메뉴 건너뛰기




Volumn 4, Issue 7, 2003, Pages 517-529

Calcium signalling: Dynamics, homeostasis and remodelling

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATASE (CALCIUM MAGNESIUM); ADENOSINE TRIPHOSPHATASE (CALCIUM); CALCIUM CHANNEL L TYPE; CALCIUM ION; CALMODULIN; CALMODULIN BINDING PROTEIN; CALNEXIN; CALRETICULIN; CD3 ANTIGEN; CHOLECYSTOKININ RECEPTOR; CYCLIC ADENOSINE DINUCLEOTIDE PHOSPHATE RIBOSE; CYCLIC AMP DEPENDENT PROTEIN KINASE; FK 506 BINDING PROTEIN; G PROTEIN COUPLED RECEPTOR; INOSITOL 1,4,5 TRISPHOSPHATE; METABOTROPIC RECEPTOR; MUSCARINIC RECEPTOR; N METHYL DEXTRO ASPARTIC ACID RECEPTOR; NICOTINIC ACID ADENINE DINUCLEOTIDE PHOSPHATE; NUCLEOTIDE; PHOSPHOLIPASE C; POLYCYSTIN; RYANODINE RECEPTOR; SPHINGOSINE 1 PHOSPHATE; TYROSINE KINASE RECEPTOR; UNCLASSIFIED DRUG; VOLTAGE GATED CHANNEL FORMING PROTEIN;

EID: 0038125598     PISSN: 14710072     EISSN: None     Source Type: Journal    
DOI: 10.1038/nrm1155     Document Type: Review
Times cited : (4614)

References (118)
  • 3
    • 0037143647 scopus 로고    scopus 로고
    • Calcium signalling: More messengers, more channels, more complexity
    • Bootman, M. D., Berridge, M. J. & Roderick, H. L. Calcium signalling: more messengers, more channels, more complexity. Curr. Biol. 12, R563-R565 (2002).
    • (2002) Curr. Biol. , vol.12
    • Bootman, M.D.1    Berridge, M.J.2    Roderick, H.L.3
  • 6
    • 0035805510 scopus 로고    scopus 로고
    • Monitoring agonist-induced phospholipase C activation in live cells by fluorescence resonance energy transfer
    • Van der Wal, J., Habets, R., Várnai, P., Balla, T. & Jalink, K. Monitoring agonist-induced phospholipase C activation in live cells by fluorescence resonance energy transfer. J. Biol. Chem. 276, 15337-15344 (2001).
    • (2001) J. Biol. Chem. , vol.276 , pp. 15337-15344
    • Van der Wal, J.1    Habets, R.2    Várnai, P.3    Balla, T.4    Jalink, K.5
  • 7
    • 1842373861 scopus 로고    scopus 로고
    • Phospholipase C isozymes selectively couple to specific neurotransmitter receptors
    • Kim, D. et al. Phospholipase C isozymes selectively couple to specific neurotransmitter receptors. Nature 389, 290-293 (1997).
    • (1997) Nature , vol.389 , pp. 290-293
    • Kim, D.1
  • 8
    • 0034107388 scopus 로고    scopus 로고
    • Gq protein α-subunits Gαq and Gα11 are localized at postsynaptic extra-junctional membrane of cerebellar Purkinje cells and hippocampal pyramidal cells
    • Tanaka, J. et al. Gq protein α-subunits Gαq and Gα11 are localized at postsynaptic extra-junctional membrane of cerebellar Purkinje cells and hippocampal pyramidal cells. Eur. J. Neurosci. 12, 781-792 (2000).
    • (2000) Eur. J. Neurosci. , vol.12 , pp. 781-792
    • Tanaka, J.1
  • 9
    • 0029795629 scopus 로고    scopus 로고
    • Control of calcium oscillations by phosphorylation of metabotropic glutamate receptors
    • Kawabate, S. et al. Control of calcium oscillations by phosphorylation of metabotropic glutamate receptors. Nature 383, 89-92 (1996).
    • (1996) Nature , vol.383 , pp. 89-92
    • Kawabate, S.1
  • 11
    • 0033522228 scopus 로고    scopus 로고
    • 2+-signalling patterns by NAADP in pancreatic acinar cells
    • 2+-signalling patterns by NAADP in pancreatic acinar cells. Nature 398, 74-76 (1999).
    • (1999) Nature , vol.398 , pp. 74-76
    • Cancela, J.M.1    Churchill, G.C.2    Galione, A.3
  • 14
    • 0345609814 scopus 로고    scopus 로고
    • Mechanisms of calcium signaling by cyclic ADP-ribose and NAADP
    • Lee, H. C. Mechanisms of calcium signaling by cyclic ADP-ribose and NAADP. Physiol. Rev. 77, 1133-1164 (1997).
    • (1997) Physiol. Rev. , vol.77 , pp. 1133-1164
    • Lee, H.C.1
  • 15
    • 0031051548 scopus 로고    scopus 로고
    • Lysine 129 of CD38 (ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase) participates in the binding of ATP to inhibit the cyclic ADP-ribose hydrolase
    • Tohgo, A. et al. Lysine 129 of CD38 (ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase) participates in the binding of ATP to inhibit the cyclic ADP-ribose hydrolase. J. Biol. Chem. 272, 3879-3882 (1997).
    • (1997) J. Biol. Chem. , vol.272 , pp. 3879-3882
    • Tohgo, A.1
  • 16
    • 0035815670 scopus 로고    scopus 로고
    • ADP-ribosyl cyclase and cyclic ADP-ribose hydrolase act as a redox sensor: A primary role for cyclic ADP-ribose in hypoxic pulmonary vasoconstriction
    • Wilson, H. L. et al. ADP-ribosyl cyclase and cyclic ADP-ribose hydrolase act as a redox sensor: a primary role for cyclic ADP-ribose in hypoxic pulmonary vasoconstriction. J. Biol. Chem. 276, 11180-11188 (2001).
    • (2001) J. Biol. Chem. , vol.276 , pp. 11180-11188
    • Wilson, H.L.1
  • 17
    • 0037184523 scopus 로고    scopus 로고
    • 2+ from reserve granules, lysosome-related organelles, in sea urchin eggs
    • 2+ from reserve granules, lysosome-related organelles, in sea urchin eggs. Cell 111, 703-708 (2002).
    • (2002) Cell , vol.111 , pp. 703-708
    • Churchill, G.C.1
  • 18
    • 0028361066 scopus 로고
    • 2+ entry in bullfrog sympathetic neurons
    • 2+ entry in bullfrog sympathetic neurons. Neuron 12, 1073-1079 (1994).
    • (1994) Neuron , vol.12 , pp. 1073-1079
    • Hua, S.-Y.1
  • 20
    • 0027083498 scopus 로고
    • 2+-dependent currents in cultured rat dorsal root ganglion neurones by a sperm factor and cyclic ADP-ribose
    • 2+-dependent currents in cultured rat dorsal root ganglion neurones by a sperm factor and cyclic ADP-ribose. Mol. Biol. Cell 3, 1415-1425 (1992).
    • (1992) Mol. Biol. Cell , vol.3 , pp. 1415-1425
    • Currie, K.P.M.1    Swann, K.2    Galione, A.3    Scott, R.H.4
  • 21
    • 0033200222 scopus 로고    scopus 로고
    • Effects of photoreleased cADP-ribose on calcium transients and calcium sparks in myocytes isolated from guinea-pig and rat ventricle
    • Cui, Y., Galione, A. & Terrar, D. A. Effects of photoreleased cADP-ribose on calcium transients and calcium sparks in myocytes isolated from guinea-pig and rat ventricle. Biochem. J. 342, 269-273 (1999).
    • (1999) Biochem. J. , vol.342 , pp. 269-273
    • Cui, Y.1    Galione, A.2    Terrar, D.A.3
  • 24
    • 0033580824 scopus 로고    scopus 로고
    • 2+ in heart cells
    • 2+ in heart cells. J. Biol. Chem. 274, 17820-17827 (1999).
    • (1999) J. Biol. Chem. , vol.274 , pp. 17820-17827
    • Rakovic, S.1
  • 25
    • 0031013367 scopus 로고    scopus 로고
    • 2+ from islet microsomes
    • 2+ from islet microsomes. J. Biol. Chem. 272, 3133-3136 (1997).
    • (1997) J. Biol. Chem. , vol.272 , pp. 3133-3136
    • Noguchi, N.1
  • 27
    • 0034624048 scopus 로고    scopus 로고
    • 2+ mobilisation requires intracellular sphingosine 1-phosphate production: Potential involvement of endogenous Edg-4 receptors
    • 3 or S1P within the same cell.
    • (2000) J. Biol. Chem. , vol.275 , pp. 38532-38539
    • Young, K.W.1
  • 28
    • 0037052338 scopus 로고    scopus 로고
    • 2+ signals triggered by different phospholipid pathways in antigen stimulation of human mast cells
    • 2+ signals triggered by different phospholipid pathways in antigen stimulation of human mast cells. J. Biol. Chem. 277, 17255-17262 (2002).
    • (2002) J. Biol. Chem. , vol.277 , pp. 17255-17262
    • Melendez, A.J.1    Khaw, A.A.2
  • 32
    • 0036080482 scopus 로고    scopus 로고
    • TRP channel proteins and signal transduction
    • Minke, B. & Cook, B. TRP channel proteins and signal transduction. Physiol. Rev. 82, 429-472 (2002).
    • (2002) Physiol. Rev. , vol.82 , pp. 429-472
    • Minke, B.1    Cook, B.2
  • 33
    • 0037040395 scopus 로고    scopus 로고
    • The TRP channels, a remarkably functional family
    • Montell, C., Birnbaumer, L. & Flockerzi, V. The TRP channels, a remarkably functional family. Cell 108, 595-598 (2002).
    • (2002) Cell , vol.108 , pp. 595-598
    • Montell, C.1    Birnbaumer, L.2    Flockerzi, V.3
  • 35
    • 0037020691 scopus 로고    scopus 로고
    • The role of calmodulin for inositol 1,4,5-trisphosphate receptor function
    • Nadif Kasri, N. et al. The role of calmodulin for inositol 1,4,5-trisphosphate receptor function. Biochim. Biophys. Acta 1600, 19-31 (2002).
    • (2002) Biochim. Biophys. Acta , vol.1600 , pp. 19-31
    • Nadif Kasri, N.1
  • 38
    • 4243715868 scopus 로고    scopus 로고
    • 3)-induced calcium release by neuronal calcium binding proteins (CaBP)
    • 3)-induced calcium release by neuronal calcium binding proteins (CaBP). J. Physiol. (Lond.) 547P, PC36 (2003).
    • (2003) J. Physiol. (Lond.) , vol.547 P
    • Roderick, H.L.1
  • 39
    • 0037225984 scopus 로고    scopus 로고
    • Association of phospholamban with a cGMP kinase signaling complex
    • Koller, A. et al. Association of phospholamban with a cGMP kinase signaling complex. Biochem. Biophys. Res. Commun. 300, 155-160 (2003).
    • (2003) Biochem. Biophys. Res. Commun. , vol.300 , pp. 155-160
    • Koller, A.1
  • 40
    • 0037080952 scopus 로고    scopus 로고
    • 3 receptor
    • 3 receptor. EMBO J. 21, 83-92 (2002).
    • (2002) EMBO J. , vol.21 , pp. 83-92
    • Yokoyama, K.1
  • 41
    • 0037131261 scopus 로고    scopus 로고
    • Protein kinase A and two phosphatases are components of the inositol 1,4,5-trisphosphate receptor macromolecular signaling complex
    • DeSouza, N. et al. Protein kinase A and two phosphatases are components of the inositol 1,4,5-trisphosphate receptor macromolecular signaling complex. J. Biol. Chem. 277, 39397-39400 (2002).
    • (2002) J. Biol. Chem. , vol.277 , pp. 39397-39400
    • DeSouza, N.1
  • 43
    • 0035827585 scopus 로고    scopus 로고
    • Calmodulin binding and inhibition of cardiac muscle calcium release channel (ryanodine receptor)
    • Balshaw, D. M., Xu, L., Yamaguchi, N., Pasek, D. A. & Meissner, G. Calmodulin binding and inhibition of cardiac muscle calcium release channel (ryanodine receptor). J. Biol. Chem. 276, 20144-20153 (2001).
    • (2001) J. Biol. Chem. , vol.276 , pp. 20144-20153
    • Balshaw, D.M.1    Xu, L.2    Yamaguchi, N.3    Pasek, D.A.4    Meissner, G.5
  • 44
    • 0036274039 scopus 로고    scopus 로고
    • Regulation of ryanodine receptors via macromolecular complexes: A novel role for leucine/isoleucine zippers
    • Marks, A. R., Marx, S. O. & Reiken, S. Regulation of ryanodine receptors via macromolecular complexes: a novel role for leucine/isoleucine zippers. Trends Cardiovasc. Med. 12, 166-170 (2002).
    • (2002) Trends Cardiovasc. Med. , vol.12 , pp. 166-170
    • Marks, A.R.1    Marx, S.O.2    Reiken, S.3
  • 45
    • 0034640113 scopus 로고    scopus 로고
    • PKA phosphorylation dissociates FKBP12.6 from the calcium release channel (ryanodine receptor): Defective regulation in failing hearts
    • Marx, S. O. et al. PKA phosphorylation dissociates FKBP12.6 from the calcium release channel (ryanodine receptor): defective regulation in failing hearts. Cell 101, 365-376 (2000).
    • (2000) Cell , vol.101 , pp. 365-376
    • Marx, S.O.1
  • 47
    • 0036278538 scopus 로고    scopus 로고
    • Junctional sarcoplasmic reticulum transmembrane proteins in the heart
    • Muller, F. U. et al. Junctional sarcoplasmic reticulum transmembrane proteins in the heart. Basic Res. Cardiol. 97, 152-155 (2002).
    • (2002) Basic Res. Cardiol. , vol.97 , pp. 152-155
    • Muller, F.U.1
  • 48
    • 0030770826 scopus 로고    scopus 로고
    • Complex formation between junctin, triadin, calsequestrin, and the ryanodine receptor. Proteins of the cardiac junctional sarcoplasmic reticulum membrane
    • Zhang, L., Kelley, J., Schmeisser, G., Kobayashi, Y. M. & Jones, L. R. Complex formation between junctin, triadin, calsequestrin, and the ryanodine receptor. Proteins of the cardiac junctional sarcoplasmic reticulum membrane. J. Biol. Chem. 272, 23389-23397 (1997). Much attention has focused on accessory cytosolic proteins as modulators of the RYRs, but there also is evidence that the transmembrane proteins junctin and triadin cooperate with the luminal protein calsequestrin to regulate the activity of these release channels.
    • (1997) J. Biol. Chem. , vol.272 , pp. 23389-23397
    • Zhang, L.1    Kelley, J.2    Schmeisser, G.3    Kobayashi, Y.M.4    Jones, L.R.5
  • 49
    • 0037317302 scopus 로고    scopus 로고
    • Polycystins 1 and 2 mediate mechanosensation in the primary cilium of kidney cells
    • Nauli, S. M. et al. J. Polycystins 1 and 2 mediate mechanosensation in the primary cilium of kidney cells. Nature Genet. 33, 129-137 (2003).
    • (2003) Nature Genet. , vol.33 , pp. 129-137
    • Nauli, S.M.1
  • 50
    • 0036122434 scopus 로고    scopus 로고
    • Polycystin-2 is an intracellular calcium release channel
    • 2+ release mode.
    • (2002) Nature Cell Biol. , vol.4 , pp. 191-197
    • Koulen, P.1
  • 52
    • 0033214702 scopus 로고    scopus 로고
    • Identification and characterisation of polycystin-2, the PKD2 gene product
    • Cai, Y. et al. Identification and characterisation of polycystin-2, the PKD2 gene product. J. Biol. Chem. 274, 28557-28565 (1999).
    • (1999) J. Biol. Chem. , vol.274 , pp. 28557-28565
    • Cai, Y.1
  • 54
    • 0033569575 scopus 로고    scopus 로고
    • Calcium dynamics and buffering in motoneurones of the mouse spinal cord
    • Palecek, J., Lips, M. B. & Keller, B. U. Calcium dynamics and buffering in motoneurones of the mouse spinal cord. J. Physiol. (Lond.) 520, 485-502 (1999).
    • (1999) J. Physiol. (Lond.) , vol.520 , pp. 485-502
    • Palecek, J.1    Lips, M.B.2    Keller, B.U.3
  • 55
    • 0033058151 scopus 로고    scopus 로고
    • Prolonged contraction-relaxation cycle of fast-twitch muscles in parvalbumin knockout mice
    • Schwaller, B. et al. Prolonged contraction-relaxation cycle of fast-twitch muscles in parvalbumin knockout mice. Am. J. Physiol. 276, C395-C403 (1999).
    • (1999) Am. J. Physiol. , vol.276
    • Schwaller, B.1
  • 56
    • 0034700170 scopus 로고    scopus 로고
    • Role of calcium-binding protein parvalbumin in short-term synaptic plasticity
    • Caillard, O. et al. Role of calcium-binding protein parvalbumin in short-term synaptic plasticity. Proc. Natl Acad. Sci. USA 97, 13372-13377 (2000).
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 13372-13377
    • Caillard, O.1
  • 59
    • 0034956470 scopus 로고    scopus 로고
    • 2+: Fast pumps reside in fast cells
    • 2+: fast pumps reside in fast cells. Cell Calcium 30, 49-57 (2001).
    • (2001) Cell Calcium , vol.30 , pp. 49-57
    • Caride, A.J.1
  • 60
    • 0036877135 scopus 로고    scopus 로고
    • The molecular physiology of the SERCA and SPCA pumps
    • Wuytack, F., Raeymaekers, L. & Missiaen, L. The molecular physiology of the SERCA and SPCA pumps. Cell Calcium 32, 279-305 (2002).
    • (2002) Cell Calcium , vol.32 , pp. 279-305
    • Wuytack, F.1    Raeymaekers, L.2    Missiaen, L.3
  • 61
    • 0028944604 scopus 로고
    • Stimulation of repetitive calcium transients in mouse eggs
    • Ozil, J. P. & Swann, K. Stimulation of repetitive calcium transients in mouse eggs. J. Physiol. (Lond.) 483, 331-346 (1995)
    • (1995) J. Physiol. (Lond.) , vol.483 , pp. 331-346
    • Ozil, J.P.1    Swann, K.2
  • 62
    • 0029030810 scopus 로고
    • Characterization of spontaneous calcium transients in nerve growth cones and their effect on growth cone migration
    • Gomez, T. M., Snow, D. M. & Letourneau, P. C. Characterization of spontaneous calcium transients in nerve growth cones and their effect on growth cone migration. Neuron 14, 1233-1246 (1995).
    • (1995) Neuron , vol.14 , pp. 1233-1246
    • Gomez, T.M.1    Snow, D.M.2    Letourneau, P.C.3
  • 64
    • 0037319274 scopus 로고    scopus 로고
    • Spontaneous calcium transients in developing cortical neurons regulate axonal outgrowth
    • Tang, F., Dent, E. W. & Kalil, K. Spontaneous calcium transients in developing cortical neurons regulate axonal outgrowth. J. Neurosci. 23, 927-936 (2003).
    • (2003) J. Neurosci. , vol.23 , pp. 927-936
    • Tang, F.1    Dent, E.W.2    Kalil, K.3
  • 65
    • 0030201466 scopus 로고    scopus 로고
    • 2+ fluctuations modulate the rate of neuronal migration
    • 2+ fluctuations modulate the rate of neuronal migration. Neuron 17, 275-285 (1996).
    • (1996) Neuron , vol.17 , pp. 275-285
    • Komuro, H.1    Rakic, P.2
  • 66
    • 0037223324 scopus 로고    scopus 로고
    • Local and global spontaneous calcium events regulate neurite outgrowth and onset of GABAergic phenotype during neural precursor differentiation
    • Ciccolini, F. et al. Local and global spontaneous calcium events regulate neurite outgrowth and onset of GABAergic phenotype during neural precursor differentiation. J. Neurosci. 23, 103-111 (2003).
    • (2003) J. Neurosci. , vol.23 , pp. 103-111
    • Ciccolini, F.1
  • 67
    • 0029895156 scopus 로고    scopus 로고
    • Calcium spiking in plant root hairs responding to Rhizobium nodulation signals
    • Ehrhardt, D. W., Wais, R. & Long, S. R. Calcium spiking in plant root hairs responding to Rhizobium nodulation signals. Cell 85, 673-681 (1996).
    • (1996) Cell , vol.85 , pp. 673-681
    • Ehrhardt, D.W.1    Wais, R.2    Long, S.R.3
  • 68
    • 0036136618 scopus 로고    scopus 로고
    • Calcium oscillations in neocortical astrocytes under epileptiform conditions
    • Tashiro, A., Goldberg, J. & Yuste, R. Calcium oscillations in neocortical astrocytes under epileptiform conditions. J. Neurobiol. 50, 45-55 (2001).
    • (2001) J. Neurobiol. , vol.50 , pp. 45-55
    • Tashiro, A.1    Goldberg, J.2    Yuste, R.3
  • 69
    • 0032526950 scopus 로고    scopus 로고
    • A calcium signaling cascade essential for myosin thick filament assembly in Xenopus myocytes
    • Ferrari, M. B., Ribbeck, K., Hagler, D. J. Jr. & Spitzer, N. C. A calcium signaling cascade essential for myosin thick filament assembly in Xenopus myocytes. J. Cell Biol. 141, 1349-1356 (1998).
    • (1998) J. Cell Biol. , vol.141 , pp. 1349-1356
    • Ferrari, M.B.1    Ribbeck, K.2    Hagler D.J., Jr.3    Spitzer, N.C.4
  • 70
    • 0034621828 scopus 로고    scopus 로고
    • 2+ oscillations in renal epithelial cells
    • 2+ oscillations in renal epithelial cells. Nature 277, 694-697 (2000).
    • (2000) Nature , vol.277 , pp. 694-697
    • Uhlén, P.1
  • 71
    • 0037135560 scopus 로고    scopus 로고
    • Calcium oscillations trigger focal adhesion disassembly in human U87 astrocytoma cells
    • Giannone, G., Rondé, P., Gaire, M., Haiech, J. & Takeda, K. Calcium oscillations trigger focal adhesion disassembly in human U87 astrocytoma cells. J. Biol. Chem. 277, 26364-26371 (2002).
    • (2002) J. Biol. Chem. , vol.277 , pp. 26364-26371
    • Giannone, G.1    Rondé, P.2    Gaire, M.3    Haiech, J.4    Takeda, K.5
  • 72
    • 0027905031 scopus 로고
    • Rhythmic exocytosis stimulated by GnRH-induced calcium oscillations in rat gonadotropes
    • Tse, A., Tse, F. W., Almers, W. & Hille, B. Rhythmic exocytosis stimulated by GnRH-induced calcium oscillations in rat gonadotropes. Science 260, 82-84 (1993).
    • (1993) Science , vol.260 , pp. 82-84
    • Tse, A.1    Tse, F.W.2    Almers, W.3    Hille, B.4
  • 73
    • 0029143569 scopus 로고
    • Decoding of cytosolic calcium oscillations in the mitochondria
    • Hajnóczky, G., Robb-Gaspers, L. D., Seitz, M. B. & Thomas, A. P. Decoding of cytosolic calcium oscillations in the mitochondria. Cell 82, 415-424 (1995).
    • (1995) Cell , vol.82 , pp. 415-424
    • Hajnóczky, G.1    Robb-Gaspers, L.D.2    Seitz, M.B.3    Thomas, A.P.4
  • 74
    • 0032580202 scopus 로고    scopus 로고
    • Calcium oscillations increase the efficiency and specificity of gene expression
    • Dolmetsch, R. E., Xu, K. & Lewis, R. S. Calcium oscillations increase the efficiency and specificity of gene expression. Nature 392,933-936 (1998).
    • (1998) Nature , vol.392 , pp. 933-936
    • Dolmetsch, R.E.1    Xu, K.2    Lewis, R.S.3
  • 76
    • 0035184203 scopus 로고    scopus 로고
    • Gonadotrophin subunit transcriptional responses to calcium signals in the rat: Evidence for regulation by pulse frequency
    • Haisenleder, D. J. et al. Gonadotrophin subunit transcriptional responses to calcium signals in the rat: evidence for regulation by pulse frequency. Biol. Reprod. 65, 1789-1793 (2001).
    • (2001) Biol. Reprod. , vol.65 , pp. 1789-1793
    • Haisenleder, D.J.1
  • 77
    • 0032966473 scopus 로고    scopus 로고
    • Gene regulation by patterned electrical activity during neural and skeletal muscle development
    • Buonanno, A. & Fields, R. D. Gene regulation by patterned electrical activity during neural and skeletal muscle development. Curr. Opin. Neurobiol. 9, 110-120 (1999).
    • (1999) Curr. Opin. Neurobiol. , vol.9 , pp. 110-120
    • Buonanno, A.1    Fields, R.D.2
  • 78
    • 0034120259 scopus 로고    scopus 로고
    • Remodelling muscles with calcineurin
    • Olsen, E. A. & Williams, R. S. Remodelling muscles with calcineurin. Bioessays 22, 510-519 (2000).
    • (2000) Bioessays , vol.22 , pp. 510-519
    • Olsen, E.A.1    Williams, R.S.2
  • 80
    • 0032582525 scopus 로고    scopus 로고
    • Protein kinase C as a molecular machine for decoding calcium and diacylglycerol signals
    • Oancea, E. & Meyer, T. Protein kinase C as a molecular machine for decoding calcium and diacylglycerol signals. Cell 95, 307-318 (1998).
    • (1998) Cell , vol.95 , pp. 307-318
    • Oancea, E.1    Meyer, T.2
  • 81
    • 0033002601 scopus 로고    scopus 로고
    • Localized intracellular calcium signaling in muscle: Calcium sparks and calcium quarks
    • Niggli, E. Localized intracellular calcium signaling in muscle: calcium sparks and calcium quarks. Annu. Rev. Physiol. 61, 311-335 (1999).
    • (1999) Annu. Rev. Physiol. , vol.61 , pp. 311-335
    • Niggli, E.1
  • 82
    • 0033983812 scopus 로고    scopus 로고
    • 2+ release sites in non-excitable cells
    • 2+ release sites in non-excitable cells. Curr. Biol. 10, 8-15 (2000).
    • (2000) Curr. Biol. , vol.10 , pp. 8-15
    • Thomas, D.1
  • 83
    • 0037158699 scopus 로고    scopus 로고
    • Directionally selective calcium signals in dendrites of starburst amacrine cells
    • Euler, T., Detwiler, P. B. & Denk, W. Directionally selective calcium signals in dendrites of starburst amacrine cells. Nature 418, 845-852 (2002).
    • (2002) Nature , vol.418 , pp. 845-852
    • Euler, T.1    Detwiler, P.B.2    Denk, W.3
  • 84
    • 0035902473 scopus 로고    scopus 로고
    • Folliculostetlate cell network: A route for long-distance communication in the anterior pituitary
    • Fauquier, T., Guérineau, N. C., McKinney, R. A., Bauer, K. & Mollard, P. Folliculostetlate cell network: A route for long-distance communication in the anterior pituitary. Proc. Natl Acad. Sci. USA 98, 8891-8896 (2001).
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 8891-8896
    • Fauquier, T.1    Guérineau, N.C.2    McKinney, R.A.3    Bauer, K.4    Mollard, P.5
  • 85
  • 87
    • 0034711510 scopus 로고    scopus 로고
    • 2+ signaling between smooth muscle and endothelium of resistance vessels
    • 2+ signaling between smooth muscle and endothelium of resistance vessels. Circ. Res. 87, 1048-1054 (2000).
    • (2000) Circ. Res. , vol.87 , pp. 1048-1054
    • Yashiro, Y.1    Duling, B.R.2
  • 89
    • 0035801541 scopus 로고    scopus 로고
    • 2+] in cardiac cells
    • 2+] in cardiac cells. EMBO J. 20, 4998-5007 (2001).
    • (2001) EMBO J. , vol.20 , pp. 4998-5007
    • Robert, V.1
  • 90
    • 0033525748 scopus 로고    scopus 로고
    • 2+, calcineurin, and NFAT
    • 2+, calcineurin, and NFAT. Cell 96, 611-614 (1999).
    • (1999) Cell , vol.96 , pp. 611-614
    • Crabtree, G.R.1
  • 92
    • 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
  • 93
    • 0036165434 scopus 로고    scopus 로고
    • MEF2: A calcium-dependent regulator of cell division, differentiation and death
    • McKinsey, T. A., Zhang, C. L. & Olsen, E. N. MEF2: a calcium-dependent regulator of cell division, differentiation and death. Trends Biochem. Sci. 27, 40-47 (2002).
    • (2002) Trends Biochem. Sci. , vol.27 , pp. 40-47
    • McKinsey, T.A.1    Zhang, C.L.2    Olsen, E.N.3
  • 94
    • 0033616141 scopus 로고    scopus 로고
    • Calcium controls the transcription of its own transporters and channels in developing neurons
    • Carafoli, E., Genazzani, A. & Guerini, D. Calcium controls the transcription of its own transporters and channels in developing neurons. Biochem. Biophys. Res. Commun. 266, 624-632 (1999).
    • (1999) Biochem. Biophys. Res. Commun. , vol.266 , pp. 624-632
    • Carafoli, E.1    Genazzani, A.2    Guerini, D.3
  • 96
    • 0034617306 scopus 로고    scopus 로고
    • 2+ exchanger isoforms in developing cerebellar neurons
    • 2+ exchanger isoforms in developing cerebellar neurons. J. Biol. Chem. 276, 20903-20910 (2000).
    • (2000) J. Biol. Chem. , vol.276 , pp. 20903-20910
    • Li, L.1    Guerini, D.2    Carafoli, E.3
  • 97
    • 0033545997 scopus 로고    scopus 로고
    • Calcineurin controls inositol 1,4,5-trisphosphate type 1 receptor expression in neurons
    • Genazzani, A. A., Carafoli, E. & Guerini, D. Calcineurin controls inositol 1,4,5-trisphosphate type 1 receptor expression in neurons. Proc. Natl Acad. Sci. USA 96, 5797-5801 (1999).
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 5797-5801
    • Genazzani, A.A.1    Carafoli, E.2    Guerini, D.3
  • 98
    • 0033554699 scopus 로고    scopus 로고
    • L-type calcium channels and GSK-3 regulate the activity of NF-ATc4 in hippocampal neurons
    • 3Rs.
    • (1999) Nature , vol.401 , pp. 703-708
    • Graef, I.A.1
  • 100
    • 0034537410 scopus 로고    scopus 로고
    • 2+ homeostasis and cardiomyocyte function
    • 2+ homeostasis and cardiomyocyte function. J. Biol. Chem. 275, 38073-38080 (2000).
    • (2000) J. Biol. Chem. , vol.275 , pp. 38073-38080
    • Ji, Y.1
  • 102
    • 0037040149 scopus 로고    scopus 로고
    • 2+ channel
    • 2+ channel. Circ. Res. 90, 174-181 (2002).
    • (2002) Circ. Res. , vol.90 , pp. 174-181
    • Song, L.-S.1
  • 103
    • 0032540267 scopus 로고    scopus 로고
    • A calcineurin-dependent transcriptional pathway for cardiac hypertrophy
    • Molkentin, J. D. et al. A calcineurin-dependent transcriptional pathway for cardiac hypertrophy. Cell 93, 215-228 (1998).
    • (1998) Cell , vol.93 , pp. 215-228
    • Molkentin, J.D.1
  • 104
    • 0035830828 scopus 로고    scopus 로고
    • Cardiac hypertrophy and impaired relaxation in transgenic mice overexpressing triadin 1
    • Kirchhefer, U. et al. Cardiac hypertrophy and impaired relaxation in transgenic mice overexpressing triadin 1. J. Biol. Chem. 276, 4142-4149 (2001).
    • (2001) J. Biol. Chem. , vol.276 , pp. 4142-4149
    • Kirchhefer, U.1
  • 105
    • 0034977701 scopus 로고    scopus 로고
    • Structural alterations in cardiac calcium release units resulting from overexpression of junctin
    • Zhang, L., Franzini-Armstrong, C., Ramesh, V. & Jones, L. R. Structural alterations in cardiac calcium release units resulting from overexpression of junctin. J. Mol. Cell. Cardiol. 33, 233-247 (2001).
    • (2001) J. Mol. Cell. Cardiol. , vol.33 , pp. 233-247
    • Zhang, L.1    Franzini-Armstrong, C.2    Ramesh, V.3    Jones, L.R.4
  • 106
    • 0032038691 scopus 로고    scopus 로고
    • Regulation of calcium signalling in transgenic mouse cardiac myocytes overexpressing calsequestrin
    • Jones, L. R. et al. Regulation of calcium signalling in transgenic mouse cardiac myocytes overexpressing calsequestrin. J. Clin. Invest. 101, 1385-1393 (1998).
    • (1998) J. Clin. Invest. , vol.101 , pp. 1385-1393
    • Jones, L.R.1
  • 107
    • 0032506233 scopus 로고    scopus 로고
    • αq leads to hypertrophy and dilated cardiomyopathy by calcineurin-dependent and independent pathways
    • αq leads to hypertrophy and dilated cardiomyopathy by calcineurin-dependent and independent pathways. Proc. Natl Acad. Sci. USA 95, 13893-13898 (1998).
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 13893-13898
    • Mende, U.1
  • 108
    • 0034212795 scopus 로고    scopus 로고
    • Remodelling of ionic currents in hypertrophied and failing hearts of transgenic mice overexpressing calsequestrin
    • Knollmann, B. C., Knollmann-Ritschel, B. E., Weissman, N. J., Jones, L. R. & Morad, M. Remodelling of ionic currents in hypertrophied and failing hearts of transgenic mice overexpressing calsequestrin. J. Physiol. (Lond.) 525, 483-498 (2000).
    • (2000) J. Physiol. (Lond.) , vol.525 , pp. 483-498
    • Knollmann, B.C.1    Knollmann-Ritschel, B.E.2    Weissman, N.J.3    Jones, L.R.4    Morad, M.5
  • 110
    • 0037154168 scopus 로고    scopus 로고
    • Activated glycogen synthase-3β suppresses cardiac hypertrophy in vivo
    • Antos, C. L. et al. Activated glycogen synthase-3β suppresses cardiac hypertrophy in vivo. Proc. Natl Acad. Sci. USA 99, 907-912 (2002).
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 907-912
    • Antos, C.L.1
  • 111
    • 0035937762 scopus 로고    scopus 로고
    • Rescue of contractile parameters and myocyte hypertrophy in calsequestrin overexpressing myocardium by phospholamban ablation
    • Sato, Y. et al. Rescue of contractile parameters and myocyte hypertrophy in calsequestrin overexpressing myocardium by phospholamban ablation. J. Biol. Chem. 275, 9392-9399 (2001).
    • (2001) J. Biol. Chem. , vol.275 , pp. 9392-9399
    • Sato, Y.1
  • 112
    • 0037362850 scopus 로고    scopus 로고
    • Rescue of cardiomyocyte dysfunction by phospholamban ablation does not prevent ventricular failure in genetic hypertrophy
    • , Song, Q. et al. Rescue of cardiomyocyte dysfunction by phospholamban ablation does not prevent ventricular failure in genetic hypertrophy. J. Clin. Invest. 111, 859-867 (2003).
    • (2003) J. Clin. Invest. , vol.111 , pp. 859-867
    • Song, Q.1
  • 113
    • 85047687537 scopus 로고    scopus 로고
    • Human phospholamban null results in lethal dilated cardiomyopathy revealing a critical difference between mouse and human
    • Haghighi, K. et al. Human phospholamban null results in lethal dilated cardiomyopathy revealing a critical difference between mouse and human. J. Clin. Invest. 111, 869-876 (2003).
    • (2003) J. Clin. Invest. , vol.111 , pp. 869-876
    • Haghighi, K.1
  • 114
    • 0037095815 scopus 로고    scopus 로고
    • Calcineurin and cardiac hypertrophy: Where have we been? where are we going?
    • Wilkins, B. J. & Molkentin, J. D. Calcineurin and cardiac hypertrophy: where have we been? where are we going? J. Physiol. 541, 1-8 (2002).
    • (2002) J. Physiol. , vol.541 , pp. 1-8
    • Wilkins, B.J.1    Molkentin, J.D.2
  • 115
    • 0037149508 scopus 로고    scopus 로고
    • Oestrogen protects FKBP12.6 null mice from cardiac hypertrophy
    • Xin, H.-B, et al. Oestrogen protects FKBP12.6 null mice from cardiac hypertrophy. Nature 416, 334-337 (2002).
    • (2002) Nature , vol.416 , pp. 334-337
    • Xin, H.-B.1
  • 116
    • 0033105384 scopus 로고    scopus 로고
    • 2+-sensitivity of SERCA2a in failing human myocardium due to reduced serine-16 phospholamban phosphorylation
    • 2+-sensitivity of SERCA2a in failing human myocardium due to reduced serine-16 phospholamban phosphorylation. J. Mol. Cell. Cardiol. 31, 479-491 (1999).
    • (1999) J. Mol. Cell. Cardiol. , vol.31 , pp. 479-491
    • Schwinger1
  • 117
    • 0344284562 scopus 로고    scopus 로고
    • Cellular basis of abnormal calcium transients of failing human ventricular myocytes
    • Piacentino III, V. et al. Cellular basis of abnormal calcium transients of failing human ventricular myocytes. Circ. Res. 92, 651-658 (2003).
    • (2003) Circ. Res. , vol.92 , pp. 651-658
    • Piacentino V. III1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.