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1
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34347236923
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Mechanisms of cardiac potassium channel trafficking
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Steele D.F., Eldstrom J., and Fedida D. Mechanisms of cardiac potassium channel trafficking. J Physiol 582 (2007) 17-26
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(2007)
J Physiol
, vol.582
, pp. 17-26
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Steele, D.F.1
Eldstrom, J.2
Fedida, D.3
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2
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36749021268
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Dynamic regulation of the voltage-gated Kv2.1 potassium channel by multisite phosphorylation
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Mohapatra D.P., Park K.S., and Trimmer J.S. Dynamic regulation of the voltage-gated Kv2.1 potassium channel by multisite phosphorylation. Biochem Soc Trans 35 (2007) 1064-1068
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(2007)
Biochem Soc Trans
, vol.35
, pp. 1064-1068
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Mohapatra, D.P.1
Park, K.S.2
Trimmer, J.S.3
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3
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55049099359
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Ion channels: from conductance to structure
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Bezanilla F. Ion channels: from conductance to structure. Neuron 60 (2008) 456-468
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(2008)
Neuron
, vol.60
, pp. 456-468
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Bezanilla, F.1
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4
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60549108756
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Intracellular regions of potassium channels: Kv2.1 and heag
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Wray D. Intracellular regions of potassium channels: Kv2.1 and heag. Eur Biophys J 38 (2009) 285-292
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(2009)
Eur Biophys J
, vol.38
, pp. 285-292
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Wray, D.1
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5
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42949173960
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Surface expression and distribution of voltage-gated potassium channels in neurons
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McKeown L., Swanton L., Robinson P., and Jones O.T. Surface expression and distribution of voltage-gated potassium channels in neurons. Mol Membr Biol 25 (2008) 332-343
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(2008)
Mol Membr Biol
, vol.25
, pp. 332-343
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McKeown, L.1
Swanton, L.2
Robinson, P.3
Jones, O.T.4
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6
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36248982122
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+ channel in a lipid membrane-like environment
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This landmark article describes the structure of a chimeric Kv channel, in which the voltage-sensor paddle has been transferred from Kv2.1 to Kv1.2. Crystallized in complex with lipids, the complete structure at 2.4 Å resolution reveals the pore and the voltage-sensors embedded in a membrane-like arrangement of lipid molecules. The data provide new ideas on possible mechanisms for voltage-sensor movement and pore gating within the lipid bilayer.
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+ channel in a lipid membrane-like environment. Nature 450 (2007) 376-382. This landmark article describes the structure of a chimeric Kv channel, in which the voltage-sensor paddle has been transferred from Kv2.1 to Kv1.2. Crystallized in complex with lipids, the complete structure at 2.4 Å resolution reveals the pore and the voltage-sensors embedded in a membrane-like arrangement of lipid molecules. The data provide new ideas on possible mechanisms for voltage-sensor movement and pore gating within the lipid bilayer.
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(2007)
Nature
, vol.450
, pp. 376-382
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Long, S.B.1
Tao, X.2
Campbell, E.B.3
MacKinnon, R.4
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7
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24044494280
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Kv1.5 surface expression is modulated by retrograde trafficking of newly endocytosed channels by the dynein motor
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This article has significant implications for understanding the way Kv channel surface expression is regulated. The experiments highlight a pathway for Kv1.5 internalization from the cell surface involving early endosomes, followed by later trafficking by the dynein motor along microtubules.
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Choi W.S., Khurana A., Mathur R., Viswanathan V., Steele D.F., and Fedida D. Kv1.5 surface expression is modulated by retrograde trafficking of newly endocytosed channels by the dynein motor. Circ Res 97 (2005) 363-371. This article has significant implications for understanding the way Kv channel surface expression is regulated. The experiments highlight a pathway for Kv1.5 internalization from the cell surface involving early endosomes, followed by later trafficking by the dynein motor along microtubules.
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(2005)
Circ Res
, vol.97
, pp. 363-371
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Choi, W.S.1
Khurana, A.2
Mathur, R.3
Viswanathan, V.4
Steele, D.F.5
Fedida, D.6
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8
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34547101445
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Membrane cholesterol modulates Kv1.5 potassium channel distribution and function in rat cardiomyocytes
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Abi-Char J., Maguy A., Coulombe A., Balse E., Ratajczak P., Samuel J.L., Nattel S., and Hatem S.N. Membrane cholesterol modulates Kv1.5 potassium channel distribution and function in rat cardiomyocytes. J Physiol 582 (2007) 1205-1217
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(2007)
J Physiol
, vol.582
, pp. 1205-1217
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Abi-Char, J.1
Maguy, A.2
Coulombe, A.3
Balse, E.4
Ratajczak, P.5
Samuel, J.L.6
Nattel, S.7
Hatem, S.N.8
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9
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15444365671
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ROMK1 channel activity is regulated by monoubiquitination
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Immunoprecipitation of proteins obtained from renal cortex and outer medulla with anti-ROMK1 antibody revealed that the channel was mono-ubiquitinated. After identification of the ubiquitination site, confocal microscopy showed that mutant ROMK1 channels which cannot be ubiquitinated have a higher density at the cell surface than wild-type ROMK1 channels. A model illustrates the potential physiological role of mono-ubiquitination in the regulation of ROMK1 internalization involving E3 ubiquitin ligase and protein tyrosine kinase activity.
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Lin D.H., Sterling H., Wang Z., Babilonia E., Yang B., Dong K., Hebert S.C., Giebisch G., and Wang W.H. ROMK1 channel activity is regulated by monoubiquitination. Proc Natl Acad Sci U S A 102 (2005) 4306-4311. Immunoprecipitation of proteins obtained from renal cortex and outer medulla with anti-ROMK1 antibody revealed that the channel was mono-ubiquitinated. After identification of the ubiquitination site, confocal microscopy showed that mutant ROMK1 channels which cannot be ubiquitinated have a higher density at the cell surface than wild-type ROMK1 channels. A model illustrates the potential physiological role of mono-ubiquitination in the regulation of ROMK1 internalization involving E3 ubiquitin ligase and protein tyrosine kinase activity.
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(2005)
Proc Natl Acad Sci U S A
, vol.102
, pp. 4306-4311
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Lin, D.H.1
Sterling, H.2
Wang, Z.3
Babilonia, E.4
Yang, B.5
Dong, K.6
Hebert, S.C.7
Giebisch, G.8
Wang, W.H.9
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10
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54049142479
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Internalized Kv1.5 traffics via Rab-dependent pathways
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Major Rab-dependent pathways regulate Kv1.5 internalization and trafficking. Rab GTPases thus constitute dynamic targets by which cells may modulate Kv1.5 functional expression.
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Zadeh A.D., Xu H., Loewen M.E., Noble G.P., Steele D.F., and Fedida D. Internalized Kv1.5 traffics via Rab-dependent pathways. J Physiol 586 (2008) 4793-4813. Major Rab-dependent pathways regulate Kv1.5 internalization and trafficking. Rab GTPases thus constitute dynamic targets by which cells may modulate Kv1.5 functional expression.
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(2008)
J Physiol
, vol.586
, pp. 4793-4813
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Zadeh, A.D.1
Xu, H.2
Loewen, M.E.3
Noble, G.P.4
Steele, D.F.5
Fedida, D.6
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11
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25444529765
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Molecular physiology of cardiac repolarization
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Nerbonne J.M., and Kass R.S. Molecular physiology of cardiac repolarization. Physiol Rev 85 (2005) 1205-1253
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(2005)
Physiol Rev
, vol.85
, pp. 1205-1253
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Nerbonne, J.M.1
Kass, R.S.2
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12
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38149003578
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+ channel Kv2.1 in adult cardiomyocytes
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In this study, infection of acutely dissociated rat cardiomyocytes with recombinant adenovirus was used to determine the subcellular localization and lateral mobility of green fluorescent protein (GFP)-Kv2.1 and yellow fluorescent protein-Kv1.4. Fluorescence recovery after photobleach (FRAP) experiments indicate that atrial Kv2.1 was immobile, whereas ventricular Kv2.1 was mobile. Also, Kv2.1 was localized to different subcellular compartments of atrial and ventricular myocytes.
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+ channel Kv2.1 in adult cardiomyocytes. Am J Physiol Heart Circ Physiol 294 (2008) H229-H237. In this study, infection of acutely dissociated rat cardiomyocytes with recombinant adenovirus was used to determine the subcellular localization and lateral mobility of green fluorescent protein (GFP)-Kv2.1 and yellow fluorescent protein-Kv1.4. Fluorescence recovery after photobleach (FRAP) experiments indicate that atrial Kv2.1 was immobile, whereas ventricular Kv2.1 was mobile. Also, Kv2.1 was localized to different subcellular compartments of atrial and ventricular myocytes.
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(2008)
Am J Physiol Heart Circ Physiol
, vol.294
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O'Connell, K.M.1
Whitesell, J.D.2
Tamkun, M.M.3
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13
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37549055114
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Kv4.3 is not required for the generation of functional Ito,f channels in adult mouse ventricles
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Niwa N., Wang W., Sha Q., Marionneau C., and Nerbonne J.M. Kv4.3 is not required for the generation of functional Ito,f channels in adult mouse ventricles. J Mol Cell Cardiol 44 (2008) 95-104
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(2008)
J Mol Cell Cardiol
, vol.44
, pp. 95-104
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Niwa, N.1
Wang, W.2
Sha, Q.3
Marionneau, C.4
Nerbonne, J.M.5
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14
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57049112014
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+ currents in neurons
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+ currents in neurons. J Physiol 586 (2008) 5609-5623
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(2008)
J Physiol
, vol.586
, pp. 5609-5623
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Maffie, J.1
Rudy, B.2
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15
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54049142897
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Targeted deletion of kcne2 impairs ventricular repolarization via disruption of I(K,slow1) and I(to,f)
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+ current and prolonged ventricular action potential duration.
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+ current and prolonged ventricular action potential duration.
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(2008)
FASEB J
, vol.22
, pp. 3648-3660
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Roepke, T.K.1
Kontogeorgis, A.2
Ovanez, C.3
Xu, X.4
Young, J.B.5
Purtell, K.6
Goldstein, P.A.7
Christini, D.J.8
Peters, N.S.9
Akar, F.G.10
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17
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40949162780
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Who needs A current? Functional remodelling in the Kv4.2-/- mouse
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Foehring R.C. Who needs A current? Functional remodelling in the Kv4.2-/- mouse. J Physiol 586 (2008) 1461
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(2008)
J Physiol
, vol.586
, pp. 1461
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Foehring, R.C.1
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20
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44849108717
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+ channel
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In this article structural alterations are investigated associated with inactivation gating and antagonist binding to a chimeric KcsA-Kv1.3 channel in a membrane setting using solid-state nuclear magnetic resonance (ssNMR)-spectroscopy. The work of this group shows that ssNMR is a useful promising technique to study the structure of membrane proteins in addition to crystal structure work.
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+ channel. Nat Struct Mol Biol 15 (2008) 605-612. In this article structural alterations are investigated associated with inactivation gating and antagonist binding to a chimeric KcsA-Kv1.3 channel in a membrane setting using solid-state nuclear magnetic resonance (ssNMR)-spectroscopy. The work of this group shows that ssNMR is a useful promising technique to study the structure of membrane proteins in addition to crystal structure work.
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(2008)
Nat Struct Mol Biol
, vol.15
, pp. 605-612
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Ader, C.1
Schneider, R.2
Hornig, S.3
Velisetty, P.4
Wilson, E.M.5
Lange, A.6
Giller, K.7
Ohmert, I.8
Martin-Eauclaire, M.F.9
Trauner, D.10
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21
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58049194119
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+ channel gating and voltage sensor toxin sensitivity depend on the mechanical state of the lipid membrane
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Membrane environmental factors that influence channel function are divisible into two general categories: lipid compositional and mechanical state. The article shows that the mechanical state can have a surprisingly large effect on Kv channel function including its pharmacological interaction with voltage-sensor toxins.
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+ channel gating and voltage sensor toxin sensitivity depend on the mechanical state of the lipid membrane. Proc Natl Acad Sci U S A 105 (2008) 19276-19281. Membrane environmental factors that influence channel function are divisible into two general categories: lipid compositional and mechanical state. The article shows that the mechanical state can have a surprisingly large effect on Kv channel function including its pharmacological interaction with voltage-sensor toxins.
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(2008)
Proc Natl Acad Sci U S A
, vol.105
, pp. 19276-19281
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Schmidt, D.1
MacKinnon, R.2
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22
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49349111148
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Functional analysis of Kv1.2 and paddle chimera Kv channels in planar lipid bilayers
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Tao X., and MacKinnon R. Functional analysis of Kv1.2 and paddle chimera Kv channels in planar lipid bilayers. J Mol Biol 382 (2008) 24-33
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(2008)
J Mol Biol
, vol.382
, pp. 24-33
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Tao, X.1
MacKinnon, R.2
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23
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36248946187
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Portability of paddle motif function and pharmacology in voltage sensors
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Alabi A.A., Bahamonde M.I., Jung H.J., Kim J.I., and Swartz K.J. Portability of paddle motif function and pharmacology in voltage sensors. Nature 450 (2007) 370-375
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(2007)
Nature
, vol.450
, pp. 370-375
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Alabi, A.A.1
Bahamonde, M.I.2
Jung, H.J.3
Kim, J.I.4
Swartz, K.J.5
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24
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33747062707
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Enzymatic activation of voltage-gated potassium channels
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This article highlights the importance of lipidic environment for Kv channel function. It is shown that sphingomyelinase activity activates Kv2.1 channels at negative potentials by shifting the midpoint of voltage-dependent activation to very negative membrane potentials.
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Ramu Y., Xu Y., and Lu Z. Enzymatic activation of voltage-gated potassium channels. Nature 442 (2006) 696-699. This article highlights the importance of lipidic environment for Kv channel function. It is shown that sphingomyelinase activity activates Kv2.1 channels at negative potentials by shifting the midpoint of voltage-dependent activation to very negative membrane potentials.
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(2006)
Nature
, vol.442
, pp. 696-699
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Ramu, Y.1
Xu, Y.2
Lu, Z.3
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25
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54049096357
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Multiple Kv1.5 targeting to membrane surface microdomains
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The results shown in this article emphasize the importance of Kv1.5 partnership interactions, for example with ancillary Kvβ2 subunits, can have marked effects on Kv1.5 targeting to lipid rafts.
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Martinez-Marmol R., Villalonga N., Sole L., Vicente R., Tamkun M.M., Soler C., and Felipe A. Multiple Kv1.5 targeting to membrane surface microdomains. J Cell Physiol 217 (2008) 667-673. The results shown in this article emphasize the importance of Kv1.5 partnership interactions, for example with ancillary Kvβ2 subunits, can have marked effects on Kv1.5 targeting to lipid rafts.
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(2008)
J Cell Physiol
, vol.217
, pp. 667-673
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Martinez-Marmol, R.1
Villalonga, N.2
Sole, L.3
Vicente, R.4
Tamkun, M.M.5
Soler, C.6
Felipe, A.7
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26
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40849145714
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Caveolin regulates kv1.5 trafficking to cholesterol-rich membrane microdomains
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McEwen D.P., Li Q., Jackson S., Jenkins P.M., and Martens J.R. Caveolin regulates kv1.5 trafficking to cholesterol-rich membrane microdomains. Mol Pharmacol 73 (2008) 678-685
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(2008)
Mol Pharmacol
, vol.73
, pp. 678-685
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McEwen, D.P.1
Li, Q.2
Jackson, S.3
Jenkins, P.M.4
Martens, J.R.5
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27
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43749083288
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Kv1.5 association modifies Kv1. 3 traffic and membrane localization
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Vicente R., Villalonga N., Calvo M., Escalada A., Solsona C., Soler C., Tamkun M.M., and Felipe A. Kv1.5 association modifies Kv1. 3 traffic and membrane localization. J Biol Chem 283 (2008) 8756-8764
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(2008)
J Biol Chem
, vol.283
, pp. 8756-8764
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Vicente, R.1
Villalonga, N.2
Calvo, M.3
Escalada, A.4
Solsona, C.5
Soler, C.6
Tamkun, M.M.7
Felipe, A.8
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29
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44949262109
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Posttranslational modification of voltage-dependent potassium channel Kv1.5:COOH-terminal palmitoylation modulates its biological properties
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The article deals with a very interesting aspect of post-translational Kv channel modification and its influence on Kv channel trafficking. It is shown that the Kv1.5 channel is palmitoylated and that its palmitoylation decreases Kv1.5 expression at the cell surface.
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Jindal H.K., Folco E.J., Liu G.X., and Koren G. Posttranslational modification of voltage-dependent potassium channel Kv1.5:COOH-terminal palmitoylation modulates its biological properties. Am J Physiol Heart Circ Physiol 294 (2008) H2012-H2021. The article deals with a very interesting aspect of post-translational Kv channel modification and its influence on Kv channel trafficking. It is shown that the Kv1.5 channel is palmitoylated and that its palmitoylation decreases Kv1.5 expression at the cell surface.
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(2008)
Am J Physiol Heart Circ Physiol
, vol.294
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Jindal, H.K.1
Folco, E.J.2
Liu, G.X.3
Koren, G.4
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30
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41749094950
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The anchoring protein SAP97 retains Kv1.5 channels in the plasma membrane of cardiac myocytes
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Abi-Char J., El-Haou S., Balse E., Neyroud N., Vranckx R., Coulombe A., and Hatem S.N. The anchoring protein SAP97 retains Kv1.5 channels in the plasma membrane of cardiac myocytes. Am J Physiol Heart Circ Physiol 294 (2008) H1851-H1861
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(2008)
Am J Physiol Heart Circ Physiol
, vol.294
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Abi-Char, J.1
El-Haou, S.2
Balse, E.3
Neyroud, N.4
Vranckx, R.5
Coulombe, A.6
Hatem, S.N.7
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31
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47349085612
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Biophysical approaches to protein-induced membrane deformations in trafficking
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This review describes the generic mechanisms underlying the process of cargo-induced membrane deformation and discusses the importance of membrane morphological changes in membrane trafficking and vesicle formation.
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Sens P., Johannes L., and Bassereau P. Biophysical approaches to protein-induced membrane deformations in trafficking. Curr Opin Cell Biol 20 (2008) 476-482. This review describes the generic mechanisms underlying the process of cargo-induced membrane deformation and discusses the importance of membrane morphological changes in membrane trafficking and vesicle formation.
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(2008)
Curr Opin Cell Biol
, vol.20
, pp. 476-482
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Sens, P.1
Johannes, L.2
Bassereau, P.3
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