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Volumn 41, Issue 4, 2004, Pages 573-586

Structural Insights into the Functional Interaction of KChIP1 with Shal-Type K+ Channels

Author keywords

[No Author keywords available]

Indexed keywords

CALCIUM BINDING PROTEIN; CALMODULIN; DIMER; UNCLASSIFIED DRUG; VOLTAGE GATED POTASSIUM CHANNEL; VOLTAGE GATED POTASSIUM CHANNEL INTERACTING PROTEIN 1;

EID: 1342333776     PISSN: 08966273     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0896-6273(04)00045-5     Document Type: Article
Times cited : (109)

References (57)
  • 2
    • 0033516487 scopus 로고    scopus 로고
    • Three-dimensional structure of guanylyl cyclase activating protein-2, a calcium-sensitive modulator of photoreceptor guanylyl cyclases
    • Ames J.B., Dizhoor A.M., Ikura M., Palczewski K., Stryer L. Three-dimensional structure of guanylyl cyclase activating protein-2, a calcium-sensitive modulator of photoreceptor guanylyl cyclases. J. Biol. Chem. 274:1999;19329-19337.
    • (1999) J. Biol. Chem. , vol.274 , pp. 19329-19337
    • Ames, J.B.1    Dizhoor, A.M.2    Ikura, M.3    Palczewski, K.4    Stryer, L.5
  • 5
    • 0035968232 scopus 로고    scopus 로고
    • Conserved Kv4 N-terminal domain critical for effects of Kv channel-interacting protein 2.2 on channel expression and gating
    • Bahring R., Dannenberg J., Peters H.C., Leicher T., Pongs O., Isbrandt D. Conserved Kv4 N-terminal domain critical for effects of Kv channel-interacting protein 2.2 on channel expression and gating. J. Biol. Chem. 276:2001;23888-23894.
    • (2001) J. Biol. Chem. , vol.276 , pp. 23888-23894
    • Bahring, R.1    Dannenberg, J.2    Peters, H.C.3    Leicher, T.4    Pongs, O.5    Isbrandt, D.6
  • 6
    • 0026077184 scopus 로고
    • Characterization of a mammalian cDNA for an inactivating voltage-sensitive K+ channel
    • Baldwin T.J., Tsaur M.L., Lopez G.A., Jan Y.N., Jan L.Y. Characterization of a mammalian cDNA for an inactivating voltage-sensitive K+ channel. Neuron. 7:1991;471-483.
    • (1991) Neuron , vol.7 , pp. 471-483
    • Baldwin, T.J.1    Tsaur, M.L.2    Lopez, G.A.3    Jan, Y.N.4    Jan, L.Y.5
  • 7
    • 0036487139 scopus 로고    scopus 로고
    • Remodelling inactivation gating of Kv4 channels by KChIP1, a small-molecular-weight calcium-binding protein
    • Beck E.J., Bowlby M., An W.F., Rhodes K.J., Covarrubias M. Remodelling inactivation gating of Kv4 channels by KChIP1, a small-molecular-weight calcium-binding protein. J. Physiol. 538:2002;691-706.
    • (2002) J. Physiol. , vol.538 , pp. 691-706
    • Beck, E.J.1    Bowlby, M.2    An, W.F.3    Rhodes, K.J.4    Covarrubias, M.5
  • 9
    • 0035853716 scopus 로고    scopus 로고
    • Immunocytochemical localization and crystal structure of human frequenin (neuronal calcium sensor 1)
    • Bourne Y., Dannenberg J., Pollmann V., Marchot P., Pongs O. Immunocytochemical localization and crystal structure of human frequenin (neuronal calcium sensor 1). J. Biol. Chem. 276:2001;11949-11955.
    • (2001) J. Biol. Chem. , vol.276 , pp. 11949-11955
    • Bourne, Y.1    Dannenberg, J.2    Pollmann, V.3    Marchot, P.4    Pongs, O.5
  • 10
    • 0032895315 scopus 로고    scopus 로고
    • Intracellular neuronal calcium sensor proteins: A family of EF-hand calcium-binding proteins in search of a function
    • Braunewell K.H., Gundelfinger E.D. Intracellular neuronal calcium sensor proteins. a family of EF-hand calcium-binding proteins in search of a function Cell Tissue Res. 295:1999;1-12.
    • (1999) Cell Tissue Res. , vol.295 , pp. 1-12
    • Braunewell, K.H.1    Gundelfinger, E.D.2
  • 11
    • 0035156560 scopus 로고    scopus 로고
    • The neuronal calcium sensor family of Ca2+-binding proteins
    • Burgoyne R.D., Weiss J.L. The neuronal calcium sensor family of Ca2+-binding proteins. Biochem. J. 353:2001;1-12.
    • (2001) Biochem. J. , vol.353 , pp. 1-12
    • Burgoyne, R.D.1    Weiss, J.L.2
  • 12
    • 0031721511 scopus 로고    scopus 로고
    • Cal, senilin: A calcium-binding protein that interacts with the presenilins and regulates the levels of a presenilin fragment
    • Buxbaum J.D., Choi E.K., Luo Y., Lilliehook C., Crowley A.C., Merriam D.E., Wasco W. Cal, senilin. a calcium-binding protein that interacts with the presenilins and regulates the levels of a presenilin fragment Nat. Med. 4:1998;1177-1181.
    • (1998) Nat. Med. , vol.4 , pp. 1177-1181
    • Buxbaum, J.D.1    Choi, E.K.2    Luo, Y.3    Lilliehook, C.4    Crowley, A.C.5    Merriam, D.E.6    Wasco, W.7
  • 14
    • 2242474818 scopus 로고    scopus 로고
    • Structure of the complex of calmodulin with the target sequence of calmodulin-dependent protein kinase I: Studies of the kinase activation mechanism
    • Clapperton J.A., Martin S.R., Smerdon S.J., Gamblin S.J., Bayley P.M. Structure of the complex of calmodulin with the target sequence of calmodulin-dependent protein kinase I. studies of the kinase activation mechanism Biochemistry. 41:2002;14669-14679.
    • (2002) Biochemistry , vol.41 , pp. 14669-14679
    • Clapperton, J.A.1    Martin, S.R.2    Smerdon, S.J.3    Gamblin, S.J.4    Bayley, P.M.5
  • 16
    • 0027429963 scopus 로고
    • Three-dimensional structure of recoverin, a calcium sensor in vision
    • Flaherty K.M., Zozulya S., Stryer L., McKay D.B. Three-dimensional structure of recoverin, a calcium sensor in vision. Cell. 75:1993;709-716.
    • (1993) Cell , vol.75 , pp. 709-716
    • Flaherty, K.M.1    Zozulya, S.2    Stryer, L.3    McKay, D.B.4
  • 17
    • 0029088936 scopus 로고
    • Structures of the troponin C regulatory domains in the apo and calcium-saturated states
    • Gagne S.M., Tsuda S., Li M.X., Smillie L.B., Sykes B.D. Structures of the troponin C regulatory domains in the apo and calcium-saturated states. Nat. Struct. Biol. 2:1995;784-789.
    • (1995) Nat. Struct. Biol. , vol.2 , pp. 784-789
    • Gagne, S.M.1    Tsuda, S.2    Li, M.X.3    Smillie, L.B.4    Sykes, B.D.5
  • 19
    • 0037135631 scopus 로고    scopus 로고
    • Modulation of Kv4-encoded K(+) currents in the mammalian myocardium by neuronal calcium sensor-1
    • Guo W., Malin S.A., Johns D.C., Jeromin A., Nerbonne J.M. Modulation of Kv4-encoded K(+) currents in the mammalian myocardium by neuronal calcium sensor-1. J. Biol. Chem. 277:2002;26436-26443.
    • (2002) J. Biol. Chem. , vol.277 , pp. 26436-26443
    • Guo, W.1    Malin, S.A.2    Johns, D.C.3    Jeromin, A.4    Nerbonne, J.M.5
  • 20
    • 0036261222 scopus 로고    scopus 로고
    • Functional interaction between KChIP1 and GFP-fused Kv4.3L co-expressed in HEK293 cells
    • Hatano N., Ohya S., Imaizumi Y. Functional interaction between KChIP1 and GFP-fused Kv4.3L co-expressed in HEK293 cells. Pflugers Arch. 444:2002;80-88.
    • (2002) Pflugers Arch. , vol.444 , pp. 80-88
    • Hatano, N.1    Ohya, S.2    Imaizumi, Y.3
  • 21
    • 0030855840 scopus 로고    scopus 로고
    • K+ channel regulation of signal propagation in dendrites of hippocampal pyramidal neurons
    • Hoffman D.A., Magee J.C., Colbert C.M., Johnston D. K+ channel regulation of signal propagation in dendrites of hippocampal pyramidal neurons. Nature. 387:1997;869-875.
    • (1997) Nature , vol.387 , pp. 869-875
    • Hoffman, D.A.1    Magee, J.C.2    Colbert, C.M.3    Johnston, D.4
  • 23
    • 0038136900 scopus 로고    scopus 로고
    • Molecular interactions of yeast frequenin (Frq1) with the phosphatidylinositol 4-kinase isoform, Pik1
    • Huttner I.G., Strahl T., Osawa M., King D.S., Ames J.B., Thorner J. Molecular interactions of yeast frequenin (Frq1) with the phosphatidylinositol 4-kinase isoform, Pik1. J. Biol. Chem. 278:2003;4862-4874.
    • (2003) J. Biol. Chem. , vol.278 , pp. 4862-4874
    • Huttner, I.G.1    Strahl, T.2    Osawa, M.3    King, D.S.4    Ames, J.B.5    Thorner, J.6
  • 24
    • 0035054180 scopus 로고    scopus 로고
    • Structure of the RCK domain from the E. coli K+ channel and demonstration of its presence in the human BK channel
    • Jiang Y., Pico A., Cadene M., Chait B.T., MacKinnon R. Structure of the RCK domain from the E. coli K+ channel and demonstration of its presence in the human BK channel. Neuron. 29:2001;593-601.
    • (2001) Neuron , vol.29 , pp. 593-601
    • Jiang, Y.1    Pico, A.2    Cadene, M.3    Chait, B.T.4    MacKinnon, R.5
  • 25
    • 0037198626 scopus 로고    scopus 로고
    • Crystal structure and mechanism of a calcium-gated potassium channel
    • Jiang Y., Lee A., Chen J., Cadene M., Chait B.T., MacKinnon R. Crystal structure and mechanism of a calcium-gated potassium channel. Nature. 417:2002;515-522.
    • (2002) Nature , vol.417 , pp. 515-522
    • Jiang, Y.1    Lee, A.2    Chen, J.3    Cadene, M.4    Chait, B.T.5    MacKinnon, R.6
  • 27
    • 1342326336 scopus 로고    scopus 로고
    • Composition of Ito channels: Kv4.2-KChIP2 complexes carry four subunits of each type
    • in press.
    • Kim, L.A., Furst, J., Butler, M.H., Xu, S., Grigorieff, N., and Goldstein, S.A. (2003). Composition of Ito channels: Kv4.2-KChIP2 complexes carry four subunits of each type. J. Biol. Chem., in press.
    • (2003) J. Biol. Chem.
    • Kim, L.A.1    Furst, J.2    Butler, M.H.3    Xu, S.4    Grigorieff, N.5    Goldstein, S.A.6
  • 29
    • 18244408825 scopus 로고    scopus 로고
    • A defect in the Kv channel-interacting protein 2 (KChIP2) gene leads to a complete loss of I(to) and confers susceptibility to ventricular tachycardia
    • Kuo H.C., Cheng C.F., Clark R.B., Lin J.J., Lin J.L., Hoshijima M., Nguyen-Tran V.T., Gu Y., Ikeda Y., Chu P.H.et al. A defect in the Kv channel-interacting protein 2 (KChIP2) gene leads to a complete loss of I(to) and confers susceptibility to ventricular tachycardia. Cell. 107:2001;801-813.
    • (2001) Cell , vol.107 , pp. 801-813
    • Kuo, H.C.1    Cheng, C.F.2    Clark, R.B.3    Lin, J.J.4    Lin, J.L.5    Hoshijima, M.6    Nguyen-Tran, V.T.7    Gu, Y.8    Ikeda, Y.9    Chu, P.H.10
  • 31
    • 0034100340 scopus 로고    scopus 로고
    • ChIPping away at potassium channel regulation
    • Li M., Adelman J.P. ChIPping away at potassium channel regulation. Nat. Neurosci. 3:2000;202-204.
    • (2000) Nat. Neurosci. , vol.3 , pp. 202-204
    • Li, M.1    Adelman, J.P.2
  • 32
    • 0032127530 scopus 로고    scopus 로고
    • Constraining ligand-binding site stoichiometry suggests that a cyclic nucleotide-gated channel is composed of two functional dimers
    • Liu D.T., Tibbs G.R., Paoletti P., Siegelbaum S.A. Constraining ligand-binding site stoichiometry suggests that a cyclic nucleotide-gated channel is composed of two functional dimers. Neuron. 21:1998;235-248.
    • (1998) Neuron , vol.21 , pp. 235-248
    • Liu, D.T.1    Tibbs, G.R.2    Paoletti, P.3    Siegelbaum, S.A.4
  • 33
    • 0036606360 scopus 로고    scopus 로고
    • ER transport signals and trafficking of potassium channels and receptors
    • Ma D., Jan L.Y. ER transport signals and trafficking of potassium channels and receptors. Curr. Opin. Neurobiol. 12:2002;287-292.
    • (2002) Curr. Opin. Neurobiol. , vol.12 , pp. 287-292
    • Ma, D.1    Jan, L.Y.2
  • 34
    • 0035887891 scopus 로고    scopus 로고
    • Molecular heterogeneity of the voltage-gated fast transient outward K+ current, I(Af), in mammalian neurons
    • Malin S.A., Nerbonne J.M. Molecular heterogeneity of the voltage-gated fast transient outward K+ current, I(Af), in mammalian neurons. J. Neurosci. 21:2001;8004-8014.
    • (2001) J. Neurosci. , vol.21 , pp. 8004-8014
    • Malin, S.A.1    Nerbonne, J.M.2
  • 35
    • 0026794065 scopus 로고
    • Target enzyme recognition by calmodulin: 2.4 a structure of a calmodulin-peptide complex
    • Meador W.E., Means A.R., Quiocho F.A. Target enzyme recognition by calmodulin. 2.4 A structure of a calmodulin-peptide complex Science. 257:1992;1251-1255.
    • (1992) Science , vol.257 , pp. 1251-1255
    • Meador, W.E.1    Means, A.R.2    Quiocho, F.A.3
  • 36
    • 0027759276 scopus 로고
    • Modulation of calmodulin plasticity in molecular recognition on the basis of x-ray structures
    • Meador W.E., Means A.R., Quiocho F.A. Modulation of calmodulin plasticity in molecular recognition on the basis of x-ray structures. Science. 262:1993;1718-1721.
    • (1993) Science , vol.262 , pp. 1718-1721
    • Meador, W.E.1    Means, A.R.2    Quiocho, F.A.3
  • 37
    • 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., Hatano N., Ohya S., Takikawa R., Watabiki T., Takasugi N., Imaizumi Y., Tomita T., Iwatsubo T. 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. 277:2002;14965- 14975.
    • (2002) J. Biol. Chem. , vol.277 , pp. 14965-14975
    • Morohashi, Y.1    Hatano, N.2    Ohya, S.3    Takikawa, R.4    Watabiki, T.5    Takasugi, N.6    Imaizumi, Y.7    Tomita, T.8    Iwatsubo, T.9
  • 39
    • 0041806652 scopus 로고    scopus 로고
    • Determining the basis of channel-tetramerization specificity by x-ray crystallography and a sequence-comparison algorithm: Family values (FamVal)
    • Nanao M.H., Zhou W., Pfaffinger P.J., Choe S. Determining the basis of channel-tetramerization specificity by x-ray crystallography and a sequence-comparison algorithm. family values (FamVal) Proc. Natl. Acad. Sci. USA. 100:2003;8670-8675.
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 8670-8675
    • Nanao, M.H.1    Zhou, W.2    Pfaffinger, P.J.3    Choe, S.4
  • 40
    • 0142184436 scopus 로고    scopus 로고
    • Role of myristoylation in the intracellular targeting of neuronal calcium sensor (NCS) proteins
    • O'Callaghan D.W., Burgoyne R.D. Role of myristoylation in the intracellular targeting of neuronal calcium sensor (NCS) proteins. Biochem. Soc. Trans. 31:2003;963-965.
    • (2003) Biochem. Soc. Trans. , vol.31 , pp. 963-965
    • O'Callaghan, D.W.1    Burgoyne, R.D.2
  • 41
    • 0031059866 scopus 로고    scopus 로고
    • Processing of x-ray diffraction data collected in oscillation mode
    • Otwinowski Z., Minor W. Processing of x-ray diffraction data collected in oscillation mode. Methods Enzymol. 276:1997;307-326.
    • (1997) Methods Enzymol. , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 42
    • 0037112678 scopus 로고    scopus 로고
    • Elucidating KChIP effects on Kv4.3 inactivation and recovery kinetics with a minimal KChIP2 isoform
    • Patel S.P., Campbell D.L., Strauss H.C. Elucidating KChIP effects on Kv4.3 inactivation and recovery kinetics with a minimal KChIP2 isoform. J. Physiol. 545:2002;5-11.
    • (2002) J. Physiol. , vol.545 , pp. 5-11
    • Patel, S.P.1    Campbell, D.L.2    Strauss, H.C.3
  • 43
    • 0242353256 scopus 로고    scopus 로고
    • Effective association of Kv channel-interacting proteins with Kv4 channel is mediated with their unique core peptide
    • Ren X., Shand S.H., Takimoto K. Effective association of Kv channel-interacting proteins with Kv4 channel is mediated with their unique core peptide. J. Biol. Chem. 278:2003;43564-43570.
    • (2003) J. Biol. Chem. , vol.278 , pp. 43564-43570
    • Ren, X.1    Shand, S.H.2    Takimoto, K.3
  • 44
    • 0037077136 scopus 로고    scopus 로고
    • A mechanism of regulating transmembrane potassium flux through a ligand-mediated conformational switch
    • Roosild T.P., Miller S., Booth I.R., Choe S. A mechanism of regulating transmembrane potassium flux through a ligand-mediated conformational switch. Cell. 109:2002;781-791.
    • (2002) Cell , vol.109 , pp. 781-791
    • Roosild, T.P.1    Miller, S.2    Booth, I.R.3    Choe, S.4
  • 45
    • 0346056815 scopus 로고    scopus 로고
    • Cytoplasmic gatekeepers of K channel flux: A structural prespective
    • Roosild T.P., Le K.T., Choe S. Cytoplasmic gatekeepers of K channel flux. a structural prespective Trends Biochem. Sci. 29:2004;39-45.
    • (2004) Trends Biochem. Sci. , vol.29 , pp. 39-45
    • Roosild, T.P.1    Le K., T.2    Choe, S.3
  • 46
    • 0036895725 scopus 로고    scopus 로고
    • PKA modulation of Kv4.2-encoded A-type potassium channels requires formation of a supramolecular complex
    • Schrader L.A., Anderson A.E., Mayne A., Pfaffinger P.J., Sweatt J.D. PKA modulation of Kv4.2-encoded A-type potassium channels requires formation of a supramolecular complex. J. Neurosci. 22:2002;10123-10133.
    • (2002) J. Neurosci. , vol.22 , pp. 10123-10133
    • Schrader, L.A.1    Anderson, A.E.2    Mayne, A.3    Pfaffinger, P.J.4    Sweatt, J.D.5
  • 47
    • 0035953757 scopus 로고    scopus 로고
    • Structure of the gating domain of a Ca2+-activated K+ channel complexed with Ca2+/calmodulin
    • Schumacher M.A., Rivard A.F., Bachinger H.P., Adelman J.P. Structure of the gating domain of a Ca2+-activated K+ channel complexed with Ca2+/calmodulin. Nature. 410:2001;1120-1124.
    • (2001) Nature , vol.410 , pp. 1120-1124
    • Schumacher, M.A.1    Rivard, A.F.2    Bachinger, H.P.3    Adelman, J.P.4
  • 48
    • 1342347452 scopus 로고    scopus 로고
    • Conservation of regulatory function in calcium-binding proteins: Human frequenin (neuronal calcium sensor-1) associates productively with yeast phosphatidylinositol 4-kinase isoform, Pik1
    • Strahl T., Grafelmann B., Dannenberg J., Thorner J., Pongs O. Conservation of regulatory function in calcium-binding proteins. human frequenin (neuronal calcium sensor-1) associates productively with yeast phosphatidylinositol 4-kinase isoform, Pik1 J. Biol. Chem. 278:2003;49589-49599.
    • (2003) J. Biol. Chem. , vol.278 , pp. 49589-49599
    • Strahl, T.1    Grafelmann, B.2    Dannenberg, J.3    Thorner, J.4    Pongs, O.5
  • 50
    • 0037178799 scopus 로고    scopus 로고
    • Palmitoylation of KChIP splicing variants is required for efficient cell surface expression of Kv4.3 channels
    • Takimoto K., Yang E.K., Conforti L. Palmitoylation of KChIP splicing variants is required for efficient cell surface expression of Kv4.3 channels. J. Biol. Chem. 277:2002;26904-26911.
    • (2002) J. Biol. Chem. , vol.277 , pp. 26904-26911
    • Takimoto, K.1    Yang, E.K.2    Conforti, L.3
  • 51
    • 0347627834 scopus 로고    scopus 로고
    • Regulation of hyperpolarization-activated HCN channels by cAMP through a gating switch in binding domain symmetry
    • Ulens C., Siegelbaum S.A. Regulation of hyperpolarization-activated HCN channels by cAMP through a gating switch in binding domain symmetry. Neuron. 40:2003;959-970.
    • (2003) Neuron , vol.40 , pp. 959-970
    • Ulens, C.1    Siegelbaum, S.A.2
  • 52
    • 0032923758 scopus 로고    scopus 로고
    • Crystal structure of recombinant bovine neurocalcin
    • Vijay-Kumar S., Kumar V.D. Crystal structure of recombinant bovine neurocalcin. Nat. Struct. Biol. 6:1999;80-88.
    • (1999) Nat. Struct. Biol. , vol.6 , pp. 80-88
    • Vijay-Kumar, S.1    Kumar, V.D.2
  • 53
    • 0037093639 scopus 로고    scopus 로고
    • Structural analysis, identification, and design of calcium-binding sites in proteins
    • Yang W., Lee H.W., Hellinga H., Yang J.J. Structural analysis, identification, and design of calcium-binding sites in proteins. Proteins. 47:2002;344-356.
    • (2002) Proteins , vol.47 , pp. 344-356
    • Yang, W.1    Lee, H.W.2    Hellinga, H.3    Yang, J.J.4
  • 54
    • 0036359353 scopus 로고    scopus 로고
    • Vector geometry mapping. A method to characterize the conformation of helix-loop-helix calcium-binding proteins
    • Yap K.L., Ames J.B., Swindells M.B., Ikura M. Vector geometry mapping. A method to characterize the conformation of helix-loop-helix calcium-binding proteins. Methods Mol. Biol. 173:2002;317-324.
    • (2002) Methods Mol. Biol. , vol.173 , pp. 317-324
    • Yap, K.L.1    Ames, J.B.2    Swindells, M.B.3    Ikura, M.4
  • 55
    • 0141831003 scopus 로고    scopus 로고
    • Structural basis for modulation and agonist specificity of HCN pacemaker channels
    • Zagotta W.N., Olivier N.B., Black K.D., Young E.C., Olson R., Gouaux E. Structural basis for modulation and agonist specificity of HCN pacemaker channels. Nature. 425:2003;200-205.
    • (2003) Nature , vol.425 , pp. 200-205
    • Zagotta, W.N.1    Olivier, N.B.2    Black, K.D.3    Young, E.C.4    Olson, R.5    Gouaux, E.6
  • 56
    • 0029160568 scopus 로고
    • Calcium-induced conformational transition revealed by the solution structure of apo calmodulin
    • Zhang M., Tanaka T., Ikura M. Calcium-induced conformational transition revealed by the solution structure of apo calmodulin. Nat. Struct. Biol. 2:1995;758-767.
    • (1995) Nat. Struct. Biol. , vol.2 , pp. 758-767
    • Zhang, M.1    Tanaka, T.2    Ikura, M.3
  • 57
    • 0032842884 scopus 로고    scopus 로고
    • Characterization of human Kv4.2 mediating a rapidly-inactivating transient voltage-sensitive K+ current
    • Zhu X.R., Wulf A., Schwarz M., Isbrandt D., Pongs O. Characterization of human Kv4.2 mediating a rapidly-inactivating transient voltage-sensitive K+ current. Receptors Channels. 6:1999;387-400.
    • (1999) Receptors Channels , vol.6 , pp. 387-400
    • Zhu, X.R.1    Wulf, A.2    Schwarz, M.3    Isbrandt, D.4    Pongs, O.5


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