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Volumn 9, Issue 412, 2016, Pages

Cholesterol modulates Orai1 channel function

Author keywords

[No Author keywords available]

Indexed keywords

CALCIUM; CALCIUM RELEASE ACTIVATED CALCIUM CHANNEL 1; CHOLESTEROL; CALCIUM CHANNEL; CHOLESTEROL OXIDASE; HISTAMINE; ORAI1 PROTEIN, HUMAN; PEPTIDE;

EID: 84955589705     PISSN: 19450877     EISSN: 19379145     Source Type: Journal    
DOI: 10.1126/scisignal.aad7808     Document Type: Article
Times cited : (84)

References (65)
  • 2
    • 0027336649 scopus 로고
    • Mitogen-regulated Ca2+ current of T lymphocytes is activated by depletion of intracellular Ca2+ stores
    • A. Zweifach, R. S. Lewis, Mitogen-regulated Ca2+ current of T lymphocytes is activated by depletion of intracellular Ca2+ stores. Proc. Natl. Acad. Sci. U.S.A. 90, 6295-6299 (1993).
    • (1993) Proc. Natl. Acad. Sci. U.S.A , vol.90 , pp. 6295-6299
    • Zweifach, A.1    Lewis, R.S.2
  • 4
    • 21844432686 scopus 로고    scopus 로고
    • STIM is a Ca2+ sensor essential for Ca2+-store-depletion-Triggered Ca2+ influx
    • J. Liou, M. L. Kim, W. D. Heo, J. T. Jones, J. W. Myers, J. E. Ferrell Jr., T. Meyer, STIM is a Ca2+ sensor essential for Ca2+-store-depletion-Triggered Ca2+ influx. Curr. Biol. 15, 1235-1241 (2005).
    • (2005) Curr. Biol , vol.15 , pp. 1235-1241
    • Liou, J.1    Kim, M.L.2    Heo, W.D.3    Jones, J.T.4    Myers, J.W.5    Ferrell, J.E.6    Meyer, T.7
  • 5
    • 27144515996 scopus 로고    scopus 로고
    • STIM1 is a Ca2+ sensor that activates CRAC channels and migrates from the Ca2+ store to the plasma membrane
    • S. L. Zhang, Y. Yu, J. Roos, J. A. Kozak, T. J. Deerinck, M. H. Ellisman, K. A. Stauderman, M. D. Cahalan, STIM1 is a Ca2+ sensor that activates CRAC channels and migrates from the Ca2+ store to the plasma membrane. Nature 437, 902-905 (2005).
    • (2005) Nature , vol.437 , pp. 902-905
    • Zhang, S.L.1    Yu, Y.2    Roos, J.3    Kozak, J.A.4    Deerinck, T.J.5    Ellisman, M.H.6    Stauderman, K.A.7    Cahalan, M.D.8
  • 9
    • 63049139104 scopus 로고    scopus 로고
    • Molecular clustering of STIM1 with Orai1/CRACM1 at the plasma membrane depends dynamically on depletion of Ca2+ stores and on electrostatic interactions
    • N. Calloway, M. Vig, J.-P. Kinet, D. Holowka, B. Baird, Molecular clustering of STIM1 with Orai1/CRACM1 at the plasma membrane depends dynamically on depletion of Ca2+ stores and on electrostatic interactions. Mol. Biol. Cell 20, 389-399 (2009).
    • (2009) Mol. Biol. Cell , vol.20 , pp. 389-399
    • Calloway, N.1    Vig, M.2    Kinet, J.-P.3    Holowka, D.4    Baird, B.5
  • 12
    • 84859886957 scopus 로고    scopus 로고
    • Structure, regulation and biophysics of ICRAC, STIM/Orai1
    • I. Derler, J. Madl, G. Schötz, C. Romanin, Structure, regulation and biophysics of ICRAC, STIM/Orai1. Adv. Exp. Med. Biol. 740, 383-410 (2012).
    • (2012) Adv. Exp. Med. Biol , vol.740 , pp. 383-410
    • Derler, I.1    Madl, J.2    Schötz, G.3    Romanin, C.4
  • 13
    • 84870655957 scopus 로고    scopus 로고
    • Crystal structure of the calcium release-Activated calcium channel Orai
    • X. Hou, L. Pedi, M. M. Diver, S. B. Long, Crystal structure of the calcium release-Activated calcium channel Orai. Science 338, 1308-1313 (2012).
    • (2012) Science , vol.338 , pp. 1308-1313
    • Hou, X.1    Pedi, L.2    Diver, M.M.3    Long, S.B.4
  • 15
    • 84885160599 scopus 로고    scopus 로고
    • The extended transmembrane Orai1 N-Terminal (ETON) region combines binding interface and gate for Orai1 activation by STIM1
    • I. Derler, P. Plenk, M. Fahrner, M. Muik, I. Jardin, R. Schindl, H. J. Gruber, K. Groschner, C. Romanin, The extended transmembrane Orai1 N-Terminal (ETON) region combines binding interface and gate for Orai1 activation by STIM1. J. Biol. Chem. 288, 29025-29034 (2013).
    • (2013) J. Biol. Chem , vol.288 , pp. 29025-29034
    • Derler, I.1    Plenk, P.2    Fahrner, M.3    Muik, M.4    Jardin, I.5    Schindl, R.6    Gruber, H.J.7    Groschner, K.8    Romanin, C.9
  • 16
    • 84875703592 scopus 로고    scopus 로고
    • Orai channel pore properties and gating by STIM: Implications from the Orai crystal structure
    • B. S. Rothberg, Y. Wang, D. L. Gill, Orai channel pore properties and gating by STIM: Implications from the Orai crystal structure. Sci. Signal. 6, pe9 (2013).
    • (2013) Sci. Signal , vol.6
    • Rothberg, B.S.1    Wang, Y.2    Gill, D.L.3
  • 17
    • 24344476722 scopus 로고    scopus 로고
    • A severe defect in CRAC Ca2+ channel activation and altered K+ channel gating in T cells from immunodeficient patients
    • S. Feske, M. Prakriya, A. Rao, R. S. Lewis, A severe defect in CRAC Ca2+ channel activation and altered K+ channel gating in T cells from immunodeficient patients. J. Exp. Med. 202, 651-662 (2005).
    • (2005) J. Exp. Med , vol.202 , pp. 651-662
    • Feske, S.1    Prakriya, M.2    Rao, A.3    Lewis, R.S.4
  • 18
    • 67650100398 scopus 로고    scopus 로고
    • Increased hydrophobicity at the N terminus/membrane interface impairs gating of the severe combined immunodeficiency-related ORAI1 mutant
    • I. Derler, M. Fahrner, O. Carugo, M. Muik, J. Bergsmann, R. Schindl, I. Frischauf, S. Eshaghi, C. Romanin, Increased hydrophobicity at the N terminus/membrane interface impairs gating of the severe combined immunodeficiency-related ORAI1 mutant. J. Biol. Chem. 284, 15903-15915 (2009).
    • (2009) J. Biol. Chem , vol.284 , pp. 15903-15915
    • Derler, I.1    Fahrner, M.2    Carugo, O.3    Muik, M.4    Bergsmann, J.5    Schindl, R.6    Frischauf, I.7    Eshaghi, S.8    Romanin, C.9
  • 20
    • 84929316222 scopus 로고    scopus 로고
    • Store-operated calcium entry: Mechanisms and modulation
    • P. G. Hogan, A. Rao, Store-operated calcium entry: Mechanisms and modulation. Biochem. Biophys. Res. Commun. 460, 40-49 (2015).
    • (2015) Biochem. Biophys. Res. Commun , vol.460 , pp. 40-49
    • Hogan, P.G.1    Rao, A.2
  • 21
    • 84861906215 scopus 로고    scopus 로고
    • Junctate is a Ca2+-sensing structural component of Orai1 and stromal interaction molecule 1 (STIM1)
    • S. Srikanth, M. Jew, K.-D. Kim, M.-K. Yee, J. Abramson, Y. Gwack, Junctate is a Ca2+-sensing structural component of Orai1 and stromal interaction molecule 1 (STIM1). Proc. Natl. Acad. Sci. U.S.A. 109, 8682-8687 (2012).
    • (2012) Proc. Natl. Acad. Sci. U.S.A , vol.109 , pp. 8682-8687
    • Srikanth, S.1    Jew, M.2    Kim, K.-D.3    Yee, M.-K.4    Abramson, J.5    Gwack, Y.6
  • 22
    • 84859735442 scopus 로고    scopus 로고
    • SARAF inactivates the store operated calcium entry machinery to prevent excess calcium refilling
    • R. Palty, A. Raveh, I. Kaminsky, R. Meller, E. Reuveny, SARAF inactivates the store operated calcium entry machinery to prevent excess calcium refilling. Cell 149, 425-438 (2012).
    • (2012) Cell , vol.149 , pp. 425-438
    • Palty, R.1    Raveh, A.2    Kaminsky, I.3    Meller, R.4    Reuveny, E.5
  • 23
    • 84865601584 scopus 로고    scopus 로고
    • Orai1 STIM1 and their associating partners
    • S. Srikanth, Y. Gwack, Orai1, STIM1, and their associating partners. J. Physiol. 590, 4169-4177 (2012).
    • (2012) J. Physiol , vol.590 , pp. 4169-4177
    • Srikanth, S.1    Gwack, Y.2
  • 25
    • 79961156737 scopus 로고    scopus 로고
    • Stimulated association of STIM1 and Orai1 is regulated by the balance of PtdIns(4,5)P2 between distinct membrane pools
    • N. Calloway, T. Owens, K. Corwith, W. Rodgers, D. Holowka, B. Baird, Stimulated association of STIM1 and Orai1 is regulated by the balance of PtdIns(4, 5)P2 between distinct membrane pools. J. Cell Sci. 124, 2602-2610 (2011).
    • (2011) J. Cell Sci. , vol.124 , pp. 2602-2610
    • Calloway, N.1    Owens, T.2    Corwith, K.3    Rodgers, W.4    Holowka, D.5    Baird, B.6
  • 26
    • 84940898131 scopus 로고    scopus 로고
    • The ER/PM microdomain PI(4,5)P2 and the regulation of STIM1-Orai1 channel function
    • X. Cao, S. Choi, J. J. Maléth, S. Park, M. Ahuja, S. Muallem, The ER/PM microdomain, PI(4, 5)P2 and the regulation of STIM1-Orai1 channel function. Cell Calcium 58, 342-348 (2015).
    • (2015) Cell Calcium , vol.58 , pp. 342-348
    • Cao, X.1    Choi, S.2    Maléth, J.J.3    Park, S.4    Ahuja, M.5    Muallem, S.6
  • 27
    • 84936748902 scopus 로고    scopus 로고
    • Cholesterol modulates CFTR confinement in the plasma membrane of primary epithelial cells
    • A. Abu-Arish, E. Pandzic, J. Goepp, E. Matthes, J. W. Hanrahan, P. W. Wiseman, Cholesterol modulates CFTR confinement in the plasma membrane of primary epithelial cells. Biophys. J. 109, 85-94 (2015).
    • (2015) Biophys. J , vol.109 , pp. 85-94
    • Abu-Arish, A.1    Pandzic, E.2    Goepp, J.3    Matthes, E.4    Hanrahan, J.W.5    Wiseman, P.W.6
  • 28
    • 36448929114 scopus 로고    scopus 로고
    • Cholesterol reporter molecules
    • G. Gimpl, K. Gehrig-Burger, Cholesterol reporter molecules. Biosci. Rep. 27, 335-358 (2007).
    • (2007) Biosci. Rep , vol.27 , pp. 335-358
    • Gimpl, G.1    Gehrig-Burger, K.2
  • 29
    • 0026612247 scopus 로고
    • Fce receptor mediated Ca2+ influx into mast cells is modulated by the concentration of cytosolic free Ca2+ ions
    • O. Dar, I. Pecht, Fce receptor mediated Ca2+ influx into mast cells is modulated by the concentration of cytosolic free Ca2+ ions. FEBS Lett. 310, 123-128 (1992).
    • (1992) FEBS Lett , vol.310 , pp. 123-128
    • Dar, O.1    Pecht, I.2
  • 30
    • 33646673117 scopus 로고    scopus 로고
    • Cholesterol deficiency in a mouse model of Smith-Lemli-Opitz syndrome reveals increased mast cell responsiveness
    • M. Kovarova, C. A. Wassif, S. Odom, K. Liao, F. D. Porter, J. Rivera, Cholesterol deficiency in a mouse model of Smith-Lemli-Opitz syndrome reveals increased mast cell responsiveness. J. Exp. Med. 203, 1161-1171 (2006).
    • (2006) J. Exp. Med , vol.203 , pp. 1161-1171
    • Kovarova, M.1    Wassif, C.A.2    Odom, S.3    Liao, K.4    Porter, F.D.5    Rivera, J.6
  • 31
    • 45449105538 scopus 로고    scopus 로고
    • Proteins and cholesterol-rich domains
    • R. M. Epand, Proteins and cholesterol-rich domains. Biochim. Biophys. Acta 1778, 1576-1582 (2008).
    • (2008) Biochim. Biophys. Acta , vol.1778 , pp. 1576-1582
    • Epand, R.M.1
  • 33
    • 84871118027 scopus 로고    scopus 로고
    • Crystal structure of calmodulin binding domain of Orai1 in complex with Ca2+calmodulin displays a unique binding mode
    • Y. Liu, X. Zheng, G. A. Mueller, M. Sobhany, E. F. DeRose, Y. Zhang, R. E. London, L. Birnbaumer, Crystal structure of calmodulin binding domain of Orai1 in complex with Ca2+calmodulin displays a unique binding mode. J. Biol. Chem. 287, 43030-43041 (2012).
    • (2012) J. Biol. Chem , vol.287 , pp. 43030-43041
    • Liu, Y.1    Zheng, X.2    Mueller, G.A.3    Sobhany, M.4    Derose, E.F.5    Zhang, Y.6    London, R.E.7    Birnbaumer, L.8
  • 34
    • 70349349160 scopus 로고    scopus 로고
    • STIM1 and calmodulin interact with Orai1 to induce Ca2+-dependent inactivation of CRAC channels
    • F. M. Mullins, C. Y. Park, R. E. Dolmetsch, R. S. Lewis, STIM1 and calmodulin interact with Orai1 to induce Ca2+-dependent inactivation of CRAC channels. Proc. Natl. Acad. Sci. U.S.A. 106, 15495-15500 (2009).
    • (2009) Proc. Natl. Acad. Sci. U.S.A , vol.106 , pp. 15495-15500
    • Mullins, F.M.1    Park, C.Y.2    Dolmetsch, R.E.3    Lewis, R.S.4
  • 35
    • 77951949270 scopus 로고    scopus 로고
    • A novel EFhand protein, CRACR2A, is a cytosolic Ca2+ sensor that stabilizes CRAC channels in T cells
    • S. Srikanth, H.-J. Jung, K.-D. Kim, P. Souda, J. Whitelegge, Y. Gwack, A novel EFhand protein, CRACR2A, is a cytosolic Ca2+ sensor that stabilizes CRAC channels in T cells. Nat. Cell Biol. 12, 436-446 (2010).
    • (2011) Nat. Cell Biol , vol.12 , pp. 436-446
    • Srikanth, S.1    Jung, H.-J.2    Kim, K.-D.3    Souda, P.4    Whitelegge, J.5    Gwack, Y.6
  • 36
    • 0031755752 scopus 로고    scopus 로고
    • Peripheral-Type benzodiazepine receptor function in cholesterol transport Identification of a putative cholesterol recognition/interaction amino acid sequence and consensus pattern
    • H. Li, V. Papadopoulos, Peripheral-Type benzodiazepine receptor function in cholesterol transport. Identification of a putative cholesterol recognition/interaction amino acid sequence and consensus pattern. Endocrinology 139, 4991-4997 (1998).
    • (1998) Endocrinology , vol.139 , pp. 4991-4997
    • Li, H.1    Papadopoulos, V.2
  • 37
    • 66749085475 scopus 로고    scopus 로고
    • A cytosolic homomerization and a modulatory domain within STIM1 C terminus determine coupling to ORAI1 channels
    • M. Muik, M. Fahrner, I. Derler, R. Schindl, J. Bergsmann, I. Frischauf, K. Groschner, C. Romanin, A cytosolic homomerization and a modulatory domain within STIM1 C terminus determine coupling to ORAI1 channels. J. Biol. Chem. 284, 8421-8426 (2009).
    • (2009) J. Biol. Chem , vol.284 , pp. 8421-8426
    • Muik, M.1    Fahrner, M.2    Derler, I.3    Schindl, R.4    Bergsmann, J.5    Frischauf, I.6    Groschner, K.7    Romanin, C.8
  • 38
    • 0028812541 scopus 로고
    • Alteration of the myometrial plasma membrane cholesterol content with b-cyclodextrin modulates the binding affinity of the oxytocin receptor
    • U. Klein, G. Gimpl, F. Fahrenholz, Alteration of the myometrial plasma membrane cholesterol content with b-cyclodextrin modulates the binding affinity of the oxytocin receptor. Biochemistry 34, 13784-13793 (1995).
    • (1995) Biochemistry , vol.34 , pp. 13784-13793
    • Klein, U.1    Gimpl, G.2    Fahrenholz, F.3
  • 39
    • 15244358803 scopus 로고    scopus 로고
    • Interaction of melittin with membrane cholesterol: A fluorescence approach
    • H. Raghuraman, A. Chattopadhyay, Interaction of melittin with membrane cholesterol: A fluorescence approach. Biophys. J. 87, 2419-2432 (2004).
    • (2004) Biophys. J , vol.87 , pp. 2419-2432
    • Raghuraman, H.1    Chattopadhyay, A.2
  • 41
    • 62549126542 scopus 로고    scopus 로고
    • A role for Orai in TRPC-mediated Ca2+ entry suggests that a TRPC:Orai complex may mediate store and receptor operated Ca2+ entry
    • Y. Liao, N. W. Plummer, M. D. George, J. Abramowitz, M. X. Zhu, L. Birnbaumer, A role for Orai in TRPC-mediated Ca2+ entry suggests that a TRPC:Orai complex may mediate store and receptor operated Ca2+ entry. Proc. Natl. Acad. Sci. U.S.A. 106, 3202-3206 (2009).
    • (2009) Proc. Natl. Acad. Sci. U.S.A , vol.106 , pp. 3202-3206
    • Liao, Y.1    Plummer, N.W.2    George, M.D.3    Abramowitz, J.4    Zhu, M.X.5    Birnbaumer, L.6
  • 42
    • 79551509372 scopus 로고    scopus 로고
    • Lipid rafts are essential for the regulation of SOCE by plasma membrane resident STIM1 in human platelets
    • N. Dionisio, C. Galán, I. Jardín, G. M. Salido, J. A. Rosado, Lipid rafts are essential for the regulation of SOCE by plasma membrane resident STIM1 in human platelets. Biochim. Biophys. Acta 1813, 431-437 (2011).
    • (2011) Biochim. Biophys. Acta , vol.1813 , pp. 431-437
    • Dionisio, N.1    Galán, C.2    Jardín, I.3    Salido, G.M.4    Rosado, J.A.5
  • 43
    • 77954958903 scopus 로고    scopus 로고
    • Lipid rafts modulate the activation but not the maintenance of store-operated Ca2+ entry
    • C. Galan, G. E. Woodard, N. Dionisio, G. M. Salido, J. A. Rosado, Lipid rafts modulate the activation but not the maintenance of store-operated Ca2+ entry. Biochim. Biophys. Acta 1803, 1083-1093 (2010).
    • (2011) Biochim. Biophys. Acta , vol.1803 , pp. 1083-1093
    • Galan, C.1    Woodard, G.E.2    Dionisio, N.3    Salido, G.M.4    Rosado, J.A.5
  • 44
    • 58549114100 scopus 로고    scopus 로고
    • Role of lipid rafts in the interaction between hTRPC1 Orai1 and STIM1
    • I. Jardin, G. M. Salido, J. A. Rosado, Role of lipid rafts in the interaction between hTRPC1, Orai1 and STIM1. Channels 2, 401-403 (2008).
    • (2008) Channels , vol.2 , pp. 401-403
    • Jardin, I.1    Salido, G.M.2    Rosado, J.A.3
  • 46
    • 84912103775 scopus 로고    scopus 로고
    • Disorder in cholesterol-binding functionality of CRAC peptides: A molecular dynamics study
    • C. M. Miller, A. C. Brown, J. Mittal, Disorder in cholesterol-binding functionality of CRAC peptides: A molecular dynamics study. J. Phys. Chem. B 2014, 13169-13174 (2014).
    • (2014) J. Phys. Chem B , vol.2014 , pp. 13169-13174
    • Miller, C.M.1    Brown, A.C.2    Mittal, J.3
  • 47
    • 0035970108 scopus 로고    scopus 로고
    • Cholesterol binding at the cholesterol recognition/interaction amino acid consensus (CRAC) of the peripheral-Type benzodiazepine receptor and inhibition of steroidogenesis by an HIV TAT-CRAC peptide
    • H. Li, Z.-x. Yao, B. Degenhardt, G. Teper, V. Papadopoulos, Cholesterol binding at the cholesterol recognition/interaction amino acid consensus (CRAC) of the peripheral-Type benzodiazepine receptor and inhibition of steroidogenesis by an HIV TAT-CRAC peptide. Proc. Natl. Acad. Sci. U.S.A. 98, 1267-1272 (2001).
    • (2001) Proc. Natl. Acad. Sci. U.S.A , vol.98 , pp. 1267-1272
    • Li, H.1    Yao, Z.-X.2    Degenhardt, B.3    Teper, G.4    Papadopoulos, V.5
  • 48
    • 77958086064 scopus 로고    scopus 로고
    • Interaction of mammalian seminal plasma protein PDC-109 with cholesterol: Implications for a putative CRAC domain
    • S. Scolari, K. Muller, R. Bittman, A. Herrmann, P. Muller, Interaction of mammalian seminal plasma protein PDC-109 with cholesterol: Implications for a putative CRAC domain. Biochemistry 49, 9027-9031 (2010).
    • (2011) Biochemistry , vol.49 , pp. 9027-9031
    • Scolari, S.1    Muller, K.2    Bittman, R.3    Herrmann, A.4    Muller, P.5
  • 52
    • 80054690502 scopus 로고    scopus 로고
    • Probing the lipid-protein interface using model transmembrane peptides with a covalently linked acyl chain
    • T. K. M. Nyholm, B. van Duyl, D. T. S. Rijkers, R. M. J. Liskamp, J. A. Killian, Probing the lipid-protein interface using model transmembrane peptides with a covalently linked acyl chain. Biophys. J. 101, 1959-1967 (2011).
    • (2011) Biophys. J , vol.101 , pp. 1959-1967
    • Nyholm, T.K.M.1    Van Duyl, B.2    Rijkers, D.T.S.3    Liskamp, R.M.J.4    Killian, J.A.5
  • 53
    • 34147179346 scopus 로고    scopus 로고
    • Regulation of the gating of BKCa channel by lipid bilayer thickness
    • C. Yuan, R. J. O'Connell, R. F. Jacob, R. P. Mason, S. N. Treistman, Regulation of the gating of BKCa channel by lipid bilayer thickness. J. Biol. Chem. 282, 7276-7286 (2007).
    • (2007) J. Biol. Chem , vol.282 , pp. 7276-7286
    • Yuan, C.1    O'connell, R.J.2    Jacob, R.F.3    Mason, R.P.4    Treistman, S.N.5
  • 54
    • 84868562084 scopus 로고    scopus 로고
    • Water permeability of aquaporin-4 channel depends on bilayer composition, thickness, and elasticity
    • J. Tong, M. M. Briggs, T. J. McIntosh, Water permeability of aquaporin-4 channel depends on bilayer composition, thickness, and elasticity. Biophys. J. 103, 1899-1908 (2012).
    • (2012) Biophys. J , vol.103 , pp. 1899-1908
    • Tong, J.1    Briggs, M.M.2    McIntosh, T.J.3
  • 55
    • 0141919745 scopus 로고    scopus 로고
    • Cholesterol depletion inhibits store-operated calcium currents and exocytotic membrane fusion in RBL-2H3 cells
    • N. Kato, M. Nakanishi, N. Hirashima, Cholesterol depletion inhibits store-operated calcium currents and exocytotic membrane fusion in RBL-2H3 cells. Biochemistry 42, 11808-11814 (2003).
    • (2003) Biochemistry , vol.42 , pp. 11808-11814
    • Kato, N.1    Nakanishi, M.2    Hirashima, N.3
  • 56
    • 84954607751 scopus 로고    scopus 로고
    • Cholesterol depletion using methyl-b-cyclodextrin
    • S. Mahammad, I. Parmryd, Cholesterol depletion using methyl-b-cyclodextrin. Methods Mol. Biol. 1232, 91-102 (2015).
    • (2015) Methods Mol. Biol , vol.1232 , pp. 91-102
    • Mahammad, S.1    Parmryd, I.2
  • 57
    • 0021895138 scopus 로고
    • A new generation of Ca2+ indicators with greatly improved fluorescence properties
    • G. Grynkiewicz, M. Poenie, R. Y. Tsien, A new generation of Ca2+ indicators with greatly improved fluorescence properties. J. Biol. Chem. 260, 3440-3450 (1985).
    • (1985) J. Biol. Chem , vol.260 , pp. 3440-3450
    • Grynkiewicz, G.1    Poenie, M.2    Tsien, R.Y.3
  • 60
    • 0034810232 scopus 로고    scopus 로고
    • Reliable and global measurement of fluorescence resonance energy transfer using fluorescence microscopes
    • Z. Xia, Y. Liu, Reliable and global measurement of fluorescence resonance energy transfer using fluorescence microscopes. Biophys. J. 81, 2395-2402 (2001).
    • (2001) Biophys. J , vol.81 , pp. 2395-2402
    • Xia, Z.1    Liu, Y.2
  • 61
    • 0038101519 scopus 로고    scopus 로고
    • FRET or no FRET: A quantitative comparison
    • C. Berney, G. Danuser, FRET or no FRET: A quantitative comparison. Biophys. J. 84, 3992-4010 (2003).
    • (2003) Biophys. J , vol.84 , pp. 3992-4010
    • Berney, C.1    Danuser, G.2
  • 63
    • 84867412996 scopus 로고    scopus 로고
    • Canonical transient receptor potential (TRPC) 1 acts as a negative regulator for vanilloid TRPV6-mediated Ca2+ influx
    • R. Schindl, R. Fritsch, I. Jardin, I. Frischauf, H. Kahr, M. Muik, M. C. Riedl, K. Groschner, C. Romanin, Canonical transient receptor potential (TRPC) 1 acts as a negative regulator for vanilloid TRPV6-mediated Ca2+ influx. J. Biol. Chem. 287, 35612-35620 (2012).
    • (2012) J. Biol. Chem , vol.287 , pp. 35612-35620
    • Schindl, R.1    Fritsch, R.2    Jardin, I.3    Frischauf, I.4    Kahr, H.5    Muik, M.6    Riedl, M.C.7    Groschner, K.8    Romanin, C.9
  • 65
    • 47249104767 scopus 로고    scopus 로고
    • Enhanced exocytotic-like insertion of Orai1 into the plasma membrane upon intracellular Ca2+ store depletion
    • G. E. Woodard, G. M. Salido, J. A. Rosado, Enhanced exocytotic-like insertion of Orai1 into the plasma membrane upon intracellular Ca2+ store depletion. Am. J. Physiol. Cell Physiol. 294, C1323-C1331 (2008).
    • (2008) Am. J. Physiol. Cell Physiol , vol.294 , pp. C1323-C1331
    • Woodard, G.E.1    Salido, G.M.2    Rosado, J.A.3


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