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Volumn 504, Issue 7478, 2013, Pages 113-118

TRPV1 structures in distinct conformations reveal activation mechanisms

Author keywords

[No Author keywords available]

Indexed keywords

VANILLOID RECEPTOR 1;

EID: 84889594608     PISSN: 00280836     EISSN: 14764687     Source Type: Journal    
DOI: 10.1038/nature12823     Document Type: Article
Times cited : (837)

References (56)
  • 1
    • 70349845440 scopus 로고    scopus 로고
    • Cellular and molecular mechanisms of pain
    • Basbaum, A. I., Bautista, D. M., Scherrer, G. & Julius, D. Cellular and molecular mechanisms of pain. Cell 139, 267-284 (2009).
    • (2009) Cell , vol.139 , pp. 267-284
    • Basbaum, A.I.1    Bautista, D.M.2    Scherrer, G.3    Julius, D.4
  • 2
    • 84866519244 scopus 로고    scopus 로고
    • Structural plasticity and dynamic selectivity of acid-sensing ion channel-spider toxin complexes
    • Baconguis, I. & Gouaux, E. Structural plasticity and dynamic selectivity of acid-sensing ion channel-spider toxin complexes. Nature 489, 400-405 (2012).
    • (2012) Nature , vol.489 , pp. 400-405
    • Baconguis, I.1    Gouaux, E.2
  • 3
    • 80053131218 scopus 로고    scopus 로고
    • Structural basis of PIP2 activation of the classical inward rectifier K1 channel Kir2. 2
    • Hansen, S. B., Tao, X. & MacKinnon, R. Structural basis of PIP2 activation of the classical inward rectifier K1 channel Kir2.2. Nature 477, 495-498 (2011).
    • (2011) Nature , vol.477 , pp. 495-498
    • Hansen, S.B.1    Tao, X.2    Mackinnon, R.3
  • 4
    • 84860785529 scopus 로고    scopus 로고
    • Molecular mechanism of ATP binding and ion channel activation in P2X receptors
    • Hattori, M. & Gouaux, E. Molecular mechanism of ATP binding and ion channel activation in P2X receptors. Nature 485, 207-212 (2012).
    • (2012) Nature , vol.485 , pp. 207-212
    • Hattori, M.1    Gouaux, E.2
  • 5
    • 84878996278 scopus 로고    scopus 로고
    • X-ray structure of the mammalian GIRK2-bc G-protein complex
    • Whorton, M. R. & MacKinnon, R. X-ray structure of the mammalian GIRK2-bc G-protein complex. Nature 498, 190-197 (2013).
    • (2013) Nature , vol.498 , pp. 190-197
    • Whorton, M.R.1    Mackinnon, R.2
  • 6
    • 84861737800 scopus 로고    scopus 로고
    • Receptor-targeting mechanisms of pain-causing toxins: How ow?
    • Bohlen, C. J. & Julius, D. Receptor-targeting mechanisms of pain-causing toxins: how ow? Toxicon 60, 254-264 (2012).
    • (2012) Toxicon , vol.60 , pp. 254-264
    • Bohlen, C.J.1    Julius, D.2
  • 7
    • 66849104240 scopus 로고    scopus 로고
    • Pharmacology of vanilloid transient receptor potential cation channels
    • Vriens, J., Appendino, G. & Nilius, B. Pharmacology of vanilloid transient receptor potential cation channels. Mol. Pharmacol. 75, 1262-1279 (2009).
    • (2009) Mol. Pharmacol. , vol.75 , pp. 1262-1279
    • Vriens, J.1    Appendino, G.2    Nilius, B.3
  • 8
    • 84889588341 scopus 로고    scopus 로고
    • Structure of the TRPV1 ion channel determined by electron cryo-microscopy
    • this issue
    • Liao, M., Cao, E., Julius, D. & Cheng, Y. Structure of the TRPV1 ion channel determined by electron cryo-microscopy. Nature http://dx.doi.org/10. 1038/nature12823 (this issue).
    • Nature
    • Liao, M.1    Cao, E.2    Julius, D.3    Cheng, Y.4
  • 9
    • 77956996917 scopus 로고    scopus 로고
    • Ion channel voltage sensors: Structure, function, and pathophysiology
    • Catterall, W. A. Ion channel voltage sensors: structure, function, and pathophysiology. Neuron 67, 915-928 (2010).
    • (2010) Neuron , vol.67 , pp. 915-928
    • Catterall, W.A.1
  • 10
    • 23244441222 scopus 로고    scopus 로고
    • Voltage sensor of Kv1. 2: Structural basis of electromechanical coupling
    • Long, S. B., Campbell, E. B. & Mackinnon, R. Voltage sensor of Kv1.2: structural basis of electromechanical coupling. Science 309, 903-908 (2005).
    • (2005) Science , vol.309 , pp. 903-908
    • Long, S.B.1    Campbell, E.B.2    Mackinnon, R.3
  • 11
    • 57749196006 scopus 로고    scopus 로고
    • Sensing voltage across lipid membranes
    • Swartz, K. J. Sensing voltage across lipid membranes. Nature 456, 891-897 (2008).
    • (2008) Nature , vol.456 , pp. 891-897
    • Swartz, K.J.1
  • 12
    • 0141706802 scopus 로고    scopus 로고
    • Evolutionary origin of inhibitor cystine knot peptides
    • Zhu, S., Darbon, H., Dyason, K., Verdonck, F. & Tytgat, J. Evolutionary origin of inhibitor cystine knot peptides. FASEB J. 17, 1765-1767 (2003).
    • (2003) FASEB J. , vol.17 , pp. 1765-1767
    • Zhu, S.1    Darbon, H.2    Dyason, K.3    Verdonck, F.4    Tytgat, J.5
  • 13
    • 23844463536 scopus 로고    scopus 로고
    • Voltage-sensor activation with a tarantula toxin as cargo
    • Phillips, L. R. et al. Voltage-sensor activation with a tarantula toxin as cargo. Nature 436, 857-860 (2005).
    • (2005) Nature , vol.436 , pp. 857-860
    • Phillips, L.R.1
  • 14
    • 0030952979 scopus 로고    scopus 로고
    • Hanatoxin modifies the gating of a voltagedependent K1 channel through multiple binding sites
    • Swartz, K. J. & MacKinnon, R. Hanatoxin modifies the gating of a voltagedependent K1 channel through multiple binding sites. Neuron 18, 665-673 (1997).
    • (1997) Neuron , vol.18 , pp. 665-673
    • Swartz, K.J.1    Mackinnon, R.2
  • 15
    • 77953271751 scopus 로고    scopus 로고
    • A bivalent tarantula toxin activates the capsaicin receptor, TRPV1, by targeting the outer pore domain
    • Bohlen, C. J. et al. A bivalent tarantula toxin activates the capsaicin receptor, TRPV1, by targeting the outer pore domain. Cell 141, 834-845 (2010).
    • (2010) Cell , vol.141 , pp. 834-845
    • Bohlen, C.J.1
  • 16
    • 33750873334 scopus 로고    scopus 로고
    • Spider toxins activate the capsaicin receptor to produce inflammatory pain
    • Siemens, J. et al. Spider toxins activate the capsaicin receptor to produce inflammatory pain. Nature 444, 208-212 (2006).
    • (2006) Nature , vol.444 , pp. 208-212
    • Siemens, J.1
  • 17
    • 77952886805 scopus 로고    scopus 로고
    • Temperature-induced opening of TRPV1 ion channel is stabilized by the pore domain
    • Grandl, J. et al. Temperature-induced opening of TRPV1 ion channel is stabilized by the pore domain. Nature Neurosci. 13, 708-714 (2010).
    • (2010) Nature Neurosci. , vol.13 , pp. 708-714
    • Grandl, J.1
  • 18
    • 42949117400 scopus 로고    scopus 로고
    • A yeast genetic screen reveals a critical role for the pore helix domain in TRP channel gating
    • Myers, B. R., Bohlen, C. J.&Julius, D. A yeast genetic screen reveals a critical role for the pore helix domain in TRP channel gating. Neuron 58, 362-373 (2008).
    • (2008) Neuron , vol.58 , pp. 362-373
    • Myers, B.R.1    Bohlen, C.J.2    Julius, D.3
  • 19
    • 77951035804 scopus 로고    scopus 로고
    • Thermosensitive TRP channel pore turret is part of the temperature activation pathway
    • Yang, F., Cui, Y., Wang, K. & Zheng, J. Thermosensitive TRP channel pore turret is part of the temperature activation pathway. Proc. Natl Acad. Sci. USA 107, 7083-7088 (2010).
    • (2010) Proc. Natl Acad. Sci. USA , vol.107 , pp. 7083-7088
    • Yang, F.1    Cui, Y.2    Wang, K.3    Zheng, J.4
  • 20
    • 0035499892 scopus 로고    scopus 로고
    • Chemistry of ion coordination and hydration revealed by a K1 channel-Fab complex at 2. 0A? Resolution
    • Zhou, Y., Morais-Cabral, J. H., Kaufman, A. & MacKinnon, R. Chemistry of ion coordination and hydration revealed by a K1 channel-Fab complex at 2.0A? resolution. Nature 414, 43-48 (2001).
    • (2001) Nature , vol.414 , pp. 43-48
    • Zhou, Y.1    Morais-Cabral, J.H.2    Kaufman, A.3    Mackinnon, R.4
  • 21
    • 84866078359 scopus 로고    scopus 로고
    • Prevention of overfitting in cryo-EM structure determination
    • Scheres, S. H. & Chen, S. Prevention of overfitting in cryo-EM structure determination. Nature Methods 9, 853-854 (2012).
    • (2012) Nature Methods , vol.9 , pp. 853-854
    • Scheres, S.H.1    Chen, S.2
  • 22
    • 1542267774 scopus 로고    scopus 로고
    • Resiniferatoxin binds to the capsaicin receptor (TRPV1) near the extracellular side of the S4 transmembrane domain
    • Chou, M. Z., Mtui, T., Gao, Y. D., Kohler, M. & Middleton, R. E. Resiniferatoxin binds to the capsaicin receptor (TRPV1) near the extracellular side of the S4 transmembrane domain. Biochemistry 43, 2501-2511 (2004).
    • (2004) Biochemistry , vol.43 , pp. 2501-2511
    • Chou, M.Z.1    Mtui, T.2    Gao, Y.D.3    Kohler, M.4    Middleton, R.E.5
  • 23
    • 2442498381 scopus 로고    scopus 로고
    • Molecular determinants of vanilloid sensitivity in TRPV1
    • Gavva, N. R. et al. Molecular determinants of vanilloid sensitivity in TRPV1. J. Biol. Chem. 279, 20283-20295 (2004).
    • (2004) J. Biol. Chem. , vol.279 , pp. 20283-20295
    • Gavva, N.R.1
  • 24
    • 0036183319 scopus 로고    scopus 로고
    • Molecular basis for species-specific sensitivity to ''hot'' chili peppers
    • Jordt, S. E. & Julius, D. Molecular basis for species-specific sensitivity to ''hot'' chili peppers. Cell 108, 421-430 (2002).
    • (2002) Cell , vol.108 , pp. 421-430
    • Jordt, S.E.1    Julius, D.2
  • 25
    • 2342439775 scopus 로고    scopus 로고
    • Identification of species-specific determinants of the action of the antagonist capsazepine and the agonist PPAHV on TRPV1
    • Phillips, E., Reeve, A., Bevan, S. & McIntyre, P. Identification of species-specific determinants of the action of the antagonist capsazepine and the agonist PPAHV on TRPV1. J. Biol. Chem. 279, 17165-17172 (2004).
    • (2004) J. Biol. Chem. , vol.279 , pp. 17165-17172
    • Phillips, E.1    Reeve, A.2    Bevan, S.3    McIntyre, P.4
  • 26
    • 0032876069 scopus 로고    scopus 로고
    • The cloned rat vanilloid receptor VR1 mediates both R-type binding and C-type calcium response in dorsal root ganglion neurons
    • Szallasi, A., Blumberg, P. M.,Annicelli, L. L., Krause, J. E.&Cortright, D. N.The cloned rat vanilloid receptor VR1 mediates both R-type binding and C-type calcium response in dorsal root ganglion neurons. Mol. Pharmacol. 56, 581-587 (1999).
    • (1999) Mol. Pharmacol. , vol.56 , pp. 581-587
    • Szallasi, A.1    Blumberg, P.M.2    Annicelli, L.L.3    Krause, J.E.4    Cortright, D.N.5
  • 27
    • 42649095142 scopus 로고    scopus 로고
    • TRPV1 shows dynamic ionic selectivity during agonist stimulation
    • Chung, M. K., Guler, A. D. & Caterina, M. J. TRPV1 shows dynamic ionic selectivity during agonist stimulation. Nature Neurosci. 11, 555-564 (2008).
    • (2008) Nature Neurosci. , vol.11 , pp. 555-564
    • Chung, M.K.1    Guler, A.D.2    Caterina, M.J.3
  • 28
    • 0034608878 scopus 로고    scopus 로고
    • Acid potentiation of the capsaicin receptor determined by a key extracellular site
    • Jordt, S. E., Tominaga, M. & Julius, D. Acid potentiation of the capsaicin receptor determined by a key extracellular site. Proc. Natl Acad. Sci. USA 97, 8134-8139 (2000).
    • (2000) Proc. Natl Acad. Sci. USA , vol.97 , pp. 8134-8139
    • Jordt, S.E.1    Tominaga, M.2    Julius, D.3
  • 29
    • 84875455117 scopus 로고    scopus 로고
    • Single residues in the outer pore of TRPV1 and TRPV3 have temperature-dependent conformations
    • Kim, S. E., Patapoutian, A. & Grandl, J. Single residues in the outer pore of TRPV1 and TRPV3 have temperature-dependent conformations. PLoS ONE 8, e59593 (2013).
    • (2013) PLoS ONE , vol.8
    • Kim, S.E.1    Patapoutian, A.2    Grandl, J.3
  • 30
    • 36348944117 scopus 로고    scopus 로고
    • Uncoupling proton activation of vanilloid receptor TRPV1
    • Ryu, S., Liu, B., Yao, J., Fu, Q. & Qin, F. Uncoupling proton activation of vanilloid receptor TRPV1. J. Neurosci. 27, 12797-12807 (2007).
    • (2007) J. Neurosci. , vol.27 , pp. 12797-12807
    • Ryu, S.1    Liu, B.2    Yao, J.3    Fu, Q.4    Qin, F.5
  • 31
    • 25144442315 scopus 로고    scopus 로고
    • Conformational changes of pore helix coupled to gating of TRPV5 by protons
    • Yeh, B. I., Kim, Y. K., Jabbar, W.& Huang, C. L. Conformational changes of pore helix coupled to gating of TRPV5 by protons. EMBO J. 24, 3224-3234 (2005).
    • (2005) EMBO J. , vol.24 , pp. 3224-3234
    • Yeh, B.I.1    Kim, Y.K.2    Jabbar, W.3    Huang, C.L.4
  • 32
    • 17044400911 scopus 로고    scopus 로고
    • A gate in the selectivity filter of potassium channels
    • Bernèche, S. & Roux, B. A gate in the selectivity filter of potassium channels. Structure 13, 591-600 (2005).
    • (2005) Structure , vol.13 , pp. 591-600
    • Bernèche, S.1    Roux, B.2
  • 33
    • 77954485089 scopus 로고    scopus 로고
    • Structural mechanism of C-type inactivation in K1 channels
    • Cuello, L. G., Jogini, V., Cortes, D. M. & Perozo, E. Structural mechanism of C-type inactivation in K1 channels. Nature 466, 203-208 (2010).
    • (2010) Nature , vol.466 , pp. 203-208
    • Cuello, L.G.1    Jogini, V.2    Cortes, D.M.3    Perozo, E.4
  • 34
    • 84874678833 scopus 로고    scopus 로고
    • C-type inactivation of voltage-gated K1 channels: Pore constriction or dilation?
    • Hoshi, T.&Armstrong, C. M. C-type inactivation of voltage-gated K1 channels: pore constriction or dilation? J. Gen. Physiol. 141, 151-160 (2013).
    • (2013) J. Gen. Physiol. , vol.141 , pp. 151-160
    • Hoshi, T.1    Armstrong, C.M.2
  • 35
    • 0037547117 scopus 로고    scopus 로고
    • Capsaicin activation of the pain receptor, VR1: Multiple open states from both partial and full binding
    • Hui, K., Liu, B. & Qin, F. Capsaicin activation of the pain receptor, VR1: multiple open states from both partial and full binding. Biophys. J. 84, 2957-2968 (2003).
    • (2003) Biophys. J. , vol.84 , pp. 2957-2968
    • Hui, K.1    Liu, B.2    Qin, F.3
  • 36
    • 0242385383 scopus 로고    scopus 로고
    • Thermodynamics of heat activation of single capsaicin ion channels VR1
    • Liu, B., Hui, K. & Qin, F. Thermodynamics of heat activation of single capsaicin ion channels VR1. Biophys. J. 85, 2988-3006 (2003).
    • (2003) Biophys. J. , vol.85 , pp. 2988-3006
    • Liu, B.1    Hui, K.2    Qin, F.3
  • 37
    • 0032169804 scopus 로고    scopus 로고
    • The cloned capsaicin receptor integrates multiple pain-producing stimuli
    • Tominaga, M. et al. The cloned capsaicin receptor integrates multiple pain-producing stimuli. Neuron 21, 531-543 (1998).
    • (1998) Neuron , vol.21 , pp. 531-543
    • Tominaga, M.1
  • 38
    • 0037198625 scopus 로고    scopus 로고
    • The open pore conformation of potassium channels
    • Jiang, Y. et al. The open pore conformation of potassium channels. Nature 417, 523-526 (2002).
    • (2002) Nature , vol.417 , pp. 523-526
    • Jiang, Y.1
  • 39
    • 77449112680 scopus 로고    scopus 로고
    • Structure-functional intimacies of transient receptor potential channels
    • Latorre, R., Zaelzer, C. & Brauchi, S. Structure-functional intimacies of transient receptor potential channels. Q. Rev. Biophys. 42, 201-246 (2009).
    • (2009) Q. Rev. Biophys. , vol.42 , pp. 201-246
    • Latorre, R.1    Zaelzer, C.2    Brauchi, S.3
  • 40
    • 77955006540 scopus 로고    scopus 로고
    • TRPV4-pathy, a novel channelopathy affecting diverse systems
    • Dai, J. et al.TRPV4-pathy, a novel channelopathy affecting diverse systems. J. Hum. Genet. 55, 400-402 (2010).
    • (2010) J. Hum. Genet. , vol.55 , pp. 400-402
    • Dai, J.1
  • 41
    • 84863251177 scopus 로고    scopus 로고
    • Exome sequencing reveals mutations in TRPV3 as a cause of Olmsted syndrome
    • Lin, Z. et al. Exome sequencing reveals mutations in TRPV3 as a cause of Olmsted syndrome. Am. J. Hum. Genet. 90, 558-564 (2012).
    • (2012) Am. J. Hum. Genet. , vol.90 , pp. 558-564
    • Lin, Z.1
  • 43
    • 36649016621 scopus 로고    scopus 로고
    • Voltage is a partial activator of rat thermosensitive TRP channels
    • Matta, J. A. & Ahern, G. P. Voltage is a partial activator of rat thermosensitive TRP channels. J. Physiol. (Lond.) 585, 469-482 (2007).
    • (2007) J. Physiol. (Lond.) , vol.585 , pp. 469-482
    • Matta, J.A.1    Ahern, G.P.2
  • 44
    • 20544455009 scopus 로고    scopus 로고
    • Gating of TRPchannels: A voltage connection? J
    • Nilius, B. et al. Gating of TRPchannels: a voltage connection? J. Physiol. (Lond.) 567, 35-44 (2005).
    • (2005) Physiol. (Lond.) , vol.567 , pp. 35-44
    • Nilius, B.1
  • 45
    • 77953752223 scopus 로고    scopus 로고
    • Forward genetic analysis reveals multiple gating mechanisms of TRPV4
    • Loukin, S., Su, Z., Zhou, X. & Kung, C. Forward genetic analysis reveals multiple gating mechanisms of TRPV4. J. Biol. Chem. 285, 19884-19890 (2010).
    • (2010) J. Biol. Chem. , vol.285 , pp. 19884-19890
    • Loukin, S.1    Su, Z.2    Zhou, X.3    Kung, C.4
  • 46
    • 84874229704 scopus 로고    scopus 로고
    • TRPV1 channels are intrinsically heat sensitive and negatively regulated by phosphoinositide lipids
    • Cao, E., Cordero-Morales, J. F., Liu, B., Qin, F. & Julius, D. TRPV1 channels are intrinsically heat sensitive and negatively regulated by phosphoinositide lipids. Neuron 77, 667-679 (2013).
    • (2013) Neuron , vol.77 , pp. 667-679
    • Cao, E.1    Cordero-Morales, J.F.2    Liu, B.3    Qin, F.4    Julius, D.5
  • 47
    • 2442636258 scopus 로고    scopus 로고
    • Endovanilloids. Putative endogenous ligands of transient receptor potential vanilloid 1 channels
    • van der Stelt, M. & Di Marzo, V. Endovanilloids. Putative endogenous ligands of transient receptor potential vanilloid 1 channels. Eur. J. Biochem. 271, 1827-1834 (2004).
    • (2004) Eur. J. Biochem. , vol.271 , pp. 1827-1834
    • Van Der Stelt, M.1    Di Marzo, V.2
  • 48
    • 33646899582 scopus 로고    scopus 로고
    • A hot-sensing cold receptor: C-terminal domain determines thermosensation in transient receptor potential channels
    • Brauchi, S., Orta, G., Salazar, M., Rosenmann, E. & Latorre, R. A hot-sensing cold receptor: C-terminal domain determines thermosensation in transient receptor potential channels. J. Neurosci. 26, 4835-4840 (2006).
    • (2006) J. Neurosci , vol.26 , pp. 4835-4840
    • Brauchi, S.1    Orta, G.2    Salazar, M.3    Rosenmann, E.4    Latorre, R.5
  • 49
    • 80655149458 scopus 로고    scopus 로고
    • The chimeric approach reveals that differences in the TRPV1 pore domain determine species-specific sensitivity to block of heat activation
    • Papakosta, M. et al. The chimeric approach reveals that differences in the TRPV1 pore domain determine species-specific sensitivity to block of heat activation. J. Biol. Chem. 286, 39663-39672 (2011).
    • (2011) J. Biol. Chem. , vol.286 , pp. 39663-39672
    • Papakosta, M.1
  • 50
    • 79960580198 scopus 로고    scopus 로고
    • Modular thermal sensors in temperature-gated transient receptor potential (TRP) channels
    • Yao, J., Liu, B. & Qin, F. Modular thermal sensors in temperature-gated transient receptor potential (TRP) channels. Proc. Natl Acad. Sci. USA 108, 11109-11114 (2011).
    • (2011) Proc. Natl Acad. Sci. USA , vol.108 , pp. 11109-11114
    • Yao, J.1    Liu, B.2    Qin, F.3
  • 51
    • 84868444740 scopus 로고    scopus 로고
    • RELION: Implementation of a Bayesian approach to cryo-EM structure determination
    • Scheres, S. H. RELION: implementation of a Bayesian approach to cryo-EM structure determination. J. Struct. Biol. 180, 519-530 (2012).
    • (2012) J. Struct. Biol. , vol.180 , pp. 519-530
    • Scheres, S.H.1
  • 52
    • 4444221565 scopus 로고    scopus 로고
    • UCSF Chimera- A visualization system for exploratory research and analysis
    • Pettersen, E. F. et al. UCSF Chimera- A visualization system for exploratory research and analysis. J. Comput. Chem. 25, 1605-1612 (2004).
    • (2004) J. Comput. Chem. , vol.25 , pp. 1605-1612
    • Pettersen, E.F.1
  • 53
    • 13244281317 scopus 로고    scopus 로고
    • Coot: Model-building tools for molecular graphics
    • Emsley, P. & Cowtan, K. Coot: model-building tools for molecular graphics. Acta Crystallogr. D 60, 2126-2132 (2004).
    • (2004) Acta Crystallogr. D , vol.60 , pp. 2126-2132
    • Emsley, P.1    Cowtan, K.2
  • 55
    • 0030404988 scopus 로고    scopus 로고
    • HOLE: A program for the analysis of the pore dimensions of ion channel structural models
    • 376
    • Smart, O. S., Neduvelil, J. G., Wang, X., Wallace, B. A. & Sansom, M. S. HOLE: a program for the analysis of the pore dimensions of ion channel structural models. J. Mol. Graph. 14, 354-360,-376 (1996).
    • (1996) J. Mol. Graph. , vol.14 , pp. 354-360
    • Smart, O.S.1    Neduvelil, J.G.2    Wang, X.3    Wallace, B.A.4    Sansom, M.S.5
  • 56
    • 0034737306 scopus 로고    scopus 로고
    • Solution structure of hanatoxin1, a gating modifier of voltage-dependent K1 channels: Common surface features of gating modifier toxins
    • Takahashi, H. et al. Solution structure of hanatoxin1, a gating modifier of voltage-dependent K1 channels: common surface features of gating modifier toxins. J. Mol. Biol. 297, 771-780 (2000).
    • (2000) J. Mol. Biol. , vol.297 , pp. 771-780
    • Takahashi, H.1


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