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Volumn 7, Issue 10, 2006, Pages 761-771

Non-conducting functions of voltage-gated ion channels

Author keywords

[No Author keywords available]

Indexed keywords

CELL ADHESION MOLECULE; ENZYME; ION CHANNEL; UNCLASSIFIED DRUG; VOLTAGE GATED ION CHANNEL;

EID: 33748943301     PISSN: 1471003X     EISSN: 14710048     Source Type: Journal    
DOI: 10.1038/nrn1988     Document Type: Review
Times cited : (174)

References (139)
  • 1
    • 33344459507 scopus 로고    scopus 로고
    • Signaling protein complexes associated with neuronal ion channels
    • Levitan, I. B., Signaling protein complexes associated with neuronal ion channels. Nature Neurosci. 9, 305-310 (2006).
    • (2006) Nature Neurosci. , vol.9 , pp. 305-310
    • Levitan, I.B.1
  • 2
    • 8144228615 scopus 로고    scopus 로고
    • Voltage-gated potassium channels in cell proliferation
    • Pardo, L. A. Voltage-gated potassium channels in cell proliferation. Physiology 19, 285-292 (2004).
    • (2004) Physiology , vol.19 , pp. 285-292
    • Pardo, L.A.1
  • 3
    • 0033570146 scopus 로고    scopus 로고
    • + channels
    • + channels. EMBO J. 18, 5540-5547 (1999).
    • (1999) EMBO J. , vol.18 , pp. 5540-5547
    • Pardo, L.A.1
  • 5
    • 4944252457 scopus 로고    scopus 로고
    • Ether a go-go potassium channels as human cervical cancer markers
    • Farias, L. M. et al. Ether a go-go potassium channels as human cervical cancer markers. Cancer Res. 64, 6996-7001 (2004).
    • (2004) Cancer Res. , vol.64 , pp. 6996-7001
    • Farias, L.M.1
  • 6
    • 0038587789 scopus 로고    scopus 로고
    • Genomic amplification and oncogenic properties of the KCNK9 potassium channel gene
    • Mu, D. et al. Genomic amplification and oncogenic properties of the KCNK9 potassium channel gene. Cancer Cell 3, 297-302 (2003).
    • (2003) Cancer Cell , vol.3 , pp. 297-302
    • Mu, D.1
  • 7
    • 9644282983 scopus 로고    scopus 로고
    • Shaker-type potassium channel subunits differentially control oligodendrocyte progenitor proliferation
    • Vautier, F., Belachew, S., Chittajallu, R. & Gallo, V. Shaker-type potassium channel subunits differentially control oligodendrocyte progenitor proliferation. GLIA 48, 337-345 (2004).
    • (2004) GLIA , vol.48 , pp. 337-345
    • Vautier, F.1    Belachew, S.2    Chittajallu, R.3    Gallo, V.4
  • 8
    • 0034662325 scopus 로고    scopus 로고
    • Modulation of Kv1.5 currents by Src tyrosine phosphorylation: Potential role in the differentiation of astrocytes
    • MacFarlane, S. N. & Sontheimer, H. Modulation of Kv1.5 currents by Src tyrosine phosphorylation: potential role in the differentiation of astrocytes. J. Neurosci. 20, 5245-5253 (2000).
    • (2000) J. Neurosci. , vol.20 , pp. 5245-5253
    • MacFarlane, S.N.1    Sontheimer, H.2
  • 9
    • 0034106948 scopus 로고    scopus 로고
    • Changes in ion channel expression accompany cell cycle progression of spinal cord astrocytes
    • MacFarlane, S. N. & Sontheimer, H. Changes in ion channel expression accompany cell cycle progression of spinal cord astrocytes. GLIA 30, 39-48 (2000)
    • (2000) GLIA , vol.30 , pp. 39-48
    • MacFarlane, S.N.1    Sontheimer, H.2
  • 10
    • 0038721967 scopus 로고    scopus 로고
    • Expression of voltage-gated potassium channels Kv1.3 and Kv1.5 in human gliomas
    • Preussat, K. et al. Expression of voltage-gated potassium channels Kv1.3 and Kv1.5 in human gliomas. Neurosci. Lett. 346, 33-36 (2003).
    • (2003) Neurosci. Lett. , vol.346 , pp. 33-36
    • Preussat, K.1
  • 11
    • 0037025337 scopus 로고    scopus 로고
    • Calcium/calmodulin-dependent protein kinase II phosphorylates and regulates the Drosophila eag potassium channel
    • Wang, Z., Wilson, G. F. & Griffith, L. C. Calcium/calmodulin- dependent protein kinase II phosphorylates and regulates the Drosophila eag potassium channel. J. Biol. Chem. 277, 24022-24029 (2002).
    • (2002) J. Biol. Chem. , vol.277 , pp. 24022-24029
    • Wang, Z.1    Wilson, G.F.2    Griffith, L.C.3
  • 12
    • 1642404319 scopus 로고    scopus 로고
    • The Eag potassium channel binds and locally activates calcium/calmodulin-dependent protein kinase II
    • Sun, X. X., Hodge, J. J., Zhou, Y., Nguyen, M. & Griffith, L. C. The Eag potassium channel binds and locally activates calcium/calmodulin-dependent protein kinase II. J. Biol. Chem. 279, 10206-10214 (2004).
    • (2004) J. Biol. Chem. , vol.279 , pp. 10206-10214
    • Sun, X.X.1    Hodge, J.J.2    Zhou, Y.3    Nguyen, M.4    Griffith, L.C.5
  • 14
    • 0032521086 scopus 로고    scopus 로고
    • Genetic dissection of functional contributions of specific potassium channel subunits in habituation of an escape circuit in Drosophila
    • Engel, J. E. & Wu, C. F. Genetic dissection of functional contributions of specific potassium channel subunits in habituation of an escape circuit in Drosophila. J. Neurosci. 18, 2254-2267 (1998).
    • (1998) J. Neurosci. , vol.18 , pp. 2254-2267
    • Engel, J.E.1    Wu, C.F.2
  • 15
    • 0027971438 scopus 로고
    • Calcium/calmodulin-dependent protein kinase II and potassium channel subunit Eag similarly affect plasticity in Drosophila
    • Griffith, L. C., Wang, J., Zhong, Y., Wu, C. F. & Greenspan, R. J. Calcium/calmodulin-dependent protein kinase II and potassium channel subunit Eag similarly affect plasticity in Drosophila. Proc. Natl Acad. Sci. USA 91, 10044-10048 (1994).
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 10044-10048
    • Griffith, L.C.1    Wang, J.2    Zhong, Y.3    Wu, C.F.4    Greenspan, R.J.5
  • 16
    • 4544277791 scopus 로고    scopus 로고
    • Expression of ether a go-go potassium channels in human gliomas
    • Patt, S. et al. Expression of ether a go-go potassium channels in human gliomas. Neurosci. Lett. 368, 249-253 (2004).
    • (2004) Neurosci. Lett. , vol.368 , pp. 249-253
    • Patt, S.1
  • 18
    • 4744343507 scopus 로고    scopus 로고
    • Regulation of calcium/calmodulin-dependent protein kinase II activation by intramolecular and intermolecular Interactions
    • Griffith, L. C. Regulation of calcium/calmodulin-dependent protein kinase II activation by intramolecular and intermolecular Interactions. J. Neurosci. 24, 8394-8398 (2004).
    • (2004) J. Neurosci. , vol.24 , pp. 8394-8398
    • Griffith, L.C.1
  • 19
    • 0032567106 scopus 로고    scopus 로고
    • Crystal structure and functional analysis of the HERG potassium channel N terminus: A leukaryotic PAS domain
    • Morais-Cabral, J. H. et al. Crystal structure and functional analysis of the HERG potassium channel N terminus: a leukaryotic PAS domain. Cell 95, 649-655 (1998).
    • (1998) Cell , vol.95 , pp. 649-655
    • Morais-Cabral, J.H.1
  • 20
    • 0024449639 scopus 로고
    • Molecular basis of functional diversity of voltage-gated potassium channels in mammalian brain
    • Stuhmer, W. et al. Molecular basis of functional diversity of voltage-gated potassium channels in mammalian brain. EMBO J. 8, 3235-3244 (1989).
    • (1989) EMBO J. , vol.8 , pp. 3235-3244
    • Stuhmer, W.1
  • 21
    • 0025284847 scopus 로고
    • Cloning and expression of cDNA and genomic clones encoding three delayed rectifier potassium channels in rat brain
    • Swanson, R. et al. Cloning and expression of cDNA and genomic clones encoding three delayed rectifier potassium channels in rat brain. Neuron 4, 929-939 (1990).
    • (1990) Neuron , vol.4 , pp. 929-939
    • Swanson, R.1
  • 22
    • 0028886969 scopus 로고
    • Immunohistochemical localization of five members of the Kv1 channel subunits: Contrasting subcellular locations and neuron-specific co-localizations in rat brain
    • Veh, R. W. et al. Immunohistochemical localization of five members of the Kv1 channel subunits: contrasting subcellular locations and neuron-specific co-localizations in rat brain. Eur. J. Neurosci. 7, 2189-2205 (1995).
    • (1995) Eur. J. Neurosci. , vol.7 , pp. 2189-2205
    • Veh, R.W.1
  • 23
    • 0028136017 scopus 로고
    • State-dependent inactivation of the Kv3 potassium channel
    • Marom, S. & Levitan, I. B. State-dependent inactivation of the Kv3 potassium channel. Biophys. J. 67, 579-589 (1994).
    • (1994) Biophys. J. , vol.67 , pp. 579-589
    • Marom, S.1    Levitan, I.B.2
  • 24
    • 2142700028 scopus 로고    scopus 로고
    • + channels as targets for specific immunomodulation
    • + channels as targets for specific immunomodulation. Trends Pharmacol. Sci. 25, 280-289 (2004).
    • (2004) Trends Pharmacol. Sci. , vol.25 , pp. 280-289
    • Chandy, G.K.1
  • 25
    • 0030695214 scopus 로고    scopus 로고
    • Expression of voltage-gated potassium channels decreases cellular protein tyrosine phosphorylation
    • Holmes, T. C., Berman, K., Swartz, J. E., Dagan, D. & Levitan, I. B. Expression of voltage-gated potassium channels decreases cellular protein tyrosine phosphorylation. J. Neurosci. 17, 8964-8974 (1997).
    • (1997) J. Neurosci. , vol.17 , pp. 8964-8974
    • Holmes, T.C.1    Berman, K.2    Swartz, J.E.3    Dagan, D.4    Levitan, I.B.5
  • 26
    • 10744231935 scopus 로고    scopus 로고
    • Kv1.3 channel gene-targeted deletion produces 'Super-Smeller Mice' with altered glomeruli, interacting scaffolding proteins, and biophysics
    • Fadool, D. A. et al. Kv1.3 channel gene-targeted deletion produces 'Super-Smeller Mice' with altered glomeruli, interacting scaffolding proteins, and biophysics. Neuron 41, 389-404 (2004).
    • (2004) Neuron , vol.41 , pp. 389-404
    • Fadool, D.A.1
  • 27
    • 0032055649 scopus 로고    scopus 로고
    • V 1.1 potassium channel causes epilepsy in mice
    • V 1.1 potassium channel causes epilepsy in mice. Neuron 20, 809-819 (1998).
    • (1998) Neuron , vol.20 , pp. 809-819
    • Smart, S.L.1
  • 28
    • 0003982199 scopus 로고    scopus 로고
    • + channel gene: Reduced body weight, impaired motor skill and muscle contraction, but no seizures
    • + channel gene: reduced body weight, impaired motor skill and muscle contraction, but no seizures. Proc. Natl Acad. Sci. USA 94, 1533-1538 (1997).
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 1533-1538
    • Ho, C.S.1    Grange, R.W.2    Joho, R.H.3
  • 29
    • 0036020148 scopus 로고    scopus 로고
    • 1-integrins on the plasma membrane of melanoma cells: Effects of cell adherence and channel blockers
    • 1-integrins on the plasma membrane of melanoma cells: effects of cell adherence and channel blockers. J. Gen. Physiol. 120, 29-37 (2002).
    • (2002) J. Gen. Physiol. , vol.120 , pp. 29-37
    • Artym, V.V.1    Petty, H.R.2
  • 31
    • 0034598810 scopus 로고    scopus 로고
    • Modulation of A-type potassium channels by a family of calcium sensors
    • An, W. F. et al. Modulation of A-type potassium channels by a family of calcium sensors. Nature 403, 553-556 (2000).
    • (2000) Nature , vol.403 , pp. 553-556
    • An, W.F.1
  • 32
    • 0037177892 scopus 로고    scopus 로고
    • Molecular cloning and characterization of CALP/KChIP4, a novel EF-hand protein interacting with presenilin 2 and voltage-gated potassium channel subunit Kv4
    • Morohashi, Y. et al. Molecular cloning and characterization of CALP/KChIP4, a novel EF-hand protein interacting with presenilin 2 and voltage-gated potassium channel subunit Kv4. J. Biol. Chem. 277, 14965-14975 (2002).
    • (2002) J. Biol. Chem. , vol.277 , pp. 14965-14975
    • Morohashi, Y.1
  • 33
    • 27844446627 scopus 로고    scopus 로고
    • Multiprotein assembly of Kv4.2, KChIP3 and DPP10 produces ternary channel complexes with ISA-like properties
    • Jerng, H. H., Kunjilwar, K. & Pfaffinger, P. J. Multiprotein assembly of Kv4.2, KChIP3 and DPP10 produces ternary channel complexes with ISA-like properties. J. Physiol. 568, 767-788 (2005).
    • (2005) J. Physiol. , vol.568 , pp. 767-788
    • Jerng, H.H.1    Kunjilwar, K.2    Pfaffinger, P.J.3
  • 34
    • 27144536610 scopus 로고    scopus 로고
    • h in rhythmically active neurons
    • h in rhythmically active neurons. J. Neurophysiol. 94, 3601-3617 (2005).
    • (2005) J. Neurophysiol. , vol.94 , pp. 3601-3617
    • MacLean, J.N.1
  • 35
    • 0141988731 scopus 로고    scopus 로고
    • h) channel gene modifies the firing activity of identified motor neurons in a small neural network
    • h) channel gene modifies the firing activity of identified motor neurons in a small neural network. J. Neurosci. 23, 9059-9067 (2003).
    • (2003) J. Neurosci. , vol.23 , pp. 9059-9067
    • Zhang, Y.1
  • 37
    • 0032304724 scopus 로고    scopus 로고
    • A superfamily of small potassium channel subunits: Form and function of the MinK-related peptides (MiRPs)
    • Abbott, G. W. & Goldstein, S. A. A superfamily of small potassium channel subunits: form and function of the MinK-related peptides (MiRPs). Quart. Rev. Biophys. 31, 357-398 (1998).
    • (1998) Quart. Rev. Biophys. , vol.31 , pp. 357-398
    • Abbott, G.W.1    Goldstein, S.A.2
  • 38
    • 3242722466 scopus 로고    scopus 로고
    • The slowpoke channel binding protein Slob from Drosophila melanogaster exhibits regulatable protein kinase activity
    • Zeng, H., Fei, H., Levitan, I. B. The slowpoke channel binding protein Slob from Drosophila melanogaster exhibits regulatable protein kinase activity. Neurosci. Lett. 65, 33-38 (2004).
    • (2004) Neurosci. Lett. , vol.65 , pp. 33-38
    • Zeng, H.1    Fei, H.2    Levitan, I.B.3
  • 39
    • 0032102975 scopus 로고    scopus 로고
    • Regulation of ion channel expression by cytoplasmic subunits
    • Trimmer, J. S. Regulation of ion channel expression by cytoplasmic subunits. Curr. Opin. Neurobiol. 8, 370-374 (1998).
    • (1998) Curr. Opin. Neurobiol. , vol.8 , pp. 370-374
    • Trimmer, J.S.1
  • 40
    • 0032970140 scopus 로고    scopus 로고
    • + channel β subunits
    • + channel β subunits. Ann. NY Acad. Sci. 868, 344-355 (1999).
    • (1999) Ann. NY Acad. Sci. , vol.868 , pp. 344-355
    • Pongs, O.1
  • 41
    • 33744970273 scopus 로고    scopus 로고
    • Modulation of voltage-dependent Shaker family potassium channels by an aldo-keto reductase
    • Weng, J., Cao, Y. & Zhou, M. Modulation of voltage-dependent Shaker family potassium channels by an aldo-keto reductase. J. Biol. Chem. 281, 15194-15200 (2006).
    • (2006) J. Biol. Chem. , vol.281 , pp. 15194-15200
    • Weng, J.1    Cao, Y.2    Zhou, M.3
  • 42
    • 4544345240 scopus 로고    scopus 로고
    • KChIPs and Kv4 α subunits as integral components of A-type potassium channels in mammalian brain
    • Rhodes, K. J. et al. KChIPs and Kv4 α subunits as integral components of A-type potassium channels in mammalian brain. J. Neurosci. 24, 7903-7915 (2004).
    • (2004) J. Neurosci. , vol.24 , pp. 7903-7915
    • Rhodes, K.J.1
  • 43
    • 0031721511 scopus 로고    scopus 로고
    • Calsenilin: A calcium-binding protein that interacts with the presenilins and regulates the levels of a presenilin fragment
    • see comment
    • Buxbaum, J. D. et al. Calsenilin: a calcium-binding protein that interacts with the presenilins and regulates the levels of a presenilin fragment. [see comment] Nature Med. 4, 1177-1181 (1998).
    • (1998) Nature Med. , vol.4 , pp. 1177-1181
    • Buxbaum, J.D.1
  • 45
    • 4444302175 scopus 로고    scopus 로고
    • A role for calsenilin and related proteins in multiple aspects of neuronal function
    • Buxbaum, J. D. A role for calsenilin and related proteins in multiple aspects of neuronal function. Biochem. Biophys. Res. Comm. 322, 1140-1144 (2004).
    • (2004) Biochem. Biophys. Res. Comm. , vol.322 , pp. 1140-1144
    • Buxbaum, J.D.1
  • 46
    • 27144489025 scopus 로고    scopus 로고
    • Transcriptional repressor DREAM regulates T-lymphocyte proliferation and cytokine gene expression
    • Savignac, M. et al. Transcriptional repressor DREAM regulates T-lymphocyte proliferation and cytokine gene expression. EMBO J. 24, 3555-3564 (2005).
    • (2005) EMBO J. , vol.24 , pp. 3555-3564
    • Savignac, M.1
  • 47
    • 33745038300 scopus 로고    scopus 로고
    • + channel expression in Mat-LyLu rat prostate cancer cell line
    • + channel expression in Mat-LyLu rat prostate cancer cell line. J. Physiol. 573, 343-356 (2006).
    • (2006) J. Physiol. , vol.573 , pp. 343-356
    • Brackenbury, W.J.1    Djamgoz, M.B.2
  • 48
    • 27944464981 scopus 로고    scopus 로고
    • Neuronal characteristics of small-cell lung cancer
    • Onganer, P. U., Seckl, M. J. & Djamgoz, M. B. Neuronal characteristics of small-cell lung cancer. Br. J. Cancer 93, 1197-1201 (2005).
    • (2005) Br. J. Cancer , vol.93 , pp. 1197-1201
    • Onganer, P.U.1    Seckl, M.J.2    Djamgoz, M.B.3
  • 50
    • 27944442711 scopus 로고    scopus 로고
    • A potential novel marker for human prostate cancer: Voltage-gated sodium channel expression in vivo
    • Diss, J. K. et al. A potential novel marker for human prostate cancer: voltage-gated sodium channel expression in vivo. Prostate Cancer Prostatic Dis. 8, 266-273 (2005).
    • (2005) Prostate Cancer Prostatic Dis. , vol.8 , pp. 266-273
    • Diss, J.K.1
  • 51
    • 23044441734 scopus 로고    scopus 로고
    • Voltage-gated sodium channel expression and potentiation of human breast cancer metastasis
    • Fraser, S. P. et al. Voltage-gated sodium channel expression and potentiation of human breast cancer metastasis. Clin. Cancer Res. 11, 5381-5389 (2005).
    • (2005) Clin. Cancer Res. , vol.11 , pp. 5381-5389
    • Fraser, S.P.1
  • 52
    • 3042638098 scopus 로고    scopus 로고
    • + channel activity
    • + channel activity. FEBS Lett. 569, 191-194 (2004).
    • (2004) FEBS Lett. , vol.569 , pp. 191-194
    • Fraser, S.P.1
  • 53
    • 1942502802 scopus 로고    scopus 로고
    • Serum concentration modifies amplitude and kinetics of voltage-gated Na+ current in the Mat-LyLu cell line of rat prostate cancer
    • Ding, Y. & Djamgoz, M. B. Serum concentration modifies amplitude and kinetics of voltage-gated Na+ current in the Mat-LyLu cell line of rat prostate cancer. Int. J. Biochem. Cell Biol. 36, 249-260 (2004).
    • (2004) Int. J. Biochem. Cell Biol. , vol.36 , pp. 249-260
    • Ding, Y.1    Djamgoz, M.B.2
  • 54
    • 10644241512 scopus 로고    scopus 로고
    • Heterophilic interactions of sodium channel β1 subunits with axonal and glial cell adhesion molecules
    • McEwen, D. P. & Isom, L. L. Heterophilic interactions of sodium channel β1 subunits with axonal and glial cell adhesion molecules. J. Biol. Chem. 279, 52744-52752 (2004).
    • (2004) J. Biol. Chem. , vol.279 , pp. 52744-52752
    • McEwen, D.P.1    Isom, L.L.2
  • 55
    • 0034646634 scopus 로고    scopus 로고
    • Sodium channel β subunits mediate homophilic cell adhesion and recruit ankyrin to points of cell-cell contact
    • Malhotra, J. D., Kazen-Gillespie, K., Hortsch, M. & Isom, L. L. Sodium channel β subunits mediate homophilic cell adhesion and recruit ankyrin to points of cell-cell contact. J. Biol. Chem. 275, 11383-11388 (2000). This work, together with reference 47, demonstrated that β1 and β2 subunits of Nav channels are cell adhesion molecules that mediate cell-cell adhesion through both homotypic interactions and interactions with other cell adhesion molecules.
    • (2000) J. Biol. Chem. , vol.275 , pp. 11383-11388
    • Malhotra, J.D.1    Kazen-Gillespie, K.2    Hortsch, M.3    Isom, L.L.4
  • 56
    • 0035939078 scopus 로고    scopus 로고
    • Sodium channel β1 and β3 subunits associate with neurofascin through their extracellular immunoglobulin-like domain
    • Ratcliffe C. F. , Westenbroek R. E. , Curtis R. & Catterall W. A. Sodium channel β1 and β3 subunits associate with neurofascin through their extracellular immunoglobulin-like domain. J. Cell Biol. 154, 427-434 (2001).
    • (2001) J. Cell Biol. , vol.154 , pp. 427-434
    • Ratcliffe, C.F.1    Westenbroek, R.E.2    Curtis, R.3    Catterall, W.A.4
  • 57
    • 4644348991 scopus 로고    scopus 로고
    • Tyrosine-phosphorylated and nonphosphorylated sodium channel β1 subunits are differentially localized in cardiac myocytes
    • Malhotra, J. D., Thyagarajan, V., Chen, C. & Isom, L. L. Tyrosine-phosphorylated and nonphosphorylated sodium channel β1 subunits are differentially localized in cardiac myocytes. J. Biol. Chem. 279, 40748-40754 (2004).
    • (2004) J. Biol. Chem. , vol.279 , pp. 40748-40754
    • Malhotra, J.D.1    Thyagarajan, V.2    Chen, C.3    Isom, L.L.4
  • 58
    • 0032418740 scopus 로고    scopus 로고
    • Interaction of voltage-gated sodium channels with the extracellular matrix molecules tenascin-C and tenascin-R
    • Srinivasan, J., Schachner, M. & Catterall, W. A. Interaction of voltage-gated sodium channels with the extracellular matrix molecules tenascin-C and tenascin-R. Proc. Natl Acad. Sci. USA 95, 15753-15757 (1998).
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 15753-15757
    • Srinivasan, J.1    Schachner, M.2    Catterall, W.A.3
  • 59
    • 0033543659 scopus 로고    scopus 로고
    • Tenascin-R is a functional modulator of sodium channel β subunits
    • Xiao, Z. C. et al. Tenascin-R is a functional modulator of sodium channel β subunits. J. Biol. Chem. 274, 26511-26517 (1999).
    • (1999) J. Biol. Chem. , vol.274 , pp. 26511-26517
    • Xiao, Z.C.1
  • 60
    • 1942501741 scopus 로고    scopus 로고
    • Sodium channel β1 subunit-mediated modulation of Nav1. 2 currents and cell surface density is dependent on interactions with contactin and ankyrin
    • McEwen, D. P., Meadows, L. S., Chen, C., Thyagarajan, V. & Isom, L. L. Sodium channel β1 subunit-mediated modulation of Nav1. 2 currents and cell surface density is dependent on interactions with contactin and ankyrin. J. Biol. Chem. 279, 16044-16049 (2004).
    • (2004) J. Biol. Chem. , vol.279 , pp. 16044-16049
    • McEwen, D.P.1    Meadows, L.S.2    Chen, C.3    Thyagarajan, V.4    Isom, L.L.5
  • 61
    • 33644819526 scopus 로고    scopus 로고
    • A common ankyrin-G-based mechanism retains KCNQ and NaV channels at electrically active domains of the axon
    • Pan, Z. et al. A common ankyrin-G-based mechanism retains KCNQ and NaV channels at electrically active domains of the axon. J. Neurosci. 26, 2599-2613 (2006).
    • (2006) J. Neurosci. , vol.26 , pp. 2599-2613
    • Pan, Z.1
  • 62
    • 0037135555 scopus 로고    scopus 로고
    • Structural requirements for interaction of sodium channel β1 subunits with ankyrin
    • Malhotra, J. D. et al. Structural requirements for interaction of sodium channel β1 subunits with ankyrin. J. Biol. Chem. 277, 26681-26688 (2002).
    • (2002) J. Biol. Chem. , vol.277 , pp. 26681-26688
    • Malhotra, J.D.1
  • 63
    • 0033915419 scopus 로고    scopus 로고
    • A sodium channel signaling complex: Modulation by associated receptor protein tyrosine phosphatase β
    • Ratcliffe, C. F. et al. A sodium channel signaling complex: modulation by associated receptor protein tyrosine phosphatase β. Nature Neurosci. 3, 437-444 (2000).
    • (2000) Nature Neurosci. , vol.3 , pp. 437-444
    • Ratcliffe, C.F.1
  • 64
    • 10944261324 scopus 로고    scopus 로고
    • Sodium channel β1 subunits promote neurite outgrowth in cerebellar granule neurons
    • Davis, T. H., Chen, C. & Isom, L. L. Sodium channel β1 subunits promote neurite outgrowth in cerebellar granule neurons. J. Biol. Chem. 279, 51424-51432 (2004).
    • (2004) J. Biol. Chem. , vol.279 , pp. 51424-51432
    • Davis, T.H.1    Chen, C.2    Isom, L.L.3
  • 65
    • 20744454142 scopus 로고    scopus 로고
    • β subunits of voltage-gated sodium channels are novel substrates of β-site amyloid precursor protein-cleaving enzyme (BACE1) and γ-secretase
    • Wong H. K. et al. β subunits of voltage-gated sodium channels are novel substrates of β-site amyloid precursor protein-cleaving enzyme (BACE1) and γ-secretase. J. Biol. Chem. 280, 23009-23017 (2005).
    • (2005) J. Biol. Chem. , vol.280 , pp. 23009-23017
    • Wong, H.K.1
  • 66
    • 20744458852 scopus 로고    scopus 로고
    • Presenilin/γ-secretase-mediated cleavage of the voltage-gated sodium channel β2-subunit regulates cell adhesion and migration
    • Kim, D. Y., MacKenzie Ingano, L. A., Carey, B. W., Pettingell, W. H. & Kovacs, D. M. Presenilin/γ-secretase-mediated cleavage of the voltage-gated sodium channel β2-subunit regulates cell adhesion and migration. J. Biol. Chem. 280, 23251-23261 (2005).
    • (2005) J. Biol. Chem. , vol.280 , pp. 23251-23261
    • Kim, D.Y.1    MacKenzie Ingano, L.A.2    Carey, B.W.3    Pettingell, W.H.4    Kovacs, D.M.5
  • 67
    • 0025809446 scopus 로고
    • Voltage-sensor of excitation-contraction coupling in skeletal muscle
    • Rios, E. & Pizzaro, G. Voltage-sensor of excitation-contraction coupling in skeletal muscle. Physiol. Rev. 71, 849-908 (1991).
    • (1991) Physiol. Rev. , vol.71 , pp. 849-908
    • Rios, E.1    Pizzaro, G.2
  • 70
    • 33644824170 scopus 로고    scopus 로고
    • 4 subunit creates a uniquely folded N-terminal protein binding domain with cell-specific expression in the cerebellar cortex
    • 4 subunit creates a uniquely folded N-terminal protein binding domain with cell-specific expression in the cerebellar cortex. J. Neurosci. 26, 2635-2644 (2006).
    • (2006) J. Neurosci. , vol.26 , pp. 2635-2644
    • Vendel, A.C.1
  • 72
    • 16544389003 scopus 로고    scopus 로고
    • Calcium- and dynamin-independent endocytosis in dorsal root ganglion neurons
    • Zhang, C. et al. Calcium- and dynamin-independent endocytosis in dorsal root ganglion neurons. Neuron 42, 225-236 (2004).
    • (2004) Neuron , vol.42 , pp. 225-236
    • Zhang, C.1
  • 73
    • 0036242425 scopus 로고    scopus 로고
    • 2+-independent but voltage-dependent secretion in mammalian dorsal root ganglion neurons
    • 2+-independent but voltage-dependent secretion in mammalian dorsal root ganglion neurons. Nature Neurosci. 5, 425-430 (2002).
    • (2002) Nature Neurosci. , vol.5 , pp. 425-430
    • Zhang, C.1    Zhou, Z.2
  • 75
    • 0035850819 scopus 로고    scopus 로고
    • Signaling to the nucleus by an L-type calcium channel-calmodulin complex through the MAP kinase pathway
    • Dolmetsch, R. E., Pajvani, U., Fife, K., Spotts, J. M. & Greenberg, M. E. Signaling to the nucleus by an L-type calcium channel-calmodulin complex through the MAP kinase pathway. Science 294, 333-339 (2001).
    • (2001) Science , vol.294 , pp. 333-339
    • Dolmetsch, R.E.1    Pajvani, U.2    Fife, K.3    Spotts, J.M.4    Greenberg, M.E.5
  • 76
    • 0032510478 scopus 로고    scopus 로고
    • Translocation of calmodulin to the nucleus supports CREB phosphorylation in hippocampal neurons
    • Deisseroth, K., Heist, E. K. & Tsien, R. W. Translocation of calmodulin to the nucleus supports CREB phosphorylation in hippocampal neurons. Nature 392, 198-202 (1998).
    • (1998) Nature , vol.392 , pp. 198-202
    • Deisseroth, K.1    Heist, E.K.2    Tsien, R.W.3
  • 77
    • 0035949578 scopus 로고    scopus 로고
    • Calcium regulation of neuronal gene expression
    • West A. E. et al. Calcium regulation of neuronal gene expression. Proc. Natl Acad. Sci. USA 98, 11024-11031 (2001).
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 11024-11031
    • West, A.E.1
  • 78
    • 0035903175 scopus 로고    scopus 로고
    • 2+ channels
    • 2+ channels. J. Biol. Chem. 276, 30794-30802 (2001).
    • (2001) J. Biol. Chem. , vol.276 , pp. 30794-30802
    • Pitt, G.S.1
  • 81
    • 0042197392 scopus 로고    scopus 로고
    • 2+ homeostasis by TRPM7
    • 2+ homeostasis by TRPM7. Cell 114, 191-200 (2003).
    • (2003) Cell , vol.114 , pp. 191-200
    • Schmitz, C.1
  • 83
    • 0035328671 scopus 로고    scopus 로고
    • Trp-p8, a novel prostate-specific gene, is up-regulated in prostate cancer and other malignancies and shares high homology with transient receptor potential calcium channel proteins
    • Tsavaler, L., Shapero, M. H., Morkowski, S. & Laus, R. Trp-p8, a novel prostate-specific gene, is up-regulated in prostate cancer and other malignancies and shares high homology with transient receptor potential calcium channel proteins. Cancer Res. 61, 3760-3769 (2001).
    • (2001) Cancer Res. , vol.61 , pp. 3760-3769
    • Tsavaler, L.1    Shapero, M.H.2    Morkowski, S.3    Laus, R.4
  • 84
    • 3042670473 scopus 로고    scopus 로고
    • The transient receptor potential superfamily of ion channels
    • Huang, C.-L. The transient receptor potential superfamily of ion channels. J. Amer. Soc. Nephrol. 15, 1690-1699 (2004).
    • (2004) J. Amer. Soc. Nephrol. , vol.15 , pp. 1690-1699
    • Huang, C.-L.1
  • 85
    • 1942501853 scopus 로고    scopus 로고
    • Dual-function ion channel/protein kinases: Novel components of vertebrate magnesium regulatory mechanisms
    • Schmitz, C., Perraud, A. L., Fleig, A. & Scharenberg, A. M. Dual-function ion channel/protein kinases: novel components of vertebrate magnesium regulatory mechanisms. Pediatric Res. 55, 734-737 (2004).
    • (2004) Pediatric Res. , vol.55 , pp. 734-737
    • Schmitz, C.1    Perraud, A.L.2    Fleig, A.3    Scharenberg, A.M.4
  • 86
    • 0035978751 scopus 로고    scopus 로고
    • ADP-ribose gating of the calcium-permeable LTRPC2 channel revealed by Nudix motif homology
    • Perraud, A. L. et al. ADP-ribose gating of the calcium-permeable LTRPC2 channel revealed by Nudix motif homology. Nature 411, 595-599 (2001).
    • (2001) Nature , vol.411 , pp. 595-599
    • Perraud, A.L.1
  • 87
    • 0035902767 scopus 로고    scopus 로고
    • 2+ influx system mediated by LTRPC2
    • 2+ influx system mediated by LTRPC2. Science 293, 1327-1330 (2001).
    • (2001) Science , vol.293 , pp. 1327-1330
    • Sano, Y.1
  • 88
    • 33646415942 scopus 로고    scopus 로고
    • TRPM2 is an ion channel that modulates hematopoietic cell death through activation of caspases and PARP cleavage
    • Zhang, W. et al. TRPM2 is an ion channel that modulates hematopoietic cell death through activation of caspases and PARP cleavage. Am. J. Physiol. 290, C1146-C1159 (2006).
    • (2006) Am. J. Physiol. , vol.290
    • Zhang, W.1
  • 89
    • 0035131504 scopus 로고    scopus 로고
    • TRP-PLIK, a bifunctional protein with kinase and ion channel activities
    • Runnels, L. W., Yue, L. & Clapham, D. E. TRP-PLIK, a bifunctional protein with kinase and ion channel activities. Science 291, 1043-1047 (2001). Demonstrated that the TRPM7 non-selective cation channel has intrinsic protein kinase activity that can phosphorylate itself and exogenous substrates, and that this kinase activity is essential for channel function.
    • (2001) Science , vol.291 , pp. 1043-1047
    • Runnels, L.W.1    Yue, L.2    Clapham, D.E.3
  • 90
    • 18544369466 scopus 로고    scopus 로고
    • Hypomagnesemia with secondary hypocalcemia is caused by mutations in TRPM6, a new member of the TRPM gene family
    • Schlingmann, K. P. et al. Hypomagnesemia with secondary hypocalcemia is caused by mutations in TRPM6, a new member of the TRPM gene family. Nature Genet. 31, 166-170 (2002).
    • (2002) Nature Genet. , vol.31 , pp. 166-170
    • Schlingmann, K.P.1
  • 91
    • 0036592004 scopus 로고    scopus 로고
    • Mutation of TRPM6 causes familial hypomagnesemia with secondary hypocalcemia
    • Walder, R. Y. et al. Mutation of TRPM6 causes familial hypomagnesemia with secondary hypocalcemia. Nature Genet. 31, 171-174 (2002).
    • (2002) Nature Genet. , vol.31 , pp. 171-174
    • Walder, R.Y.1
  • 92
    • 0942265537 scopus 로고    scopus 로고
    • Characterization of the protein kinase activity of TRPM7/ChaK1, a protein kinase fused to the transient receptor potential ion channel
    • Ryazanova, L. V., Dorovkov, M. V., Ansari, A. & Ryazanov, A. G. Characterization of the protein kinase activity of TRPM7/ChaK1, a protein kinase fused to the transient receptor potential ion channel. J. Biol. Chem. 279, 3708-3716 (2004).
    • (2004) J. Biol. Chem. , vol.279 , pp. 3708-3716
    • Ryazanova, L.V.1    Dorovkov, M.V.2    Ansari, A.3    Ryazanov, A.G.4
  • 93
    • 1942437482 scopus 로고    scopus 로고
    • Receptor-mediated regulation of the TRPM7 channel through its endogenous protein kinase domain
    • Takezawa, R. et al. Receptor-mediated regulation of the TRPM7 channel through its endogenous protein kinase domain. Proc. Natl Acad. Sci. USA. 101, 6009-6014 (2004).
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 6009-6014
    • Takezawa, R.1
  • 94
    • 27844523226 scopus 로고    scopus 로고
    • The channel kinases TRPM6 and TRPM7 are functionally nonredundant
    • Schmitz, C. et al. The channel kinases TRPM6 and TRPM7 are functionally nonredundant. J. Biol. Chem. 280, 37763-37771 (2005).
    • (2005) J. Biol. Chem. , vol.280 , pp. 37763-37771
    • Schmitz, C.1
  • 95
    • 0035806961 scopus 로고    scopus 로고
    • The Caenorhabditis elegans autosomal dominant polycystic kidney disease gene homologs lov-1 and pkd-2 act in the same pathway
    • Barr, M. M. et al. The Caenorhabditis elegans autosomal dominant polycystic kidney disease gene homologs lov-1 and pkd-2 act in the same pathway. Curr Biol. 11, 1341-1346 (2001).
    • (2001) Curr Biol. , vol.11 , pp. 1341-1346
    • Barr, M.M.1
  • 96
    • 0033598394 scopus 로고    scopus 로고
    • A polycystic kidney-disease gene homologue required for male mating behaviour in C. elegans
    • Barr, M. M. & Sternberg, P. W. A polycystic kidney-disease gene homologue required for male mating behaviour in C. elegans. Nature 401, 386-389 (1999).
    • (1999) Nature , vol.401 , pp. 386-389
    • Barr, M.M.1    Sternberg, P.W.2
  • 97
    • 2942584916 scopus 로고    scopus 로고
    • The N-terminal extracellular domain is required for polycystin-1- dependent channel activity
    • Babich, V. et al. The N-terminal extracellular domain is required for polycystin-1-dependent channel activity. J. Biol. Chem. 279, 25582-25589 (2004).
    • (2004) J. Biol. Chem. , vol.279 , pp. 25582-25589
    • Babich, V.1
  • 98
    • 33644861926 scopus 로고    scopus 로고
    • Polycystin-2 regulates proliferation and branching morphogenesis in kidney epithelial cells
    • Grimm, D. H. et al. Polycystin-2 regulates proliferation and branching morphogenesis in kidney epithelial cells. J. Biol. Chem. 281, 137-144 (2006).
    • (2006) J. Biol. Chem. , vol.281 , pp. 137-144
    • Grimm, D.H.1
  • 99
    • 0032508040 scopus 로고    scopus 로고
    • A family of hyperpolarization-activated mammalian cation channels
    • Ludwig, A., Zong, X., Jeglitsch, M., Hoffmann, F. & Biel, M. A family of hyperpolarization-activated mammalian cation channels. Nature 393, 587-591 (1998).
    • (1998) Nature , vol.393 , pp. 587-591
    • Ludwig, A.1    Zong, X.2    Jeglitsch, M.3    Hoffmann, F.4    Biel, M.5
  • 100
    • 0032876976 scopus 로고    scopus 로고
    • Differential distribution of four hyperpolarization-activated cation channels in mouse brain
    • Moosmang, S., Biel, M., Hofmann, F. & Ludwig A. Differential distribution of four hyperpolarization-activated cation channels in mouse brain. Biol. Chem. 380, 975-980 (1999).
    • (1999) Biol. Chem. , vol.380 , pp. 975-980
    • Moosmang, S.1    Biel, M.2    Hofmann, F.3    Ludwig, A.4
  • 101
    • 0034734788 scopus 로고    scopus 로고
    • Cloning and localization of the hyperpolarization-activated cyclic nucleotide gated channel family in rat brain
    • Monteggia, L. M., Eisch, A. J., Tang, M., Kaczmarek, L. K. & Nestler, E. J., Cloning and localization of the hyperpolarization-activated cyclic nucleotide gated channel family in rat brain. Mol. Brain. Res. 81, 129-139 (2000).
    • (2000) Mol. Brain. Res. , vol.81 , pp. 129-139
    • Monteggia, L.M.1    Eisch, A.J.2    Tang, M.3    Kaczmarek, L.K.4    Nestler, E.J.5
  • 102
    • 3042687500 scopus 로고    scopus 로고
    • Calcium influx through HCN channels does not contribute to cAMP-enhanced transmission
    • Zhong, N., Beaumont, V. & Zucker, R. S. Calcium influx through HCN channels does not contribute to cAMP-enhanced transmission. J. Neurophysiol. 92, 644-647 (2004).
    • (2004) J. Neurophysiol. , vol.92 , pp. 644-647
    • Zhong, N.1    Beaumont, V.2    Zucker, R.S.3
  • 103
    • 2442477647 scopus 로고    scopus 로고
    • 2+, hyperpolarization and cyclic nucleotide-activated channel activation, and actin in temporal synaptic tagging
    • 2+, hyperpolarization and cyclic nucleotide-activated channel activation, and actin in temporal synaptic tagging. J. Neurosci. 24, 4205-4212 (2004).
    • (2004) J. Neurosci. , vol.24 , pp. 4205-4212
    • Zhong, N.1    Zucker, R.S.2
  • 104
    • 0037075203 scopus 로고    scopus 로고
    • h activation and actin: Involvement in long-term facilitation and cAMP-induced synaptic enhancement
    • h activation and actin: involvement in long-term facilitation and cAMP-induced synaptic enhancement. Neuron 33, 601-613 (2002).
    • (2002) Neuron , vol.33 , pp. 601-613
    • Beaumont, V.1    Zhong, N.2    Froemke, R.C.3    Ball, R.W.4    Zucker, R.S.5
  • 105
    • 0033993989 scopus 로고    scopus 로고
    • Enhancement of synaptic transmission by cyclic AMP modulation of presynaptic Ih channels
    • Beaumont, V. & Zucker, R. S. Enhancement of synaptic transmission by cyclic AMP modulation of presynaptic Ih channels. Nature Neurosci. 3, 133-141 (2000).
    • (2000) Nature Neurosci. , vol.3 , pp. 133-141
    • Beaumont, V.1    Zucker, R.S.2
  • 106
    • 17044424577 scopus 로고    scopus 로고
    • Sites of proteolytic processing and noncovalent association of the distal C-terminal domain of CaV1. 1 channels in skeletal muscle
    • Hulme, J. T. et al. Sites of proteolytic processing and noncovalent association of the distal C-terminal domain of CaV1. 1 channels in skeletal muscle. Proc. Natl Acad. Sci. USA 102, 5274-5279 (2005).
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 5274-5279
    • Hulme, J.T.1
  • 107
    • 0029915158 scopus 로고    scopus 로고
    • N-methyl-D-aspartate receptor-induced proteolytic conversion of postsynaptic class C L-type calcium channels in hippocampal neurons
    • Hell, J. W. et al. N-methyl-D-aspartate receptor-induced proteolytic conversion of postsynaptic class C L-type calcium channels in hippocampal neurons. Proc. Natl Acad. Sci. USA 93, 3362-3367 (1996).
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 3362-3367
    • Hell, J.W.1
  • 108
    • 0035824482 scopus 로고    scopus 로고
    • Signal transduction. RIPping tyrosine kinase receptors apart
    • Heldin, C. H. & Ericsson, J. Signal transduction. RIPping tyrosine kinase receptors apart. Science 294, 2111-2113 (2001).
    • (2001) Science , vol.294 , pp. 2111-2113
    • Heldin, C.H.1    Ericsson, J.2
  • 109
    • 85047694216 scopus 로고    scopus 로고
    • Mechanical stimuli induce cleavage and nuclear translocation of the polycystin-1 C terminus
    • Chauvet, V. et al. Mechanical stimuli induce cleavage and nuclear translocation of the polycystin-1 C terminus. J. Clin. Invest. 114, 1433-1443 (2004).
    • (2004) J. Clin. Invest. , vol.114 , pp. 1433-1443
    • Chauvet, V.1
  • 110
    • 0026530216 scopus 로고
    • Regulation of adenylyl cyclase from Paramecium by an intrinsic potassium conductance
    • Schultz, J. E., Klumpp, S., Benz, R., Schurhoff-Goeters, W. J. & Schmid, A. Regulation of adenylyl cyclase from Paramecium by an intrinsic potassium conductance. Science 255, 600-603 (1992).
    • (1992) Science , vol.255 , pp. 600-603
    • Schultz, J.E.1    Klumpp, S.2    Benz, R.3    Schurhoff-Goeters, W.J.4    Schmid, A.5
  • 111
    • 0018400806 scopus 로고
    • Ionic mechanisms of excitation in Paramecium
    • Eckert, R. & Brehm, P. Ionic mechanisms of excitation in Paramecium. Ann. Rev. Biophys. Bioeng. 8, 353-383 (1979).
    • (1979) Ann. Rev. Biophys. Bioeng. , vol.8 , pp. 353-383
    • Eckert, R.1    Brehm, P.2
  • 112
    • 0027568931 scopus 로고
    • Guanine nucleotides modulate calcium currents in a marine Paramecium
    • Bernal, J. & Ehrlich, B. E. Guanine nucleotides modulate calcium currents in a marine Paramecium. J. Exp. Biol. 176, 117-133 (1993).
    • (1993) J. Exp. Biol. , vol.176 , pp. 117-133
    • Bernal, J.1    Ehrlich, B.E.2
  • 114
    • 21744438625 scopus 로고    scopus 로고
    • Phosphoinositide phosphatase activity coupled to an intrinsic voltage sensor
    • Murata, Y., Iwasaki, H., Sasaki, M., Inaba, K. & Okamura, Y. Phosphoinositide phosphatase activity coupled to an intrinsic voltage sensor. Nature 435, 1239-1243 (2005). Provides an example in which evolution has linked the voltage-sensing S1-S4 segments of voltage-gated channels to a phosphoinositide phosphatase, producing a voltage-sensitive enzyme with no apparent channel activity.
    • (2005) Nature , vol.435 , pp. 1239-1243
    • Murata, Y.1    Iwasaki, H.2    Sasaki, M.3    Inaba, K.4    Okamura, Y.5
  • 115
    • 33646229810 scopus 로고    scopus 로고
    • A voltage sensor-domain protein is a voltage-gated proton channel
    • Sasaki, M., Takagi, M. & Okamura, Y. A voltage sensor-domain protein is a voltage-gated proton channel. Science 312, 589-592 (2006).
    • (2006) Science , vol.312 , pp. 589-592
    • Sasaki, M.1    Takagi, M.2    Okamura, Y.3
  • 116
    • 33646358260 scopus 로고    scopus 로고
    • A voltage-gated proton-selective channel lacking the pore domain
    • Ramsey, I. S., Moran, M. M., Chong, J. A. & Clapham, D. E. A voltage-gated proton-selective channel lacking the pore domain. Nature 440, 1213-1216 (2006).
    • (2006) Nature , vol.440 , pp. 1213-1216
    • Ramsey, I.S.1    Moran, M.M.2    Chong, J.A.3    Clapham, D.E.4
  • 117
    • 0000521423 scopus 로고    scopus 로고
    • Mediation of neuronal apoptosis by enhancement of outward potassium current
    • Yu, S. P. et al. Mediation of neuronal apoptosis by enhancement of outward potassium current. Science 278, 114-117 (1997).
    • (1997) Science , vol.278 , pp. 114-117
    • Yu, S.P.1
  • 119
    • 0345240928 scopus 로고    scopus 로고
    • Potassium is a critical regulator of apoptotic enzymes in vitro and in vivo
    • Hughes, F. M. Jr & Cidlowski, J. A. Potassium is a critical regulator of apoptotic enzymes in vitro and in vivo. Adv. Enz. Regul. 39, 157-171 (1999).
    • (1999) Adv. Enz. Regul. , vol.39 , pp. 157-171
    • Hughes Jr., F.M.1    Cidlowski, J.A.2
  • 120
    • 0038755195 scopus 로고    scopus 로고
    • Mediation of neuronal apoptosis by Kv2.1-encoded potassium channels
    • Pal, S., Hartnett, K. A., Nerbonne, J. M., Levitan, E. S. & Aizenman, E. Mediation of neuronal apoptosis by Kv2.1-encoded potassium channels. J. Neurosci. 23, 4798-4802 (2003).
    • (2003) J. Neurosci. , vol.23 , pp. 4798-4802
    • Pal, S.1    Hartnett, K.A.2    Nerbonne, J.M.3    Levitan, E.S.4    Aizenman, E.5
  • 121
    • 33746880609 scopus 로고    scopus 로고
    • Mitochondrial factors with duals roles in death and survival
    • Cheng, W.-C. et al. Mitochondrial factors with duals roles in death and survival. Oncogene 25, 4697-4705 (2006).
    • (2006) Oncogene , vol.25 , pp. 4697-4705
    • Cheng, W.-C.1
  • 123
    • 0036086809 scopus 로고    scopus 로고
    • Apoptosis recruits two-pore domain potassium channels used for homeostatic volume regulation
    • Trimarchi, J. R., Liu, L., Smith, P. J. & Keefe, D. L. Apoptosis recruits two-pore domain potassium channels used for homeostatic volume regulation. Am. J. Physiol. 282, C588-C594 (2002).
    • (2002) Am. J. Physiol. , vol.282
    • Trimarchi, J.R.1    Liu, L.2    Smith, P.J.3    Keefe, D.L.4
  • 124
    • 0041355326 scopus 로고    scopus 로고
    • Stimulation of Kv1.3 potassium channels by death receptors during apoptosis in Jurkat T lymphocytes
    • Storey, N. M., Gomez-Angelats, M., Bortner, C. D., Armstrong, D. L. & Cidlowski, J. A. Stimulation of Kv1.3 potassium channels by death receptors during apoptosis in Jurkat T lymphocytes. J. Biol. Chem. 278, 33319-33326 (2003).
    • (2003) J. Biol. Chem. , vol.278 , pp. 33319-33326
    • Storey, N.M.1    Gomez-Angelats, M.2    Bortner, C.D.3    Armstrong, D.L.4    Cidlowski, J.A.5
  • 125
    • 33645300737 scopus 로고    scopus 로고
    • From molecule to malady
    • Ashcroft F. M. From molecule to malady. Nature 440, 440-447 (2006).
    • (2006) Nature , vol.440 , pp. 440-447
    • Ashcroft, F.M.1
  • 126
    • 33645421783 scopus 로고    scopus 로고
    • Mutations in voltage-gated potassium channel KCNC3 cause degenerative and developmental central nervous system phenotypes
    • Waters, M. F. et al. Mutations in voltage-gated potassium channel KCNC3 cause degenerative and developmental central nervous system phenotypes. Nature Genet. 38, 447-451 (2006).
    • (2006) Nature Genet. , vol.38 , pp. 447-451
    • Waters, M.F.1
  • 127
    • 17344367657 scopus 로고    scopus 로고
    • +-channel β1 subunit gene SCN1B
    • +-channel β1 subunit gene SCN1B. Nature Genet. 19, 366-370 (1998).
    • (1998) Nature Genet. , vol.19 , pp. 366-370
    • Wallace, R.H.1
  • 128
    • 0037115031 scopus 로고    scopus 로고
    • Functional and biochemical analysis of a sodium channel β1 subunit mutation responsible for generalized epilepsy with febrile seizures plus type 1
    • Meadows, L. S. et al. Functional and biochemical analysis of a sodium channel β1 subunit mutation responsible for generalized epilepsy with febrile seizures plus type 1. J. Neurosci. 22, 10699-10709 (2002).
    • (2002) J. Neurosci. , vol.22 , pp. 10699-10709
    • Meadows, L.S.1
  • 129
    • 33746530608 scopus 로고    scopus 로고
    • Sodium channel β4 subunit: Down-regulation and possible involvement in neuritic degeneration in Huntington's disease transgenic mice
    • Oyama, F. et al. Sodium channel β4 subunit: down-regulation and possible involvement in neuritic degeneration in Huntington's disease transgenic mice. J. Neurochem. 98, 518-529 (2006).
    • (2006) J. Neurochem. , vol.98 , pp. 518-529
    • Oyama, F.1
  • 130
    • 6544269945 scopus 로고    scopus 로고
    • Isolation of a novel potassium channel gene hSKCa3 containing a polymorphic CAG repeat: A candidate for schizophrenia and bipolar disorder?
    • Chandy, K. G. et al. Isolation of a novel potassium channel gene hSKCa3 containing a polymorphic CAG repeat: a candidate for schizophrenia and bipolar disorder? Mol. Psychiatry 3, 2-7 (1998).
    • (1998) Mol. Psychiatry , vol.3 , pp. 2-7
    • Chandy, K.G.1
  • 131
    • 0035958882 scopus 로고    scopus 로고
    • Nuclear localization and dominant-negative suppression by a mutant SKCa3 N-terminal channel fragment identified in a patient with schizophrenia
    • Miller, M. J. et al. Nuclear localization and dominant-negative suppression by a mutant SKCa3 N-terminal channel fragment identified in a patient with schizophrenia. J. Biol. Chem. 276, 27753-27756 (2001).
    • (2001) J. Biol. Chem. , vol.276 , pp. 27753-27756
    • Miller, M.J.1
  • 132
    • 0026542166 scopus 로고
    • Differential expression of two distinct forms of mRNA encoding members of a dipeptidyl aminopeptidase family
    • Wada, K. et al. Differential expression of two distinct forms of mRNA encoding members of a dipeptidyl aminopeptidase family. Proc. Natl Acad. Sci. USA 89, 197-201 (1992).
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 197-201
    • Wada, K.1
  • 133
    • 0037421685 scopus 로고    scopus 로고
    • + channels
    • + channels. Neuron 37, 449-461 (2003).
    • (2003) Neuron , vol.37 , pp. 449-461
    • Nadal, M.S.1
  • 134
    • 0038343840 scopus 로고    scopus 로고
    • Cloning and characterization of dipeptidyl peptidase 10, a new member of an emerging subgroup of serine proteases
    • Qi, S. Y., Riviere, P. J. Trojnar, J., Junien, J. L. & Akinsanya, K. O. Cloning and characterization of dipeptidyl peptidase 10, a new member of an emerging subgroup of serine proteases. Biochem. J. 373, 179-189 (2003).
    • (2003) Biochem. J. , vol.373 , pp. 179-189
    • Qi, S.Y.1    Riviere, P.J.2    Trojnar, J.3    Junien, J.L.4    Akinsanya, K.O.5
  • 135
    • 21344464599 scopus 로고    scopus 로고
    • DPP10 modulates Kv4-mediated A-type potassium channels
    • Zagha, E. et al. DPP10 modulates Kv4-mediated A-type potassium channels. J. Biol. Chem. 280, 18853-18861 (2005).
    • (2005) J. Biol. Chem. , vol.280 , pp. 18853-18861
    • Zagha, E.1
  • 136
    • 0035110301 scopus 로고    scopus 로고
    • Biosynthesis and characterization of the brain-specific membrane protein DPPX, a dipeptidyl peptidase IV-related protein
    • Kin, Y., Misumi, Y. & Ikehara, Y. Biosynthesis and characterization of the brain-specific membrane protein DPPX, a dipeptidyl peptidase IV-related protein. J. Biochem. 129, 289-295 (2001).
    • (2001) J. Biochem. , vol.129 , pp. 289-295
    • Kin, Y.1    Misumi, Y.2    Ikehara, Y.3
  • 137
    • 23444436221 scopus 로고    scopus 로고
    • Microglia Kv1. 3 channels contribute to their ability to kill neurons
    • Fordyce, C. B., Jagasia, R., Zhu, X. & Schlichter, L. C. Microglia Kv1. 3 channels contribute to their ability to kill neurons. J. Neurosci. 25, 7139-7149 (2005).
    • (2005) J. Neurosci. , vol.25 , pp. 7139-7149
    • Fordyce, C.B.1    Jagasia, R.2    Zhu, X.3    Schlichter, L.C.4
  • 138
    • 0032054272 scopus 로고    scopus 로고
    • Down-regulation of the novel gene melastatin correlates with potential for melanoma metastasis
    • Duncan, L. M. et al. Down-regulation of the novel gene melastatin correlates with potential for melanoma metastasis. Cancer Res. 58, 1515-1520 (1998).
    • (1998) Cancer Res. , vol.58 , pp. 1515-1520
    • Duncan, L.M.1
  • 139
    • 29544449966 scopus 로고    scopus 로고
    • TRPV6 potentiates calcium-dependent cell proliferation
    • Schwarz, E. C. et al. TRPV6 potentiates calcium-dependent cell proliferation. Cell Calcium 39, 163-173 (2006).
    • (2006) Cell Calcium , vol.39 , pp. 163-173
    • Schwarz, E.C.1


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