메뉴 건너뛰기




Volumn 1838, Issue 2, 2014, Pages 682-691

The ion channels to cytoskeleton connection as potential mechanism of mechanosensitivity

Author keywords

Bilayer mechanism; C. elegans; Dual tether single tether mechanism; Hair cell; Mechanosensory transduction channel

Indexed keywords

CALCIUM CHANNEL; EPITHELIAL SODIUM CHANNEL; MEMBRANE PROTEIN; PIEZO 1; PIEZO 2; POLYCYSTIN 1; POLYCYSTIN 2; POTASSIUM CHANNEL; PROTEIN TRAAK; PROTEIN TREK1; PROTEIN TREK2; SODIUM CHANNEL; TRANSIENT RECEPTOR POTENTIAL CHANNEL 1; TRANSIENT RECEPTOR POTENTIAL CHANNEL 6; TRANSIENT RECEPTOR POTENTIAL CHANNEL A1; TRANSIENT RECEPTOR POTENTIAL CHANNEL M3; TRANSIENT RECEPTOR POTENTIAL CHANNEL M4; UNCLASSIFIED DRUG; VANILLOID RECEPTOR 1; VANILLOID RECEPTOR 2; VANILLOID RECEPTOR 4;

EID: 84892151878     PISSN: 00052736     EISSN: 18792642     Source Type: Journal    
DOI: 10.1016/j.bbamem.2013.07.015     Document Type: Review
Times cited : (106)

References (158)
  • 1
    • 0028387348 scopus 로고
    • There must be a prokaryote somewhere: Microbiology's search for itself
    • C.R. Woese There must be a prokaryote somewhere: microbiology's search for itself Microbiol. Rev. 58 1994 1 9
    • (1994) Microbiol. Rev. , vol.58 , pp. 1-9
    • Woese, C.R.1
  • 2
    • 83755186704 scopus 로고    scopus 로고
    • Bacterial mechanosensitive channels as a paradigm for mechanosensory transduction
    • B. Martinac Bacterial mechanosensitive channels as a paradigm for mechanosensory transduction Cell Physiol. Biochem. 28 2011 1051 1060
    • (2011) Cell Physiol. Biochem. , vol.28 , pp. 1051-1060
    • Martinac, B.1
  • 3
    • 77957089158 scopus 로고
    • Mechanosensitive ion channels in microbes and the early evolutionary origin of solvent sensing
    • T. Claudio, Academic Press New York
    • C. Kung, Y. Saimi, and B. Martinac Mechanosensitive ion channels in microbes and the early evolutionary origin of solvent sensing T. Claudio, Current Topics in Membranes and Transport 1990 Academic Press New York 9451 9455
    • (1990) Current Topics in Membranes and Transport , pp. 9451-9455
    • Kung, C.1    Saimi, Y.2    Martinac, B.3
  • 4
    • 0035855845 scopus 로고    scopus 로고
    • Molecular basis of mechanosensory transduction
    • DOI 10.1038/35093011
    • P.G. Gillespie, and R.G. Walker Molecular basis of mechanosensory transduction Nature 413 2001 194 202 (Pubitemid 32867884)
    • (2001) Nature , vol.413 , Issue.6852 , pp. 194-202
    • Gillespie, P.G.1    Walker, R.G.2
  • 5
    • 0035069134 scopus 로고    scopus 로고
    • Molecular basis of mechanotransduction in living cells
    • O.P. Hamill, and B. Martinac Molecular basis of mechanotransduction in living cells Physiol. Rev. 81 2001 685 740 (Pubitemid 32267076)
    • (2001) Physiological Reviews , vol.81 , Issue.2 , pp. 685-740
    • Hamill, O.P.1    Martinac, B.2
  • 6
    • 58049196875 scopus 로고    scopus 로고
    • Neurosensory mechanotransduction
    • M. Chalfie Neurosensory mechanotransduction Nat. Rev. Mol. Cell Biol. 10 2009 44 52
    • (2009) Nat. Rev. Mol. Cell Biol. , vol.10 , pp. 44-52
    • Chalfie, M.1
  • 8
    • 0345196593 scopus 로고    scopus 로고
    • Protection of Escherichia coli cells against extreme turgor by activation of MscS and MscL mechanosensitive channels: Identification of genes required for MscS activity
    • N. Levina, S. Totemeyer, N.R. Stokes, P. Louis, M.A. Jones, and I.R. Booth Protection of Escherichia coli cells against extreme turgor by activation of MscS and MscL mechanosensitive channels: identification of genes required for MscS activity EMBO J. 18 1999 1730 1737 (Pubitemid 29158517)
    • (1999) EMBO Journal , vol.18 , Issue.7 , pp. 1730-1737
    • Levina, N.1    Totemeyer, S.2    Stokes, N.R.3    Louis, P.4    Jones, M.A.5    Booth, I.R.6
  • 9
    • 0030934807 scopus 로고    scopus 로고
    • Induced membrane hypo/hyper-mechanosensitivity: A limitation of patch- clamp recording
    • DOI 10.1146/annurev.physiol.59.1.621
    • O.P. Hamill, and D.W. McBride Jr. Induced membrane hypo/hyper- mechanosensitivity: a limitation of patch-clamp recording Annu. Rev. Physiol. 59 1997 621 631 (Pubitemid 27142458)
    • (1997) Annual Review of Physiology , vol.59 , pp. 621-631
    • Hamill, O.P.1    McBride Jr., D.W.2
  • 11
    • 0035232894 scopus 로고    scopus 로고
    • Mechanoprotection of the plasma membrane in neurons and other non-erythroid cells by the spectrin-based membrane skeleton
    • C.E. Morris Mechanoprotection of the plasma membrane in neurons and other non-erythroid cells by the spectrin-based membrane skeleton Cell. Mol. Biol. Lett. 6 2001 703 720 (Pubitemid 33678440)
    • (2001) Cellular and Molecular Biology Letters , vol.6 , Issue.3 , pp. 703-720
    • Morris, C.E.1
  • 12
    • 33646485148 scopus 로고    scopus 로고
    • The membrane skeleton: Mechanoprotector and mediator of mechanosensitive surface area
    • C.E. Morris The membrane skeleton: mechanoprotector and mediator of mechanosensitive surface area Cell. Mol. Biol. Lett. 6 2001 222 223
    • (2001) Cell. Mol. Biol. Lett. , vol.6 , pp. 222-223
    • Morris, C.E.1
  • 13
    • 0035863013 scopus 로고    scopus 로고
    • Cell surface area regulation and membrane tension
    • C.E. Morris, and U. Homann Cell surface area regulation and membrane tension J. Membr. Biol. 179 2001 79 102 (Pubitemid 32121602)
    • (2001) Journal of Membrane Biology , vol.179 , Issue.2 , pp. 79-102
    • Morris, C.E.1    Homann, U.2
  • 14
    • 0033060992 scopus 로고    scopus 로고
    • Activation of mechanosensitive currents in traumatized membrane
    • X. Wan, P. Juranka, and C.E. Morris Activation of mechanosensitive currents in traumatized membrane Am. J. Physiol. 276 1999 C318 C327
    • (1999) Am. J. Physiol. , vol.276
    • Wan, X.1    Juranka, P.2    Morris, C.E.3
  • 15
    • 0031935411 scopus 로고    scopus 로고
    • Neuronal swelling and surface area regulation: Elevated intracellular calcium is not a requirement
    • T.L. Herring, I.M. Slotin, J.M. Baltz, and C.E. Morris Neuronal swelling and surface area regulation: elevated intracellular calcium is not a requirement Am. J. Physiol. 274 1998 C272 C281
    • (1998) Am. J. Physiol. , vol.274
    • Herring, T.L.1    Slotin, I.M.2    Baltz, J.M.3    Morris, C.E.4
  • 16
    • 0032402931 scopus 로고    scopus 로고
    • Neuronal plasma membrane dynamics evoked by osmomechanical perturbations
    • DOI 10.1007/s002329900464
    • L.R. Mills, and C.E. Morris Neuronal plasma membrane dynamics evoked by osmomechanical perturbations J. Membr. Biol. 166 1998 223 235 (Pubitemid 28557791)
    • (1998) Journal of Membrane Biology , vol.166 , Issue.3 , pp. 223-235
    • Mills, L.R.1    Morris, C.E.2
  • 17
    • 54749142144 scopus 로고    scopus 로고
    • Membrane tension in swelling and shrinking molluscan neurons
    • J.W. Dai, M.P. Sheetz, T. Herring, and C.E. Morris Membrane tension in swelling and shrinking molluscan neurons Mol. Biol. Cell 7 1996 2614
    • (1996) Mol. Biol. Cell , vol.7 , pp. 2614
    • Dai, J.W.1    Sheetz, M.P.2    Herring, T.3    Morris, C.E.4
  • 18
    • 7844227792 scopus 로고    scopus 로고
    • Actin and filopodial dynamics in osmotically perturbed molluscan neurons
    • C.S. Cohan, E.A. Welnhofer, T.L. Herring, and C.E. Morris Actin and filopodial dynamics in osmotically perturbed molluscan neurons Mol. Biol. Cell 8 1997 1482
    • (1997) Mol. Biol. Cell , vol.8 , pp. 1482
    • Cohan, C.S.1    Welnhofer, E.A.2    Herring, T.L.3    Morris, C.E.4
  • 19
    • 84892369198 scopus 로고
    • Capacitance changes of neurons during large osmomechanical perturbations
    • X. Wan, and C.E. Morris Capacitance changes of neurons during large osmomechanical perturbations FASEB J. 8 1994 A113
    • (1994) FASEB J. , vol.8 , pp. 113
    • Wan, X.1    Morris, C.E.2
  • 21
    • 33947360830 scopus 로고    scopus 로고
    • 2P channels: Focus on TREK1
    • DOI 10.1038/nrn2117, PII NRN2117
    • E. Honore The neuronal background K2P channels: focus on TREK1 Nat. Rev. Neurosci. 8 2007 251 261 (Pubitemid 46452327)
    • (2007) Nature Reviews Neuroscience , vol.8 , Issue.4 , pp. 251-261
    • Honore, E.1
  • 22
    • 13944263659 scopus 로고    scopus 로고
    • TRPC1 forms the stretch-activated cation channel in vertebrate cells
    • DOI 10.1038/ncb1218
    • R. Maroto, A. Raso, T.G. Wood, A. Kurosky, B. Martinac, and O.P. Hamill TRPC1 forms the stretch-activated cation channel in vertebrate cells Nat. Cell Biol. 7 2005 179 185 (Pubitemid 40268133)
    • (2005) Nature Cell Biology , vol.7 , Issue.2 , pp. 179-185
    • Maroto, R.1    Raso, A.2    Wood, T.G.3    Kurosky, A.4    Martinac, B.5    Hamill, O.P.6
  • 23
    • 0034652431 scopus 로고    scopus 로고
    • Mechanically gated channel activity in cytoskeleton-deficient plasma membrane blebs and vesicles from Xenopus oocytes
    • Y. Zhang, F. Gao, V.L. Popov, J.W. Wen, and O.P. Hamill Mechanically gated channel activity in cytoskeleton-deficient plasma membrane blebs and vesicles from Xenopus oocytes J. Physiol. 523 Pt 1 2000 117 130 (Pubitemid 30135825)
    • (2000) Journal of Physiology , vol.523 , Issue.1 , pp. 117-130
    • Zhang, Y.1    Gao, F.2    Popov, V.L.3    Wen, J.W.4    Hamill, O.P.5
  • 24
    • 0024433313 scopus 로고
    • How the ear's works work
    • DOI 10.1038/341397a0
    • A.J. Hudspeth How the ear's works work Nature 341 1989 397 404 (Pubitemid 19241904)
    • (1989) Nature , vol.341 , Issue.6241 , pp. 397-404
    • Hudspeth, A.J.1
  • 25
    • 34147155869 scopus 로고    scopus 로고
    • Models of hair cell mechanotransduction
    • O.P. Hamill, Academic Press San Diego
    • S. Bechstedt, and J. Howard Models of hair cell mechanotransduction O.P. Hamill, Mechanosensitive Ion Channels, Part B vol. 59 2007 Academic Press San Diego 399 424
    • (2007) Mechanosensitive Ion Channels, Part B , vol.59 , pp. 399-424
    • Bechstedt, S.1    Howard, J.2
  • 26
    • 0029097756 scopus 로고
    • Gating-spring models of mechanoelectrical transduction by hair cells of the internal ear
    • V.S. Markin, and A.J. Hudspeth Gating-spring models of mechanoelectrical transduction by hair cells of the internal ear Annu. Rev. Biophys. Biomol. Struct. 24 1995 59 83
    • (1995) Annu. Rev. Biophys. Biomol. Struct. , vol.24 , pp. 59-83
    • Markin, V.S.1    Hudspeth, A.J.2
  • 27
    • 65449123914 scopus 로고    scopus 로고
    • Bottoms up: Transduction channels at tip link bases
    • K.J. Spinelli, and P.G. Gillespie Bottoms up: transduction channels at tip link bases Nat. Neurosci. 12 2009 529 530
    • (2009) Nat. Neurosci. , vol.12 , pp. 529-530
    • Spinelli, K.J.1    Gillespie, P.G.2
  • 28
    • 65549128486 scopus 로고    scopus 로고
    • Localization of inner hair cell mechanotransducer channels using high-speed calcium imaging
    • M. Beurg, R. Fettiplace, J.H. Nam, and A.J. Ricci Localization of inner hair cell mechanotransducer channels using high-speed calcium imaging Nat. Neurosci. 12 2009 553 558
    • (2009) Nat. Neurosci. , vol.12 , pp. 553-558
    • Beurg, M.1    Fettiplace, R.2    Nam, J.H.3    Ricci, A.J.4
  • 30
    • 33646061333 scopus 로고    scopus 로고
    • TRPA1 contributes to cold, mechanical, and chemical nociception but is not essential for hair-cell transduction
    • K.Y. Kwan, A.J. Allchorne, M.A. Vollrath, A.P. Christensen, D.S. Zhang, C.J. Woolf, and D.P. Corey TRPA1 contributes to cold, mechanical, and chemical nociception but is not essential for hair-cell transduction Neuron 50 2006 277 289
    • (2006) Neuron , vol.50 , pp. 277-289
    • Kwan, K.Y.1    Allchorne, A.J.2    Vollrath, M.A.3    Christensen, A.P.4    Zhang, D.S.5    Woolf, C.J.6    Corey, D.P.7
  • 31
    • 1842475312 scopus 로고    scopus 로고
    • Noxious cold ion channel TRPA1 is activated by pungent compounds and bradykinin
    • DOI 10.1016/S0896-6273(04)00150-3, PII S0896627304001503
    • M. Bandell, G.M. Story, S.W. Hwang, V. Viswanath, S.R. Eid, M.J. Petrus, T.J. Earley, and A. Patapoutian Noxious cold ion channel TRPA1 is activated by pungent compounds and bradykinin Neuron 41 2004 849 857 (Pubitemid 38429729)
    • (2004) Neuron , vol.41 , Issue.6 , pp. 849-857
    • Bandell, M.1    Story, G.M.2    Hwang, S.W.3    Viswanath, V.4    Eid, S.R.5    Petrus, M.J.6    Earley, T.J.7    Patapoutian, A.8
  • 32
    • 34147126483 scopus 로고    scopus 로고
    • Hair cell mechanotransduction: The dynamic interplay between structure and function
    • O.P. Hamill, Academic Press San Diego
    • A.J. Ricci, and B. Kachar Hair cell mechanotransduction: the dynamic interplay between structure and function O.P. Hamill, Mechanosensitive Ion Channels Part B vol. 59 2007 Academic Press San Diego 339 374
    • (2007) Mechanosensitive Ion Channels Part B , vol.59 , pp. 339-374
    • Ricci, A.J.1    Kachar, B.2
  • 35
    • 0034703498 scopus 로고    scopus 로고
    • Gating energies and forces of the mammalian hair cell transducer channel and related hair bundle mechanics
    • S.M. van Netten, and C.J. Kros Gating energies and forces of the mammalian hair cell transducer channel and related hair bundle mechanics Proc. Biol. Sci. 267 2000 1915 1923
    • (2000) Proc. Biol. Sci. , vol.267 , pp. 1915-1923
    • Van Netten, S.M.1    Kros, C.J.2
  • 36
    • 33644849450 scopus 로고    scopus 로고
    • Nanospring behaviour of ankyrin repeats
    • DOI 10.1038/nature04437, PII N04437
    • G. Lee, K. Abdi, Y. Jiang, P. Michaely, V. Bennett, and P.E. Marszalek Nanospring behaviour of ankyrin repeats Nature 440 2006 246 249 (Pubitemid 43372106)
    • (2006) Nature , vol.440 , Issue.7081 , pp. 246-249
    • Lee, G.1    Abdi, K.2    Jiang, Y.3    Michaely, P.4    Bennett, V.5    Marszalek, P.E.6
  • 39
    • 70349448090 scopus 로고    scopus 로고
    • Mechanotransduction by hair cells: Models, molecules, and mechanisms
    • P.G. Gillespie, and U. Muller Mechanotransduction by hair cells: models, molecules, and mechanisms Cell 139 2009 33 44
    • (2009) Cell , vol.139 , pp. 33-44
    • Gillespie, P.G.1    Muller, U.2
  • 40
    • 84865281061 scopus 로고    scopus 로고
    • Mechanosensitive Ca(2 +) permeant cation channels in human prostate tumor cells
    • R. Maroto, A. Kurosky, and O.P. Hamill Mechanosensitive Ca(2 +) permeant cation channels in human prostate tumor cells Channels (Austin) 6 2012 290 307
    • (2012) Channels (Austin) , vol.6 , pp. 290-307
    • Maroto, R.1    Kurosky, A.2    Hamill, O.P.3
  • 41
    • 16644397827 scopus 로고    scopus 로고
    • The MEC-4 DEG/ENaC channel of Caenorhabditis elegans touch receptor neurons transduces mechanical signals
    • DOI 10.1038/nn1362
    • R. O'Hagan, M. Chalfie, and M.B. Goodman The MEC-4 DEG/ENaC channel of Caenorhabditis elegans touch receptor neurons transduces mechanical signals Nat. Neurosci. 8 2008 43 50 (Pubitemid 41236730)
    • (2005) Nature Neuroscience , vol.8 , Issue.1 , pp. 43-50
    • O'Hagan, R.1    Chalfie, M.2    Goodman, M.B.3
  • 42
    • 3042853029 scopus 로고    scopus 로고
    • Mechanosensitive ion channels: Molecules of mechanotransduction
    • DOI 10.1242/jcs.01232
    • B. Martinac Mechanosensitive ion channels: molecules of mechanotransduction J. Cell Sci. 117 2004 2449 2460 (Pubitemid 38877841)
    • (2004) Journal of Cell Science , vol.117 , Issue.12 , pp. 2449-2460
    • Martinac, B.1
  • 43
    • 84875523320 scopus 로고    scopus 로고
    • Stiffened lipid platforms at molecular force foci
    • A. Anishkin, and C. Kung Stiffened lipid platforms at molecular force foci Proc. Natl. Acad. Sci. U. S. A. 110 2013 4886 4892
    • (2013) Proc. Natl. Acad. Sci. U. S. A. , vol.110 , pp. 4886-4892
    • Anishkin, A.1    Kung, C.2
  • 44
    • 0346655136 scopus 로고    scopus 로고
    • V channels to lipid rafts
    • DOI 10.1016/j.tips.2003.11.007
    • J.R. Martens, K. O'Connell, and M. Tamkun Targeting of ion channels to membrane microdomains: localization of KV channels to lipid rafts Trends Pharmacol. Sci. 25 2004 16 21 (Pubitemid 38076952)
    • (2004) Trends in Pharmacological Sciences , vol.25 , Issue.1 , pp. 16-21
    • Martens, J.R.1    O'Connell, K.2    Tamkun, M.3
  • 45
    • 32444447144 scopus 로고    scopus 로고
    • Involvement of lipid rafts and caveolae in cardiac ion channel function
    • DOI 10.1016/j.cardiores.2005.11.013, PII S0008636305005250
    • A. Maguy, T.E. Hebert, and S. Nattel Involvement of lipid rafts and caveolae in cardiac ion channel function Cardiovasc. Res. 69 2006 798 807 (Pubitemid 43227978)
    • (2006) Cardiovascular Research , vol.69 , Issue.4 , pp. 798-807
    • Maguy, A.1    Hebert, T.E.2    Nattel, S.3
  • 48
    • 34249651256 scopus 로고    scopus 로고
    • Cooperative gating and spatial organization of membrane proteins through elastic interactions
    • T. Ursell, K.C. Huang, E. Peterson, and R. Phillips Cooperative gating and spatial organization of membrane proteins through elastic interactions PLoS Comput. Biol. 3 2007 e81
    • (2007) PLoS Comput. Biol. , vol.3 , pp. 81
    • Ursell, T.1    Huang, K.C.2    Peterson, E.3    Phillips, R.4
  • 50
    • 0025114667 scopus 로고
    • Mechanosensitive ion channels of E. Coli activated by amphipaths
    • B. Martinac, J. Adler, and C. Kung Mechanosensitive ion channels of E. coli activated by amphipaths Nature 348 1990 261 263
    • (1990) Nature , vol.348 , pp. 261-263
    • Martinac, B.1    Adler, J.2    Kung, C.3
  • 51
    • 0023675507 scopus 로고
    • Mechanical transduction in biological systems
    • F. Sachs Mechanical transduction in biological systems Crit. Rev. Biomed. Eng. 16 1988 141 169
    • (1988) Crit. Rev. Biomed. Eng. , vol.16 , pp. 141-169
    • Sachs, F.1
  • 52
    • 0031627135 scopus 로고    scopus 로고
    • Mechanosensitive ion channels in nonspecialized cells
    • Springer-Verlag Berlin Berlin (33)
    • F. Sachs, and C.E. Morris Mechanosensitive ion channels in nonspecialized cells Reviews of Physiology Biochemistry and Pharmacology vol. 132 1998 Springer-Verlag Berlin Berlin 1 77 (33)
    • (1998) Reviews of Physiology Biochemistry and Pharmacology , vol.132 , pp. 1-77
    • Sachs, F.1    Morris, C.E.2
  • 54
    • 84864464300 scopus 로고    scopus 로고
    • Mechanosensitivity of nicotinic receptors
    • N.C. Pan, J.J. Ma, and H.B. Peng Mechanosensitivity of nicotinic receptors Pflugers Arch. 464 2012 193 203
    • (2012) Pflugers Arch. , vol.464 , pp. 193-203
    • Pan, N.C.1    Ma, J.J.2    Peng, H.B.3
  • 55
    • 0036725152 scopus 로고    scopus 로고
    • Physical principles underlying the transduction of bilayer deformation forces during mechanosensitive channel gating
    • DOI 10.1038/nsb827
    • E. Perozo, A. Kloda, D.M. Cortes, and B. Martinac Physical principles underlying the transduction of bilayer deformation forces during mechanosensitive channel gating Nat. Struct. Biol. 9 2002 696 703 (Pubitemid 34977304)
    • (2002) Nature Structural Biology , vol.9 , Issue.9 , pp. 696-703
    • Perozo, E.1    Kloda, A.2    Cortes, D.M.3    Martinac, B.4
  • 56
    • 17244380947 scopus 로고    scopus 로고
    • Lipid rafts and membrane dynamics
    • DOI 10.1242/jcs.01681
    • L. Rajendran, and K. Simons Lipid rafts and membrane dynamics J. Cell Sci. 118 2005 1099 1102 (Pubitemid 40528680)
    • (2005) Journal of Cell Science , vol.118 , Issue.6 , pp. 1099-1102
    • Rajendran, L.1    Simons, K.2
  • 58
    • 80051782287 scopus 로고    scopus 로고
    • Cholesterol depletion-induced inhibition of stretch-activated channels is mediated via actin rearrangement
    • V.I. Chubinskiy-Nadezhdin, Y.A. Negulyaev, and E.A. Morachevskaya Cholesterol depletion-induced inhibition of stretch-activated channels is mediated via actin rearrangement Biochem. Biophys. Res. Commun. 412 2011 80 85
    • (2011) Biochem. Biophys. Res. Commun. , vol.412 , pp. 80-85
    • Chubinskiy-Nadezhdin, V.I.1    Negulyaev, Y.A.2    Morachevskaya, E.A.3
  • 59
    • 0028942853 scopus 로고
    • Mechanosensitive channels
    • H. Sackin Mechanosensitive channels Annu. Rev. Physiol. 57 1995 333 353
    • (1995) Annu. Rev. Physiol. , vol.57 , pp. 333-353
    • Sackin, H.1
  • 60
    • 33745176187 scopus 로고    scopus 로고
    • Mechanosensitive ion channels in skeletal muscle: A link in the membrane pathology of muscular dystrophy
    • DOI 10.1111/j.1440-1681.2006.04393.x
    • J.B. Lansman, and A. Franco-Obregon Mechanosensitive ion channels in skeletal muscle: a link in the membrane pathology of muscular dystrophy Clin. Exp. Pharmacol. Physiol. 33 2006 649 656 (Pubitemid 43894029)
    • (2006) Clinical and Experimental Pharmacology and Physiology , vol.33 , Issue.7 , pp. 649-656
    • Lansman, J.B.1    Franco-Obregon, A.2
  • 61
    • 0027172919 scopus 로고
    • Mechanotransduction across the cell surface and through the cytoskeleton
    • N. Wang, J.P. Butler, and D.E. Ingber Mechanotransduction across the cell surface and through the cytoskeleton Science 260 1993 1124 1127 (Pubitemid 23186787)
    • (1993) Science , vol.260 , Issue.5111 , pp. 1124-1127
    • Wang, N.1    Butler, J.P.2    Ingber, D.E.3
  • 62
    • 33744488545 scopus 로고    scopus 로고
    • Cellular mechanotransduction: Putting all the pieces together again
    • DOI 10.1096/fj.05-5424rev
    • D.E. Ingber Cellular mechanotransduction: putting all the pieces together again FASEB J. 20 2006 811 827 (Pubitemid 44943939)
    • (2006) FASEB Journal , vol.20 , Issue.7 , pp. 811-827
    • Ingber, D.E.1
  • 63
    • 0030899760 scopus 로고    scopus 로고
    • Tensegrity: The architectural basis of cellular mechanotransduction
    • DOI 10.1146/annurev.physiol.59.1.575
    • D.E. Ingber Tensegrity: the architectural basis of cellular mechanotransduction Annu. Rev. Physiol. 59 1997 575 599 (Pubitemid 27142456)
    • (1997) Annual Review of Physiology , vol.59 , pp. 575-599
    • Ingber, D.E.1
  • 64
    • 34047149908 scopus 로고    scopus 로고
    • Activation of mechanosensitive ion channels by forces transmitted through integrins and the cytoskeleton
    • O.P. Hamill, Elsevier San Diego
    • B.D. Matthews, C.K. Thodeti, and D. Ingber Activation of mechanosensitive ion channels by forces transmitted through integrins and the cytoskeleton O.P. Hamill, Mechanosensitive Ion Channels Part A vol. 58 2007 Elsevier San Diego 59 85
    • (2007) Mechanosensitive Ion Channels Part A , vol.58 , pp. 59-85
    • Matthews, B.D.1    Thodeti, C.K.2    Ingber, D.3
  • 65
    • 84892373925 scopus 로고    scopus 로고
    • The role of actin filaments as a force-transmitter and force-sensor
    • M.S. Yong de Shi, Boris Martinac, Keiji Naruse, Wojciech Dzwolak, Shanghai Scientific and Technological Literature Publishing House Shanghai
    • H. Tatsumi, K. Hayakawa, H. Hirata, and M. Sokabe The role of actin filaments as a force-transmitter and force-sensor M.S. Yong de Shi, Boris Martinac, Keiji Naruse, Wojciech Dzwolak, Recent Advances in Mechanobiology vol. 1 2012 Shanghai Scientific and Technological Literature Publishing House Shanghai 153 160
    • (2012) Recent Advances in Mechanobiology , vol.1 , pp. 153-160
    • Tatsumi, H.1    Hayakawa, K.2    Hirata, H.3    Sokabe, M.4
  • 66
    • 40949165235 scopus 로고    scopus 로고
    • Actin stress fibers transmit and focus force to activate mechanosensitive channels
    • DOI 10.1242/jcs.022053
    • K. Hayakawa, H. Tatsumi, and M. Sokabe Actin stress fibers transmit and focus force to activate mechanosensitive channels J. Cell Sci. 121 2008 496 503 (Pubitemid 351405058)
    • (2008) Journal of Cell Science , vol.121 , Issue.4 , pp. 496-503
    • Hayakawa, K.1    Tatsumi, H.2    Sokabe, M.3
  • 67
    • 84869138346 scopus 로고    scopus 로고
    • Molecular force transduction by ion channels: Diversity and unifying principles
    • S. Sukharev, and F. Sachs Molecular force transduction by ion channels: diversity and unifying principles J. Cell Sci. 125 2012 3075 3083
    • (2012) J. Cell Sci. , vol.125 , pp. 3075-3083
    • Sukharev, S.1    Sachs, F.2
  • 68
    • 33645773666 scopus 로고    scopus 로고
    • Local force and geometry sensing regulate cell functions
    • V. Vogel, and M. Sheetz Local force and geometry sensing regulate cell functions Nat. Rev. Mol. Cell Biol. 7 2006 265 275
    • (2006) Nat. Rev. Mol. Cell Biol. , vol.7 , pp. 265-275
    • Vogel, V.1    Sheetz, M.2
  • 69
    • 79251591301 scopus 로고    scopus 로고
    • Visualizing dynamic cytoplasmic forces with a compliance-matched FRET sensor
    • F. Meng, and F. Sachs Visualizing dynamic cytoplasmic forces with a compliance-matched FRET sensor J. Cell Sci. 124 2011 261 269
    • (2011) J. Cell Sci. , vol.124 , pp. 261-269
    • Meng, F.1    Sachs, F.2
  • 70
    • 85027919980 scopus 로고    scopus 로고
    • Real time FRET based detection of mechanical stress in cytoskeletal and extracellular matrix proteins
    • F. Meng, T.M. Suchyna, E. Lazakovitch, R.M. Gronostajski, and F. Sachs Real time FRET based detection of mechanical stress in cytoskeletal and extracellular matrix proteins Cell. Mol. Bioeng. 4 2011 148 159
    • (2011) Cell. Mol. Bioeng. , vol.4 , pp. 148-159
    • Meng, F.1    Suchyna, T.M.2    Lazakovitch, E.3    Gronostajski, R.M.4    Sachs, F.5
  • 71
    • 44349176807 scopus 로고    scopus 로고
    • A fluorescence energy transfer-based mechanical stress sensor for specific proteins in situ
    • DOI 10.1111/j.1742-4658.2008.06461.x
    • F. Meng, T.M. Suchyna, and F. Sachs A fluorescence energy transfer-based mechanical stress sensor for specific proteins in situ FEBS J. 275 2008 3072 3087 (Pubitemid 351743583)
    • (2008) FEBS Journal , vol.275 , Issue.12 , pp. 3072-3087
    • Meng, F.1    Suchyna, T.M.2    Sachs, F.3
  • 73
    • 79960098421 scopus 로고    scopus 로고
    • Genetically encoded force sensors for measuring mechanical forces in proteins
    • Y. Wang, F. Meng, and F. Sachs Genetically encoded force sensors for measuring mechanical forces in proteins Commun. Integr. Biol. 4 2011 385 390
    • (2011) Commun. Integr. Biol. , vol.4 , pp. 385-390
    • Wang, Y.1    Meng, F.2    Sachs, F.3
  • 74
    • 84858122144 scopus 로고    scopus 로고
    • Measuring strain of structural proteins in vivo in real time
    • P. Kohl, F. Sachs, M.R. Franz, Oxford University Press Oxford
    • F. Meng, and F. Sachs Measuring strain of structural proteins in vivo in real time P. Kohl, F. Sachs, M.R. Franz, Cardiac Mechano-electric Coupling and Arrhythmia: From Pipette to Patient 2011 Oxford University Press Oxford 431 434
    • (2011) Cardiac Mechano-electric Coupling and Arrhythmia: From Pipette to Patient , pp. 431-434
    • Meng, F.1    Sachs, F.2
  • 75
    • 0024536382 scopus 로고
    • Genetic control of differentiation of the Caenorhabditis elegans touch receptor neuronsw
    • M. Chalfie, and M. Au Genetic control of differentiation of the Caenorhabditis elegans touch receptor neurons Science 243 1989 1027 1033 (Pubitemid 19072579)
    • (1989) Science , vol.243 , Issue.4894 , pp. 1027-1033
    • Chalfie, M.1    Au, M.2
  • 76
    • 0028157551 scopus 로고
    • A transmembrane domain of the putative channel subunit MEC-4 influences mechanotransduction and neurodegeneration in C. Elegans
    • DOI 10.1038/367470a0
    • K. Hong, and M. Driscoll A transmembrane domain of the putative channel subunit MEC-4 influences mechanotransduction and neurodegeneration in C. elegans Nature 367 1994 470 473 (Pubitemid 24046050)
    • (1994) Nature , vol.367 , Issue.6462 , pp. 470-473
    • Hong, K.1    Driscoll, M.2
  • 77
    • 0037607542 scopus 로고    scopus 로고
    • Transducing Touch in Caenorhabditis elegans
    • DOI 10.1146/annurev.physiol.65.092101.142659
    • M.B. Goodman, and E.M. Schwarz Transducing touch in Caenorhabditis elegans Annu. Rev. Physiol. 65 2003 429 452 (Pubitemid 38249162)
    • (2003) Annual Review of Physiology , vol.65 , pp. 429-452
    • Goodman, M.B.1    Schwarz, E.M.2
  • 78
    • 83755191975 scopus 로고    scopus 로고
    • Mechanosensory transduction
    • M. Montal, Elsevier Amsterdam
    • B. Martinac, and A. Kloda Mechanosensory transduction M. Montal, Comprehensive Biophysics vol. 6(18) 2011 Elsevier Amsterdam 1 55
    • (2011) Comprehensive Biophysics , vol.618 , pp. 1-55
    • Martinac, B.1    Kloda, A.2
  • 79
    • 0036307827 scopus 로고    scopus 로고
    • Epithelial sodium channel/degenerin family of ion channels: A variety of functions for a shared structure
    • S. Kellenberger, and L. Schild Epithelial sodium channel/degenerin family of ion channels: a variety of functions for a shared structure Physiol. Rev. 82 2002 735 767 (Pubitemid 34743337)
    • (2002) Physiological Reviews , vol.82 , Issue.3 , pp. 735-767
    • Kellenberger, S.1    Schild, L.2
  • 81
    • 0030033429 scopus 로고    scopus 로고
    • Gating of Na channels in the rat cortical collecting tubule: Effects of voltage and membrane stretch
    • DOI 10.1085/jgp.107.1.35
    • L.G. Palmer, and G. Frindt Gating of Na channels in the rat cortical collecting tubule: effects of voltage and membrane stretch J. Gen. Physiol. 107 1996 35 45 (Pubitemid 26028779)
    • (1996) Journal of General Physiology , vol.107 , Issue.1 , pp. 35-45
    • Palmer, L.G.1    Frindt, G.2
  • 82
    • 4043098394 scopus 로고    scopus 로고
    • Steroids and exogenous γ-ENaC subunit modulate cation channels formed by α-ENaC in human B lymphocytes
    • DOI 10.1074/jbc.M405455200
    • H.P. Ma, O. Al-Khalili, S. Ramosevac, S. Saxena, Y.Y. Liang, D.G. Warnock, and D.C. Eaton Steroids and exogenous gamma-ENaC subunit modulate cation channels formed by alpha-ENaC in human B lymphocytes J. Biol. Chem. 279 2004 33206 33212 (Pubitemid 39062966)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.32 , pp. 33206-33212
    • Ma, H.-P.1    Al-Khalili, O.2    Ramosevac, S.3    Saxena, S.4    Liang, Y.-Y.5    Warnock, D.G.6    Eaton, D.C.7
  • 83
    • 14244258187 scopus 로고    scopus 로고
    • Mutations in the pore region modify epithelial sodium channel gating by shear stress
    • DOI 10.1074/jbc.M413123200
    • M.D. Carattino, S. Sheng, and T.R. Kleyman Mutations in the pore region modify epithelial sodium channel gating by shear stress J. Biol. Chem. 280 2005 4393 4401 (Pubitemid 40288603)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.6 , pp. 4393-4401
    • Carattino, M.D.1    Sheng, S.2    Kleyman, T.R.3
  • 84
    • 2942659140 scopus 로고    scopus 로고
    • ENaC-membrane interactions: Regulation of channel activity by membrane order
    • DOI 10.1085/jgp.200308983
    • M.S. Awayda, W. Shao, F. Guo, M. Zeidel, and W.G. Hill ENaC-membrane interactions: regulation of channel activity by membrane order J. Gen. Physiol. 123 2004 709 727 (Pubitemid 38781376)
    • (2004) Journal of General Physiology , vol.123 , Issue.6 , pp. 709-727
    • Awayda, M.S.1    Shao, W.2    Guo, F.3    Zeidel, M.4    Hill, W.G.5
  • 85
    • 7244260316 scopus 로고    scopus 로고
    • + channel proteins: Components of a vascular mechanosensor
    • DOI 10.1161/01.HYP.0000144465.56360.ad
    • + channel proteins: components of a vascular mechanosensor Hypertension 44 2004 643 648 (Pubitemid 39435233)
    • (2004) Hypertension , vol.44 , Issue.5 , pp. 643-648
    • Drummond, H.A.1    Gebremedhin, D.2    Harder, D.R.3
  • 87
    • 23644451510 scopus 로고    scopus 로고
    • A possible unifying principle for mechanosensation
    • DOI 10.1038/nature03896
    • C. Kung A possible unifying principle for mechanosensation Nature 436 2005 647 654 (Pubitemid 41117260)
    • (2005) Nature , vol.436 , Issue.7051 , pp. 647-654
    • Kung, C.1
  • 88
    • 84907114882 scopus 로고
    • Biophysics of mechanoreception
    • F. Sachs Biophysics of mechanoreception Membr. Biochem. 6 1986 173 195
    • (1986) Membr. Biochem. , vol.6 , pp. 173-195
    • Sachs, F.1
  • 89
    • 34047128546 scopus 로고    scopus 로고
    • Force from lipids: Physical principles of gating mechanosensitive channels by mechanical force revealed by chemical manipulation of cellular membranes
    • B. Martinac Force from lipids: physical principles of gating mechanosensitive channels by mechanical force revealed by chemical manipulation of cellular membranes Chem. Educ. 10 2 2005 107 114
    • (2005) Chem. Educ. , vol.10 , Issue.2 , pp. 107-114
    • Martinac, B.1
  • 91
    • 17044401714 scopus 로고    scopus 로고
    • In search of the hair-cell gating spring elastic properties of ankyrin and cadherin repeats
    • M. Sotomayor, D.P. Corey, and K. Schulten In search of the hair-cell gating spring elastic properties of ankyrin and cadherin repeats Structure 13 2005 669 682
    • (2005) Structure , vol.13 , pp. 669-682
    • Sotomayor, M.1    Corey, D.P.2    Schulten, K.3
  • 92
    • 38449107210 scopus 로고    scopus 로고
    • Nanoscale organization of the MEC-4 DEG/ENaC sensory mechanotransduction channel in Caenorhabditis elegans touch receptor neurons
    • DOI 10.1523/JNEUROSCI.4179-07.2007
    • J.G. Cueva, A. Mulholland, and M.B. Goodman Nanoscale organization of the MEC-4 DEG/ENaC sensory mechanotransduction channel in Caenorhabditis elegans touch receptor neurons J. Neurosci. 27 2007 14089 14098 (Pubitemid 351377855)
    • (2007) Journal of Neuroscience , vol.27 , Issue.51 , pp. 14089-14098
    • Cueva, J.G.1    Mulholland, A.2    Goodman, M.B.3
  • 95
    • 0028943223 scopus 로고
    • Characterization of mechanosensitive channels in Escherichia coli cytoplasmic membrane by whole-cell patch clamp recording
    • C. Cui, D.O. Smith, and J. Adler Characterization of mechanosensitive channels in Escherichia coli cytoplasmic membrane by whole-cell patch clamp recording J. Membr. Biol. 144 1995 31 42
    • (1995) J. Membr. Biol. , vol.144 , pp. 31-42
    • Cui, C.1    Smith, D.O.2    Adler, J.3
  • 96
    • 0037155047 scopus 로고    scopus 로고
    • Transient receptor potential channels regulate myogenic tone of resistance arteries
    • DOI 10.1161/hh0302.105662
    • D.G. Welsh, A.D. Morielli, M.T. Nelson, and J.E. Brayden Transient receptor potential channels regulate myogenic tone of resistance arteries Circ. Res. 90 2002 248 250 (Pubitemid 34633924)
    • (2002) Circulation Research , vol.90 , Issue.3 , pp. 248-250
    • Welsh, D.G.1    Morielli, A.D.2    Nelson, M.T.3    Brayden, J.E.4
  • 101
    • 84865478995 scopus 로고    scopus 로고
    • Adjoint variable method for two-dimensional plasmonic structures
    • O.S. Ahmed, M.H. Bakr, X. Li, and T. Nomura Adjoint variable method for two-dimensional plasmonic structures Opt. Lett. 37 2012 3453 3455
    • (2012) Opt. Lett. , vol.37 , pp. 3453-3455
    • Ahmed, O.S.1    Bakr, M.H.2    Li, X.3    Nomura, T.4
  • 102
    • 0242266967 scopus 로고    scopus 로고
    • TRPV2 Is a Component of Osmotically Sensitive Cation Channels in Murine Aortic Myocytes
    • DOI 10.1161/01.RES.0000097263.10220.0C
    • K. Muraki, Y. Iwata, Y. Katanosaka, T. Ito, S. Ohya, M. Shigekawa, and Y. Imaizumi TRPV2 is a component of osmotically sensitive cation channels in murine aortic myocytes Circ. Res. 93 2003 829 838 (Pubitemid 37363057)
    • (2003) Circulation Research , vol.93 , Issue.9 , pp. 829-838
    • Muraki, K.1    Iwata, Y.2    Katanosaka, Y.3    Ito, T.4    Ohya, S.5    Shigekawa, M.6    Imaizumi, Y.7
  • 103
    • 35748985570 scopus 로고    scopus 로고
    • Transient receptor potential channels in mechanosensing and cell volume regulation
    • S.F. Pedersen, and B. Nilius Transient receptor potential channels in mechanosensing and cell volume regulation Methods Enzymol. 428 2007 183 207
    • (2007) Methods Enzymol. , vol.428 , pp. 183-207
    • Pedersen, S.F.1    Nilius, B.2
  • 106
    • 34247372291 scopus 로고    scopus 로고
    • Membrane stretch-induced activation of a TRPM4-like nonselective cation channel in cerebral artery myocytes
    • DOI 10.1254/jphs.FP0061332
    • H. Morita, A. Honda, R. Inoue, Y. Ito, K. Abe, M.T. Nelson, and J.E. Brayden Membrane stretch-induced activation of a TRPM4-like nonselective cation channel in cerebral artery myocytes J. Pharmacol. Sci. 103 2007 417 426 (Pubitemid 46640694)
    • (2007) Journal of Pharmacological Sciences , vol.103 , Issue.4 , pp. 417-426
    • Morita, H.1    Honda, A.2    Inoue, R.3    Ito, Y.4    Abe, K.5    Nelson, M.T.6    Brayden, J.E.7
  • 107
    • 14944348415 scopus 로고    scopus 로고
    • Activation of the melastatin-related cation channel TRMP3 by D-erytho-sphingosine
    • DOI 10.1124/mol.104.006734
    • C. Grimm, R. Kraft, G. Schultz, and C. Harteneck Activation of the melastatin-related cation channel TRPM3 by d-erythro-sphingosine [corrected] Mol. Pharmacol. 67 2005 798 805 (Pubitemid 40365327)
    • (2005) Molecular Pharmacology , vol.67 , Issue.3 , pp. 798-805
    • Grimm, C.1    Kraft, R.2    Schultz, G.3    Harteneck, C.4
  • 108
  • 109
    • 0038498142 scopus 로고    scopus 로고
    • Molecular and functional characterization of the melastatin-related cation channel TRPM3
    • DOI 10.1074/jbc.M300945200
    • C. Grimm, R. Kraft, S. Sauerbruch, G. Schultz, and C. Harteneck Molecular and functional characterization of the melastatin-related cation channel TRPM3 J. Biol. Chem. 278 2003 21493 21501 (Pubitemid 36792546)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.24 , pp. 21493-21501
    • Grimm, C.1    Kraft, R.2    Sauerbruch, S.3    Schultz, G.4    Harteneck, C.5
  • 111
    • 0041831249 scopus 로고    scopus 로고
    • The renal cell primary cilium functions as a flow sensor
    • DOI 10.1097/00041552-200309000-00006
    • H.A. Praetorius, and K.R. Spring The renal cell primary cilium functions as a flow sensor Curr. Opin. Nephrol. Hypertens. 12 2003 517 520 (Pubitemid 37083112)
    • (2003) Current Opinion in Nephrology and Hypertension , vol.12 , Issue.5 , pp. 517-520
    • Praetorius, H.A.1    Spring, K.R.2
  • 112
    • 84867288262 scopus 로고    scopus 로고
    • Photomechanical responses in Drosophila photoreceptors
    • R.C. Hardie, and K. Franze Photomechanical responses in Drosophila photoreceptors Science 338 2012 260 263
    • (2012) Science , vol.338 , pp. 260-263
    • Hardie, R.C.1    Franze, K.2
  • 115
    • 0035371189 scopus 로고    scopus 로고
    • + channels
    • DOI 10.1016/S0166-2236(00)01810-5, PII S0166223600018105
    • + channels Trends Neurosci. 24 2001 339 346 (Pubitemid 32455435)
    • (2001) Trends in Neurosciences , vol.24 , Issue.6 , pp. 339-346
    • Patel, A.J.1    Honore, E.2
  • 117
    • 23744506839 scopus 로고    scopus 로고
    • 2P channel TREK-1 and the actin cytoskeleton
    • DOI 10.1038/sj.embor.7400449
    • I. Lauritzen, J. Chemin, E. Honore, M. Jodar, N. Guy, M. Lazdunski, and A. Jane Patel Cross-talk between the mechano-gated K2P channel TREK-1 and the actin cytoskeleton EMBO Rep. 6 2005 642 648 (Pubitemid 41122432)
    • (2005) EMBO Reports , vol.6 , Issue.7 , pp. 642-648
    • Lauritzen, I.1    Chemin, J.2    Honore, E.3    Jodar, M.4    Guy, N.5    Lazdunski, M.6    Patel, A.J.7
  • 118
    • 34147116791 scopus 로고    scopus 로고
    • Regulation of the mechano-gated K2P channel TREK-1 by membrane phospholipids
    • O.P. Hamill, Academic Press San Diego
    • J. Chemin, A.J. Patel, P. Delmas, F. Sachs, M. Lazdunski, and E. Honore Regulation of the mechano-gated K2P channel TREK-1 by membrane phospholipids O.P. Hamill, Mechanosensitive Ion Channels Part B vol. 59 2007 Academic Press San Diego 155 189
    • (2007) Mechanosensitive Ion Channels Part B , vol.59 , pp. 155-189
    • Chemin, J.1    Patel, A.J.2    Delmas, P.3    Sachs, F.4    Lazdunski, M.5    Honore, E.6
  • 122
    • 79960498823 scopus 로고    scopus 로고
    • The mechanosensitive ion channel Piezo1 is inhibited by the peptide GsMTx4
    • C. Bae, F. Sachs, and P.A. Gottlieb The mechanosensitive ion channel Piezo1 is inhibited by the peptide GsMTx4 Biochemistry 50 2011 6295 6300
    • (2011) Biochemistry , vol.50 , pp. 6295-6300
    • Bae, C.1    Sachs, F.2    Gottlieb, P.A.3
  • 123
    • 33846426807 scopus 로고    scopus 로고
    • Mechanosensitive ion channels and the peptide inhibitor GsMTx-4: History, properties, mechanisms and pharmacology
    • DOI 10.1016/j.toxicon.2006.09.030, PII S0041010106003564
    • C.L. Bowman, P.A. Gottlieb, T.M. Suchyna, Y.K. Murphy, and F. Sachs Mechanosensitive ion channels and the peptide inhibitor GsMTx-4: history, properties, mechanisms and pharmacology Toxicon 49 2007 249 270 (Pubitemid 46148998)
    • (2007) Toxicon , vol.49 , Issue.2 , pp. 249-270
    • Bowman, C.L.1    Gottlieb, P.A.2    Suchyna, T.M.3    Murphy, Y.K.4    Sachs, F.5
  • 124
    • 84865295955 scopus 로고    scopus 로고
    • Piezo1: Properties of a cation selective mechanical channel
    • P.A. Gottlieb, and F. Sachs Piezo1: properties of a cation selective mechanical channel Channels (Austin) 6 2012 214 219
    • (2012) Channels (Austin) , vol.6 , pp. 214-219
    • Gottlieb, P.A.1    Sachs, F.2
  • 125
    • 84865297043 scopus 로고    scopus 로고
    • Gating the mechanical channel Piezo1: A comparison between whole-cell and patch recording
    • P.A. Gottlieb, C. Bae, and F. Sachs Gating the mechanical channel Piezo1: a comparison between whole-cell and patch recording Channels (Austin) 6 2012 282 289
    • (2012) Channels (Austin) , vol.6 , pp. 282-289
    • Gottlieb, P.A.1    Bae, C.2    Sachs, F.3
  • 126
    • 84876440709 scopus 로고    scopus 로고
    • Touch sense: Functional organization and molecular determinants of mechanosensitive receptors
    • Y. Roudaut, A. Lonigro, B. Coste, J. Hao, P. Delmas, and M. Crest Touch sense: functional organization and molecular determinants of mechanosensitive receptors Channels (Austin) 6 2012 234 245
    • (2012) Channels (Austin) , vol.6 , pp. 234-245
    • Roudaut, Y.1    Lonigro, A.2    Coste, B.3    Hao, J.4    Delmas, P.5    Crest, M.6
  • 128
    • 24644491716 scopus 로고    scopus 로고
    • Assessment of potential stimuli for mechano-dependent gating of MscL: Effects of pressure, tension, and lipid headgroups
    • DOI 10.1021/bi0509649
    • P. Moe, and P. Blount Assessment of potential stimuli for mechano-dependent gating of MscL: effects of pressure, tension, and lipid headgroups Biochemistry 44 2005 12239 12244 (Pubitemid 41285722)
    • (2005) Biochemistry , vol.44 , Issue.36 , pp. 12239-12244
    • Moe, P.1    Blount, P.2
  • 130
    • 33845355027 scopus 로고    scopus 로고
    • Interaction of epithelial ion channels with the actin-based cytoskeleton
    • C. Mazzochi, D.J. Benos, and P.R. Smith Interaction of epithelial ion channels with the actin-based cytoskeleton Am. J. Physiol. Renal Physiol. 291 2006 F1113 F1122
    • (2006) Am. J. Physiol. Renal Physiol. , vol.291
    • Mazzochi, C.1    Benos, D.J.2    Smith, P.R.3
  • 131
    • 33646580380 scopus 로고    scopus 로고
    • The carboxyl terminus of the α-subunit of the amiloride-sensitive epithelial sodium channel binds to F-actin
    • DOI 10.1074/jbc.M509386200
    • C. Mazzochi, J.K. Bubien, P.R. Smith, and D.J. Benos The carboxyl terminus of the alpha-subunit of the amiloride-sensitive epithelial sodium channel binds to F-actin J. Biol. Chem. 281 2006 6528 6538 (Pubitemid 43847586)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.10 , pp. 6528-6538
    • Mazzochi, C.1    Bubien, J.K.2    Smith, P.R.3    Benos, D.J.4
  • 135
    • 33846807748 scopus 로고    scopus 로고
    • Transient receptor potential cation channels in disease
    • DOI 10.1152/physrev.00021.2006
    • B. Nilius, G. Owsianik, T. Voets, and J.A. Peters Transient receptor potential cation channels in disease Physiol. Rev. 87 2007 165 217 (Pubitemid 46207713)
    • (2007) Physiological Reviews , vol.87 , Issue.1 , pp. 165-217
    • Nilius, B.1    Owsianik, G.2    Voets, T.3    Peters, J.A.4
  • 137
    • 33745976773 scopus 로고    scopus 로고
    • 2 + signaling
    • 2 + signaling Cell Calcium 40 2006 261 275
    • (2006) Cell Calcium , vol.40 , pp. 261-275
    • Minke, B.1
  • 138
    • 11144258738 scopus 로고    scopus 로고
    • Block of native and cloned vanilloid receptor 1 (TRPV1) by aminoglycoside antibiotics
    • DOI 10.1016/j.pain.2004.09.042, PII S0304395904004828
    • M. Raisinghani, and L.S. Premkumar Block of native and cloned vanilloid receptor 1 (TRPV1) by aminoglycoside antibiotics Pain 113 2005 123 133 (Pubitemid 40038453)
    • (2005) Pain , vol.113 , Issue.1-2 , pp. 123-133
    • Raisinghani, M.1    Premkumar, L.S.2
  • 139
    • 0033162068 scopus 로고    scopus 로고
    • Translocation of a calcium-permeable cation channel induced by insulin-like growth factor-I
    • M. Kanzaki, Y.Q. Zhang, H. Mashima, L. Li, H. Shibata, and I. Kojima Translocation of a calcium-permeable cation channel induced by insulin-like growth factor-I Nat. Cell Biol. 1 1999 165 170 (Pubitemid 129656021)
    • (1999) Nature Cell Biology , vol.1 , Issue.3 , pp. 165-170
    • Kanzaki, M.1    Zhang, Y.-Q.2    Mashima, H.3    Li, L.4    Shibata, H.5    Kojima, I.6
  • 143
    • 33846940717 scopus 로고    scopus 로고
    • Insights into TRPM4 function, regulation and physiological role
    • R. Vennekens, and B. Nilius Insights into TRPM4 function, regulation and physiological role Handb. Exp. Pharmacol. 2007 269 285
    • (2007) Handb. Exp. Pharmacol. , pp. 269-285
    • Vennekens, R.1    Nilius, B.2
  • 145
    • 84874432860 scopus 로고    scopus 로고
    • Sphingosine and FTY720 are potent inhibitors of the transient receptor potential melastatin 7 (TRPM7) channels
    • X. Qin, Z. Yue, B. Sun, W. Yang, J. Xie, E. Ni, Y. Feng, R. Mahmood, Y. Zhang, and L. Yue Sphingosine and FTY720 are potent inhibitors of the transient receptor potential melastatin 7 (TRPM7) channels Br. J. Pharmacol. 168 2013 1294 1312
    • (2013) Br. J. Pharmacol. , vol.168 , pp. 1294-1312
    • Qin, X.1    Yue, Z.2    Sun, B.3    Yang, W.4    Xie, J.5    Ni, E.6    Feng, Y.7    Mahmood, R.8    Zhang, Y.9    Yue, L.10
  • 146
    • 33846312821 scopus 로고    scopus 로고
    • TRPM7 is a stretch- and swelling-activated cation channel involved in volume regulation in human epithelial cells
    • T. Numata, T. Shimizu, and Y. Okada TRPM7 is a stretch- and swelling-activated cation channel involved in volume regulation in human epithelial cells Am. J. Physiol. Cell Physiol. 292 2007 C460 C467
    • (2007) Am. J. Physiol. Cell Physiol. , vol.292
    • Numata, T.1    Shimizu, T.2    Okada, Y.3
  • 147
    • 70350339080 scopus 로고    scopus 로고
    • Polycystins under pressure
    • B. Nilius Polycystins under pressure Cell 139 2009 466 467
    • (2009) Cell , vol.139 , pp. 466-467
    • Nilius, B.1
  • 149
    • 79960011784 scopus 로고    scopus 로고
    • Structural model of the TRPP2/PKD1 C-terminal coiled-coil complex produced by a combined computational and experimental approach
    • J. Zhu, Y. Yu, M.H. Ulbrich, M.H. Li, E.Y. Isacoff, B. Honig, and J. Yang Structural model of the TRPP2/PKD1 C-terminal coiled-coil complex produced by a combined computational and experimental approach Proc. Natl. Acad. Sci. U. S. A. 108 2011 10133 10138
    • (2011) Proc. Natl. Acad. Sci. U. S. A. , vol.108 , pp. 10133-10138
    • Zhu, J.1    Yu, Y.2    Ulbrich, M.H.3    Li, M.H.4    Isacoff, E.Y.5    Honig, B.6    Yang, J.7
  • 153
    • 0033679959 scopus 로고    scopus 로고
    • Molecular and functional properties of two-pore-domain potassium channels
    • F. Lesage, and M. Lazdunski Molecular and functional properties of two-pore-domain potassium channels Am. J. Physiol. Renal Physiol. 279 2000 F793 F801
    • (2000) Am. J. Physiol. Renal Physiol. , vol.279
    • Lesage, F.1    Lazdunski, M.2
  • 155
    • 0033578649 scopus 로고    scopus 로고
    • Mechano- or acid stimulation, two interactive modes of activation of the TREK-1 potassium channel
    • F. Maingret, A.J. Patel, F. Lesage, M. Lazdunski, and E. Honore Mechano- or acid stimulation, two interactive modes of activation of the TREK-1 potassium channel J. Biol. Chem. 274 1999 26691 26696
    • (1999) J. Biol. Chem. , vol.274 , pp. 26691-26696
    • Maingret, F.1    Patel, A.J.2    Lesage, F.3    Lazdunski, M.4    Honore, E.5
  • 157
    • 55749097445 scopus 로고    scopus 로고
    • Polymodal regulation of NMDA receptor channels
    • A. Kloda, B. Martinac, and D.J. Adams Polymodal regulation of NMDA receptor channels Channels (Austin) 1 2007 334 343
    • (2007) Channels (Austin) , vol.1 , pp. 334-343
    • Kloda, A.1    Martinac, B.2    Adams, D.J.3
  • 158
    • 78149349552 scopus 로고    scopus 로고
    • Mechanosensitive channels: In touch with Piezo
    • R. Xiao, and X.Z. Xu Mechanosensitive channels: in touch with Piezo Curr. Biol. 20 2010 R936 R938
    • (2010) Curr. Biol. , vol.20
    • Xiao, R.1    Xu, X.Z.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.