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Volumn 1, Issue 4, 2002, Pages 241-258

'New' functions for 'old' proteins: The role of the calcium-binding proteins calbindin D-28k, calretinin and parvalbumin, in cerebellar physiology. Studies with knockout mice

Author keywords

Ataxia; Calcium binding protein; Knockout mice; Purkinje cells; Synaptic plasticity

Indexed keywords

CALBINDIN; CALCIUM BINDING PROTEIN; CALRETININ; PARVALBUMIN; CALCIUM;

EID: 0042233504     PISSN: 14734222     EISSN: 14734230     Source Type: Journal    
DOI: 10.1080/147342202320883551     Document Type: Review
Times cited : (340)

References (152)
  • 1
    • 37049247532 scopus 로고
    • Vitamin D3-induced calcium-binding protein in chick intestinal mucosa
    • Wasserman RH, Taylor AN. Vitamin D3-induced calcium-binding protein in chick intestinal mucosa. Science 1966; 152: 791-793.
    • (1966) Science , vol.152 , pp. 791-793
    • Wasserman, R.H.1    Taylor, A.N.2
  • 2
    • 0023608936 scopus 로고
    • Calretinin: A gene for a novel calcium-binding protein expressed principally in neurons
    • Rogers JH. Calretinin: A gene for a novel calcium-binding protein expressed principally in neurons. J Cell Biol 1987; 105: 1343-1353.
    • (1987) J Cell Biol , vol.105 , pp. 1343-1353
    • Rogers, J.H.1
  • 3
    • 0016391170 scopus 로고
    • Isolation of a parvalbumin from rabbit muscle
    • Pechere JF. Isolation of a parvalbumin from rabbit muscle. C R Acad Sci Hebd Seances Acad Sci D 1974; 278: 2577-2579.
    • (1974) C R Acad Sci Hebd Seances Acad Sci D , vol.278 , pp. 2577-2579
    • Pechere, J.F.1
  • 4
    • 0018816959 scopus 로고
    • Structure and evolution of calcium-modulated proteins
    • Kretsinger RH. Structure and evolution of calcium-modulated proteins. CRC Crit Rev Biochem 1980; 8: 119-174.
    • (1980) CRC Crit Rev Biochem , vol.8 , pp. 119-174
    • Kretsinger, R.H.1
  • 5
    • 0032454584 scopus 로고    scopus 로고
    • Classification and evolution of EF-hand proteins
    • Kawasaki H, Nakayama S, Kretsinger RH. Classification and evolution of EF-hand proteins. Biometals 1998; 11: 277-295.
    • (1998) Biometals , vol.11 , pp. 277-295
    • Kawasaki, H.1    Nakayama, S.2    Kretsinger, R.H.3
  • 6
    • 0029669991 scopus 로고    scopus 로고
    • The S100 family of EF-hand calcium-binding proteins: Functions and pathology
    • Schäfer BW, Heizmann CW. The S100 family of EF-hand calcium-binding proteins: functions and pathology. Trends Biol Sci 1996; 21: 134-140.
    • (1996) Trends Biol Sci , vol.21 , pp. 134-140
    • Schäfer, B.W.1    Heizmann, C.W.2
  • 7
    • 0004094694 scopus 로고    scopus 로고
    • Celio M, Pauls T, Schwaller B, editors. Oxford: Oxford University Press
    • Celio M, Pauls T, Schwaller B, editors. Guidebook to the calcium-binding proteins. Oxford: Oxford University Press, 1996.
    • (1996) Guidebook to the Calcium-binding Proteins
  • 8
    • 0027279396 scopus 로고
    • Calcium binding by chick calretinin and rat calbindin D28k synthesised in bacteria
    • Cheung WT, Richards DE, Rogers JH. Calcium binding by chick calretinin and rat calbindin D28k synthesised in bacteria. Eur J Biochem 1993; 215: 401-410.
    • (1993) Eur J Biochem , vol.215 , pp. 401-410
    • Cheung, W.T.1    Richards, D.E.2    Rogers, J.H.3
  • 10
    • 0018380478 scopus 로고
    • Magnesium and calcium binding to parvalbumins: Evidence for differences between parvalbumins and an explanation of their relaxing function
    • Haiech J, Derancourt J, Pechere J-F, Demaille JG. Magnesium and calcium binding to parvalbumins: evidence for differences between parvalbumins and an explanation of their relaxing function. Biochemistry 1979; 18: 2752-2758.
    • (1979) Biochemistry , vol.18 , pp. 2752-2758
    • Haiech, J.1    Derancourt, J.2    Pechere, J.-F.3    Demaille, J.G.4
  • 11
    • 0035875483 scopus 로고    scopus 로고
    • 2+ concentration and inhibition of NMDA responses in cultured rat neurons
    • 2+ concentration and inhibition of NMDA responses in cultured rat neurons. J Physiol (Lond) 2001; 533: 729-743.
    • (2001) J Physiol (Lond) , vol.533 , pp. 729-743
    • Li-Smerin, Y.1    Levitan, E.S.2    Johnson, J.W.3
  • 13
    • 0025918658 scopus 로고
    • 2+ dissociation rates correlated with changes in relaxation rate of frog muscle fibres
    • 2+ dissociation rates correlated with changes in relaxation rate of frog muscle fibres. J Physiol (Lond) 1991; 441: 285-304.
    • (1991) J Physiol (Lond) , vol.441 , pp. 285-304
    • Hou, T.-T.1    Johnson, J.D.2    Rall, J.A.3
  • 14
    • 0021379023 scopus 로고
    • 45Ca autoradiography on nitrocellulose membrane after sodium dodecyl sulfate gel electrophoresis
    • 45Ca autoradiography on nitrocellulose membrane after sodium dodecyl sulfate gel electrophoresis. J Biochem (Tokyo) 1984; 95: 511-519.
    • (1984) J Biochem (Tokyo) , vol.95 , pp. 511-519
    • Maruyama, K.1    Mikawa, T.2    Ebashi, S.3
  • 16
    • 0017833674 scopus 로고
    • Evidence for a membrane-bound fraction of chick intestinal calcium-binding protein
    • Feher JJ, Wasserman RH. Evidence for a membrane-bound fraction of chick intestinal calcium-binding protein. Biochim Biophys Acta 1978; 540: 134-143.
    • (1978) Biochim Biophys Acta , vol.540 , pp. 134-143
    • Feher, J.J.1    Wasserman, R.H.2
  • 17
    • 0024497928 scopus 로고
    • Calmodulin binding to the intestinal brush-border membrane: Comparison to other calcium-binding proteins
    • Bikle D, Munson S, Christakos S, Kumar R, Buckendahl P. Calmodulin binding to the intestinal brush-border membrane: comparison to other calcium-binding proteins. Biochim Biophys Acta 1989; 1010: 122-127.
    • (1989) Biochim Biophys Acta , vol.1010 , pp. 122-127
    • Bikle, D.1    Munson, S.2    Christakos, S.3    Kumar, R.4    Buckendahl, P.5
  • 18
    • 0028972028 scopus 로고
    • Calbindin 28kDa and calbindin 30kDa (calretinin) are substantially localised in the particulate fraction of rat brain
    • Hubbard MJ, McHugh NJ. Calbindin 28kDa and calbindin 30kDa (calretinin) are substantially localised in the particulate fraction of rat brain. FEBS Lett 1995; 374: 333-337.
    • (1995) FEBS Lett , vol.374 , pp. 333-337
    • Hubbard, M.J.1    McHugh, N.J.2
  • 19
    • 0033623505 scopus 로고    scopus 로고
    • Calbindin28kDa is specifically associated with extranuclear constituents of the dense particulate fraction
    • Sayer RJ, Turnbull CI, Hubbard MJ. Calbindin28kDa is specifically associated with extranuclear constituents of the dense particulate fraction. Cell Tissue Res 2000; 302: 171-180.
    • (2000) Cell Tissue Res , vol.302 , pp. 171-180
    • Sayer, R.J.1    Turnbull, C.I.2    Hubbard, M.J.3
  • 20
    • 0029074494 scopus 로고
    • Distribution of calretinin, calbindinD28k and parvalbumin in subcellular fractions of rat cerebellum: Effects of calcium
    • Winsky L, Kuznicki J. Distribution of calretinin, calbindinD28k and parvalbumin in subcellular fractions of rat cerebellum: effects of calcium. J Neurochem 1995; 65: 381-388.
    • (1995) J Neurochem , vol.65 , pp. 381-388
    • Winsky, L.1    Kuznicki, J.2
  • 21
    • 0034714431 scopus 로고    scopus 로고
    • Association between the calcium-binding protein calretinin and cytoskeletal components in the human colon adenocarcinoma cell line WiDr
    • Marilley D, Schwaller B. Association between the calcium-binding protein calretinin and cytoskeletal components in the human colon adenocarcinoma cell line WiDr. Exp Cell Res 2000; 259: 12-22.
    • (2000) Exp Cell Res , vol.259 , pp. 12-22
    • Marilley, D.1    Schwaller, B.2
  • 22
    • 0021746336 scopus 로고
    • Membrane-associated vitamin D-induced calcium-binding protein (CaBP): Quantification by a radioimmunoassay and evidence for a specific CaBP in purified intestinal brush borders
    • Shimura F, Wasserman RH. Membrane-associated vitamin D-induced calcium-binding protein (CaBP): quantification by a radioimmunoassay and evidence for a specific CaBP in purified intestinal brush borders. Endocrinology 1984; 115: 1964-1972.
    • (1984) Endocrinology , vol.115 , pp. 1964-1972
    • Shimura, F.1    Wasserman, R.H.2
  • 23
    • 0027276416 scopus 로고
    • Evidence for calcium mediated conformational changes in calbindin-D28K (the vitamin D-induced calcium binding protein) interactions with chick intestinal brush border membrane alkaline phosphatase as studied via photoaffinity labeling techniques
    • Leathers VL, Norman AW. Evidence for calcium mediated conformational changes in calbindin-D28K (the vitamin D-induced calcium binding protein) interactions with chick intestinal brush border membrane alkaline phosphatase as studied via photoaffinity labeling techniques. J Cell Biochem 1993; 52: 243-252.
    • (1993) J Cell Biochem , vol.52 , pp. 243-252
    • Leathers, V.L.1    Norman, A.W.2
  • 25
    • 0026567734 scopus 로고
    • Calretinin in rat brain: An immunohistochemical study
    • Résibois A, Rogers JH. Calretinin in rat brain: an immunohistochemical study. Neurosci 1992; 46: 101-134.
    • (1992) Neurosci , vol.46 , pp. 101-134
    • Résibois, A.1    Rogers, J.H.2
  • 26
    • 0030614739 scopus 로고    scopus 로고
    • Calretinin-containing neurons in rat cerebellar granule cell cultures
    • Marini AM, Strauss KI, Jacobowitz DM. Calretinin-containing neurons in rat cerebellar granule cell cultures. Brain Res Bull 1997; 42: 279-288.
    • (1997) Brain Res Bull , vol.42 , pp. 279-288
    • Marini, A.M.1    Strauss, K.I.2    Jacobowitz, D.M.3
  • 28
    • 0024805357 scopus 로고
    • Immunoreactivity for calretinin and other calcium-binding proteins in cerebellum
    • Rogers JH. Immunoreactivity for calretinin and other calcium-binding proteins in cerebellum. Neurosci 1989; 31: 711-721.
    • (1989) Neurosci , vol.31 , pp. 711-721
    • Rogers, J.H.1
  • 29
    • 0027276557 scopus 로고
    • Ultrastructural localization of calretinin immunoreactivity in lobule V of the rat cerebellum
    • Arai R, Jacobowitz DM, Deura S. Ultrastructural localization of calretinin immunoreactivity in lobule V of the rat cerebellum. Brain Res 1993; 613: 300-304.
    • (1993) Brain Res , vol.613 , pp. 300-304
    • Arai, R.1    Jacobowitz, D.M.2    Deura, S.3
  • 30
    • 0028339973 scopus 로고
    • The unipolar brush cells of the rat cerebellar cortex and cochlear nucleus are calretinin-positive: A study by light and electron microscopic immunocytochemistry
    • Floris A, Dino M, Jacobowitz DM, Mugnaini E. The unipolar brush cells of the rat cerebellar cortex and cochlear nucleus are calretinin-positive: a study by light and electron microscopic immunocytochemistry. Anat Embryol (Berl) 1994; 189: 495-520.
    • (1994) Anat Embryol (Berl) , vol.189 , pp. 495-520
    • Floris, A.1    Dino, M.2    Jacobowitz, D.M.3    Mugnaini, E.4
  • 31
    • 0033402374 scopus 로고    scopus 로고
    • Distribution of unipolar brush cells and other calretinin immunoreactive components in the mammalian cerebellar cortex
    • Dino MR, Willard FH, Mugnaini E. Distribution of unipolar brush cells and other calretinin immunoreactive components in the mammalian cerebellar cortex. J Neurocytol 1999; 28: 99-123.
    • (1999) J Neurocytol , vol.28 , pp. 99-123
    • Dino, M.R.1    Willard, F.H.2    Mugnaini, E.3
  • 32
    • 0033854618 scopus 로고    scopus 로고
    • Unipolar brush cells of the vestibulocerebellum: Afferents and targets
    • Dino MR, Nunzi MG, Anelli R, Mugnaini E. Unipolar brush cells of the vestibulocerebellum: afferents and targets. Prog Brain Res 2000; 124: 123-137.
    • (2000) Prog Brain Res , vol.124 , pp. 123-137
    • Dino, M.R.1    Nunzi, M.G.2    Anelli, R.3    Mugnaini, E.4
  • 33
    • 0034161492 scopus 로고    scopus 로고
    • Serotonin-driven long-range inhibitory connections in the cerebellar cortex
    • Dieudonne S, Dumoulin A. Serotonin-driven long-range inhibitory connections in the cerebellar cortex. J Neurosci 2000; 20: 1837-1848.
    • (2000) J Neurosci , vol.20 , pp. 1837-1848
    • Dieudonne, S.1    Dumoulin, A.2
  • 34
    • 0031883158 scopus 로고    scopus 로고
    • Calcium-binding proteins in primate cerebellum
    • Fortin M, Marchand R, Parent A. Calcium-binding proteins in primate cerebellum. Neurosci Res 1998; 30: 155-168.
    • (1998) Neurosci Res , vol.30 , pp. 155-168
    • Fortin, M.1    Marchand, R.2    Parent, A.3
  • 35
    • 0027386859 scopus 로고
    • Intracellular concentration of parvalbumin in nerve cells
    • Plogmann D, Celio MR. Intracellular concentration of parvalbumin in nerve cells. Brain Res 1993; 600: 273-279.
    • (1993) Brain Res , vol.600 , pp. 273-279
    • Plogmann, D.1    Celio, M.R.2
  • 36
    • 0027316317 scopus 로고
    • Axons and axon terminals of cerebellar Purkinje cells and basket cells have higher levels of parvalbumin immunoreactivity than somata and dendrites: Quantitative analysis by immunogold labeling
    • Kosaka T, Kosaka K, Nakayama T, Hunziker W, Heizmann CW. Axons and axon terminals of cerebellar Purkinje cells and basket cells have higher levels of parvalbumin immunoreactivity than somata and dendrites: quantitative analysis by immunogold labeling. Exp Brain Res 1993; 93: 483-491.
    • (1993) Exp Brain Res , vol.93 , pp. 483-491
    • Kosaka, T.1    Kosaka, K.2    Nakayama, T.3    Hunziker, W.4    Heizmann, C.W.5
  • 37
    • 0029958287 scopus 로고    scopus 로고
    • High endogenous calcium buffering in Purkinje cells from rat cerebellar slices
    • Fierro L, Llano I. High endogenous calcium buffering in Purkinje cells from rat cerebellar slices. J Physiol (Lond) 1996; 496: 617-625.
    • (1996) J Physiol (Lond) , vol.496 , pp. 617-625
    • Fierro, L.1    Llano, I.2
  • 39
    • 0025358573 scopus 로고
    • Calbindin D-28k and parvalbumin in the rat nervous system
    • Celio MR. Calbindin D-28k and parvalbumin in the rat nervous system. Neuroscience 1990; 35: 375-475.
    • (1990) Neuroscience , vol.35 , pp. 375-475
    • Celio, M.R.1
  • 41
    • 0033135299 scopus 로고    scopus 로고
    • Electrotonic coupling interacts with intrinsic properties to generate synchronized activity in cerebellar networks of inhibitory interneurons
    • Mann-Metzer P, Yarom Y. Electrotonic coupling interacts with intrinsic properties to generate synchronized activity in cerebellar networks of inhibitory interneurons. J Neurosci 1999; 19: 3298-3306.
    • (1999) J Neurosci , vol.19 , pp. 3298-3306
    • Mann-Metzer, P.1    Yarom, Y.2
  • 42
    • 0035380761 scopus 로고    scopus 로고
    • Electrical synapses between GABA-releasing interneurons
    • Galarreta M, Hestrin S. Electrical synapses between GABA-releasing interneurons. Nat Rev Neurosci 2001; 2: 425-433.
    • (2001) Nat Rev Neurosci , vol.2 , pp. 425-433
    • Galarreta, M.1    Hestrin, S.2
  • 43
    • 0026580562 scopus 로고
    • 2+ binding properties in the human cerebellar cortex: Distribution of parvalbumin and calbindin D-28k immunoreactivity
    • 2+ binding properties in the human cerebellar cortex: distribution of parvalbumin and calbindin D-28k immunoreactivity. Anat Embryol 1992; 185: 163-167.
    • (1992) Anat Embryol , vol.185 , pp. 163-167
    • Scotti, A.L.1    Nitsch, C.2
  • 44
    • 0031019589 scopus 로고    scopus 로고
    • Ataxia and altered dendritic calcium signaling in mice carrying a targeted null mutation of the calbindin D28k gene
    • Airaksinen MS, Eilers J, Garaschuk O, Thoenen H, Konnerth A, Meyer M. Ataxia and altered dendritic calcium signaling in mice carrying a targeted null mutation of the calbindin D28k gene. Proc Natl Acad Sci USA 1997; 94: 1488-1493.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 1488-1493
    • Airaksinen, M.S.1    Eilers, J.2    Garaschuk, O.3    Thoenen, H.4    Konnerth, A.5    Meyer, M.6
  • 47
    • 0028853910 scopus 로고
    • Calcium signaling in a narrow somatic submembrane shell during synaptic activity in cerebellar Purkinje neurons
    • Eilers J, Callewaert G, Armstrong C, Konnerth A. Calcium signaling in a narrow somatic submembrane shell during synaptic activity in cerebellar Purkinje neurons. Proc Natl Acad Sci USA 1995; 92: 10272-10276.
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 10272-10276
    • Eilers, J.1    Callewaert, G.2    Armstrong, C.3    Konnerth, A.4
  • 48
    • 0023413721 scopus 로고
    • Autoradiographic localization of cerebellar excitatory amino acid binding sites in the mouse
    • Olson JM, Greenamyre JT, Penney JB, Young AB. Autoradiographic localization of cerebellar excitatory amino acid binding sites in the mouse. Neuroscience 1987; 22: 913-923.
    • (1987) Neuroscience , vol.22 , pp. 913-923
    • Olson, J.M.1    Greenamyre, J.T.2    Penney, J.B.3    Young, A.B.4
  • 50
    • 0028977967 scopus 로고
    • 2+ signalling in fine dendrites and spines of cerebellar Purkinje neurons
    • 2+ signalling in fine dendrites and spines of cerebellar Purkinje neurons. Nature 1995; 373: 155-158.
    • (1995) Nature , vol.373 , pp. 155-158
    • Eilers, J.1    Augustine, G.J.2    Konnerth, A.3
  • 51
    • 0032585513 scopus 로고    scopus 로고
    • A new class of synaptic response involving calcium release in dendritic spines
    • Takechi H, Eilers J, Konnerth A. A new class of synaptic response involving calcium release in dendritic spines. Nature 1998; 396: 757-760.
    • (1998) Nature , vol.396 , pp. 757-760
    • Takechi, H.1    Eilers, J.2    Konnerth, A.3
  • 52
    • 0029113189 scopus 로고
    • Two types of calcium response limited to single spines in cerebellar Purkinje cells
    • Denk W, Sugimori M, Llinas R. Two types of calcium response limited to single spines in cerebellar Purkinje cells. Proc Natl Acad Sci USA 1995; 92: 8279-8282.
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 8279-8282
    • Denk, W.1    Sugimori, M.2    Llinas, R.3
  • 53
    • 0032585614 scopus 로고    scopus 로고
    • Local calcium signalling by inositol-1,4,5-trisphosphate in Purkinje cell dendrites
    • Finch EA, Augustine GJ. Local calcium signalling by inositol-1,4,5- trisphosphate in Purkinje cell dendrites. Nature 1998; 396: 753-756.
    • (1998) Nature , vol.396 , pp. 753-756
    • Finch, E.A.1    Augustine, G.J.2
  • 54
    • 0029665633 scopus 로고    scopus 로고
    • 2+ release by InsP3 in cerebellar Purkinje neurones
    • 2+ release by InsP3 in cerebellar Purkinje neurones. Acta Physiol Scand 1996; 157: 381-394.
    • (1996) Acta Physiol Scand , vol.157 , pp. 381-394
    • Ogden, D.1    Khodakhah, K.2
  • 55
    • 0033680563 scopus 로고    scopus 로고
    • Coincidence detection in single dendritic spines mediated by calcium release
    • Wang SS, Denk W, Hausser M. Coincidence detection in single dendritic spines mediated by calcium release. Nat Neurosci 2000; 3: 1266-1273.
    • (2000) Nat Neurosci , vol.3 , pp. 1266-1273
    • Wang, S.S.1    Denk, W.2    Hausser, M.3
  • 57
    • 0027102174 scopus 로고
    • Two types of ryanodine receptors in mouse brain: Skeletal muscle type exclusively in Purkinje cells and cardiac muscle type in various neurons
    • Kuwajima G, Futatsugi A, Niinobe M, Nakanishi S, Mikoshiba K. Two types of ryanodine receptors in mouse brain: skeletal muscle type exclusively in Purkinje cells and cardiac muscle type in various neurons. Neuron 1992; 9: 1133-1142.
    • (1992) Neuron , vol.9 , pp. 1133-1142
    • Kuwajima, G.1    Futatsugi, A.2    Niinobe, M.3    Nakanishi, S.4    Mikoshiba, K.5
  • 59
    • 0028970644 scopus 로고
    • 2+ stores, is required for the induction of LTD in cultured cerebellar Purkinje cells
    • 2+ stores, is required for the induction of LTD in cultured cerebellar Purkinje cells. J Neurophysiol 1995; 74: 2184-2188.
    • (1995) J Neurophysiol , vol.74 , pp. 2184-2188
    • Kohda, K.1    Inoue, T.2    Mikoshiba, K.3
  • 60
    • 0028199796 scopus 로고
    • Calcium-induced calcium release in cerebellar Purkinje cells
    • Llano I, DiPolo R, Marty A. Calcium-induced calcium release in cerebellar Purkinje cells. Neuron 1994; 12: 663-673.
    • (1994) Neuron , vol.12 , pp. 663-673
    • Llano, I.1    DiPolo, R.2    Marty, A.3
  • 62
    • 0032528073 scopus 로고    scopus 로고
    • Intracellular calcium clearance in Purkinje cell somata from rat cerebellar slices
    • Fierro L, DiPolo R, Llano I. Intracellular calcium clearance in Purkinje cell somata from rat cerebellar slices. J Physiol (Lond) 1998; 510: 499-512.
    • (1998) J Physiol (Lond) , vol.510 , pp. 499-512
    • Fierro, L.1    DiPolo, R.2    Llano, I.3
  • 63
    • 0033864506 scopus 로고    scopus 로고
    • 2+-transporting ATPases
    • 2+-transporting ATPases. Eur J Biochem 2000; 267: 5284-5290.
    • (2000) Eur J Biochem , vol.267 , pp. 5284-5290
    • Shull, G.E.1
  • 64
    • 0000181567 scopus 로고    scopus 로고
    • Plasma membrane calcium ATPases as critical regulators of calcium homeostasis during neuronal cell function
    • Garcia ML, Strehler EE. Plasma membrane calcium ATPases as critical regulators of calcium homeostasis during neuronal cell function. Front Biosci 1999; 4: D869-882.
    • (1999) Front Biosci , vol.4
    • Garcia, M.L.1    Strehler, E.E.2
  • 65
    • 0032130859 scopus 로고    scopus 로고
    • The calcium pump of the plasma membrane: Membrane targeting, calcium binding sites, tissue-specific isoform expression
    • Guerini D, Garcia-Martin E, Zecca A, Guidi F, Carafoli E. The calcium pump of the plasma membrane: membrane targeting, calcium binding sites, tissue-specific isoform expression. Acta Physiol Scand Suppl 1998; 643: 265-273.
    • (1998) Acta Physiol Scand Suppl , vol.643 , pp. 265-273
    • Guerini, D.1    Garcia-Martin, E.2    Zecca, A.3    Guidi, F.4    Carafoli, E.5
  • 66
    • 0027135818 scopus 로고
    • Immunocytochemical localization of the plasma membrane calcium pump, calbindin-D28k, and parvalbumin in Purkinje cells of avian and mammalian cerebellum
    • de Talamoni N, Smith CA, Wasserman RH, Beltramino C, Fullmer CS, Penniston JT. Immunocytochemical localization of the plasma membrane calcium pump, calbindin-D28k, and parvalbumin in Purkinje cells of avian and mammalian cerebellum. Proc Natl Acad Sci USA 1993; 90: 11949-11953.
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 11949-11953
    • De Talamoni, N.1    Smith, C.A.2    Wasserman, R.H.3    Beltramino, C.4    Fullmer, C.S.5    Penniston, J.T.6
  • 67
    • 0032801648 scopus 로고    scopus 로고
    • Sodium/calcium exchange: Its physiological implications
    • Blaustein MP, Lederer WJ. Sodium/calcium exchange: its physiological implications. Physiol Rev 1999; 79: 763-854.
    • (1999) Physiol Rev , vol.79 , pp. 763-854
    • Blaustein, M.P.1    Lederer, W.J.2
  • 69
    • 0031780887 scopus 로고    scopus 로고
    • Competitive calcium binding: Implications for dendritic calcium signaling
    • Markram H, Roth A, Helmchen F. Competitive calcium binding: implications for dendritic calcium signaling. J Comput Neurosci 1998; 5: 331-348.
    • (1998) J Comput Neurosci , vol.5 , pp. 331-348
    • Markram, H.1    Roth, A.2    Helmchen, F.3
  • 70
    • 0029065159 scopus 로고
    • Dendritic spines as basic functional units of neuronal integration
    • Yuste R, Denk W. Dendritic spines as basic functional units of neuronal integration. Nature 1995; 375: 682-684.
    • (1995) Nature , vol.375 , pp. 682-684
    • Yuste, R.1    Denk, W.2
  • 71
    • 0033947688 scopus 로고    scopus 로고
    • From form to function: Calcium compartmentalization in dendritic spines
    • Yuste R, Majewska A, Holthoff K. From form to function: calcium compartmentalization in dendritic spines. Nat Neurosci 2000; 3: 653-659.
    • (2000) Nat Neurosci , vol.3 , pp. 653-659
    • Yuste, R.1    Majewska, A.2    Holthoff, K.3
  • 72
    • 0031059220 scopus 로고    scopus 로고
    • Vulnerability of mid-brain dopaminergic neurons in calbindin-D-28k- deficient mice: Lack of evidence for a neuroprotective role of endogenous calbindin in MPTP-treated and weaver mice
    • Airaksinen MS, Thoenen H, Meyer M. Vulnerability of mid-brain dopaminergic neurons in calbindin-D-28k-deficient mice: lack of evidence for a neuroprotective role of endogenous calbindin in MPTP-treated and weaver mice. Eur J Neurosci 1997; 9: 120-127.
    • (1997) Eur J Neurosci , vol.9 , pp. 120-127
    • Airaksinen, M.S.1    Thoenen, H.2    Meyer, M.3
  • 73
    • 0031972129 scopus 로고    scopus 로고
    • Calcium-binding proteins in the retina of a calbindin-null mutant mouse
    • Wässle H, Peichl L, Airaksinen MS, Meyer M. Calcium-binding proteins in the retina of a calbindin-null mutant mouse. Cell Tissue Res 1998; 292: 211-218.
    • (1998) Cell Tissue Res , vol.292 , pp. 211-218
    • Wässle, H.1    Peichl, L.2    Airaksinen, M.S.3    Meyer, M.4
  • 74
    • 0034111417 scopus 로고    scopus 로고
    • Alterations in Purkinje cell spines of calbindin D-28 k and parvalbumin knock-out mice
    • Vecellio M, Schwaller B, Meyer M, Hunziker W, Celio MR. Alterations in Purkinje cell spines of calbindin D-28 k and parvalbumin knock-out mice. Eur J Neurosci 2000; 12: 945-954.
    • (2000) Eur J Neurosci , vol.12 , pp. 945-954
    • Vecellio, M.1    Schwaller, B.2    Meyer, M.3    Hunziker, W.4    Celio, M.R.5
  • 75
    • 0034489127 scopus 로고    scopus 로고
    • Cre recombinase expression in cerebellar Purkinje cells
    • Barski JJ, Dethleffsen K, Meyer M. Cre recombinase expression in cerebellar Purkinje cells. Genesis 2000; 28: 93-98.
    • (2000) Genesis , vol.28 , pp. 93-98
    • Barski, J.J.1    Dethleffsen, K.2    Meyer, M.3
  • 78
    • 0032107048 scopus 로고    scopus 로고
    • Calbindin-D28k fails to protect hippocampal neurons against ischemia in spite of its cytoplasmic calcium buffering properties: Evidence from calbindin-D28k knockout mice
    • Klapstein GJ, Vietla S, Lieberman DN, Gray PA, Airaksinen MS, Thoenen H, Meyer M, Mody I. Calbindin-D28k fails to protect hippocampal neurons against ischemia in spite of its cytoplasmic calcium buffering properties: evidence from calbindin-D28k knockout mice. Neuroscience 1998; 85: 361-373.
    • (1998) Neuroscience , vol.85 , pp. 361-373
    • Klapstein, G.J.1    Vietla, S.2    Lieberman, D.N.3    Gray, P.A.4    Airaksinen, M.S.5    Thoenen, H.6    Meyer, M.7    Mody, I.8
  • 79
    • 0035868689 scopus 로고    scopus 로고
    • 2+ buffers in facilitating and depressing nerve terminals of pyramidal cells in layer 2/3 of the rat neocortex indicates a target cell-specific difference in presynaptic calcium dynamics
    • 2+ buffers in facilitating and depressing nerve terminals of pyramidal cells in layer 2/3 of the rat neocortex indicates a target cell-specific difference in presynaptic calcium dynamics. J Physiol (Lond) 2001; 531: 807-826.
    • (2001) J Physiol (Lond) , vol.531 , pp. 807-826
    • Rozov, A.1    Burnashev, N.2    Sakmann, B.3    Neher, E.4
  • 80
    • 0031067017 scopus 로고    scopus 로고
    • 2+ diffusion near the membrane: Implications for secretion in neuroendocrine cells
    • 2+ diffusion near the membrane: implications for secretion in neuroendocrine cells. Biophys J 1997; 72: 674-690.
    • (1997) Biophys J , vol.72 , pp. 674-690
    • Klingauf, J.1    Neher, E.2
  • 81
  • 83
    • 0033198175 scopus 로고    scopus 로고
    • Glutamatergic synaptic responses and long-term potentiation are impaired in the CA1 hippocampal area of calbindin D(28k)-deficient mice
    • Jouvenceau A, Potier B, Battini R, Ferrari S, Dutar P, Billard JM. Glutamatergic synaptic responses and long-term potentiation are impaired in the CA1 hippocampal area of calbindin D(28k)-deficient mice. Synapse 1999; 33: 172-180.
    • (1999) Synapse , vol.33 , pp. 172-180
    • Jouvenceau, A.1    Potier, B.2    Battini, R.3    Ferrari, S.4    Dutar, P.5    Billard, J.M.6
  • 84
    • 0025781309 scopus 로고
    • Postsynaptic and presynaptic effects of the calcium chelator BAPTA on synaptic transmission in rat hippocampal dentate granule neurons
    • Niesen C, Charlton MP, Carlen PL. Postsynaptic and presynaptic effects of the calcium chelator BAPTA on synaptic transmission in rat hippocampal dentate granule neurons. Brain Res 1991; 555: 319-325.
    • (1991) Brain Res , vol.555 , pp. 319-325
    • Niesen, C.1    Charlton, M.P.2    Carlen, P.L.3
  • 86
    • 0029835618 scopus 로고    scopus 로고
    • Determinants of the time course of facilitation at the granule cell to Purkinje cell synapse
    • Atluri PP, Regehr WG. Determinants of the time course of facilitation at the granule cell to Purkinje cell synapse. J Neurosci 1996; 16: 5661-5671.
    • (1996) J Neurosci , vol.16 , pp. 5661-5671
    • Atluri, P.P.1    Regehr, W.G.2
  • 87
    • 0020645428 scopus 로고
    • Interaction between responses in Purkinje cells evoked by climbing fibre impulses and parallel fibre volleys in the cat
    • Campbell NC, Ekerot CF, Hesslow G. Interaction between responses in Purkinje cells evoked by climbing fibre impulses and parallel fibre volleys in the cat. J Physiol (Lond) 1983; 340: 225-238.
    • (1983) J Physiol (Lond) , vol.340 , pp. 225-238
    • Campbell, N.C.1    Ekerot, C.F.2    Hesslow, G.3
  • 88
    • 0026483821 scopus 로고
    • Stellate cell inhibition of Purkinje cells in the turtle cerebellum in vitro
    • Midtgaard J. Stellate cell inhibition of Purkinje cells in the turtle cerebellum in vitro. J Physiol (Lond) 1992; 457: 355-367.
    • (1992) J Physiol (Lond) , vol.457 , pp. 355-367
    • Midtgaard, J.1
  • 89
    • 0029620817 scopus 로고
    • Impaired motor coordination correlates with persistent multiple climbing fiber innervation in PKC gamma mutant mice
    • Chen C, Kano M, Abeliovich A, Chen L, Bao S, Kim JJ, Hashimoto K, Thompson RF, Tonegawa S. Impaired motor coordination correlates with persistent multiple climbing fiber innervation in PKC gamma mutant mice. Cell 1995; 83: 1233-1242.
    • (1995) Cell , vol.83 , pp. 1233-1242
    • Chen, C.1    Kano, M.2    Abeliovich, A.3    Chen, L.4    Bao, S.5    Kim, J.J.6    Hashimoto, K.7    Thompson, R.F.8    Tonegawa, S.9
  • 91
    • 0029942861 scopus 로고    scopus 로고
    • The cerebellum: A neuronal learning machine?
    • Raymond JL, Lisberger SG, Mauk MD. The cerebellum: a neuronal learning machine? Science 1996; 272: 1126-1131.
    • (1996) Science , vol.272 , pp. 1126-1131
    • Raymond, J.L.1    Lisberger, S.G.2    Mauk, M.D.3
  • 92
    • 0028946285 scopus 로고
    • Dynamic organization of motor control within the olivocerebellar system
    • Welsh JP, Lang EJ, Suglhara I, Llinas R. Dynamic organization of motor control within the olivocerebellar system. Nature 1995; 374: 453-157.
    • (1995) Nature , vol.374 , pp. 453-1157
    • Welsh, J.P.1    Lang, E.J.2    Suglhara, I.3    Llinas, R.4
  • 93
    • 0029887817 scopus 로고    scopus 로고
    • Cerebellum implicated in sensory acquisition and discrimination rather than motor control
    • Gao JH, Parsons LM, Bower JM, Xiong J, Li J, Fox PT. Cerebellum implicated in sensory acquisition and discrimination rather than motor control. Science 1996; 272: 545-547.
    • (1996) Science , vol.272 , pp. 545-547
    • Gao, J.H.1    Parsons, L.M.2    Bower, J.M.3    Xiong, J.4    Li, J.5    Fox, P.T.6
  • 94
    • 0027730919 scopus 로고
    • Calcium buffering properties of calbindin D28k and parvalbumin in rat sensory neurones
    • Chard PS, Bleakman D, Christakos S, Fullmer CS, Miller RJ. Calcium buffering properties of calbindin D28k and parvalbumin in rat sensory neurones. J Physiol (Lond) 1993; 472: 341-357.
    • (1993) J Physiol (Lond) , vol.472 , pp. 341-357
    • Chard, P.S.1    Bleakman, D.2    Christakos, S.3    Fullmer, C.S.4    Miller, R.J.5
  • 95
    • 0034214269 scopus 로고    scopus 로고
    • 2+ buffering properties between excitatory and inhibitory hippocampal neurons from the rat
    • 2+ buffering properties between excitatory and inhibitory hippocampal neurons from the rat. J Physiol (Lond) 2000; 525: 405-418.
    • (2000) J Physiol (Lond) , vol.525 , pp. 405-418
    • Lee, S.H.1    Rosenmund, C.2    Schwaller, B.3    Neher, E.4
  • 96
    • 0020392253 scopus 로고
    • Correlation of parvalbumin concentration with relaxation speed in mammalian muscles
    • Heizmann CW, Berchtold MW, Rowlerson AM. Correlation of parvalbumin concentration with relaxation speed in mammalian muscles. Proc Natl Acad Sci USA 1982; 79: 7243-7247.
    • (1982) Proc Natl Acad Sci USA , vol.79 , pp. 7243-7247
    • Heizmann, C.W.1    Berchtold, M.W.2    Rowlerson, A.M.3
  • 100
    • 0029904130 scopus 로고    scopus 로고
    • Single-domain/bound calcium hypothesis of transmitter release and facilitation
    • Bertram R, Sherman A, Stanley EF. Single-domain/bound calcium hypothesis of transmitter release and facilitation. J Neurophysiol 1996; 75: 1919-1931.
    • (1996) J Neurophysiol , vol.75 , pp. 1919-1931
    • Bertram, R.1    Sherman, A.2    Stanley, E.F.3
  • 101
    • 0028171906 scopus 로고
    • 2+ and short-term synaptic plasticity
    • 2+ and short-term synaptic plasticity. Nature 1994; 371: 603-606.
    • (1994) Nature , vol.371 , pp. 603-606
    • Karniya, H.1    Zucker, R.S.2
  • 102
    • 0034652279 scopus 로고    scopus 로고
    • Interplay between facilitation, depression, and residual calcium at three presynaptic terminals
    • Dittman JS, Kreitzer AC, Regehr WG. Interplay between facilitation, depression, and residual calcium at three presynaptic terminals. J Neurosci 2000; 20: 1374-1385.
    • (2000) J Neurosci , vol.20 , pp. 1374-1385
    • Dittman, J.S.1    Kreitzer, A.C.2    Regehr, W.G.3
  • 103
    • 0032435180 scopus 로고    scopus 로고
    • 2+ signals
    • 2+ signals. Cell Calcium 1998; 24: 345-357.
    • (1998) Cell Calcium , vol.24 , pp. 345-357
    • Neher, E.1
  • 104
    • 0032008553 scopus 로고    scopus 로고
    • 2+ microdomains: New tools for understanding their roles in neurotransmitter release
    • 2+ microdomains: new tools for understanding their roles in neurotransmitter release. Neuron 1998; 20: 389-399.
    • (1998) Neuron , vol.20 , pp. 389-399
    • Neher, E.1
  • 106
    • 0027237532 scopus 로고
    • Correlation of physiological subgroupings of nonpyramidal cells with parvalbumin- and calbindinD28k-immunoreactive neurons in layer V of rat frontal cortex
    • Kawaguchi Y, Kubota Y. Correlation of physiological subgroupings of nonpyramidal cells with parvalbumin- and calbindinD28k-immunoreactive neurons in layer V of rat frontal cortex. J Neurophysiol 1993; 70: 387-396.
    • (1993) J Neurophysiol , vol.70 , pp. 387-396
    • Kawaguchi, Y.1    Kubota, Y.2
  • 107
    • 0027535780 scopus 로고
    • Groupings of nonpyramidal and pyramidal cells with specific physiological and morphological characteristics
    • Kawaguchi Y. Groupings of nonpyramidal and pyramidal cells with specific physiological and morphological characteristics. J Neurophysiol 1993; 69: 416-431.
    • (1993) J Neurophysiol , vol.69 , pp. 416-431
    • Kawaguchi, Y.1
  • 108
    • 0013873739 scopus 로고
    • The inhibitory interneurones within the cerebellar cortex
    • Eccles JC, Llinas R, Sasaki K. The inhibitory interneurones within the cerebellar cortex. Exp Brain Res 1966; 1: 1-16.
    • (1966) Exp Brain Res , vol.1 , pp. 1-16
    • Eccles, J.C.1    Llinas, R.2    Sasaki, K.3
  • 110
    • 0033915583 scopus 로고    scopus 로고
    • Calretinin modifies presynaptic calcium signaling in frog saccular hair cells
    • Edmonds B, Reyes R, Schwaller B, Roberts WM. Calretinin modifies presynaptic calcium signaling in frog saccular hair cells. Nat Neurosci 2000; 3: 786-790.
    • (2000) Nat Neurosci , vol.3 , pp. 786-790
    • Edmonds, B.1    Reyes, R.2    Schwaller, B.3    Roberts, W.M.4
  • 111
    • 0024473444 scopus 로고
    • Dendritic spines of rat cerebellar Purkinje cells: Serial electron microscopy with reference to their biophysical characteristics
    • Harris KM, Stevens JK. Dendritic spines of rat cerebellar Purkinje cells: serial electron microscopy with reference to their biophysical characteristics. J Neurosci 1988; 9: 2982-2997.
    • (1988) J Neurosci , vol.9 , pp. 2982-2997
    • Harris, K.M.1    Stevens, J.K.2
  • 112
    • 0032742098 scopus 로고    scopus 로고
    • Release of calcium from stores alters the morphology of dendritic spines in cultured hippocampal neurons
    • Korkotian E, Segal M. Release of calcium from stores alters the morphology of dendritic spines in cultured hippocampal neurons. Proc Natl Acad Sci USA 1999; 96: 12068-12072.
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 12068-12072
    • Korkotian, E.1    Segal, M.2
  • 113
    • 0032797839 scopus 로고    scopus 로고
    • Geometry of dendritic spines affects calcium dynamics in hippocampal neurons: Theory and experiments
    • Volfovsky N, Parnas H, Segal M, Korkotian E. Geometry of dendritic spines affects calcium dynamics in hippocampal neurons: theory and experiments. J Neurophysiol 1999; 82: 450-462.
    • (1999) J Neurophysiol , vol.82 , pp. 450-462
    • Volfovsky, N.1    Parnas, H.2    Segal, M.3    Korkotian, E.4
  • 114
    • 0034668918 scopus 로고    scopus 로고
    • Regulation of spine calcium dynamics by rapid spine motility
    • Majewska A, Tashiro A, Yuste R. Regulation of spine calcium dynamics by rapid spine motility. J Neurosci 2000; 20: 8262-8268.
    • (2000) J Neurosci , vol.20 , pp. 8262-8268
    • Majewska, A.1    Tashiro, A.2    Yuste, R.3
  • 115
    • 17144433225 scopus 로고    scopus 로고
    • Deficiency in the relaxation factor parvalbumin increases the fatigue-resistance in fast-twitch muscle, upregulates mitochondria, and increases vascularisation
    • Chen G, Carroll S, Racay P, Dick J, Pette D, Traub I, Vrbova G, Eggli P, Celio MR, Schwaller B. Deficiency in the relaxation factor parvalbumin increases the fatigue-resistance in fast-twitch muscle, upregulates mitochondria, and increases vascularisation. Am J Physiol (Cell Physiol) 2001; 281: C114-C122.
    • (2001) Am J Physiol (Cell Physiol) , vol.281
    • Chen, G.1    Carroll, S.2    Racay, P.3    Dick, J.4    Pette, D.5    Traub, I.6    Vrbova, G.7    Eggli, P.8    Celio, M.R.9    Schwaller, B.10
  • 116
    • 0030816143 scopus 로고    scopus 로고
    • Inhibition of mitochondrial calcium uptake slows down relaxation in mitochondria-rich skeletal muscles
    • Gillis JM. Inhibition of mitochondrial calcium uptake slows down relaxation in mitochondria-rich skeletal muscles. J Muscle Res Cell Motil 1997; 18: 473-483.
    • (1997) J Muscle Res Cell Motil , vol.18 , pp. 473-483
    • Gillis, J.M.1
  • 117
    • 2642712492 scopus 로고    scopus 로고
    • Calcium-dependent inactivation of high-threshold calcium currents in human dentate gyrus granule cells
    • Nägerl UV, Mody I. Calcium-dependent inactivation of high-threshold calcium currents in human dentate gyrus granule cells. J Physiol (Lond) 1998; 509: 39-45.
    • (1998) J Physiol (Lond) , vol.509 , pp. 39-45
    • Nägerl, U.V.1    Mody, I.2
  • 119
    • 0025681742 scopus 로고
    • Relationship of neuronal vulnerability and calcium binding protein immunoreactivity in ischemia
    • Freund TF, Buzsaki G, Leon A, Baimbridge KG, Somogyi P. Relationship of neuronal vulnerability and calcium binding protein immunoreactivity in ischemia. Exp Brain Res 1990; 83: 55-66.
    • (1990) Exp Brain Res , vol.83 , pp. 55-66
    • Freund, T.F.1    Buzsaki, G.2    Leon, A.3    Baimbridge, K.G.4    Somogyi, P.5
  • 120
    • 0026536514 scopus 로고
    • Pattern of neuronal death in the rat hippocampus after status epilepticus. Relationship to calcium binding protein content and ischemic vulnerability
    • Freund TF, Ylinen A, Miettinen R, Pitkanen A, Lahtinen H, Baimbridge KG, Riekkinen PJ. Pattern of neuronal death in the rat hippocampus after status epilepticus. Relationship to calcium binding protein content and ischemic vulnerability. Brain Res Bull 1992; 28: 27-38.
    • (1992) Brain Res Bull , vol.28 , pp. 27-38
    • Freund, T.F.1    Ylinen, A.2    Miettinen, R.3    Pitkanen, A.4    Lahtinen, H.5    Baimbridge, K.G.6    Riekkinen, P.J.7
  • 121
    • 0028275114 scopus 로고
    • Poor correlation between delayed neuronal death induced by transient forebrain ischemia, and immunoreactivity for parvalbumin and calbindin D-28k in developing gerbil hippocampus
    • Tortosa A, Ferrer I. Poor correlation between delayed neuronal death induced by transient forebrain ischemia, and immunoreactivity for parvalbumin and calbindin D-28k in developing gerbil hippocampus. Acta Neuropathol 1994; 88: 67-74.
    • (1994) Acta Neuropathol , vol.88 , pp. 67-74
    • Tortosa, A.1    Ferrer, I.2
  • 122
    • 0019793207 scopus 로고
    • Regional neurone damage after cerebral ischaemia in the normo- and hypoglycaemic rat
    • Diemer NH, Siemkowicz E. Regional neurone damage after cerebral ischaemia in the normo- and hypoglycaemic rat. Neuropathol Appl Neurobiol 1981; 7: 217-227.
    • (1981) Neuropathol Appl Neurobiol , vol.7 , pp. 217-227
    • Diemer, N.H.1    Siemkowicz, E.2
  • 123
    • 0034044955 scopus 로고    scopus 로고
    • Neurodegenerative and morphogenic changes in a mouse model of temporal lobe epilepsy do not depend on the expression of the calcium-binding proteins parvalbumin, calbindin, or calretinin
    • Bouilleret V, Schwaller B, Schurmans S, Celio MR, Fritschy JM. Neurodegenerative and morphogenic changes in a mouse model of temporal lobe epilepsy do not depend on the expression of the calcium-binding proteins parvalbumin, calbindin, or calretinin. Neuroscience 2000; 97: 47-58.
    • (2000) Neuroscience , vol.97 , pp. 47-58
    • Bouilleret, V.1    Schwaller, B.2    Schurmans, S.3    Celio, M.R.4    Fritschy, J.M.5
  • 124
    • 0034711544 scopus 로고    scopus 로고
    • Seizure-induced neuronal death is associated with induction of c-Jun N-terminal kinase and is dependent on genetic background
    • Schauwecker PE. Seizure-induced neuronal death is associated with induction of c-Jun N-terminal kinase and is dependent on genetic background. Brain Res 2000; 884: 116-128.
    • (2000) Brain Res , vol.884 , pp. 116-128
    • Schauwecker, P.E.1
  • 125
    • 0030887853 scopus 로고    scopus 로고
    • Genetic determinants of susceptibility to excitotoxic cell death: Implications for gene targeting approaches
    • Schauwecker PE, Steward O. Genetic determinants of susceptibility to excitotoxic cell death: implications for gene targeting approaches. Proc Natl Acad Sci USA 1997; 94: 4103-4108.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 4103-4108
    • Schauwecker, P.E.1    Steward, O.2
  • 127
    • 0035800644 scopus 로고    scopus 로고
    • Calretinin and calbindin D-28k delay the onset of cell death after excitotoxic stimulation in transfected P19 cells
    • D'Orlando C, Fellay B, Schwaller B, Salicio V, Bloc A, Gotzos V, Celio MR. Calretinin and calbindin D-28k delay the onset of cell death after excitotoxic stimulation in transfected P19 cells. Brain Res 2001; 909: 145-158.
    • (2001) Brain Res , vol.909 , pp. 145-158
    • D'Orlando, C.1    Fellay, B.2    Schwaller, B.3    Salicio, V.4    Bloc, A.5    Gotzos, V.6    Celio, M.R.7
  • 128
    • 0029665882 scopus 로고    scopus 로고
    • Expression of calbindin-D28k in motoneuron hybrid cells after retroviral infection with calbindin-D28k cDNA prevents amyotrophic lateral sclerosis IgG-mediated cytotoxicity
    • Ho BK, Alexianu ME, Colom LV, Mohamed AH, Serrano F, Appel SH. Expression of calbindin-D28k in motoneuron hybrid cells after retroviral infection with calbindin-D28k cDNA prevents amyotrophic lateral sclerosis IgG-mediated cytotoxicity. Proc Natl Acad Sci USA 1996; 93: 6796-6801.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 6796-6801
    • Ho, B.K.1    Alexianu, M.E.2    Colom, L.V.3    Mohamed, A.H.4    Serrano, F.5    Appel, S.H.6
  • 129
    • 0028292347 scopus 로고
    • Mapping of the colocalization of calretinin and tyrosine hydroxylase in the rat substantia nigra and ventral tegmental area
    • Isaacs K, Jacobowitz D. Mapping of the colocalization of calretinin and tyrosine hydroxylase in the rat substantia nigra and ventral tegmental area. Exp Brain Res 1994; 99: 34-42.
    • (1994) Exp Brain Res , vol.99 , pp. 34-42
    • Isaacs, K.1    Jacobowitz, D.2
  • 130
    • 0028198969 scopus 로고
    • Vulnerability to excitotoxic stimuli of cultured rat hippocampal neurons containing the calcium-binding proteins calretinin and calbindin D28k
    • Möckel V, Fischer G. Vulnerability to excitotoxic stimuli of cultured rat hippocampal neurons containing the calcium-binding proteins calretinin and calbindin D28k. Brain Res 1994; 648: 109-120.
    • (1994) Brain Res , vol.648 , pp. 109-120
    • Möckel, V.1    Fischer, G.2
  • 131
    • 0028814951 scopus 로고
    • Calretinin-immunoreactivity neurons are resistant to B-amyloid toxicity in vitro
    • Pike CJ, Cotman CW. Calretinin-immunoreactivity neurons are resistant to B-amyloid toxicity in vitro. Brain Res 1995; 671: 293-298.
    • (1995) Brain Res , vol.671 , pp. 293-298
    • Pike, C.J.1    Cotman, C.W.2
  • 132
    • 0029942572 scopus 로고    scopus 로고
    • Neuroprotective properties of calretinin against the HIV-1 gp120 toxicity
    • Diop AG, Dussartre C, Barthe D, Hugon J. Neuroprotective properties of calretinin against the HIV-1 gp120 toxicity. Neurosci Res Commun 1996; 18: 107-114.
    • (1996) Neurosci Res Commun , vol.18 , pp. 107-114
    • Diop, A.G.1    Dussartre, C.2    Barthe, D.3    Hugon, J.4
  • 135
    • 0029839623 scopus 로고    scopus 로고
    • Striatal interneurons in Huntington's disease: Selective increase in the density of calretinin-immunoreactive medium-sized neurons
    • Cicchetti F, Parent A. Striatal interneurons in Huntington's disease: selective increase in the density of calretinin-immunoreactive medium-sized neurons. Mov Disord 1996; 11: 619-626.
    • (1996) Mov Disord , vol.11 , pp. 619-626
    • Cicchetti, F.1    Parent, A.2
  • 136
    • 0027231535 scopus 로고
    • Calretinin-immunoreactive neocortical interneurons are unaffected in Alzheimer's disease
    • Hof PR, Nimchinsky EA, Celio MR, Bouras C, Morrison JH. Calretinin-immunoreactive neocortical interneurons are unaffected in Alzheimer's disease. Neurosci Lett 1993; 152: 145-148.
    • (1993) Neurosci Lett , vol.152 , pp. 145-148
    • Hof, P.R.1    Nimchinsky, E.A.2    Celio, M.R.3    Bouras, C.4    Morrison, J.H.5
  • 137
    • 0028583129 scopus 로고
    • Does the calcium binding protein calretinin protect dopaminergic neurons against degeneration in Parkinson's disease?
    • Mouatt-Prigent A, Agid Y, Hirsch EC. Does the calcium binding protein calretinin protect dopaminergic neurons against degeneration in Parkinson's disease? Brain Res 1994; 668: 62-70.
    • (1994) Brain Res , vol.668 , pp. 62-70
    • Mouatt-Prigent, A.1    Agid, Y.2    Hirsch, E.C.3
  • 138
    • 0031149760 scopus 로고    scopus 로고
    • The cellular basis for the relative resistance of parvalbumin and calretinin immunoreactive neocortical neurons to the pathology of Alzheimer's disease
    • Sampson VL, Morrison JH, Vickers JC. The cellular basis for the relative resistance of parvalbumin and calretinin immunoreactive neocortical neurons to the pathology of Alzheimer's disease. Exp Neurol 1997; 145: 295-302.
    • (1997) Exp Neurol , vol.145 , pp. 295-302
    • Sampson, V.L.1    Morrison, J.H.2    Vickers, J.C.3
  • 139
    • 0029897105 scopus 로고    scopus 로고
    • Inhibition of the proliferative cycle and apoptotic events in WiDr cells after down-regulation of the calcium-binding protein calretinin using antisense oligodeoxynucleotides
    • Gander JC, Gotzos V, Fellay B, Schwaller B. Inhibition of the proliferative cycle and apoptotic events in WiDr cells after down-regulation of the calcium-binding protein calretinin using antisense oligodeoxynucleotides. Exp Cell Res 1996; 225: 399-410.
    • (1996) Exp Cell Res , vol.225 , pp. 399-410
    • Gander, J.C.1    Gotzos, V.2    Fellay, B.3    Schwaller, B.4
  • 141
    • 0030056030 scopus 로고    scopus 로고
    • Decreased parvalbumin immunoreactivity in surviving Purkinje cells of patients with spinocerebellar ataxia-1
    • Vig PJ, Fratkin JD, Desaiah D, Currier RD, Subramony SH. Decreased parvalbumin immunoreactivity in surviving Purkinje cells of patients with spinocerebellar ataxia-1. Neurology 1996; 47: 249-253.
    • (1996) Neurology , vol.47 , pp. 249-253
    • Vig, P.J.1    Fratkin, J.D.2    Desaiah, D.3    Currier, R.D.4    Subramony, S.H.5
  • 142
    • 0031883824 scopus 로고    scopus 로고
    • Reduced immunoreactivity to calcium-binding proteins in Purkinje cells precedes onset of ataxia in spinocerebellar ataxia-1 transgenic mice
    • Vig PJ, Subramony SH, Burright EN, Fratkin JD, McDaniel DO, Desaiah D, Qin Z. Reduced immunoreactivity to calcium-binding proteins in Purkinje cells precedes onset of ataxia in spinocerebellar ataxia-1 transgenic mice. Neurology 1998; 50: 106-113.
    • (1998) Neurology , vol.50 , pp. 106-113
    • Vig, P.J.1    Subramony, S.H.2    Burright, E.N.3    Fratkin, J.D.4    McDaniel, D.O.5    Desaiah, D.6    Qin, Z.7
  • 143
    • 0034653926 scopus 로고    scopus 로고
    • Relationship between ataxin-1 nuclear inclusions and Purkinje cell specific proteins in SCA-1 transgenic mice
    • Vig PJ, Subramony SH, Qin Z, McDaniel DO, Fratkin JD. Relationship between ataxin-1 nuclear inclusions and Purkinje cell specific proteins in SCA-1 transgenic mice. J Neurol Sci 2000; 174: 100-110.
    • (2000) J Neurol Sci , vol.174 , pp. 100-110
    • Vig, P.J.1    Subramony, S.H.2    Qin, Z.3    McDaniel, D.O.4    Fratkin, J.D.5
  • 144
    • 0033360170 scopus 로고    scopus 로고
    • Spread of dendritic excitation in layer 2/3 pyramidal neurons in rat barrel cortex in vivo
    • Svoboda K, Helmchen F, Denk W, Tank DW. Spread of dendritic excitation in layer 2/3 pyramidal neurons in rat barrel cortex in vivo. Nat Neurosci 1999; 2: 65-73.
    • (1999) Nat Neurosci , vol.2 , pp. 65-73
    • Svoboda, K.1    Helmchen, F.2    Denk, W.3    Tank, D.W.4
  • 145
    • 0035959949 scopus 로고    scopus 로고
    • A miniature head-mounted two-photon microscope, high-resolution brain imaging in freely moving animals
    • Helmchen F, Fee MS, Tank DW, Denk W. A miniature head-mounted two-photon microscope, high-resolution brain imaging in freely moving animals. Neuron 2001; 31: 903-912.
    • (2001) Neuron , vol.31 , pp. 903-912
    • Helmchen, F.1    Fee, M.S.2    Tank, D.W.3    Denk, W.4
  • 147
    • 0028221324 scopus 로고
    • Calcium and magnesium binding to rat parvalbumin
    • Eberhard M, Erne P. Calcium and magnesium binding to rat parvalbumin. Eur J Biochem 1994; 222: 21-26.
    • (1994) Eur J Biochem , vol.222 , pp. 21-26
    • Eberhard, M.1    Erne, P.2
  • 149
    • 0031105139 scopus 로고    scopus 로고
    • Chick calretinin: Purification, composition, and metal binding activity of native and recombinant forms
    • Stevens J, Rogers JH. Chick calretinin: purification, composition, and metal binding activity of native and recombinant forms. Protein Expr Purif 1997; 9: 171-181.
    • (1997) Protein Expr Purif , vol.9 , pp. 171-181
    • Stevens, J.1    Rogers, J.H.2
  • 150
    • 0031465835 scopus 로고    scopus 로고
    • 2+ chelators incorporated non-disruptively into intact human red cells
    • 2+ chelators incorporated non-disruptively into intact human red cells. J Physiol (Lond) 1997; 505: 403-410.
    • (1997) J Physiol (Lond) , vol.505 , pp. 403-410
    • Tiffert, T.1    Lew, V.L.2


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