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Volumn 138, Issue 2, 2011, Pages 211-229

D4cpv-calsequestrin: A sensitive ratiometric biosensor accurately targeted to the calcium store of skeletal muscle

Author keywords

[No Author keywords available]

Indexed keywords

CALCIUM; CALSEQUESTRIN; LIGAND;

EID: 79961104191     PISSN: 00221295     EISSN: 15407748     Source Type: Journal    
DOI: 10.1085/jgp.201010591     Document Type: Article
Times cited : (30)

References (49)
  • 1
    • 26444575860 scopus 로고    scopus 로고
    • Retrotranslocation of the chaperone calreticulin from the endoplasmic reticulum lumen to the cytosol
    • doi:10.1128/MCB.25.20.8844-8853.2005
    • Afshar, N., B.E. Black, and B.M. Paschal. 2005. Retrotranslocation of the chaperone calreticulin from the endoplasmic reticulum lumen to the cytosol. Mol. Cell. Biol. 25:8844-8853. doi:10.1128/MCB.25.20.8844-8853.2005.
    • (2005) Mol. Cell. Biol. , vol.25 , pp. 8844-8853
    • Afshar, N.1    Black, B.E.2    Paschal, B.M.3
  • 2
    • 0024537756 scopus 로고
    • Fluorescence microscopy in three dimensions
    • doi:10.1016/S0091-679X(08)60986-3
    • Agard, D.A., Y. Hiraoka, P. Shaw, and J.W. Sedat. 1989. Fluorescence microscopy in three dimensions. Methods Cell Biol. 30:353-377. doi:10.1016/S0091-679X(08)60986-3.
    • (1989) Methods Cell Biol , vol.30 , pp. 353-377
    • Agard, D.A.1    Hiraoka, Y.2    Shaw, P.3    Sedat, J.W.4
  • 4
    • 0041353449 scopus 로고    scopus 로고
    • Sarcoplasmic reticulum calcium release compared in slow-twitch and fast-twitch fibres of mouse muscle
    • doi:10.1113/jphysiol .2003.041608
    • Baylor, S.M., and S. Hollingworth. 2003. Sarcoplasmic reticulum calcium release compared in slow-twitch and fast-twitch fibres of mouse muscle. J. Physiol. 551:125-138. doi:10.1113/jphysiol .2003.041608.
    • (2003) J. Physiol. , vol.551 , pp. 125-138
    • Baylor, S.M.1    Hollingworth, S.2
  • 6
    • 69549105810 scopus 로고    scopus 로고
    • Different fibre populations distinguished by their calcium transient characteristics in enzymatically dissociated murine flexor digitorum brevis and soleus muscles
    • doi:10.1007/s10974-009-9181-1
    • Calderón, J.C., P. Bolaños, S.H. Torres, G. Rodríguez-Arroyo, and C. Caputo. 2009. Different fibre populations distinguished by their calcium transient characteristics in enzymatically dissociated murine flexor digitorum brevis and soleus muscles. J. Muscle Res. Cell Motil. 30:125-137. doi:10.1007/s10974-009-9181-1.
    • (2009) J. Muscle Res. Cell Motil. , vol.30 , pp. 125-137
    • Calderón, J.C.1    Bolaños, P.2    Torres, S.H.3    Rodríguez-Arroyo, G.4    Caputo, C.5
  • 7
    • 78650673284 scopus 로고    scopus 로고
    • Massive alterations of sarcoplasmic reticulum free calcium in skeletal muscle fibers lacking calsequestrin revealed by a genetically encoded probe
    • doi:10.1073/pnas.1009168108
    • Canato, M., M. Scorzeto, M. Giacomello, F. Protasi, C. Reggiani, and G.J. Stienen. 2010. Massive alterations of sarcoplasmic reticulum free calcium in skeletal muscle fibers lacking calsequestrin revealed by a genetically encoded probe. Proc. Natl. Acad. Sci. USA. 107:22326-22331. doi:10.1073/pnas.1009168108.
    • (2010) Proc. Natl. Acad. Sci. USA , vol.107 , pp. 22326-22331
    • Canato, M.1    Scorzeto, M.2    Giacomello, M.3    Protasi, F.4    Reggiani, C.5    Stienen, G.J.6
  • 8
    • 0029665074 scopus 로고    scopus 로고
    • 2+ in sarcoplasmic reticulum in perfused rabbit heart loaded with 1,2-bis(2-amino-5,6- difluorophenoxy)ethane-N,N,N',N'-tetraacetic acid by 19F NMR
    • doi:10.1074/jbc.271.13.7398
    • 2+ in sarcoplasmic reticulum in perfused rabbit heart loaded with 1,2-bis(2-amino-5,6- difluorophenoxy)ethane-N,N,N',N'-tetraacetic acid by 19F NMR. J. Biol. Chem. 271:7398-7403. doi:10.1074/jbc.271.13.7398.
    • (1996) J. Biol. Chem. , vol.271 , pp. 7398-7403
    • Chen, W.1    Steenbergen, C.2    Levy, L.A.3    Vance, J.4    London, R.E.5    Murphy, E.6
  • 9
    • 0028240392 scopus 로고
    • Novel functions for calreticulin: interaction with integrins and modulation of gene expression?
    • doi:10.1016/0968-0004(94)90001-9
    • Dedhar, S. 1994. Novel functions for calreticulin: interaction with integrins and modulation of gene expression? Trends Biochem. Sci. 19:269-271. doi:10.1016/0968-0004(94)90001-9.
    • (1994) Trends Biochem. Sci. , vol.19 , pp. 269-271
    • Dedhar, S.1
  • 11
    • 0038758748 scopus 로고    scopus 로고
    • Measurements of the free luminal ER Ca(2+) concentration with targeted "cameleon" fluorescent proteins
    • doi:10.1016/ S0143-4160(03)00081-2
    • Demaurex, N., and M. Frieden. 2003. Measurements of the free luminal ER Ca(2+) concentration with targeted "cameleon" fluorescent proteins. Cell Calcium. 34:109-119. doi:10.1016/ S0143-4160(03)00081-2.
    • (2003) Cell Calcium , vol.34 , pp. 109-119
    • Demaurex, N.1    Frieden, M.2
  • 12
    • 33646090608 scopus 로고    scopus 로고
    • Quantitative evaluation of mammalian skeletal muscle as a heterologous protein expression system
    • doi:10.1016/j.pep.2005.10.018
    • DiFranco, M., P. Neco, J. Capote, P. Meera, and J.L. Vergara. 2006. Quantitative evaluation of mammalian skeletal muscle as a heterologous protein expression system. Protein Expr. Purif. 47:281-288. doi:10.1016/j.pep.2005.10.018.
    • (2006) Protein Expr. Purif. , vol.47 , pp. 281-288
    • DiFranco, M.1    Neco, P.2    Capote, J.3    Meera, P.4    Vergara, J.L.5
  • 13
    • 0029974228 scopus 로고    scopus 로고
    • Total and sarcoplasmic reticulum calcium contents of skinned fibres from rat skeletal muscle
    • Fryer, M.W., and D.G. Stephenson. 1996. Total and sarcoplasmic reticulum calcium contents of skinned fibres from rat skeletal muscle. J. Physiol. 493:357-370.
    • (1996) J. Physiol. , vol.493 , pp. 357-370
    • Fryer, M.W.1    Stephenson, D.G.2
  • 14
    • 0030999715 scopus 로고    scopus 로고
    • Spatially and functionally distinct Ca2+ stores in sarcoplasmic and endoplasmic reticulum
    • doi:10.1126/science.275.5306.1643
    • Golovina, V.A., and M.P. Blaustein. 1997. Spatially and functionally distinct Ca2+ stores in sarcoplasmic and endoplasmic reticulum. Science. 275:1643-1648. doi:10.1126/science.275.5306.1643.
    • (1997) Science , vol.275 , pp. 1643-1648
    • Golovina, V.A.1    Blaustein, M.P.2
  • 15
    • 18244417721 scopus 로고    scopus 로고
    • Insulin-like growth factor-1 prevents age-related decrease in specific force and intracellular Ca2+ in single intact muscle fibres from transgenic mice
    • doi:10.1113/jphysiol.2003.048165
    • Gonzalez, E., M.L. Messi, Z. Zheng, and O. Delbono. 2003. Insulin-like growth factor-1 prevents age-related decrease in specific force and intracellular Ca2+ in single intact muscle fibres from transgenic mice. J. Physiol. 552:833-844. doi:10.1113/jphysiol.2003.048165.
    • (2003) J. Physiol , vol.552 , pp. 833-844
    • Gonzalez, E.1    Messi, M.L.2    Zheng, Z.3    Delbono, O.4
  • 16
    • 0031956092 scopus 로고    scopus 로고
    • Quantitative fluorescence resonance energy transfer measurements using fluorescence microscopy
    • doi:10 .1016/S0006-3495(98)77976-7
    • Gordon, G.W., G. Berry, X.H. Liang, B. Levine, and B. Herman. 1998. Quantitative fluorescence resonance energy transfer measurements using fluorescence microscopy. Biophys. J. 74:2702-2713. doi:10 .1016/S0006-3495(98)77976-7.
    • (1998) Biophys. J , vol.74 , pp. 2702-2713
    • Gordon, G.W.1    Berry, G.2    Liang, X.H.3    Levine, B.4    Herman, B.5
  • 18
    • 0028212476 scopus 로고
    • Teaching active transport at the turn of the twenty- first century: recent discoveries and conceptual changes
    • doi:10.1016/S0006-3495(94)80872-0
    • Inesi, G. 1994. Teaching active transport at the turn of the twenty- first century: recent discoveries and conceptual changes. Biophys. J. 66:554-560. doi:10.1016/S0006-3495(94)80872-0.
    • (1994) Biophys. J. , vol.66 , pp. 554-560
    • Inesi, G.1
  • 19
    • 77950922844 scopus 로고    scopus 로고
    • 2+ depletion in adult skeletal muscle fibres measured with the biosensor D1ER
    • doi:10.1007/s00424-009-0778-4
    • 2+ depletion in adult skeletal muscle fibres measured with the biosensor D1ER. Pflugers Arch. 459:725-735. doi:10.1007/s00424-009-0778-4.
    • (2010) Pflugers Arch , vol.459 , pp. 725-735
    • Jiménez-Moreno, R.1    Wang, Z.M.2    Messi, M.L.3    Delbono, O.4
  • 20
    • 0027249749 scopus 로고
    • Reduction of calcium inactivation of sarcoplasmic reticulum calcium release by fura-2 in voltage-clamped cut twitch fibers from frog muscle
    • doi:10.1085/jgp.102.2.333
    • Jong, D.S., P.C. Pape, W.K. Chandler, and S.M. Baylor. 1993. Reduction of calcium inactivation of sarcoplasmic reticulum calcium release by fura-2 in voltage-clamped cut twitch fibers from frog muscle. J. Gen. Physiol. 102:333-370. doi:10.1085/jgp.102.2.333.
    • (1993) J. Gen. Physiol. , vol.102 , pp. 333-370
    • Jong, D.S.1    Pape, P.C.2    Chandler, W.K.3    Baylor, S.M.4
  • 21
    • 0035384875 scopus 로고    scopus 로고
    • The use of the indicator fluo-5N to measure sarcoplasmic reticulum calcium in single muscle fibres of the cane toad
    • doi:10.1111/j.1469-7793.2001.00087.x
    • Kabbara, A.A., and D.G. Allen. 2001. The use of the indicator fluo-5N to measure sarcoplasmic reticulum calcium in single muscle fibres of the cane toad. J. Physiol. 534:87-97. doi:10.1111/j.1469- 7793.2001.00087.x.
    • (2001) J. Physiol. , vol.534 , pp. 87-97
    • Kabbara, A.A.1    Allen, D.G.2
  • 22
    • 0141919841 scopus 로고    scopus 로고
    • Unitary Ca2+ current through mammalian cardiac and amphibian skeletal muscle ryanodine receptor Channels under near-physiological ionic conditions
    • doi:10.1085/jgp .200308843
    • Kettlun, C., A. González, E. Ríos, and M. Fill. 2003. Unitary Ca2+ current through mammalian cardiac and amphibian skeletal muscle ryanodine receptor Channels under near-physiological ionic conditions. J. Gen. Physiol. 122:407-417. doi:10.1085/jgp .200308843.
    • (2003) J. Gen. Physiol. , vol.122 , pp. 407-417
    • Kettlun, C.1    González, A.2    Ríos, E.3    Fill, M.4
  • 23
    • 24944581712 scopus 로고    scopus 로고
    • Confocal imaging of [Ca2+] in cellular organelles by SEER, shifted excitation and emission ratioing of fluorescence
    • doi:10.1113/jphysiol.2005.087973
    • Launikonis, B.S., J. Zhou, L. Royer, T.R. Shannon, G. Brum, and E. Ríos. 2005. Confocal imaging of [Ca2+] in cellular organelles by SEER, shifted excitation and emission ratioing of fluorescence. J. Physiol. 567:523-543. doi:10.1113/jphysiol.2005.087973.
    • (2005) J. Physiol. , vol.567 , pp. 523-543
    • Launikonis, B.S.1    Zhou, J.2    Royer, L.3    Shannon, T.R.4    Brum, G.5    Ríos, E.6
  • 24
    • 33644557363 scopus 로고    scopus 로고
    • Depletion "skraps" and dynamic buffering inside the cellular calcium store
    • doi:10.1073/pnas.0511252103
    • Launikonis, B.S., J. Zhou, L. Royer, T.R. Shannon, G. Brum, and E. Ríos. 2006. Depletion "skraps" and dynamic buffering inside the cellular calcium store. Proc. Natl. Acad. Sci. USA. 103:2982-2987. doi:10.1073/pnas.0511252103.
    • (2006) Proc. Natl. Acad. Sci. USA. , vol.103 , pp. 2982-2987
    • Launikonis, B.S.1    Zhou, J.2    Royer, L.3    Shannon, T.R.4    Brum, G.5    Ríos, E.6
  • 25
    • 0032589749 scopus 로고    scopus 로고
    • Unitary Ca2+ current through cardiac ryanodine receptor channels under quasi-physiological ionic conditions
    • doi:10.1085/jgp.113.2.177
    • Mejía-Alvarez, R., C. Kettlun, E. Ríos, M. Stern, and M. Fill. 1999. Unitary Ca2+ current through cardiac ryanodine receptor channels under quasi-physiological ionic conditions. J. Gen. Physiol. 113:177-186. doi:10.1085/jgp.113.2.177.
    • (1999) J. Gen. Physiol. , vol.113 , pp. 177-186
    • Mejía-Alvarez, R.1    Kettlun, C.2    Ríos, E.3    Stern, M.4    Fill, M.5
  • 26
    • 0027364752 scopus 로고
    • Three-dimensional visualization of multi-channel volume data: the amSFP algorithm
    • doi:10.1002/cyto.990140705
    • Messerli, J.M., H.T. van der Voort, E. Rungger-Brändle, and J.C. Perriard. 1993. Three-dimensional visualization of multi-channel volume data: the amSFP algorithm. Cytometry. 14:725-735. doi:10.1002/cyto.990140705.
    • (1993) Cytometry , vol.14 , pp. 725-735
    • Messerli, J.M.1    van der Voort, H.T.2    Rungger-Brändle, E.3    Perriard, J.C.4
  • 27
    • 0030610646 scopus 로고    scopus 로고
    • Fluorescent indicators for Ca2+ based on green fluorescent proteins and calmodulin
    • doi:10.1038/42264
    • Miyawaki, A., J. Llopis, R. Heim, J.M. McCaffery, J.A. Adams, M. Ikura, and R.Y. Tsien. 1997. Fluorescent indicators for Ca2+ based on green fluorescent proteins and calmodulin. Nature. 388:882-887. doi:10.1038/42264.
    • (1997) Nature , vol.388 , pp. 882-887
    • Miyawaki, A.1    Llopis, J.2    Heim, R.3    McCaffery, J.M.4    Adams, J.A.5    Ikura, M.6    Tsien, R.Y.7
  • 28
    • 58349090860 scopus 로고    scopus 로고
    • Calsequestrin content and SERCA determine normal and maximal Ca2+ storage levels in sarcoplasmic reticulum of fast- and slow-twitch fibres of rat
    • doi:10.1113/jphysiol.2008.163162
    • Murphy, R.M., N.T. Larkins, J.P. Mollica, N.A. Beard, and G.D. Lamb. 2009. Calsequestrin content and SERCA determine normal and maximal Ca2+ storage levels in sarcoplasmic reticulum of fastand slow-twitch fibres of rat. J. Physiol. 587:443-460. doi:10.1113/jphysiol.2008.163162.
    • (2009) J. Physiol , vol.587 , pp. 443-460
    • Murphy, R.M.1    Larkins, N.T.2    Mollica, J.P.3    Beard, N.A.4    Lamb, G.D.5
  • 29
    • 0031057326 scopus 로고    scopus 로고
    • Relationship between depolarization-induced force responses and Ca2+ content in skeletal muscle fibres of rat and toad
    • Owen, V.J., G.D. Lamb, D.G. Stephenson, and M.W. Fryer. 1997. Relationship between depolarization-induced force responses and Ca2+ content in skeletal muscle fibres of rat and toad. J. Physiol. 498:571-586.
    • (1997) J. Physiol. , vol.498 , pp. 571-586
    • Owen, V.J.1    Lamb, G.D.2    Stephenson, D.G.3    Fryer, M.W.4
  • 30
    • 34347230164 scopus 로고    scopus 로고
    • Measuring calcium signaling using genetically targetable fluorescent indicators
    • doi:10.1038/nprot.2006.172
    • Palmer, A.E., and R.Y. Tsien. 2006. Measuring calcium signaling using genetically targetable fluorescent indicators. Nat. Protoc. 1:1057-1065. doi:10.1038/nprot.2006.172.
    • (2006) Nat. Protoc. , vol.1 , pp. 1057-1065
    • Palmer, A.E.1    Tsien, R.Y.2
  • 31
    • 33646570865 scopus 로고    scopus 로고
    • Ca2+ indicators based on computationally redesigned calmodulin-peptide pairs
    • doi:10.1016/j.chembiol.2006.03.007
    • Palmer, A.E., M. Giacomello, T. Kortemme, S.A. Hires, V. Lev-Ram, D. Baker, and R.Y. Tsien. 2006. Ca2+ indicators based on computationally redesigned calmodulin-peptide pairs. Chem. Biol. 13:521-530. doi:10.1016/j.chembiol.2006.03.007.
    • (2006) Chem. Biol. , vol.13 , pp. 521-530
    • Palmer, A.E.1    Giacomello, M.2    Kortemme, T.3    Hires, S.A.4    Lev-Ram, V.5    Baker, D.6    Tsien, R.Y.7
  • 32
    • 0027297091 scopus 로고
    • Effect of fura-2 on action potential-stimulated calcium release in cut twitch fibers from frog muscle
    • doi:10 .1085/jgp.102.2.295
    • Pape, P.C., D.S. Jong, W.K. Chandler, and S.M. Baylor. 1993. Effect of fura-2 on action potential-stimulated calcium release in cut twitch fibers from frog muscle. J. Gen. Physiol. 102:295-332. doi:10 .1085/jgp.102.2.295.
    • (1993) J. Gen. Physiol. , vol.102 , pp. 295-332
    • Pape, P.C.1    Jong, D.S.2    Chandler, W.K.3    Baylor, S.M.4
  • 33
    • 34248158200 scopus 로고    scopus 로고
    • Role of calsequestrin evaluated from changes in free and total calcium concentrations in the sarcoplasmic reticulum of frog cut skeletal muscle fibres
    • doi:10.1113/jphysiol.2006.126474
    • Pape, P.C., K. Fénelon, C.R. Lamboley, and D. Stachura. 2007. Role of calsequestrin evaluated from changes in free and total calcium concentrations in the sarcoplasmic reticulum of frog cut skeletal muscle fibres. J. Physiol. 581:319-367. doi:10.1113/jphysiol.2006.126474.
    • (2007) J. Physiol. , vol.581 , pp. 319-367
    • Pape, P.C.1    Fénelon, K.2    Lamboley, C.R.3    Stachura, D.4
  • 34
    • 0021357835 scopus 로고
    • Energetics of the calcium-transporting ATPase
    • Pickart, C.M., and W.P. Jencks. 1984. Energetics of the calcium-transporting ATPase. J. Biol. Chem. 259:1629-1643.
    • (1984) J. Biol. Chem. , vol.259 , pp. 1629-1643
    • Pickart, C.M.1    Jencks, W.P.2
  • 35
    • 4544294545 scopus 로고    scopus 로고
    • How source content determines intracellular Ca2+ release kinetics, Simultaneous measurement of [Ca2+] transients and [H+] displacement in skeletal muscle
    • doi:10.1085/jgp.200409071
    • Pizarro, G., and E. Ríos. 2004. How source content determines intracellular Ca2+ release kinetics. Simultaneous measurement of [Ca2+] transients and [H+] displacement in skeletal muscle. J. Gen. Physiol. 124:239-258. doi:10.1085/jgp.200409071.
    • (2004) J. Gen. Physiol. , vol.124 , pp. 239-258
    • Pizarro, G.1    Ríos, E.2
  • 36
    • 33748313279 scopus 로고    scopus 로고
    • The elusive role of store depletion in the control of intracellular calcium release
    • doi:10 .1007/s10974-006-9082-5
    • Ríos, E., B.S. Launikonis, L. Royer, G. Brum, and J. Zhou. 2006. The elusive role of store depletion in the control of intracellular calcium release. J. Muscle Res. Cell Motil. 27:337-350. doi:10 .1007/s10974-006-9082-5.
    • (2006) J. Muscle Res. Cell Motil. , vol.27 , pp. 337-350
    • Ríos, E.1    Launikonis, B.S.2    Royer, L.3    Brum, G.4    Zhou, J.5
  • 37
    • 0026069822 scopus 로고
    • In vitro interaction of a polypeptide homologous to human Ro/SS-A antigen (calreticulin) with a highly conserved amino acid sequence in the cytoplasmic domain of integrin alpha subunits
    • doi:10.1021/bi00105a008
    • Rojiani, M.V., B.B. Finlay, V. Gray, and S. Dedhar. 1991. In vitro interaction of a polypeptide homologous to human Ro/SS-A antigen (calreticulin) with a highly conserved amino acid sequence in the cytoplasmic domain of integrin alpha subunits. Biochemistry. 30:9859-9866. doi:10.1021/bi00105a008.
    • (1991) Biochemistry , vol.30 , pp. 9859-9866
    • Rojiani, M.V.1    Finlay, B.B.2    Gray, V.3    Dedhar, S.4
  • 38
    • 53249134525 scopus 로고    scopus 로고
    • Evolution and modulation of intracellular calcium release during long-lasting, depleting depolarization in mouse muscle
    • doi:10.1113/jphysiol.2008.157990
    • Royer, L., S. Pouvreau, and E. Ríos. 2008. Evolution and modulation of intracellular calcium release during long-lasting, depleting depolarization in mouse muscle. J. Physiol. 586:4609-4629. doi:10.1113/jphysiol.2008.157990.
    • (2008) J. Physiol. , vol.586 , pp. 4609-4629
    • Royer, L.1    Pouvreau, S.2    Ríos, E.3
  • 39
    • 77956233084 scopus 로고    scopus 로고
    • Paradoxical buffering of calcium by calsequestrin demonstrated for the calcium store of skeletal muscle
    • doi:10 .1085/jgp.201010454
    • Royer, L., M. Sztretye, C. Manno, S. Pouvreau, J. Zhou, B.C. Knollmann, F. Protasi, P.D. Allen, and E. Ríos. 2010. Paradoxical buffering of calcium by calsequestrin demonstrated for the calcium store of skeletal muscle. J. Gen. Physiol. 136:325-338. doi:10 .1085/jgp.201010454.
    • (2010) J. Gen. Physiol. , vol.136 , pp. 325-338
    • Royer, L.1    Sztretye, M.2    Manno, C.3    Pouvreau, S.4    Zhou, J.5    Knollmann, B.C.6    Protasi, F.7    Allen, P.D.8    Ríos, E.9
  • 40
    • 33646111422 scopus 로고    scopus 로고
    • 2+ and cytosolic cAMP dynamics in mouse skeletal muscle
    • doi:10.1083/jcb.200601160
    • 2+ and cytosolic cAMP dynamics in mouse skeletal muscle. J. Cell Biol. 173:187-193. doi:10.1083/jcb.200601160.
    • (2006) J. Cell Biol. , vol.173 , pp. 187-193
    • Rudolf, R.1    Magalhães, P.J.2    Pozzan, T.3
  • 41
    • 0023551042 scopus 로고
    • Depletion of calcium from the sarcoplasmic reticulum during calcium release in frog skeletal muscle
    • Schneider, M.F., B.J. Simon, and G. Szucs. 1987. Depletion of calcium from the sarcoplasmic reticulum during calcium release in frog skeletal muscle. J. Physiol. 392:167-192.
    • (1987) J. Physiol. , vol.392 , pp. 167-192
    • Schneider, M.F.1    Simon, B.J.2    Szucs, G.3
  • 42
    • 0034624196 scopus 로고    scopus 로고
    • 2+) and interacts with triadin
    • doi:10.1016/S0014-5793(00)02246-8
    • 2+) and interacts with triadin. FEBS Lett. 486:178-182. doi:10.1016/S0014-5793(00)02246-8.
    • (2000) FEBS Lett , vol.486 , pp. 178-182
    • Shin, D.W.1    Ma, J.2    Kim, D.H.3
  • 43
    • 79961112228 scopus 로고    scopus 로고
    • Permeability of the calcium store membrane and its changes during function, directly measured in mouse skeletal muscle cells
    • Sztretye, M., J. Yi, L. Figueroa, J. Zhou, L. Royer, P.D. Allen, and E. Ríos. 2011. Permeability of the calcium store membrane and its changes during function, directly measured in mouse skeletal muscle cells. J. Gen. Physiol. 138:231-247.
    • (2011) J. Gen. Physiol. , vol.138 , pp. 231-247
    • Sztretye, M.1    Yi, J.2    Figueroa, L.3    Zhou, J.4    Royer, L.5    Allen, P.D.6    Ríos, E.7
  • 44
    • 0141482017 scopus 로고    scopus 로고
    • Calsequestrin determines the functional size and stability of cardiac intracellular calcium stores: Mechanism for hereditary arrhythmia
    • doi:10.1073/pnas.1932318100
    • Terentyev, D., S. Viatchenko-Karpinski, I. Györke, P. Volpe, S.C. Williams, and S. Györke. 2003. Calsequestrin determines the functional size and stability of cardiac intracellular calcium stores: Mechanism for hereditary arrhythmia. Proc. Natl. Acad. Sci. USA. 100:11759-11764. doi:10.1073/pnas.1932318100.
    • (2003) Proc. Natl. Acad. Sci. USA. , vol.100 , pp. 11759-11764
    • Terentyev, D.1    Viatchenko-Karpinski, S.2    Györke, I.3    Volpe, P.4    Williams, S.C.5    Györke, S.6
  • 46
    • 0032750498 scopus 로고    scopus 로고
    • Patch-clamp recording of charge movement, Ca2+ current, and Ca2+ transients in adult skeletal muscle fibers
    • doi:10.1016/S0006-3495(99)77104-3
    • Wang, Z.M., M.L. Messi, and O. Delbono. 1999. Patch-clamp recording of charge movement, Ca2+ current, and Ca2+ transients in adult skeletal muscle fibers. Biophys. J. 77:2709-2716. doi:10.1016/S0006-3495(99)77104-3.
    • (1999) Biophys. J. , vol.77 , pp. 2709-2716
    • Wang, Z.M.1    Messi, M.L.2    Delbono, O.3
  • 47
    • 0029910837 scopus 로고    scopus 로고
    • A theoretical study of calcium microdomains in turtle hair cells
    • doi:10.1016/S0006-3495(96)79429-8
    • Wu, Y.C., T. Tucker, and R. Fettiplace. 1996. A theoretical study of calcium microdomains in turtle hair cells. Biophys. J. 71:2256-2275. doi:10.1016/S0006-3495(96)79429-8.
    • (1996) Biophys. J. , vol.71 , pp. 2256-2275
    • Wu, Y.C.1    Tucker, T.2    Fettiplace, R.3
  • 48
    • 78649718110 scopus 로고    scopus 로고
    • 2+ leak in normal and failing rabbit ventricular myocytes
    • doi:10.1113/jphysiol.2010.197913
    • 2+ leak in normal and failing rabbit ventricular myocytes. J. Physiol. 588:4743-4757. doi:10.1113/jphysiol.2010.197913.
    • (2010) J. Physiol. , vol.588 , pp. 4743-4757
    • Zima, A.V.1    Bovo, E.2    Bers, D.M.3    Blatter, L.A.4
  • 49
    • 78049309952 scopus 로고    scopus 로고
    • 2(+) in the sarcoplasmic reticulum lumen of mammalian skeletal muscle
    • doi:10.1016/j.bpj.2010.08.032
    • 2(+) in the sarcoplasmic reticulum lumen of mammalian skeletal muscle. Biophys. J. 99:2705-2714. doi:10.1016/j.bpj.2010.08.032.
    • (2010) Biophys. J. , vol.99 , pp. 2705-2714
    • Ziman, A.P.1    Ward, C.W.2    Rodney, G.G.3    Lederer, W.J.4    Bloch, R.J.5


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