. 736-750
    • Straub, I.1    Krügel, U.2    Mohr, F.3    Teichert, J.4    Rizun, O.5    Konrad, M.6
  • 98
    • 24744433102 scopus 로고    scopus 로고
    • Novel potent antagonists of transient receptor potential channel, vanilloid subfamily member 1: structure-activity relationship of 1,3-diarylalkyl thioureas possessing new vanilloid equivalents
    • doi: 10.1021/jm0502790
    • Suh, Y.-G., Lee, Y.-S., Min, K.-H., Park, O.-H., Kim, J.-K., Seung, H.-S., et al. (2005). Novel potent antagonists of transient receptor potential channel, vanilloid subfamily member 1: structure-activity relationship of 1,3-diarylalkyl thioureas possessing new vanilloid equivalents. J. Med. Chem. 48, 5823-5836. doi: 10.1021/jm0502790.
    • (2005) J. Med. Chem. , vol.48 , pp. 5823-5836
    • Suh, Y.-G.1    Lee, Y.-S.2    Min, K.-H.3    Park, O.-H.4    Kim, J.-K.5    Seung, H.-S.6
  • 99
    • 34447515681 scopus 로고    scopus 로고
    • Contribution of the putative inner-pore region to the gating of the transient receptor potential vanilloid subtype 1 channel (TRPV1)
    • doi: 10.1523/JNEUROSCI.1956-07.2007
    • Susankova, K., Ettrich, R., Vyklicky, L., Teisinger, J., and Vlachova, V. (2007). Contribution of the putative inner-pore region to the gating of the transient receptor potential vanilloid subtype 1 channel (TRPV1). J. Neurosci. 27, 7578-7585. doi: 10.1523/JNEUROSCI.1956-07.2007.
    • (2007) J. Neurosci. , vol.27 , pp. 7578-7585
    • Susankova, K.1    Ettrich, R.2    Vyklicky, L.3    Teisinger, J.4    Vlachova, V.5
  • 100
    • 0032970173 scopus 로고    scopus 로고
    • Vanilloid (Capsaicin) receptors and mechanisms
    • Szallasi, A., and Blumberg, P. M. (1999). Vanilloid (Capsaicin) receptors and mechanisms. Pharmacol. Rev. 51, 159-212.
    • (1999) Pharmacol. Rev. , vol.51 , pp. 159-212
    • Szallasi, A.1    Blumberg, P.M.2
  • 101
    • 84870063505 scopus 로고    scopus 로고
    • 1,8-cineole, a TRPM8 agonist, is a novel natural antagonist of human TRPA1
    • doi: 10.1186/1744-8069-8-86
    • Takaishi, M., Fujita, F., Uchida, K., Yamamoto, S.Sawa da Shimizu, M., Hatai Uotsu, C., et al. (2012). 1,8-cineole, a TRPM8 agonist, is a novel natural antagonist of human TRPA1. Mol. Pain 8:86. doi: 10.1186/1744-8069-8-86.
    • (2012) Mol. Pain , vol.8 , pp. 86
    • Takaishi, M.1    Fujita, F.2    Uchida, K.3    Yamamoto, S.4    Sawa da Shimizu, M.5    Hatai Uotsu, C.6
  • 102
    • 38549092780 scopus 로고    scopus 로고
    • Prostaglandin-induced activation of nociceptive neurons via direct interaction with transient receptor potential A1 (TRPA1)
    • doi: 10.1124/mol.107.040832
    • Taylor-Clark, T. E., Undem, B. J., Macglashan, D. W. Jr., Ghatta, S., Carr, M. J., and McAlexander, M. A. (2008). Prostaglandin-induced activation of nociceptive neurons via direct interaction with transient receptor potential A1 (TRPA1). Mol. Pharmacol. 73, 274-281. doi: 10.1124/mol.107.040832.
    • (2008) Mol. Pharmacol. , vol.73 , pp. 274-281
    • Taylor-Clark, T.E.1    Undem, B.J.2    Macglashan Jr., D.W.3    Ghatta, S.4    Carr, M.J.5    McAlexander, M.A.6
  • 103
    • 0032169804 scopus 로고    scopus 로고
    • The cloned capsaicin receptor integrates multiple pain-producing stimuli
    • doi: 10.1016/S0896-6273(00)80564-4
    • Tominaga, M., Caterina, M. J., Malmberg, A. B., Rosen, T. A., Gilbert, H., Skinner, K., et al. (1998). The cloned capsaicin receptor integrates multiple pain-producing stimuli. Neuron 21, 531-543. doi: 10.1016/S0896-6273(00)80564-4.
    • (1998) Neuron , vol.21 , pp. 531-543
    • Tominaga, M.1    Caterina, M.J.2    Malmberg, A.B.3    Rosen, T.A.4    Gilbert, H.5    Skinner, K.6
  • 104
    • 79953218015 scopus 로고    scopus 로고
    • Localization of the PIP2 Sensor of TRPV1 Ion Channels
    • doi: 10.1074/jbc.M110.192526
    • Ufret-Vincenty, C. A., Klein, R. M., Hua, L., Angueyra, J., and Gordon, S. E. (2011). Localization of the PIP2 Sensor of TRPV1 Ion Channels. J. Biol. Chem. 286, 9688-9698. doi: 10.1074/jbc.M110.192526.
    • (2011) J. Biol. Chem. , vol.286 , pp. 9688-9698
    • Ufret-Vincenty, C.A.1    Klein, R.M.2    Hua, L.3    Angueyra, J.4    Gordon, S.E.5
  • 105
    • 51349083674 scopus 로고    scopus 로고
    • Identification of molecular determinants of channel gating in the transient receptor potential box of vanilloid receptor I
    • doi: 10.1096/fj.08-107425
    • Valente, P., García-Sanz, N., Gomis, A., Fernández-Carvajal, A., Fernández-Ballester, G., Viana, F., et al. (2008). Identification of molecular determinants of channel gating in the transient receptor potential box of vanilloid receptor I. FASEB J. 22, 3298-3309. doi: 10.1096/fj.08-107425.
    • (2008) FASEB J. , vol.22 , pp. 3298-3309
    • Valente, P.1    García-Sanz, N.2    Gomis, A.3    Fernández-Carvajal, A.4    Fernández-Ballester, G.5    Viana, F.6
  • 106
    • 78149431236 scopus 로고    scopus 로고
    • Near-membrane dynamics and capture of TRPM8 channels within transient confinement domains
    • e13290. doi: 10.1371/journal.pone.0013290
    • Veliz, L. A., Toro, C. A., Vivar, J. P., Arias, L. A., Villegas, J., Castro, M. A., et al. (2010). Near-membrane dynamics and capture of TRPM8 channels within transient confinement domains. PLoS ONE 5:e13290. doi: 10.1371/journal.pone.0013290.
    • (2010) PLoS ONE , vol.5
    • Veliz, L.A.1    Toro, C.A.2    Vivar, J.P.3    Arias, L.A.4    Villegas, J.5    Castro, M.A.6
  • 107
    • 33847050898 scopus 로고    scopus 로고
    • TRPM8 voltage sensor mutants reveal a mechanism for integrating thermal and chemical stimuli
    • doi: 10.1038/nchembio862
    • Voets, T., Owsianik, G., Janssens, A., Talavera, K., and Nilius, B. (2007). TRPM8 voltage sensor mutants reveal a mechanism for integrating thermal and chemical stimuli. Nat. Chem. Biol. 3, 174-182. doi: 10.1038/nchembio862.
    • (2007) Nat. Chem. Biol. , vol.3 , pp. 174-182
    • Voets, T.1    Owsianik, G.2    Janssens, A.3    Talavera, K.4    Nilius, B.5
  • 108
    • 24644439900 scopus 로고    scopus 로고
    • Sensing with TRP channels
    • doi: 10.1038/nchembio0705-85
    • Voets, T., Talavera, K., Owsianik, G., and Nilius, B. (2005). Sensing with TRP channels. Nat. Chem. Biol. 1, 85-92. doi: 10.1038/nchembio0705-85.
    • (2005) Nat. Chem. Biol. , vol.1 , pp. 85-92
    • Voets, T.1    Talavera, K.2    Owsianik, G.3    Nilius, B.4
  • 110
    • 41949096621 scopus 로고    scopus 로고
    • Herbal compounds and toxins modulating TRP channels
    • doi: 10.2174/157015908783769644
    • Vriens, J., Nilius, B., and Vennekens, R. (2008). Herbal compounds and toxins modulating TRP channels. Curr. Neuropharmacol. 6, 79-96. doi: 10.2174/157015908783769644.
    • (2008) Curr. Neuropharmacol. , vol.6 , pp. 79-96
    • Vriens, J.1    Nilius, B.2    Vennekens, R.3
  • 111
    • 0029898994 scopus 로고    scopus 로고
    • Similarities and differences in the structure-activity relationships of capsaicin and resiniferatoxin analogues
    • doi: 10.1021/jm960139d
    • Walpole, C. S., Bevan, S., Bloomfield, G., Breckenridge, R., James, I. F., Ritchie, T., et al. (1996). Similarities and differences in the structure-activity relationships of capsaicin and resiniferatoxin analogues. J. Med. Chem. 39, 2939-2952. doi: 10.1021/jm960139d.
    • (1996) J. Med. Chem. , vol.39 , pp. 2939-2952
    • Walpole, C.S.1    Bevan, S.2    Bloomfield, G.3    Breckenridge, R.4    James, I.F.5    Ritchie, T.6
  • 112
    • 0027296078 scopus 로고
    • Analogues of capsaicin with agonist activity as novel analgesic agents; structure-activity studies. 2. The amide bond "B-region"
    • doi: 10.1021/jm00068a015
    • Walpole, C. S., Wrigglesworth, R., Bevan, S., Campbell, E. A., Dray, A., James, I. F., et al. (1993a). Analogues of capsaicin with agonist activity as novel analgesic agents; structure-activity studies. 2. The amide bond "B-region." J. Med. Chem. 36, 2373-2380. doi: 10.1021/jm00068a015.
    • (1993) J. Med. Chem. , vol.36 , pp. 2373-2380
    • Walpole, C.S.1    Wrigglesworth, R.2    Bevan, S.3    Campbell, E.A.4    Dray, A.5    James, I.F.6
  • 113
    • 0027270897 scopus 로고
    • Analogues of capsaicin with agonist activity as novel analgesic agents; structure-activity studies. 3. The hydrophobic side-chain "C-region"
    • doi: 10.1021/jm00068a016
    • Walpole, C. S., Wrigglesworth, R., Bevan, S., Campbell, E. A., Dray, A., James, I. F., et al. (1993b). Analogues of capsaicin with agonist activity as novel analgesic agents; structure-activity studies. 3. The hydrophobic side-chain "C-region." J. Med. Chem. 36, 2381-2389. doi: 10.1021/jm00068a016.
    • (1993) J. Med. Chem. , vol.36 , pp. 2381-2389
    • Walpole, C.S.1    Wrigglesworth, R.2    Bevan, S.3    Campbell, E.A.4    Dray, A.5    James, I.F.6
  • 114
    • 0027291395 scopus 로고
    • Analogues of capsaicin with agonist activity as novel analgesic agents; structure-activity studies. 1. The aromatic "A-region"
    • doi: 10.1021/jm00068a014
    • Walpole, C. S., Wrigglesworth, R., Bevan, S., Campbell, E. A., Dray, A., James, I. F., et al. (1993c). Analogues of capsaicin with agonist activity as novel analgesic agents; structure-activity studies. 1. The aromatic "A-region." J. Med. Chem. 36, 2362-2372. doi: 10.1021/jm00068a014.
    • (1993) J. Med. Chem. , vol.36 , pp. 2362-2372
    • Walpole, C.S.1    Wrigglesworth, R.2    Bevan, S.3    Campbell, E.A.4    Dray, A.5    James, I.F.6
  • 116
    • 80053485088 scopus 로고    scopus 로고
    • + channel and gating regulation by G proteins, PIP2, and sodium
    • doi: 10.1016/j.cell.2011.07.046
    • + channel and gating regulation by G proteins, PIP2, and sodium. Cell 147, 199-208. doi: 10.1016/j.cell.2011.07.046.
    • (2011) Cell , vol.147 , pp. 199-208
    • Whorton, M.R.1    MacKinnon, R.2
  • 117
    • 82655181351 scopus 로고    scopus 로고
    • Menthol attenuates respiratory irritation responses to multiple cigarette smoke irritants
    • doi: 10.1096/fj.11-188383
    • Willis, D. N., Liu, B., Ha, M. A., Jordt, S.-E., and Morris, J. B. (2011). Menthol attenuates respiratory irritation responses to multiple cigarette smoke irritants. FASEB J. 25, 4434-4444. doi: 10.1096/fj.11-188383.
    • (2011) FASEB J. , vol.25 , pp. 4434-4444
    • Willis, D.N.1    Liu, B.2    Ha, M.A.3    Jordt, S.-E.4    Morris, J.B.5
  • 118
    • 84879075593 scopus 로고    scopus 로고
    • Functionally important amino acid residues in the transient receptor potential vanilloid 1 (TRPV1) ion channel-an overview of the current mutational data
    • doi: 10.1186/1744-8069-9-30
    • Winter, Z., Buhala, A., Ötvös, F., Jósvay, K., Vizler, C., Dombi, G., et al. (2013). Functionally important amino acid residues in the transient receptor potential vanilloid 1 (TRPV1) ion channel-an overview of the current mutational data. Mol. Pain 9, 30. doi: 10.1186/1744-8069-9-30.
    • (2013) Mol. Pain , vol.9 , pp. 30
    • Winter, Z.1    Buhala, A.2    Ötvös, F.3    Jósvay, K.4    Vizler, C.5    Dombi, G.6
  • 119
    • 55749087512 scopus 로고    scopus 로고
    • Identification of transmembrane domain 5 as a critical molecular determinant of menthol sensitivity in mammalian TRPA1 channels
    • doi: 10.1523/JNEUROSCI.2772-08.2008
    • Xiao, B., Dubin, A. E., Bursulaya, B., Viswanath, V., Jegla, T. J., and Patapoutian, A. (2008). Identification of transmembrane domain 5 as a critical molecular determinant of menthol sensitivity in mammalian TRPA1 channels. J. Neurosci. 28, 9640-9651. doi: 10.1523/JNEUROSCI.2772-08.2008.
    • (2008) J. Neurosci. , vol.28 , pp. 9640-9651
    • Xiao, B.1    Dubin, A.E.2    Bursulaya, B.3    Viswanath, V.4    Jegla, T.J.5    Patapoutian, A.6
  • 120
    • 79960580198 scopus 로고    scopus 로고
    • Modular thermal sensors in temperature-gated transient receptor potential (TRP) channels
    • doi: 10.1073/pnas.1105196108
    • Yao, J., Liu, B., and Qin, F. (2011). Modular thermal sensors in temperature-gated transient receptor potential (TRP) channels. Proc. Natl. Acad. Sci. U.S.A. 108, 11109-11114. doi: 10.1073/pnas.1105196108.
    • (2011) Proc. Natl. Acad. Sci. U.S.A. , vol.108 , pp. 11109-11114
    • Yao, J.1    Liu, B.2    Qin, F.3
  • 121
    • 0141831003 scopus 로고    scopus 로고
    • Structural basis for modulation and agonist specificity of HCN pacemaker channels
    • doi: 10.1038/nature01922
    • Zagotta, W. N., Olivier, N. B., Black, K. D., Young, E. C., Olson, R., and Gouaux, E. (2003). Structural basis for modulation and agonist specificity of HCN pacemaker channels. Nature 425, 200-205. doi: 10.1038/nature01922.
    • (2003) Nature , vol.425 , pp. 200-205
    • Zagotta, W.N.1    Olivier, N.B.2    Black, K.D.3    Young, E.C.4    Olson, R.5    Gouaux, E.6
  • 122
    • 0028800096 scopus 로고
    • Molecular cloning of a widely expressed human homologue for the Drosophila trp gene
    • doi: 10.1016/0014-5793(95)01038-G
    • Zhu, X., Chu, P. B., Peyton, M., and Birnbaumer, L. (1995). Molecular cloning of a widely expressed human homologue for the Drosophila trp gene. FEBS Lett. 373, 193-198. doi: 10.1016/0014-5793(95)01038-G.
    • (1995) FEBS Lett. , vol.373 , pp. 193-198
    • Zhu, X.1    Chu, P.B.2    Peyton, M.3    Birnbaumer, L.4
  • 123
    • 81055141456 scopus 로고    scopus 로고
    • Transient receptor potential cation channel, subfamily C, member 5 (TRPC5) is a cold-transducer in the peripheral nervous system
    • doi: 10.1073/pnas.1115387108
    • Zimmermann, K., Lennerz, J. K., Hein, A., Link, A. S., Kaczmarek, J. S., Delling, M., et al. (2011). Transient receptor potential cation channel, subfamily C, member 5 (TRPC5) is a cold-transducer in the peripheral nervous system. Proc. Natl. Acad. Sci. U.S.A. 108, 18114-18119. doi: 10.1073/pnas.1115387108.
    • (2011) Proc. Natl. Acad. Sci. U.S.A. , vol.108 , pp. 18114-18119
    • Zimmermann, K.1    Lennerz, J.K.2    Hein, A.3    Link, A.S.4    Kaczmarek, J.S.5    Delling, M.6


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