메뉴 건너뛰기




Volumn 25, Issue 3, 2018, Pages 252-260

Cryo-EM and X-ray structures of TRPV4 reveal insight into ion permeation and gating mechanisms

Author keywords

[No Author keywords available]

Indexed keywords

CATION CHANNEL; VANILLOID RECEPTOR 4; ION; VANILLOID RECEPTOR; XENOPUS PROTEIN;

EID: 85042587034     PISSN: 15459993     EISSN: 15459985     Source Type: Journal    
DOI: 10.1038/s41594-018-0037-5     Document Type: Article
Times cited : (168)

References (85)
  • 1
    • 0347504835 scopus 로고    scopus 로고
    • TRP channels as cellular sensors
    • Clapham, D. E. TRP channels as cellular sensors. Nature 426, 517-524 (2003).
    • (2003) Nature , vol.426 , pp. 517-524
    • Clapham, D.E.1
  • 4
    • 79952683619 scopus 로고    scopus 로고
    • The transient receptor potential family of ion channels
    • Nilius, B. & Owsianik, G. The transient receptor potential family of ion channels. Genome Biol. 12, 218 (2011).
    • (2011) Genome Biol. , vol.12 , pp. 218
    • Nilius, B.1    Owsianik, G.2
  • 7
    • 0345659198 scopus 로고    scopus 로고
    • Abnormal osmotic regulation in trpv4-/-mice
    • Liedtke, W. & Friedman, J. M. Abnormal osmotic regulation in trpv4-/-mice. Proc. Natl Acad. Sci. USA 100, 13698-13703 (2003).
    • (2003) Proc. Natl Acad. Sci. USA , vol.100 , pp. 13698-13703
    • Liedtke, W.1    Friedman, J.M.2
  • 8
    • 0034306198 scopus 로고    scopus 로고
    • OTRPC4 a nonselective cation channel that confers sensitivity to extracellular osmolarity
    • Strotmann, R., Harteneck, C., Nunnenmacher, K., Schultz, G. & Plant, T. D. OTRPC4, a nonselective cation channel that confers sensitivity to extracellular osmolarity. Nat. Cell Biol. 2, 695-702 (2000).
    • (2000) Nat. Cell Biol. , vol.2 , pp. 695-702
    • Strotmann, R.1    Harteneck, C.2    Nunnenmacher, K.3    Schultz, G.4    Plant, T.D.5
  • 9
    • 0034721648 scopus 로고    scopus 로고
    • Vanilloid receptor-related osmotically activated channel (VR-OAC), a candidate vertebrate osmoreceptor
    • Liedtke, W. et al. Vanilloid receptor-related osmotically activated channel (VR-OAC), a candidate vertebrate osmoreceptor. Cell 103, 525-535 (2000).
    • (2000) Cell , vol.103 , pp. 525-535
    • Liedtke, W.1
  • 11
    • 50049122815 scopus 로고    scopus 로고
    • TRPV4-mediated calcium influx regulates terminal differentiation of osteoclasts
    • Masuyama, R. et al. TRPV4-mediated calcium influx regulates terminal differentiation of osteoclasts. Cell Metab. 8, 257-265 (2008).
    • (2008) Cell Metab. , vol.8 , pp. 257-265
    • Masuyama, R.1
  • 12
    • 84860476825 scopus 로고    scopus 로고
    • Elementary Ca2+ signals through endothelial TRPV4 channels regulate vascular function
    • Sonkusare, S. K. et al. Elementary Ca2+ signals through endothelial TRPV4 channels regulate vascular function. Science 336, 597-601 (2012).
    • (2012) Science , vol.336 , pp. 597-601
    • Sonkusare, S.K.1
  • 13
    • 84869101137 scopus 로고    scopus 로고
    • TRPV4 is a regulator of adipose oxidative metabolism, inflammation, and energy homeostasis
    • Ye, L. et al. TRPV4 is a regulator of adipose oxidative metabolism, inflammation, and energy homeostasis. Cell 151, 96-110 (2012).
    • (2012) Cell , vol.151 , pp. 96-110
    • Ye, L.1
  • 14
    • 0041695412 scopus 로고    scopus 로고
    • Hypotonicity induces TRPV4-mediated nociception in rat
    • Alessandri-Haber, N. et al. Hypotonicity induces TRPV4-mediated nociception in rat. Neuron 39, 497-511 (2003).
    • (2003) Neuron , vol.39 , pp. 497-511
    • Alessandri-Haber, N.1
  • 15
    • 2342666609 scopus 로고    scopus 로고
    • Transient receptor potential vanilloid 4 is essential in chemotherapy-induced neuropathic pain in the rat
    • Alessandri-Haber, N. et al. Transient receptor potential vanilloid 4 is essential in chemotherapy-induced neuropathic pain in the rat. J. Neurosci. 24, 4444-4452 (2004).
    • (2004) J. Neurosci. , vol.24 , pp. 4444-4452
    • Alessandri-Haber, N.1
  • 16
    • 0037697228 scopus 로고    scopus 로고
    • Temperature-modulated diversity of TRPV4 channel gating: Activation by physical stresses and phorbol ester derivatives through protein kinase C-dependent and-independent pathways
    • Gao, X., Wu, L. & O'Neil, R. G. Temperature-modulated diversity of TRPV4 channel gating: activation by physical stresses and phorbol ester derivatives through protein kinase C-dependent and-independent pathways. J. Biol. Chem. 278, 27129-27137 (2003).
    • (2003) J. Biol. Chem. , vol.278 , pp. 27129-27137
    • Gao, X.1    Wu, L.2    O'Neil, R.G.3
  • 17
    • 33745952250 scopus 로고    scopus 로고
    • Evidence for a functional role of endothelial transient receptor potential V4 in shear stress-induced vasodilatation
    • Köhler, R. et al. Evidence for a functional role of endothelial transient receptor potential V4 in shear stress-induced vasodilatation. Arterioscler. Thromb. Vasc. Biol. 26, 1495-1502 (2006).
    • (2006) Arterioscler. Thromb. Vasc. Biol. , vol.26 , pp. 1495-1502
    • Köhler, R.1
  • 18
    • 0036703646 scopus 로고    scopus 로고
    • Heat-evoked activation of the ion channel, TRPV4
    • Güler, A. D. et al. Heat-evoked activation of the ion channel, TRPV4. J. Neurosci. 22, 6408-6414 (2002).
    • (2002) J. Neurosci. , vol.22 , pp. 6408-6414
    • Güler, A.D.1
  • 19
    • 0037033077 scopus 로고    scopus 로고
    • Heat-evoked activation of TRPV4 channels in a HEK293 cell expression system and in native mouse aorta endothelial cells
    • Watanabe, H. et al. Heat-evoked activation of TRPV4 channels in a HEK293 cell expression system and in native mouse aorta endothelial cells. J. Biol. Chem. 277, 47044-47051 (2002).
    • (2002) J. Biol. Chem. , vol.277 , pp. 47044-47051
    • Watanabe, H.1
  • 20
    • 0037134482 scopus 로고    scopus 로고
    • Activation of TRPV4 channels (hVRL-2/mTRP12) by phorbol derivatives
    • Watanabe, H. et al. Activation of TRPV4 channels (hVRL-2/mTRP12) by phorbol derivatives. J. Biol. Chem. 277, 13569-13577 (2002).
    • (2002) J. Biol. Chem. , vol.277 , pp. 13569-13577
    • Watanabe, H.1
  • 21
    • 0043267987 scopus 로고    scopus 로고
    • Anandamide and arachidonic acid use epoxyeicosatrienoic acids to activate TRPV4 channels
    • Watanabe, H. et al. Anandamide and arachidonic acid use epoxyeicosatrienoic acids to activate TRPV4 channels. Nature 424, 434-438 (2003).
    • (2003) Nature , vol.424 , pp. 434-438
    • Watanabe, H.1
  • 22
    • 84873413090 scopus 로고    scopus 로고
    • The puzzle of TRPV4 channelopathies
    • Nilius, B. & Voets, T. The puzzle of TRPV4 channelopathies. EMBO Rep. 14, 152-163 (2013).
    • (2013) EMBO Rep. , vol.14 , pp. 152-163
    • Nilius, B.1    Voets, T.2
  • 23
    • 84983788995 scopus 로고    scopus 로고
    • TRPV4: Molecular conductor of a diverse orchestra
    • White, J. P. M. et al. TRPV4: molecular conductor of a diverse orchestra. Physiol. Rev. 96, 911-973 (2016).
    • (2016) Physiol. Rev. , vol.96 , pp. 911-973
    • White, J.P.M.1
  • 24
    • 84889607320 scopus 로고    scopus 로고
    • Structure of the TRPV1 ion channel determined by electron cryo-microscopy
    • Liao, M., Cao, E., Julius, D. & Cheng, Y. Structure of the TRPV1 ion channel determined by electron cryo-microscopy. Nature 504, 107-112 (2013).
    • (2013) Nature , vol.504 , pp. 107-112
    • Liao, M.1    Cao, E.2    Julius, D.3    Cheng, Y.4
  • 25
    • 84889594608 scopus 로고    scopus 로고
    • TRPV1 structures in distinct conformations reveal activation mechanisms
    • Cao, E., Liao, M., Cheng, Y. & Julius, D. TRPV1 structures in distinct conformations reveal activation mechanisms. Nature 504, 113-118 (2013).
    • (2013) Nature , vol.504 , pp. 113-118
    • Cao, E.1    Liao, M.2    Cheng, Y.3    Julius, D.4
  • 26
    • 84969627248 scopus 로고    scopus 로고
    • TRPV1 structures in nanodiscs reveal mechanisms of ligand and lipid action
    • Gao, Y., Cao, E., Julius, D. & Cheng, Y. TRPV1 structures in nanodiscs reveal mechanisms of ligand and lipid action. Nature 534, 347-351 (2016).
    • (2016) Nature , vol.534 , pp. 347-351
    • Gao, Y.1    Cao, E.2    Julius, D.3    Cheng, Y.4
  • 27
    • 84956830463 scopus 로고    scopus 로고
    • Cryo-electron microscopy structure of the TRPV2 ion channel
    • Zubcevic, L. et al. Cryo-electron microscopy structure of the TRPV2 ion channel. Nat. Struct. Mol. Biol. 23, 180-186 (2016).
    • (2016) Nat. Struct. Mol. Biol. , vol.23 , pp. 180-186
    • Zubcevic, L.1
  • 28
    • 84962635518 scopus 로고    scopus 로고
    • Structure of the full-length TRPV2 channel by cryo-EM
    • Huynh, K. W. et al. Structure of the full-length TRPV2 channel by cryo-EM. Nat. Commun. 7, 11130 (2016).
    • (2016) Nat. Commun. , vol.7 , pp. 11130
    • Huynh, K.W.1
  • 29
    • 84975688014 scopus 로고    scopus 로고
    • Crystal structure of the epithelial calcium channel TRPV6
    • Saotome, K., Singh, A. K., Yelshanskaya, M. V. & Sobolevsky, A. I. Crystal structure of the epithelial calcium channel TRPV6. Nature 534, 506-511 (2016).
    • (2016) Nature , vol.534 , pp. 506-511
    • Saotome, K.1    Singh, A.K.2    Yelshanskaya, M.V.3    Sobolevsky, A.I.4
  • 30
    • 85028908980 scopus 로고    scopus 로고
    • Swapping of transmembrane domains in the epithelial calcium channel TRPV6
    • Singh, A. K., Saotome, K. & Sobolevsky, A. I. Swapping of transmembrane domains in the epithelial calcium channel TRPV6. Sci. Rep. 7, 10669 (2017).
    • (2017) Sci. Rep. , vol.7 , pp. 10669
    • Singh, A.K.1    Saotome, K.2    Sobolevsky, A.I.3
  • 31
    • 84981510441 scopus 로고    scopus 로고
    • Structure of the voltage-gated K+ channel Eag1 reveals an alternative voltage sensing mechanism
    • Whicher, J. R. & MacKinnon, R. Structure of the voltage-gated K+ channel Eag1 reveals an alternative voltage sensing mechanism. Science 353, 664-669 (2016).
    • (2016) Science , vol.353 , pp. 664-669
    • Whicher, J.R.1    MacKinnon, R.2
  • 32
    • 85016145318 scopus 로고    scopus 로고
    • Cryo-EM structure of the open high-conductance Ca2+-activated K+ channel
    • Tao, X., Hite, R. K. & MacKinnon, R. Cryo-EM structure of the open high-conductance Ca2+-activated K+ channel. Nature 541, 46-51 (2017).
    • (2017) Nature , vol.541 , pp. 46-51
    • Tao, X.1    Hite, R.K.2    MacKinnon, R.3
  • 33
    • 85009210607 scopus 로고    scopus 로고
    • Structures of the human HCN1 hyperpolarization-activated channel
    • e11
    • Lee, C. H. & MacKinnon, R. Structures of the Human HCN1 Hyperpolarization-Activated Channel. Cell 168, 111-120. e11 (2017).
    • (2017) Cell , vol.168 , pp. 111-120
    • Lee, C.H.1    MacKinnon, R.2
  • 34
    • 84864649745 scopus 로고    scopus 로고
    • Structural and biochemical consequences of disease-causing mutations in the ankyrin repeat domain of the human TRPV4 channel
    • Inada, H., Procko, E., Sotomayor, M. & Gaudet, R. Structural and biochemical consequences of disease-causing mutations in the ankyrin repeat domain of the human TRPV4 channel. Biochemistry 51, 6195-6206 (2012).
    • (2012) Biochemistry , vol.51 , pp. 6195-6206
    • Inada, H.1    Procko, E.2    Sotomayor, M.3    Gaudet, R.4
  • 35
    • 84923349290 scopus 로고    scopus 로고
    • TRPV4 channel activity is modulated by direct interaction of the ankyrin domain to PI(4, 5)P2
    • Takahashi, N. et al. TRPV4 channel activity is modulated by direct interaction of the ankyrin domain to PI(4, 5)P2. Nat. Commun. 5, 4994 (2014).
    • (2014) Nat. Commun. , vol.5 , pp. 4994
    • Takahashi, N.1
  • 36
    • 77951248588 scopus 로고    scopus 로고
    • A 3. 5-nm structure of rat TRPV4 cation channel revealed by Zernike phase-contrast cryoelectron microscopy
    • Shigematsu, H., Sokabe, T., Danev, R., Tominaga, M. & Nagayama, K. A 3. 5-nm structure of rat TRPV4 cation channel revealed by Zernike phase-contrast cryoelectron microscopy. J. Biol. Chem. 285, 11210-11218 (2010).
    • (2010) J. Biol. Chem. , vol.285 , pp. 11210-11218
    • Shigematsu, H.1    Sokabe, T.2    Danev, R.3    Tominaga, M.4    Nagayama, K.5
  • 37
    • 39849110422 scopus 로고    scopus 로고
    • The C-terminal domain of TRPV4 is essential for plasma membrane localization
    • Becker, D., Müller, M., Leuner, K. & Jendrach, M. The C-terminal domain of TRPV4 is essential for plasma membrane localization. Mol. Membr. Biol. 25, 139-151 (2008).
    • (2008) Mol. Membr. Biol. , vol.25 , pp. 139-151
    • Becker, D.1    Müller, M.2    Leuner, K.3    Jendrach, M.4
  • 38
    • 84876242735 scopus 로고    scopus 로고
    • A TRPV4 channel C-terminal folding recognition domain critical for trafficking and function
    • Lei, L. et al. A TRPV4 channel C-terminal folding recognition domain critical for trafficking and function. J. Biol. Chem. 288, 10427-10439 (2013).
    • (2013) J. Biol. Chem. , vol.288 , pp. 10427-10439
    • Lei, L.1
  • 39
    • 23244456428 scopus 로고    scopus 로고
    • Crystal structure of a mammalian voltage-dependent Shaker family K+ channel
    • Long, S. B., Campbell, E. B. & Mackinnon, R. Crystal structure of a mammalian voltage-dependent Shaker family K+ channel. Science 309, 897-903 (2005).
    • (2005) Science , vol.309 , pp. 897-903
    • Long, S.B.1    Campbell, E.B.2    MacKinnon, R.3
  • 40
    • 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
  • 41
    • 36248982122 scopus 로고    scopus 로고
    • Atomic structure of a voltage-dependent K+ channel in a lipid membrane-like environment
    • Long, S. B., Tao, X., Campbell, E. B. & MacKinnon, R. Atomic structure of a voltage-dependent K+ channel in a lipid membrane-like environment. Nature 450, 376-382 (2007).
    • (2007) Nature , vol.450 , pp. 376-382
    • Long, S.B.1    Tao, X.2    Campbell, E.B.3    MacKinnon, R.4
  • 42
    • 84938524668 scopus 로고    scopus 로고
    • The integrity of the TRP domain is pivotal for correct TRPV1 channel gating
    • Gregorio-Teruel, L. et al. The integrity of the TRP domain is pivotal for correct TRPV1 channel gating. Biophys. J. 109, 529-541 (2015).
    • (2015) Biophys. J. , vol.109 , pp. 529-541
    • Gregorio-Teruel, L.1
  • 43
    • 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
  • 44
    • 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
  • 45
    • 84861217903 scopus 로고    scopus 로고
    • Selective disruption of high sensitivity heat activation but not capsaicin activation of TRPV1 channels by pore turret mutations
    • Cui, Y. et al. Selective disruption of high sensitivity heat activation but not capsaicin activation of TRPV1 channels by pore turret mutations. J. Gen. Physiol. 139, 273-283 (2012).
    • (2012) J. Gen. Physiol. , vol.139 , pp. 273-283
    • Cui, Y.1
  • 46
    • 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
  • 47
    • 0037072735 scopus 로고    scopus 로고
    • Molecular determinants of permeation through the cation channel TRPV4
    • Voets, T. et al. Molecular determinants of permeation through the cation channel TRPV4. J. Biol. Chem. 277, 33704-33710 (2002).
    • (2002) J. Biol. Chem. , vol.277 , pp. 33704-33710
    • Voets, T.1
  • 48
    • 33645318420 scopus 로고    scopus 로고
    • Atomic structure of a Na+-and K+-conducting channel
    • Shi, N., Ye, S., Alam, A., Chen, L. & Jiang, Y. Atomic structure of a Na+-and K+-conducting channel. Nature 440, 570-574 (2006).
    • (2006) Nature , vol.440 , pp. 570-574
    • Shi, N.1    Ye, S.2    Alam, A.3    Chen, L.4    Jiang, Y.5
  • 49
    • 79551660280 scopus 로고    scopus 로고
    • Tuning the ion selectivity of tetrameric cation channels by changing the number of ion binding sites
    • Derebe, M. G. et al. Tuning the ion selectivity of tetrameric cation channels by changing the number of ion binding sites. Proc. Natl Acad. Sci. USA 108, 598-602 (2011).
    • (2011) Proc. Natl Acad. Sci. USA , vol.108 , pp. 598-602
    • Derebe, M.G.1
  • 50
    • 84887802264 scopus 로고    scopus 로고
    • Sodium and potassium competition in potassium-selective and non-selective channels
    • Sauer, D. B., Zeng, W., Canty, J., Lam, Y. & Jiang, Y. Sodium and potassium competition in potassium-selective and non-selective channels. Nat. Commun. 4, 2721 (2013).
    • (2013) Nat. Commun. , vol.4 , pp. 2721
    • Sauer, D.B.1    Zeng, W.2    Canty, J.3    Lam, Y.4    Jiang, Y.5
  • 51
    • 84956673406 scopus 로고    scopus 로고
    • Determinants of cation transport selectivity: Equilibrium binding and transport kinetics
    • Lockless, S. W. Determinants of cation transport selectivity: equilibrium binding and transport kinetics. J. Gen. Physiol. 146, 3-13 (2015).
    • (2015) J. Gen. Physiol. , vol.146 , pp. 3-13
    • Lockless, S.W.1
  • 52
    • 84881407173 scopus 로고    scopus 로고
    • Importance of lipid-pore loop interface for potassium channel structure and function
    • van der Cruijsen, E. A. W. et al. Importance of lipid-pore loop interface for potassium channel structure and function. Proc. Natl Acad. Sci. USA 110, 13008-13013 (2013).
    • (2013) Proc. Natl Acad. Sci. USA , vol.110 , pp. 13008-13013
    • Van Der Cruijsen, E.A.W.1
  • 53
    • 84921813003 scopus 로고    scopus 로고
    • Physical mechanism for gating and mechanosensitivity of the human TRAAK K+ channel
    • Brohawn, S. G., Campbell, E. B. & MacKinnon, R. Physical mechanism for gating and mechanosensitivity of the human TRAAK K+ channel. Nature 516, 126-130 (2014).
    • (2014) Nature , vol.516 , pp. 126-130
    • Brohawn, S.G.1    Campbell, E.B.2    MacKinnon, R.3
  • 54
    • 84994059356 scopus 로고    scopus 로고
    • Pore architecture of TRIC channels and insights into their gating mechanism
    • Yang, H. et al. Pore architecture of TRIC channels and insights into their gating mechanism. Nature 538, 537-541 (2016).
    • (2016) Nature , vol.538 , pp. 537-541
    • Yang, H.1
  • 55
    • 34250327530 scopus 로고    scopus 로고
    • Determinants of 4 alpha-phorbol sensitivity in transmembrane domains 3 and 4 of the cation channel TRPV4
    • Vriens, J., Owsianik, G., Janssens, A., Voets, T. & Nilius, B. Determinants of 4 alpha-phorbol sensitivity in transmembrane domains 3 and 4 of the cation channel TRPV4. J. Biol. Chem. 282, 12796-12803 (2007).
    • (2007) J. Biol. Chem. , vol.282 , pp. 12796-12803
    • Vriens, J.1    Owsianik, G.2    Janssens, A.3    Voets, T.4    Nilius, B.5
  • 56
    • 80054985573 scopus 로고    scopus 로고
    • Mutations in TRPV4 cause an inherited arthropathy of hands and feet
    • Lamandé, S. R. et al. Mutations in TRPV4 cause an inherited arthropathy of hands and feet. Nat. Genet. 43, 1142-1146 (2011).
    • (2011) Nat. Genet. , vol.43 , pp. 1142-1146
    • Lamandé, S.R.1
  • 58
    • 61549126051 scopus 로고    scopus 로고
    • Mutations in the gene encoding the calcium-permeable ion channel TRPV4 produce spondylometaphyseal dysplasia, Kozlowski type and metatropic dysplasia
    • Krakow, D. et al. Mutations in the gene encoding the calcium-permeable ion channel TRPV4 produce spondylometaphyseal dysplasia, Kozlowski type and metatropic dysplasia. Am. J. Hum. Genet. 84, 307-315 (2009).
    • (2009) Am. J. Hum. Genet. , vol.84 , pp. 307-315
    • Krakow, D.1
  • 59
    • 77951717570 scopus 로고    scopus 로고
    • Dominant TRPV4 mutations in nonlethal and lethal metatropic dysplasia
    • Camacho, N. et al. Dominant TRPV4 mutations in nonlethal and lethal metatropic dysplasia. Am. J. Med. Genet. A. 152A, 1169-1177 (2010).
    • (2010) Am. J. Med. Genet. A. , vol.152 A , pp. 1169-1177
    • Camacho, N.1
  • 60
    • 77952748007 scopus 로고    scopus 로고
    • Novel and recurrent TRPV4 mutations and their association with distinct phenotypes within the TRPV4 dysplasia family
    • Dai, J. et al. Novel and recurrent TRPV4 mutations and their association with distinct phenotypes within the TRPV4 dysplasia family. J. Med. Genet. 47, 704-709 (2010).
    • (2010) J. Med. Genet. , vol.47 , pp. 704-709
    • Dai, J.1
  • 61
    • 77952751595 scopus 로고    scopus 로고
    • Spondylo-epiphyseal dysplasia, Maroteaux type (pseudo-Morquio syndrome type 2), and parastremmatic dysplasia are caused by TRPV4 mutations
    • Nishimura, G. et al. Spondylo-epiphyseal dysplasia, Maroteaux type (pseudo-Morquio syndrome type 2), and parastremmatic dysplasia are caused by TRPV4 mutations. Am. J. Med. Genet. A. 152A, 1443-1449 (2010).
    • Am. J. Med. Genet. A. 152A, 1443-1449 (2010)
    • Nishimura, G.1
  • 62
    • 75749139617 scopus 로고    scopus 로고
    • Mutations in TRPV4 cause Charcot-Marie-Tooth disease type 2C
    • Landouré, G. et al. Mutations in TRPV4 cause Charcot-Marie-Tooth disease type 2C. Nat. Genet. 42, 170-174 (2010).
    • (2010) Nat. Genet. , vol.42 , pp. 170-174
    • Landouré, G.1
  • 63
    • 75749129360 scopus 로고    scopus 로고
    • Alterations in the ankyrin domain of TRPV4 cause congenital distal SMA, scapuloperoneal SMA and HMSN2C
    • Auer-Grumbach, M. et al. Alterations in the ankyrin domain of TRPV4 cause congenital distal SMA, scapuloperoneal SMA and HMSN2C. Nat. Genet. 42, 160-164 (2010).
    • (2010) Nat. Genet. , vol.42 , pp. 160-164
    • Auer-Grumbach, M.1
  • 64
    • 84865000128 scopus 로고    scopus 로고
    • TRPV4 mutations in children with congenital distal spinal muscular atrophy
    • Fiorillo, C. et al. TRPV4 mutations in children with congenital distal spinal muscular atrophy. Neurogenetics 13, 195-203 (2012).
    • (2012) Neurogenetics , vol.13 , pp. 195-203
    • Fiorillo, C.1
  • 65
    • 75749083221 scopus 로고    scopus 로고
    • Scapuloperoneal spinal muscular atrophy and CMT2C are allelic disorders caused by alterations in TRPV4
    • Deng, H.-X. et al. Scapuloperoneal spinal muscular atrophy and CMT2C are allelic disorders caused by alterations in TRPV4. Nat. Genet. 42, 165-169 (2010).
    • (2010) Nat. Genet. , vol.42 , pp. 165-169
    • Deng, H.-X.1
  • 66
    • 25644458666 scopus 로고    scopus 로고
    • Automated electron microscope tomography using robust prediction of specimen movements
    • Mastronarde, D. N. Automated electron microscope tomography using robust prediction of specimen movements. J. Struct. Biol. 152, 36-51 (2005).
    • (2005) J. Struct. Biol. , vol.152 , pp. 36-51
    • Mastronarde, D.N.1
  • 67
    • 85014129582 scopus 로고    scopus 로고
    • MotionCor2: Anisotropic correction of beam-induced motion for improved cryo-electron microscopy
    • Zheng, S. Q. et al. MotionCor2: anisotropic correction of beam-induced motion for improved cryo-electron microscopy. Nat. Methods 14, 331-332 (2017).
    • (2017) Nat. Methods , vol.14 , pp. 331-332
    • Zheng, S.Q.1
  • 68
    • 84868444740 scopus 로고    scopus 로고
    • RELION: Implementation of a Bayesian approach to cryo-EM structure determination
    • Scheres, S. H. W. 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.W.1
  • 69
    • 84922727036 scopus 로고    scopus 로고
    • Semi-automated selection of cryo-EM particles in RELION-1
    • Scheres, S. H. W. Semi-automated selection of cryo-EM particles in RELION-1. 3. J. Struct. Biol. 189, 114-122 (2015).
    • (2015) 3. J. Struct. Biol. , vol.189 , pp. 114-122
    • Scheres, S.H.W.1
  • 70
    • 84946488108 scopus 로고    scopus 로고
    • CTFFIND4: Fast and accurate defocus estimation from electron micrographs
    • Rohou, A. & Grigorieff, N. CTFFIND4: Fast and accurate defocus estimation from electron micrographs. J. Struct. Biol. 192, 216-221 (2015).
    • (2015) J. Struct. Biol. , vol.192 , pp. 216-221
    • Rohou, A.1    Grigorieff, N.2
  • 71
    • 85013784291 scopus 로고    scopus 로고
    • Single-particle refinement and variability analysis in EMAN2
    • Ludtke, S. J. Single-particle refinement and variability analysis in EMAN2. 1. Methods Enzymol. 579, 159-189 (2016).
    • (2016) 1. Methods Enzymol. , vol.579 , pp. 159-189
    • Ludtke, S.J.1
  • 72
    • 84883447961 scopus 로고    scopus 로고
    • Likelihood-based classification of cryo-EM images using FREALIGN
    • Lyumkis, D., Brilot, A. F., Theobald, D. L. & Grigorieff, N. Likelihood-based classification of cryo-EM images using FREALIGN. J. Struct. Biol. 183, 377-388 (2013).
    • (2013) J. Struct. Biol. , vol.183 , pp. 377-388
    • Lyumkis, D.1    Brilot, A.F.2    Theobald, D.L.3    Grigorieff, N.4
  • 73
    • 0142042865 scopus 로고    scopus 로고
    • Optimal determination of particle orientation, absolute hand, and contrast loss in single-particle electron cryomicroscopy
    • Rosenthal, P. B. & Henderson, R. Optimal determination of particle orientation, absolute hand, and contrast loss in single-particle electron cryomicroscopy. J. Mol. Biol. 333, 721-745 (2003).
    • (2003) J. Mol. Biol. , vol.333 , pp. 721-745
    • Rosenthal, P.B.1    Henderson, R.2
  • 74
    • 84894623755 scopus 로고    scopus 로고
    • Quantifying the local resolution of cryo-EM density maps
    • Kucukelbir, A., Sigworth, F. J. & Tagare, H. D. Quantifying the local resolution of cryo-EM density maps. Nat. Methods 11, 63-65 (2014).
    • (2014) Nat. Methods , vol.11 , pp. 63-65
    • Kucukelbir, A.1    Sigworth, F.J.2    Tagare, H.D.3
  • 75
    • 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
  • 77
    • 76449098262 scopus 로고    scopus 로고
    • PHENIX: A comprehensive Python-based system for macromolecular structure solution
    • Adams, P. D. et al. PHENIX: a comprehensive Python-based system for macromolecular structure solution. Acta Crystallogr. D Biol. Crystallogr. 66, 213-221 (2010).
    • (2010) Acta Crystallogr. D Biol. Crystallogr. , vol.66 , pp. 213-221
    • Adams, P.D.1
  • 78
    • 84921777915 scopus 로고    scopus 로고
    • Tools for macromolecular model building and refinement into electron cryo-microscopy reconstructions
    • Brown, A. et al. Tools for macromolecular model building and refinement into electron cryo-microscopy reconstructions. Acta Crystallogr. D Biol. Crystallogr. 71, 136-153 (2015).
    • (2015) Acta Crystallogr. D Biol. Crystallogr. , vol.71 , pp. 136-153
    • Brown, A.1
  • 79
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski, Z. & Minor, W. Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol. 276, 307-326 (1997).
    • (1997) Methods Enzymol. , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 80
    • 33846426122 scopus 로고    scopus 로고
    • Solving structures of protein complexes by molecular replacement with Phaser
    • McCoy, A. J. Solving structures of protein complexes by molecular replacement with Phaser. Acta Crystallogr. D Biol. Crystallogr. 63, 32-41 (2007).
    • (2007) Acta Crystallogr. D Biol. Crystallogr. , vol.63 , pp. 32-41
    • McCoy, A.J.1
  • 82
    • 80054078476 scopus 로고    scopus 로고
    • Fast, scalable generation of high-quality protein multiple sequence alignments using Clustal Omega
    • Sievers, F. et al. Fast, scalable generation of high-quality protein multiple sequence alignments using Clustal Omega. Mol. Syst. Biol. 7, 539 (2011).
    • (2011) Mol. Syst. Biol. , vol.7 , pp. 539
    • Sievers, F.1
  • 83
    • 65349114255 scopus 로고    scopus 로고
    • ALINE: A WYSIWYG protein-sequence alignment editor for publication-quality alignments. Acta Crystallogr
    • Bond, C. S. & Schüttelkopf, A. W. ALINE: a WYSIWYG protein-sequence alignment editor for publication-quality alignments. Acta Crystallogr. D Biol. Crystallogr. 65, 510-512 (2009).
    • (2009) D Biol. Crystallogr. , vol.65 , pp. 510-512
    • Bond, C.S.1    Schüttelkopf, A.W.2
  • 84
    • 0028246420 scopus 로고
    • Microinjection technique: Routine system for characterization of microcapillaries by bubble pressure measurement
    • Schnorf, M., Potrykus, I. & Neuhaus, G. Microinjection technique: routine system for characterization of microcapillaries by bubble pressure measurement. Exp. Cell Res. 210, 260-267 (1994).
    • (1994) Exp. Cell Res. , vol.210 , pp. 260-267
    • Schnorf, M.1    Potrykus, I.2    Neuhaus, G.3
  • 85
    • 84970949820 scopus 로고    scopus 로고
    • Differential mechanisms of Cantú syndrome-associated gain of function mutations in the ABCC9 (SUR2) subunit of the KATP channel
    • Cooper, P. E., Sala-Rabanal, M., Lee, S. J. & Nichols, C. G. Differential mechanisms of Cantú syndrome-associated gain of function mutations in the ABCC9 (SUR2) subunit of the KATP channel. J. Gen. Physiol. 146, 527-540 (2015).
    • (2015) J. Gen. Physiol. , vol.146 , pp. 527-540
    • Cooper, P.E.1    Sala-Rabanal, M.2    Lee, S.J.3    Nichols, C.G.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.