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Volumn 109, Issue 1-2, 2002, Pages 69-83

Voltage-gated Ca2+ channel CaV1.3 subunit expressed in the hair cell epithelium of the sacculus of the trout Oncorhynchus mykiss: Cloning and comparison across vertebrate classes

Author keywords

Calcium channel subunit; Calcium dependent inactivation; Calmodulin; Dihydropyridines; Hair cell; L type voltage gated calcium channel; Octavolateralis; Phosphorylation; Sacculus; Synaptic complex; Teleost

Indexed keywords

CALCIUM CHANNEL; CALCIUM CHANNEL L TYPE; PRIMER DNA; PROTEIN SUBUNIT; CALCIUM; DIHYDROPYRIDINE DERIVATIVE;

EID: 0037203242     PISSN: 0169328X     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0169-328X(02)00522-3     Document Type: Article
Times cited : (16)

References (93)
  • 1
    • 0030931637 scopus 로고    scopus 로고
    • 1C subunit involved in Ca-dependent inactivation
    • 1C subunit involved in Ca-dependent inactivation. J. Gen. Physiol. 110:1997;379-389.
    • (1997) J. Gen. Physiol. , vol.110 , pp. 379-389
    • Adams, B.1    Tanabe, T.2
  • 3
    • 0028918074 scopus 로고
    • The calcium-activated potassium channels of turtle hair cells
    • Art J.J., Wu Y.-C., Fettiplace R. The calcium-activated potassium channels of turtle hair cells. J. Gen. Physiol. 105:1995;49-72.
    • (1995) J. Gen. Physiol. , vol.105 , pp. 49-72
    • Art, J.J.1    Wu, Y.-C.2    Fettiplace, R.3
  • 7
    • 0030888221 scopus 로고    scopus 로고
    • Importance of the different β subunits in the membrane expression of the α1A and α2 calcium channel subunits: Studies using a depolarization-sensitive α1A antibody
    • Brice N.L., Berrow N.S., Campbell V., Page K.M., Brickley K., Tedder I., Dolphin A.C. Importance of the different β subunits in the membrane expression of the α1A and α2 calcium channel subunits: studies using a depolarization-sensitive α1A antibody. Eur. J. Neurosci. 9:1997;749-759.
    • (1997) Eur. J. Neurosci. , vol.9 , pp. 749-759
    • Brice, N.L.1    Berrow, N.S.2    Campbell, V.3    Page, K.M.4    Brickley, K.5    Tedder, I.6    Dolphin, A.C.7
  • 8
    • 0036083552 scopus 로고    scopus 로고
    • The zebrafish: A new model organism for integrative physiology
    • Briggs J.P. The zebrafish: a new model organism for integrative physiology. Am. J. Physiol. Regul. Integr. Comp. Physiol. 282:2002;R3-9.
    • (2002) Am. J. Physiol. Regul. Integr. Comp. Physiol. , vol.282 , pp. 3-9
    • Briggs, J.P.1
  • 9
    • 0030609887 scopus 로고    scopus 로고
    • 2+ channels by benzothiazepines and phenylalkylamines: Class-specific pharmacology and underlying molecular determinants
    • 2+ channels by benzothiazepines and phenylalkylamines: class-specific pharmacology and underlying molecular determinants. Mol. Pharmacol. 51:1997;872-881.
    • (1997) Mol. Pharmacol. , vol.51 , pp. 872-881
    • Cai, D.1    Mulle, J.G.2    Yue, D.T.3
  • 10
    • 0032588572 scopus 로고    scopus 로고
    • 2+ channels and snare proteins in neurotransmitter release
    • 2+ channels and snare proteins in neurotransmitter release. Ann. NY Acad. Sci. 868:1999;144-159.
    • (1999) Ann. NY Acad. Sci. , vol.868 , pp. 144-159
    • Catterall, W.A.1
  • 12
    • 0033605131 scopus 로고    scopus 로고
    • Voltage and calcium use the same molecular determinants to inactivate calcium channels
    • Cens T., Restituito S., Galas S., Charnet P. Voltage and calcium use the same molecular determinants to inactivate calcium channels. J. Biol. Chem. 274:1999;5483-5490.
    • (1999) J. Biol. Chem. , vol.274 , pp. 5483-5490
    • Cens, T.1    Restituito, S.2    Galas, S.3    Charnet, P.4
  • 13
    • 0029089412 scopus 로고
    • ATP modulation of L-type calcium channel currents in guinea pig outer hair cells
    • Chen C., Nenov A., Norris C.H., Bobbin R.P. ATP modulation of L-type calcium channel currents in guinea pig outer hair cells. Hear. Res. 86:1995;25-33.
    • (1995) Hear. Res. , vol.86 , pp. 25-33
    • Chen, C.1    Nenov, A.2    Norris, C.H.3    Bobbin, R.P.4
  • 14
    • 0023277545 scopus 로고
    • Single-step method of RNA isolation by acid guanidinium thiocyanate-phenol-chloroform extraction
    • Chomczynski P., Sacchi N. Single-step method of RNA isolation by acid guanidinium thiocyanate-phenol-chloroform extraction. Anal. Biochem. 162:1987;156-159.
    • (1987) Anal. Biochem. , vol.162 , pp. 156-159
    • Chomczynski, P.1    Sacchi, N.2
  • 15
    • 0029795275 scopus 로고    scopus 로고
    • Specific phosphorylation of a site in the full-length form of the α1 subunit of the cardiac L-type calcium channel by adenosine 3′,5′-cyclic monophosphate-dependent protein kinase
    • De Jongh K.S., Murphy B.J., Colvin A.A., Hell J.W., Takahashi M., Catterall W.A. Specific phosphorylation of a site in the full-length form of the α1 subunit of the cardiac L-type calcium channel by adenosine 3′,5′-cyclic monophosphate-dependent protein kinase. Biochemistry. 35:1996;10392-10402.
    • (1996) Biochemistry , vol.35 , pp. 10392-10402
    • De Jongh, K.S.1    Murphy, B.J.2    Colvin, A.A.3    Hell, J.W.4    Takahashi, M.5    Catterall, W.A.6
  • 16
    • 0031033757 scopus 로고    scopus 로고
    • Direct binding of G-protein βγ complex to voltage-dependent calcium channels
    • De Waard M., Liu H., Walker D., Scott V.E.S., Gurnett C.A., Campbell K.P. Direct binding of G-protein βγ complex to voltage-dependent calcium channels. Nature. 385:1997;446-450.
    • (1997) Nature , vol.385 , pp. 446-450
    • De Waard, M.1    Liu, H.2    Walker, D.3    Scott, V.E.S.4    Gurnett, C.A.5    Campbell, K.P.6
  • 18
    • 0031963368 scopus 로고    scopus 로고
    • Mechanisms of modulation of voltage-dependent calcium channels by G proteins
    • Dolphin A.C. Mechanisms of modulation of voltage-dependent calcium channels by G proteins. J. Physiol. 506:1998;3-11.
    • (1998) J. Physiol. , vol.506 , pp. 3-11
    • Dolphin, A.C.1
  • 20
    • 0026693075 scopus 로고
    • Analysis of muscarinic receptor subtypes in the mouse cochlea by means of the polymerase chain reaction
    • Drescher D.G., Upadhyay S., Wilcox E.R., Fex J. Analysis of muscarinic receptor subtypes in the mouse cochlea by means of the polymerase chain reaction. J. Neurochem. 59:1992;765-767.
    • (1992) J. Neurochem. , vol.59 , pp. 765-767
    • Drescher, D.G.1    Upadhyay, S.2    Wilcox, E.R.3    Fex, J.4
  • 21
    • 0025966822 scopus 로고
    • N-Acetylhistidine, glutamate, and β-alanine are concentrated in a receptor cell layer of the trout inner ear
    • Drescher M.J., Drescher D.G. N-Acetylhistidine, glutamate, and β-alanine are concentrated in a receptor cell layer of the trout inner ear. J. Neurochem. 56:1991;658-664.
    • (1991) J. Neurochem. , vol.56 , pp. 658-664
    • Drescher, M.J.1    Drescher, D.G.2
  • 22
    • 0026767221 scopus 로고
    • Glutamate, of the endogenous primary α-amino acids, is specifically released from hair cells by elevated extracellular potassium
    • Drescher M.J., Drescher D.G. Glutamate, of the endogenous primary α-amino acids, is specifically released from hair cells by elevated extracellular potassium. J. Neurochem. 59:1992;93-98.
    • (1992) J. Neurochem. , vol.59 , pp. 93-98
    • Drescher, M.J.1    Drescher, D.G.2
  • 23
    • 0023519485 scopus 로고
    • Potassium-evoked release of endogenous primary amine-containing compounds from the trout saccular macula and saccular nerve in vitro
    • Drescher M.J., Drescher D.G., Hatfield J.S. Potassium-evoked release of endogenous primary amine-containing compounds from the trout saccular macula and saccular nerve in vitro. Brain Res. 417:1987;39-50.
    • (1987) Brain Res. , vol.417 , pp. 39-50
    • Drescher, M.J.1    Drescher, D.G.2    Hatfield, J.S.3
  • 24
    • 0028096838 scopus 로고
    • Structural determinants of the blockade of N-type calcium channels by a peptide neurotoxin
    • Ellinor P.T., Zhang J.-F., Horne W.A., Tsien R.W. Structural determinants of the blockade of N-type calcium channels by a peptide neurotoxin. Nature. 372:1994;272-275.
    • (1994) Nature , vol.372 , pp. 272-275
    • Ellinor, P.T.1    Zhang, J.-F.2    Horne, W.A.3    Tsien, R.W.4
  • 25
    • 0025077422 scopus 로고
    • Calcium currents in hair cells isolated from the cochlea of the chick
    • Fuchs P.A., Evans M.G., Murrow B.W. Calcium currents in hair cells isolated from the cochlea of the chick. J. Physiol. 429:1990;553-568.
    • (1990) J. Physiol. , vol.429 , pp. 553-568
    • Fuchs, P.A.1    Evans, M.G.2    Murrow, B.W.3
  • 26
    • 0030042273 scopus 로고    scopus 로고
    • Transfer of 1,4-dihydropyridine sensitivity from L-type to class A (B1) calcium channels
    • Grabner M., Wang Z., Hering S., Striessnig J., Glossmann H. Transfer of 1,4-dihydropyridine sensitivity from L-type to class A (B1) calcium channels. Neuron. 16:1996;207-218.
    • (1996) Neuron , vol.16 , pp. 207-218
    • Grabner, M.1    Wang, Z.2    Hering, S.3    Striessnig, J.4    Glossmann, H.5
  • 27
    • 0024358456 scopus 로고
    • Characterization of the phosphorylation sites in the chicken and bovine myristoylated alanine-rich C kinase substrate protein, a prominent cellular substrate for protein kinase C
    • Graff J.M., Stumpo D.J., Blackshear P.J. Characterization of the phosphorylation sites in the chicken and bovine myristoylated alanine-rich C kinase substrate protein, a prominent cellular substrate for protein kinase C. J. Biol. Chem. 264:1989;11912-11919.
    • (1989) J. Biol. Chem. , vol.264 , pp. 11912-11919
    • Graff, J.M.1    Stumpo, D.J.2    Blackshear, P.J.3
  • 28
    • 0012474971 scopus 로고
    • The mammalian cochlea expresses mRNA for subunits of the L-type calcium channel
    • Green G.E., Drescher D.G. The mammalian cochlea expresses mRNA for subunits of the L-type calcium channel. Soc. Neurosci. Abstr. 19:1993;1418.
    • (1993) Soc. Neurosci. Abstr. , vol.19 , pp. 1418
    • Green, G.E.1    Drescher, D.G.2
  • 31
    • 0025334586 scopus 로고
    • Pursuing the structure and function of voltage-gated channels
    • Guy H.R., Conti F. Pursuing the structure and function of voltage-gated channels. Trends Neurosci. 13:1990;201-206.
    • (1990) Trends Neurosci. , vol.13 , pp. 201-206
    • Guy, H.R.1    Conti, F.2
  • 35
    • 0029153731 scopus 로고
    • Molecular determinants of high affinity phenylalkylamine block of L-type calcium channels
    • Hockerman G.H., Johnson B.D., Scheuer T., Catterall W.A. Molecular determinants of high affinity phenylalkylamine block of L-type calcium channels. J. Biol. Chem. 270:1995;22119-22122.
    • (1995) J. Biol. Chem. , vol.270 , pp. 22119-22122
    • Hockerman, G.H.1    Johnson, B.D.2    Scheuer, T.3    Catterall, W.A.4
  • 38
    • 0028582185 scopus 로고
    • Crystal structure of the tyrosine kinase domain of the human insulin receptor
    • Hubbard S.R., Wei L., Ellis L., Hendrickson W.A. Crystal structure of the tyrosine kinase domain of the human insulin receptor. Nature. 372:1994;746-754.
    • (1994) Nature , vol.372 , pp. 746-754
    • Hubbard, S.R.1    Wei, L.2    Ellis, L.3    Hendrickson, W.A.4
  • 39
    • 0001166495 scopus 로고
    • Sensitivity, polarity, and conductance change in the response of vertebrate hair cells to controlled mechanical stimuli
    • Hudspeth A.J., Corey D.P. Sensitivity, polarity, and conductance change in the response of vertebrate hair cells to controlled mechanical stimuli. Proc. Natl. Acad. Sci. USA. 74:1977;2407-2411.
    • (1977) Proc. Natl. Acad. Sci. USA , vol.74 , pp. 2407-2411
    • Hudspeth, A.J.1    Corey, D.P.2
  • 40
    • 0023917702 scopus 로고
    • Kinetic analysis of voltage- and ion-dependent conductances in saccular hair cells of the bull-frog, Rana catesbeiana
    • Hudspeth A.J., Lewis R.S. Kinetic analysis of voltage- and ion-dependent conductances in saccular hair cells of the bull-frog, Rana catesbeiana. J. Physiol. (London). 400:1988;237-274.
    • (1988) J. Physiol. (London) , vol.400 , pp. 237-274
    • Hudspeth, A.J.1    Lewis, R.S.2
  • 42
    • 0028873594 scopus 로고
    • Molecular diversity and functional characterization of voltage-dependent calcium channels (CACN4) expressed in pancreatic β-cells
    • Ihara Y., Yamada Y., Fujii Y., Gonoi T., Yano H., Yasuda K., Inagaki N., Seino Y., Seino S. Molecular diversity and functional characterization of voltage-dependent calcium channels (CACN4) expressed in pancreatic β-cells. Mol. Endocrinol. 9:1995;121-130.
    • (1995) Mol. Endocrinol. , vol.9 , pp. 121-130
    • Ihara, Y.1    Yamada, Y.2    Fujii, Y.3    Gonoi, T.4    Yano, H.5    Yasuda, K.6    Inagaki, N.7    Seino, Y.8    Seino, S.9
  • 43
    • 0037052727 scopus 로고    scopus 로고
    • Muscarinic receptor subtypes are differentially distributed in the rat cochlea
    • Khan K.M., Drescher M.J., Hatfield J.S., Khan A.-M., Drescher D.G. Muscarinic receptor subtypes are differentially distributed in the rat cochlea. Neuroscience. 111:2002;291-302.
    • (2002) Neuroscience , vol.111 , pp. 291-302
    • Khan, K.M.1    Drescher, M.J.2    Hatfield, J.S.3    Khan, A.-M.4    Drescher, D.G.5
  • 47
    • 0020475449 scopus 로고
    • A simple method for displaying the hydropathic character of a protein
    • Kyte J., Doolittle R.F. A simple method for displaying the hydropathic character of a protein. J. Mol. Biol. 157:1982;105-132.
    • (1982) J. Mol. Biol. , vol.157 , pp. 105-132
    • Kyte, J.1    Doolittle, R.F.2
  • 49
    • 0020510439 scopus 로고
    • Voltage- and ion-dependent conductances in solitary vertebrate hair cells
    • Lewis R.S., Hudspeth A.J. Voltage- and ion-dependent conductances in solitary vertebrate hair cells. Nature. 304:1983;538-541.
    • (1983) Nature , vol.304 , pp. 538-541
    • Lewis, R.S.1    Hudspeth, A.J.2
  • 51
  • 52
    • 0031588988 scopus 로고    scopus 로고
    • 1-β interaction in voltage-gated cardiac L-type calcium channels
    • 1-β interaction in voltage-gated cardiac L-type calcium channels. FEBS Lett. 407:1997;137-140.
    • (1997) FEBS Lett. , vol.407 , pp. 137-140
    • Marquart, A.1    Flockerzi, V.2
  • 53
    • 0024328801 scopus 로고
    • Primary structure and functional expression of the cardiac dihydropyridine-sensitive calcium channel
    • Mikami A., Imoto K., Tanabe T., Niidome T., Mori Y., Takeshima H., Narumiya S., Numa S. Primary structure and functional expression of the cardiac dihydropyridine-sensitive calcium channel. Nature. 340:1989;230-233.
    • (1989) Nature , vol.340 , pp. 230-233
    • Mikami, A.1    Imoto, K.2    Tanabe, T.3    Niidome, T.4    Mori, Y.5    Takeshima, H.6    Narumiya, S.7    Numa, S.8
  • 56
    • 0035951378 scopus 로고    scopus 로고
    • 2+ channel currents but not for the negative shift of activation
    • 2+ channel currents but not for the negative shift of activation. FEBS Lett. 489:2001;87-91.
    • (2001) FEBS Lett. , vol.489 , pp. 87-91
    • Naguro, I.1    Nagao, T.2    Adachi-Akahane, S.3
  • 57
    • 0033063883 scopus 로고    scopus 로고
    • Selective expression of serotonin receptor transcripts in the mammalian cochlea and its subdivisions
    • Oh C.K., Drescher M.J., Hatfield J.S., Drescher D.G. Selective expression of serotonin receptor transcripts in the mammalian cochlea and its subdivisions. Mol. Brain Res. 70:1999;135-140.
    • (1999) Mol. Brain Res. , vol.70 , pp. 135-140
    • Oh, C.K.1    Drescher, M.J.2    Hatfield, J.S.3    Drescher, D.G.4
  • 58
    • 0028605745 scopus 로고
    • The amino terminus of a calcium channel β subunit sets rates of channel inactivation independently of the subunit's effect on activation
    • Olcese R., Qin N., Schneider T., Neely A., Wei X., Stefani E., Birnbaumer L. The amino terminus of a calcium channel β subunit sets rates of channel inactivation independently of the subunit's effect on activation. Neuron. 13:1994;1433-1438.
    • (1994) Neuron , vol.13 , pp. 1433-1438
    • Olcese, R.1    Qin, N.2    Schneider, T.3    Neely, A.4    Wei, X.5    Stefani, E.6    Birnbaumer, L.7
  • 61
    • 0025113220 scopus 로고
    • Casein kinase 2: An 'eminence grise' in cellular regulation?
    • Pinna L.A. Casein kinase 2: an 'eminence grise' in cellular regulation? Biochim. Biophys. Acta. 1054:1990;267-284.
    • (1990) Biochim. Biophys. Acta , vol.1054 , pp. 267-284
    • Pinna, L.A.1
  • 62
    • 0030581751 scopus 로고    scopus 로고
    • How do protein kinases recognize their substrates?
    • Pinna L.A., Ruzzene M. How do protein kinases recognize their substrates? Biochim. Biophys. Acta. 1314:1996;191-225.
    • (1996) Biochim. Biophys. Acta , vol.1314 , pp. 191-225
    • Pinna, L.A.1    Ruzzene, M.2
  • 66
    • 0030945196 scopus 로고    scopus 로고
    • Sequence motifs for calmodulin recognition
    • Rhoads A.R., Friedberg F. Sequence motifs for calmodulin recognition. FASEB J. 11:1997;331-340.
    • (1997) FASEB J. , vol.11 , pp. 331-340
    • Rhoads, A.R.1    Friedberg, F.2
  • 67
    • 0025514341 scopus 로고
    • Colocalization of ion channels involved in frequency selectivity and synaptic transmission at presynaptic active zones of hair cells
    • Roberts W.M., Jacobs R.A., Hudspeth A.J. Colocalization of ion channels involved in frequency selectivity and synaptic transmission at presynaptic active zones of hair cells. J. Neurosci. 10:1990;3664-3684.
    • (1990) J. Neurosci. , vol.10 , pp. 3664-3684
    • Roberts, W.M.1    Jacobs, R.A.2    Hudspeth, A.J.3
  • 68
    • 0023756035 scopus 로고
    • CAMP-dependent protein kinase rapidly phosphorylates serine-687 of the skeletal muscle receptor for calcium channel blockers
    • Röhrkasten A., Meyer H.E., Nastainczyk W., Sieber M., Hofmann F. cAMP-dependent protein kinase rapidly phosphorylates serine-687 of the skeletal muscle receptor for calcium channel blockers. J. Biol. Chem. 263:1988;15325-15329.
    • (1988) J. Biol. Chem. , vol.263 , pp. 15325-15329
    • Röhrkasten, A.1    Meyer, H.E.2    Nastainczyk, W.3    Sieber, M.4    Hofmann, F.5
  • 69
    • 0026742961 scopus 로고
    • Specific phosphorylation of a COOH-terminal site on the full-length form of the α1 subunit of the skeletal muscle calcium channel by cAMP-dependent protein kinase
    • Rotman E.I., De Jongh K.S., Florio V., Lai Y., Catterall W.A. Specific phosphorylation of a COOH-terminal site on the full-length form of the α1 subunit of the skeletal muscle calcium channel by cAMP-dependent protein kinase. J. Biol. Chem. 267:1992;16100-16105.
    • (1992) J. Biol. Chem. , vol.267 , pp. 16100-16105
    • Rotman, E.I.1    De Jongh, K.S.2    Florio, V.3    Lai, Y.4    Catterall, W.A.5
  • 70
    • 0033006442 scopus 로고    scopus 로고
    • SNARE complex at the ribbon synapses of cochlear hair cells: Analysis of synaptic vesicle- and synaptic membrane-associated proteins
    • Safieddine S., Wenthold R.J. SNARE complex at the ribbon synapses of cochlear hair cells: analysis of synaptic vesicle- and synaptic membrane-associated proteins. Eur. J. Neurosci. 11:1999;803-812.
    • (1999) Eur. J. Neurosci. , vol.11 , pp. 803-812
    • Safieddine, S.1    Wenthold, R.J.2
  • 72
    • 0034916230 scopus 로고    scopus 로고
    • PDZ domains and the organization of supramolecular complexes
    • Sheng M., Sala C. PDZ domains and the organization of supramolecular complexes. Annu. Rev. Neurosci. 24:2001;1-29.
    • (2001) Annu. Rev. Neurosci. , vol.24 , pp. 1-29
    • Sheng, M.1    Sala, C.2
  • 73
    • 0028595727 scopus 로고
    • Identification of a syntaxin-binding site on N-type calcium channels
    • Sheng Z.-H., Rettig J., Takahashi M., Catterall W.A. Identification of a syntaxin-binding site on N-type calcium channels. Neuron. 13:1994;1303-1313.
    • (1994) Neuron , vol.13 , pp. 1303-1313
    • Sheng, Z.-H.1    Rettig, J.2    Takahashi, M.3    Catterall, W.A.4
  • 78
    • 0035884555 scopus 로고    scopus 로고
    • Chick cochlear hair cell exocytosis mediated by dihydropyridine-sensitive calcium channels
    • Spassova M., Eisen M.D., Saunders J.C., Parsons T.D. Chick cochlear hair cell exocytosis mediated by dihydropyridine-sensitive calcium channels. J. Physiol. 535:2001;689-696.
    • (2001) J. Physiol. , vol.535 , pp. 689-696
    • Spassova, M.1    Eisen, M.D.2    Saunders, J.C.3    Parsons, T.D.4
  • 79
    • 0034637479 scopus 로고    scopus 로고
    • Fast inactivation of voltage-dependent calcium channels. A hinged-lid mechanism?
    • Stotz S.C., Hamid J., Spaetgens R.L., Jarvis S.E., Zamponi G.W. Fast inactivation of voltage-dependent calcium channels. A hinged-lid mechanism? J. Biol. Chem. 275:2000;24575-24582.
    • (2000) J. Biol. Chem. , vol.275 , pp. 24575-24582
    • Stotz, S.C.1    Hamid, J.2    Spaetgens, R.L.3    Jarvis, S.E.4    Zamponi, G.W.5
  • 81
    • 0028851715 scopus 로고
    • Two types of calcium channels in bullfrog saccular hair cells
    • Su Z.-L., Jiang S.-C., Gu R., Yang W.-P. Two types of calcium channels in bullfrog saccular hair cells. Hear. Res. 87:1995;62-68.
    • (1995) Hear. Res. , vol.87 , pp. 62-68
    • Su, Z.-L.1    Jiang, S.-C.2    Gu, R.3    Yang, W.-P.4
  • 82
    • 0029026392 scopus 로고
    • The synaptic vesicle cycle: A cascade of protein-protein interactions
    • Südhof T.C. The synaptic vesicle cycle: a cascade of protein-protein interactions. Nature. 375:1995;645-653.
    • (1995) Nature , vol.375 , pp. 645-653
    • Südhof, T.C.1
  • 84
    • 0016627986 scopus 로고
    • Troponin and parvalbumin calcium binding regions predicted in myosin light chain and T4 lysozyme
    • Tufty R.M., Kretsinger R.H. Troponin and parvalbumin calcium binding regions predicted in myosin light chain and T4 lysozyme. Science. 187:1975;167-169.
    • (1975) Science , vol.187 , pp. 167-169
    • Tufty, R.M.1    Kretsinger, R.H.2
  • 91
    • 0028920610 scopus 로고
    • Kinetic analysis of barium currents in chick cochlear hair cells
    • Zidanic M., Fuchs P.A. Kinetic analysis of barium currents in chick cochlear hair cells. Biophys. J. 68:1995;1323-1336.
    • (1995) Biophys. J. , vol.68 , pp. 1323-1336
    • Zidanic, M.1    Fuchs, P.A.2
  • 92
    • 0345465665 scopus 로고    scopus 로고
    • Calmodulin supports both inactivation and facilitation of L-type calcium channels
    • Zühlke R.D., Pitt G.S., Deisseroth K., Tsien R.W., Reuter H. Calmodulin supports both inactivation and facilitation of L-type calcium channels. Nature. 399:1999;159-162.
    • (1999) Nature , vol.399 , pp. 159-162
    • Zühlke, R.D.1    Pitt, G.S.2    Deisseroth, K.3    Tsien, R.W.4    Reuter, H.5


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