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Volumn 8, Issue 6, 2013, Pages

Functional Characterization of the Cardiac Ryanodine Receptor Pore-Forming Region

Author keywords

[No Author keywords available]

Indexed keywords

PHOSPHOLIPID; POTASSIUM CHANNEL; RYANODINE RECEPTOR 2;

EID: 84878918033     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0066542     Document Type: Article
Times cited : (7)

References (36)
  • 1
    • 0037049977 scopus 로고    scopus 로고
    • Cardiac excitation-contraction coupling
    • Bers DM, (2002) Cardiac excitation-contraction coupling. Nature 415: 198-205.
    • (2002) Nature , vol.415 , pp. 198-205
    • Bers, D.M.1
  • 2
    • 16644368098 scopus 로고    scopus 로고
    • A model of the putative pore region of the cardiac ryanodine receptor channel
    • Welch W, Rheault S, West DJ, Williams AJ, (2004) A model of the putative pore region of the cardiac ryanodine receptor channel. Biophys J 87: 2335-2351.
    • (2004) Biophys J , vol.87 , pp. 2335-2351
    • Welch, W.1    Rheault, S.2    West, D.J.3    Williams, A.J.4
  • 3
    • 66249106753 scopus 로고    scopus 로고
    • A structural model of the pore-forming region of the skeletal muscle ryanodine receptor (RyR1)
    • Ramachandran S, Serohijos AW, Xu L, Meissner G, Dokholyan NV, (2009) A structural model of the pore-forming region of the skeletal muscle ryanodine receptor (RyR1). PLoS Comput Biol 5: e1000367.
    • (2009) PLoS Comput Biol , vol.5
    • Ramachandran, S.1    Serohijos, A.W.2    Xu, L.3    Meissner, G.4    Dokholyan, N.V.5
  • 5
    • 22444444618 scopus 로고    scopus 로고
    • Internal structure and visualization of transmembrane domains of the RyR1 calcium release channel by cryo-EM
    • Samso M, Wagenknecht T, Allen PD, (2005) Internal structure and visualization of transmembrane domains of the RyR1 calcium release channel by cryo-EM. Nat Struct Mol Biol 12: 539-544.
    • (2005) Nat Struct Mol Biol , vol.12 , pp. 539-544
    • Samso, M.1    Wagenknecht, T.2    Allen, P.D.3
  • 6
    • 67649637588 scopus 로고    scopus 로고
    • Coordinated movement of cytoplasmic and transmembrane domains of RyR1 upon gating
    • Samso M, Feng W, Pessah IN, Allen PD, (2009) Coordinated movement of cytoplasmic and transmembrane domains of RyR1 upon gating. PLoS Biol 7: e85.
    • (2009) PLoS Biol , vol.7
    • Samso, M.1    Feng, W.2    Pessah, I.N.3    Allen, P.D.4
  • 9
    • 77957924708 scopus 로고    scopus 로고
    • Solution structure and phospholipid interactions of the isolated voltage-sensor domain from KvAP
    • Butterwick JA, MacKinnon R, (2010) Solution structure and phospholipid interactions of the isolated voltage-sensor domain from KvAP. J Mol Biol 403: 591-606.
    • (2010) J Mol Biol , vol.403 , pp. 591-606
    • Butterwick, J.A.1    MacKinnon, R.2
  • 10
    • 79955549892 scopus 로고    scopus 로고
    • Simplified bacterial "pore" channel provides insight into the assembly, stability, and structure of sodium channels
    • McCusker EC, D'Avanzo N, Nichols CG, Wallace BA, (2011) Simplified bacterial "pore" channel provides insight into the assembly, stability, and structure of sodium channels. J Biol Chem 286: 16386-16391.
    • (2011) J Biol Chem , vol.286 , pp. 16386-16391
    • McCusker, E.C.1    D'Avanzo, N.2    Nichols, C.G.3    Wallace, B.A.4
  • 11
    • 59649113542 scopus 로고    scopus 로고
    • Molecular template for a voltage sensor in a novel K+ channel. III. Functional reconstitution of a sensorless pore module from a prokaryotic Kv channel
    • Santos JS, Grigoriev SM, Montal M, (2008) Molecular template for a voltage sensor in a novel K+ channel. III. Functional reconstitution of a sensorless pore module from a prokaryotic Kv channel. J Gen Physiol 132: 651-666.
    • (2008) J Gen Physiol , vol.132 , pp. 651-666
    • Santos, J.S.1    Grigoriev, S.M.2    Montal, M.3
  • 12
    • 57749196006 scopus 로고    scopus 로고
    • Sensing voltage across lipid membranes
    • Swartz KJ, (2008) Sensing voltage across lipid membranes. Nature 456: 891-897.
    • (2008) Nature , vol.456 , pp. 891-897
    • Swartz, K.J.1
  • 13
    • 79961050460 scopus 로고    scopus 로고
    • Voltage-gated sodium channel (NaV) protein dissection creates a set of functional pore-only proteins
    • Shaya D, Kreir M, Robbins RA, Wong S, Hammon J, et al. (2011) Voltage-gated sodium channel (NaV) protein dissection creates a set of functional pore-only proteins. Proc Natl Acad Sci U S A.
    • (2011) Proc Natl Acad Sci U S A
    • Shaya, D.1    Kreir, M.2    Robbins, R.A.3    Wong, S.4    Hammon, J.5
  • 14
    • 0025193465 scopus 로고
    • Ca2(+)-activated K+ current involvement in neuronal function revealed by in situ single-channel analysis in Helix neurones
    • Gola M, Ducreux C, Chagneux H, (1990) Ca2(+)-activated K+ current involvement in neuronal function revealed by in situ single-channel analysis in Helix neurones. J Physiol 420: 73-109.
    • (1990) J Physiol , vol.420 , pp. 73-109
    • Gola, M.1    Ducreux, C.2    Chagneux, H.3
  • 15
    • 0003443746 scopus 로고    scopus 로고
    • 3rd Edition, Chapter 12: Sunderland, MA: Sinauer Associates, Inc
    • Hille B (2001) Ion Channels in Excitable Membranes, 3rd Edition, Chapter 12: Sunderland, MA: Sinauer Associates, Inc.
    • (2001) Ion Channels in Excitable Membranes
    • Hille, B.1
  • 16
    • 0027939709 scopus 로고
    • Modification of the gating of the cardiac sarcoplasmic reticulum Ca(2+)-release channel by H2O2 and dithiothreitol
    • Boraso A, Williams AJ, (1994) Modification of the gating of the cardiac sarcoplasmic reticulum Ca(2+)-release channel by H2O2 and dithiothreitol. Am J Physiol 267: H1010-1016.
    • (1994) Am J Physiol , vol.267
    • Boraso, A.1    Williams, A.J.2
  • 17
    • 34548690336 scopus 로고    scopus 로고
    • Overexpression and purification of the RyR1 pore-forming region
    • Kang GB, Song HE, Song DW, Kim MK, Rho SH, et al. (2007) Overexpression and purification of the RyR1 pore-forming region. Protein Pept Lett 14: 742-746.
    • (2007) Protein Pept Lett , vol.14 , pp. 742-746
    • Kang, G.B.1    Song, H.E.2    Song, D.W.3    Kim, M.K.4    Rho, S.H.5
  • 18
    • 0026673801 scopus 로고
    • A model for ionic conduction in the ryanodine receptor channel of sheep cardiac muscle sarcoplasmic reticulum
    • Tinker A, Lindsay AR, Williams AJ, (1992) A model for ionic conduction in the ryanodine receptor channel of sheep cardiac muscle sarcoplasmic reticulum. J Gen Physiol 100: 495-517.
    • (1992) J Gen Physiol , vol.100 , pp. 495-517
    • Tinker, A.1    Lindsay, A.R.2    Williams, A.J.3
  • 19
    • 0025913205 scopus 로고
    • Monovalent cation conductance in the ryanodine receptor-channel of sheep cardiac muscle sarcoplasmic reticulum
    • Lindsay AR, Manning SD, Williams AJ, (1991) Monovalent cation conductance in the ryanodine receptor-channel of sheep cardiac muscle sarcoplasmic reticulum. J Physiol 439: 463-480.
    • (1991) J Physiol , vol.439 , pp. 463-480
    • Lindsay, A.R.1    Manning, S.D.2    Williams, A.J.3
  • 20
    • 0034981326 scopus 로고    scopus 로고
    • Light at the end of the Ca(2+)-release channel tunnel: structures and mechanisms involved in ion translocation in ryanodine receptor channels
    • Williams AJ, West DJ, Sitsapesan R, (2001) Light at the end of the Ca(2+)-release channel tunnel: structures and mechanisms involved in ion translocation in ryanodine receptor channels. Q Rev Biophys 34: 61-104.
    • (2001) Q Rev Biophys , vol.34 , pp. 61-104
    • Williams, A.J.1    West, D.J.2    Sitsapesan, R.3
  • 21
    • 34548405635 scopus 로고    scopus 로고
    • Pharmacological regulators of intracellular calcium release channels
    • West DJ, Williams AJ, (2007) Pharmacological regulators of intracellular calcium release channels. Curr Pharm Des 13: 2428-2442.
    • (2007) Curr Pharm Des , vol.13 , pp. 2428-2442
    • West, D.J.1    Williams, A.J.2
  • 22
    • 84866323507 scopus 로고    scopus 로고
    • The contribution of hydrophobic residues in the pore-forming region of the ryanodine receptor channel to block by large tetraalkylammonium cations and Shaker B inactivation peptides
    • Mason SA, Viero C, Euden J, Bannister M, West D, et al. (2012) The contribution of hydrophobic residues in the pore-forming region of the ryanodine receptor channel to block by large tetraalkylammonium cations and Shaker B inactivation peptides. J Gen Physiol 140: 325-339.
    • (2012) J Gen Physiol , vol.140 , pp. 325-339
    • Mason, S.A.1    Viero, C.2    Euden, J.3    Bannister, M.4    West, D.5
  • 23
    • 0036212694 scopus 로고    scopus 로고
    • Block of the ryanodine receptor channel by neomycin is relieved at high holding potentials
    • Mead F, Williams AJ, (2002) Block of the ryanodine receptor channel by neomycin is relieved at high holding potentials. Biophys J 82: 1953-1963.
    • (2002) Biophys J , vol.82 , pp. 1953-1963
    • Mead, F.1    Williams, A.J.2
  • 24
    • 0033616799 scopus 로고    scopus 로고
    • Luminal loop of the ryanodine receptor: a pore-forming segment?
    • Balshaw D, Gao L, Meissner G, (1999) Luminal loop of the ryanodine receptor: a pore-forming segment? Proc Natl Acad Sci U S A 96: 3345-3347.
    • (1999) Proc Natl Acad Sci U S A , vol.96 , pp. 3345-3347
    • Balshaw, D.1    Gao, L.2    Meissner, G.3
  • 25
    • 23944436197 scopus 로고    scopus 로고
    • The Gln4863Ala mutation within a putative, pore-lining trans-membrane helix of the cardiac ryanodine receptor channel alters both the kinetics of ryanoid interaction and the subsequent fractional conductance
    • Ranatunga KM, Moreno-King TM, Tanna B, Wang R, Chen SR, et al. (2005) The Gln4863Ala mutation within a putative, pore-lining trans-membrane helix of the cardiac ryanodine receptor channel alters both the kinetics of ryanoid interaction and the subsequent fractional conductance. Mol Pharmacol 68: 840-846.
    • (2005) Mol Pharmacol , vol.68 , pp. 840-846
    • Ranatunga, K.M.1    Moreno-King, T.M.2    Tanna, B.3    Wang, R.4    Chen, S.R.5
  • 26
    • 0026580708 scopus 로고
    • Ion conduction and discrimination in the sarcoplasmic reticulum ryanodine receptor/calcium-release channel
    • Williams AJ, (1992) Ion conduction and discrimination in the sarcoplasmic reticulum ryanodine receptor/calcium-release channel. J Muscle Res Cell Motil 13: 7-26.
    • (1992) J Muscle Res Cell Motil , vol.13 , pp. 7-26
    • Williams, A.J.1
  • 27
    • 0036584482 scopus 로고    scopus 로고
    • Ion conduction and selectivity in the ryanodine receptor channel
    • Williams AJ, (2002) Ion conduction and selectivity in the ryanodine receptor channel. Front Biosci 7: d1223-1230.
    • (2002) Front Biosci , vol.7
    • Williams, A.J.1
  • 28
    • 26044445278 scopus 로고    scopus 로고
    • The interaction of ryanoids with individual ryanodine receptor channels
    • Williams AJ, Tanna B, (2004) The interaction of ryanoids with individual ryanodine receptor channels. Biol Res 37: 527-538.
    • (2004) Biol Res , vol.37 , pp. 527-538
    • Williams, A.J.1    Tanna, B.2
  • 29
    • 2442549767 scopus 로고    scopus 로고
    • Molecular regulation of cardiac ryanodine receptor ion channel
    • Meissner G, (2004) Molecular regulation of cardiac ryanodine receptor ion channel. Cell Calcium 35: 621-628.
    • (2004) Cell Calcium , vol.35 , pp. 621-628
    • Meissner, G.1
  • 30
    • 3242692393 scopus 로고    scopus 로고
    • Macromolecular complexes regulating cardiac ryanodine receptor function
    • Bers DM, (2004) Macromolecular complexes regulating cardiac ryanodine receptor function. J Mol Cell Cardiol 37: 417-429.
    • (2004) J Mol Cell Cardiol , vol.37 , pp. 417-429
    • Bers, D.M.1
  • 31
    • 0025869897 scopus 로고
    • Functional characterisation of the ryanodine receptor purified from sheep cardiac muscle sarcoplasmic reticulum
    • Lindsay AR, Williams AJ, (1991) Functional characterisation of the ryanodine receptor purified from sheep cardiac muscle sarcoplasmic reticulum. Biochim Biophys Acta 1064: 89-102.
    • (1991) Biochim Biophys Acta , vol.1064 , pp. 89-102
    • Lindsay, A.R.1    Williams, A.J.2
  • 32
    • 62649166490 scopus 로고    scopus 로고
    • Changes in negative charge at the luminal mouth of the pore alter ion handling and gating in the cardiac ryanodine-receptor
    • Mead-Savery FC, Wang R, Tanna-Topan B, Chen SR, Welch W, et al. (2009) Changes in negative charge at the luminal mouth of the pore alter ion handling and gating in the cardiac ryanodine-receptor. Biophys J 96: 1374-1387.
    • (2009) Biophys J , vol.96 , pp. 1374-1387
    • Mead-Savery, F.C.1    Wang, R.2    Tanna-Topan, B.3    Chen, S.R.4    Welch, W.5
  • 33
    • 0141888445 scopus 로고    scopus 로고
    • A single ring of charged amino acids at one end of the pore can control ion selectivity in the 5-HT3 receptor
    • Thompson AJ, Lummis SC, (2003) A single ring of charged amino acids at one end of the pore can control ion selectivity in the 5-HT3 receptor. Br J Pharmacol 140: 359-365.
    • (2003) Br J Pharmacol , vol.140 , pp. 359-365
    • Thompson, A.J.1    Lummis, S.C.2
  • 34
    • 58149302945 scopus 로고    scopus 로고
    • Anion-cation permeability correlates with hydrated counterion size in glycine receptor channels
    • Sugiharto S, Lewis TM, Moorhouse AJ, Schofield PR, Barry PH, (2008) Anion-cation permeability correlates with hydrated counterion size in glycine receptor channels. Biophys J 95: 4698-4715.
    • (2008) Biophys J , vol.95 , pp. 4698-4715
    • Sugiharto, S.1    Lewis, T.M.2    Moorhouse, A.J.3    Schofield, P.R.4    Barry, P.H.5
  • 35
    • 0027730901 scopus 로고
    • Probing the structure of the conduction pathway of the sheep cardiac sarcoplasmic reticulum calcium-release channel with permeant and impermeant organic cations
    • Tinker A, Williams AJ, (1993) Probing the structure of the conduction pathway of the sheep cardiac sarcoplasmic reticulum calcium-release channel with permeant and impermeant organic cations. J Gen Physiol 102: 1107-1129.
    • (1993) J Gen Physiol , vol.102 , pp. 1107-1129
    • Tinker, A.1    Williams, A.J.2
  • 36
    • 0028878142 scopus 로고
    • Measuring the length of the pore of the sheep cardiac sarcoplasmic reticulum calcium-release channel using related trimethylammonium ions as molecular calipers
    • Tinker A, Williams AJ, (1995) Measuring the length of the pore of the sheep cardiac sarcoplasmic reticulum calcium-release channel using related trimethylammonium ions as molecular calipers. Biophys J 68: 111-120.
    • (1995) Biophys J , vol.68 , pp. 111-120
    • Tinker, A.1    Williams, A.J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.