메뉴 건너뛰기




Volumn 2, Issue 2, 2012, Pages 1045-1060

Calcium pumps: Why So many?

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATASE (CALCIUM); ATP2C1 PROTEIN, HUMAN; CALCIUM; ISOENZYME; PLASMA MEMBRANE CALCIUM TRANSPORTING ADENOSINE TRIPHOSPHATASE; SARCOPLASMIC RETICULUM CALCIUM TRANSPORTING ADENOSINE TRIPHOSPHATASE;

EID: 84862201030     PISSN: None     EISSN: 20404603     Source Type: Journal    
DOI: 10.1002/cphy.c110034     Document Type: Article
Times cited : (33)

References (166)
  • 1
    • 0030813544 scopus 로고    scopus 로고
    • Insulin receptor substrate proteins create a link between the tyrosine phosphorylation cascade and the Ca2+-ATPases in muscle and heart
    • Algenstaedt P, Antonetti DA, Yaffe MB, Kahn CR. Insulin receptor substrate proteins create a link between the tyrosine phosphorylation cascade and the Ca2+-ATPases in muscle and heart. J Biol Chem. 272, 1997, 23696-23702.
    • (1997) J Biol Chem , vol.272 , pp. 23696-23702
    • Algenstaedt, P.1    Antonetti, D.A.2    Yaffe, M.B.3    Kahn, C.R.4
  • 2
    • 0027097849 scopus 로고
    • The yeast Ca(2+)-ATPase homologue, PMR1, is required for normal Golgi function and localizes in a novel Golgi-like distribution
    • Antebi A, Fink GR. The yeast Ca(2+)-ATPase homologue, PMR1, is required for normal Golgi function and localizes in a novel Golgi-like distribution. Mol Biol Cell. 3, 1992, 633-654.
    • (1992) Mol Biol Cell , vol.3 , pp. 633-654
    • Antebi, A.1    Fink, G.R.2
  • 4
    • 0030905733 scopus 로고    scopus 로고
    • Functional Co-expression of the canine cardiac Ca2+ pump and phospholamban in Spodoptera frugiperda (Sf21) cells reveals new insights on ATPase regulation
    • Autry JM, Jones LR. Functional Co-expression of the canine cardiac Ca2+ pump and phospholamban in Spodoptera frugiperda (Sf21) cells reveals new insights on ATPase regulation. J Biol Chem. 272, 1997, 15872-15880.
    • (1997) J Biol Chem , vol.272 , pp. 15872-15880
    • Autry, J.M.1    Jones, L.R.2
  • 5
    • 0031964372 scopus 로고    scopus 로고
    • Evolution of substrate specificities in the P-type ATPase superfamily
    • Axelsen KB, Palmgren MG. Evolution of substrate specificities in the P-type ATPase superfamily. J Mol Evol. 46, 1998, 84-101.
    • (1998) J Mol Evol , vol.46 , pp. 84-101
    • Axelsen, K.B.1    Palmgren, M.G.2
  • 7
    • 0028825579 scopus 로고
    • The membrane topology of the rat sarcoplasmic and endoplasmic reticulum calcium ATPases by in vitro translation scanning
    • Bayle D, Weeks D, Sachs G. The membrane topology of the rat sarcoplasmic and endoplasmic reticulum calcium ATPases by in vitro translation scanning. J Biol Chem. 270, 1995, 25678-25684.
    • (1995) J Biol Chem , vol.270 , pp. 25678-25684
    • Bayle, D.1    Weeks, D.2    Sachs, G.3
  • 11
    • 2642511500 scopus 로고    scopus 로고
    • expression, function, and localization of a novel (sixth) isoform of the human sarco/endoplasmic reticulum Ca2+ATPase 3 gene
    • Identification
    • Bobe R, Bredoux R, Corvazier E, Andersen JP, Clausen JD, Dode L, Kovacs T, Enouf J. Identification, expression, function, and localization of a novel (sixth) isoform of the human sarco/endoplasmic reticulum Ca2+ATPase 3 gene. J Biol Chem. 279, 2004, 24297-24306.
    • (2004) J Biol Chem , vol.279 , pp. 24297-24306
    • Bobe, R.1    Bredoux, R.2    Corvazier, E.3    Andersen, J.P.4    Clausen, J.D.5    Dode, L.6    Kovacs, T.7    Enouf, J.8
  • 12
    • 0038515285 scopus 로고    scopus 로고
    • Insulin receptor substrate 1 regulation of sarco-endoplasmic reticulum calcium ATPase 3 in insulin-secreting beta-cells
    • Borge PD, Jr., Wolf BA. Insulin receptor substrate 1 regulation of sarco-endoplasmic reticulum calcium ATPase 3 in insulin-secreting beta-cells. J Biol Chem. 278, 2003, 11359-11368.
    • (2003) J Biol Chem , vol.278 , pp. 11359-11368
    • Borge Jr., P.D.1    Wolf, B.A.2
  • 14
    • 0022558845 scopus 로고
    • Two Ca2+ATPase genes: homologies andmechanistic implications of deduced amino acid sequences
    • Brandl CJ, Green NM, Korczak B, MacLennan DH. Two Ca2+ATPase genes: homologies andmechanistic implications of deduced amino acid sequences. Cell. 44, 1986, 597-607.
    • (1986) Cell , vol.44 , pp. 597-607
    • Brandl, C.J.1    Green, N.M.2    Korczak, B.3    MacLennan, D.H.4
  • 15
    • 70349653079 scopus 로고    scopus 로고
    • Calcium pumps in health and disease
    • BriniM, Carafoli E. Calcium pumps in health and disease. Physiol Rev. 89, 2009, 1341-1378.
    • (2009) Physiol Rev , vol.89 , pp. 1341-1378
    • Brini, M.1    Carafoli, E.2
  • 16
    • 0043092064 scopus 로고    scopus 로고
    • Acomparative functional analysis of plasma membrane Ca2+ pump isoforms in intact cells
    • BriniM, Coletto L, Pierobon N, KraevN, Guerini D, Carafoli E. Acomparative functional analysis of plasma membrane Ca2+ pump isoforms in intact cells. J Biol Chem. 278, 2003, 24500-24508.
    • (2003) J Biol Chem , vol.278 , pp. 24500-24508
    • Brini, M.1    Coletto, L.2    Pierobon, N.3    Kraev, N.4    Guerini, D.5    Carafoli, E.6
  • 17
    • 77957277448 scopus 로고    scopus 로고
    • Deletions and mutations in the acidic lipid-binding region of the plasma membrane Ca2+ pump: a study on different splicing variants of isoform 2
    • BriniM, Di Leva F, Ortega CK, Domi T, OttoliniD, Leonardi E, Tosatto SC, Carafoli E. Deletions and mutations in the acidic lipid-binding region of the plasma membrane Ca2+ pump: a study on different splicing variants of isoform 2. J Biol Chem. 285, 2010, 30779-30791.
    • (2010) J Biol Chem , vol.285 , pp. 30779-30791
    • Brini, M.1    Di Leva, F.2    Ortega, C.K.3    Domi, T.4    Ottolini, D.5    Leonardi, E.6    Tosatto, S.C.7    Carafoli, E.8
  • 18
    • 0026580488 scopus 로고
    • Identification of two domains which mediate the binding of activating phospholipids to the plasma-membrane Ca2+ pump
    • Brodin P, Falchetto R, Vorherr T, Carafoli E. Identification of two domains which mediate the binding of activating phospholipids to the plasma-membrane Ca2+ pump. Eur J Biochem. 204, 1992, 939-946.
    • (1992) Eur J Biochem , vol.204 , pp. 939-946
    • Brodin, P.1    Falchetto, R.2    Vorherr, T.3    Carafoli, E.4
  • 19
    • 0034646835 scopus 로고    scopus 로고
    • GRP94 (endoplasmin) co-purifies with and is phosphorylated by Golgi apparatus casein kinase
    • Brunati AM, Contri A, Muenchbach M, James P, Marin O, Pinna LA. GRP94 (endoplasmin) co-purifies with and is phosphorylated by Golgi apparatus casein kinase. FEBS Lett. 471, 2000, 151-155.
    • (2000) FEBS Lett , vol.471 , pp. 151-155
    • Brunati, A.M.1    Contri, A.2    Muenchbach, M.3    James, P.4    Marin, O.5    Pinna, L.A.6
  • 21
    • 0024441203 scopus 로고
    • cDNA cloning, functional expression, and mRNA tissue distribution of a third organellar Ca2+ pump
    • Burk SE, Lytton J, MacLennan DH, Shull GE. cDNA cloning, functional expression, and mRNA tissue distribution of a third organellar Ca2+ pump. J Biol Chem. 264, 1989, 18561-18568.
    • (1989) J Biol Chem , vol.264 , pp. 18561-18568
    • Burk, S.E.1    Lytton, J.2    MacLennan, D.H.3    Shull, G.E.4
  • 23
    • 0027231872 scopus 로고
    • Increased frequency of calcium waves in Xenopus laevis oocytes that express a calcium-ATPase
    • Camacho P, Lechleiter JD. Increased frequency of calcium waves in Xenopus laevis oocytes that express a calcium-ATPase. Science. 260, 1993, 226-229.
    • (1993) Science , vol.260 , pp. 226-229
    • Camacho, P.1    Lechleiter, J.D.2
  • 24
    • 0028113894 scopus 로고
    • Biogenesis: plasma membrane calcium ATPase: 15 years of work on the purified enzyme
    • Carafoli E. Biogenesis: plasma membrane calcium ATPase: 15 years of work on the purified enzyme. FASEB J. 8, 1994, 993-1002.
    • (1994) FASEB J , vol.8 , pp. 993-1002
    • Carafoli, E.1
  • 25
    • 62149106324 scopus 로고    scopus 로고
    • Physiological implications of the interaction between the plasma membrane calcium pump and nNOS
    • Cartwright EJ, Oceandy D, Neyses L. Physiological implications of the interaction between the plasma membrane calcium pump and nNOS. Pflugers Arch. 457, 2009, 665-671.
    • (2009) Pflugers Arch , vol.457 , pp. 665-671
    • Cartwright, E.J.1    Oceandy, D.2    Neyses, L.3
  • 27
    • 0026338163 scopus 로고
    • Milieu-induced, selective aggregation of regulated secretory proteins in the trans-Golgi network
    • Chanat E, Huttner WB. Milieu-induced, selective aggregation of regulated secretory proteins in the trans-Golgi network. J Cell Biol. 115, 1991, 1505-1519.
    • (1991) J Cell Biol , vol.115 , pp. 1505-1519
    • Chanat, E.1    Huttner, W.B.2
  • 28
    • 0038381495 scopus 로고    scopus 로고
    • Alternative splicing of the first intracellular loop of plasma membrane Ca2+-ATPase isoform 2 alters its membrane targeting
    • Chicka MC, Strehler EE. Alternative splicing of the first intracellular loop of plasma membrane Ca2+-ATPase isoform 2 alters its membrane targeting. J Biol Chem. 278, 2003, 18464-18470.
    • (2003) J Biol Chem , vol.278 , pp. 18464-18470
    • Chicka, M.C.1    Strehler, E.E.2
  • 30
    • 0024399371 scopus 로고
    • Location of high affinity Ca2+-binding sites within the predicted transmembrane domain of the sarcoplasmic reticulum Ca2+-ATPase
    • Clarke DM, Loo TW, Inesi G, MacLennan DH. Location of high affinity Ca2+-binding sites within the predicted transmembrane domain of the sarcoplasmic reticulum Ca2+-ATPase. Nature. 339, 1989, 476-478.
    • (1989) Nature , vol.339 , pp. 476-478
    • Clarke, D.M.1    Loo, T.W.2    Inesi, G.3    MacLennan, D.H.4
  • 31
    • 0025236388 scopus 로고
    • Functional consequences of alterations to polar amino acids located in the transmembrane domain of the Ca2(+)-ATPase of sarcoplasmic reticulum
    • Clarke DM, Loo TW, MacLennan DH. Functional consequences of alterations to polar amino acids located in the transmembrane domain of the Ca2(+)-ATPase of sarcoplasmic reticulum. J Biol Chem. 265, 1990, 6262-6267.
    • (1990) J Biol Chem , vol.265 , pp. 6262-6267
    • Clarke, D.M.1    Loo, T.W.2    MacLennan, D.H.3
  • 33
    • 0018401053 scopus 로고
    • Energy interconversion by the Ca2+-dependent ATPase of the sarcoplasmic reticulum
    • de Meis L, Vianna AL. Energy interconversion by the Ca2+-dependent ATPase of the sarcoplasmic reticulum. Annu Rev Biochem. 48, 1979, 275-292.
    • (1979) Annu Rev Biochem , vol.48 , pp. 275-292
    • de Meis, L.1    Vianna, A.L.2
  • 34
    • 1242352036 scopus 로고    scopus 로고
    • Plasma membrane Ca(2+)-ATPase (PMCA) translocates to filopodia during platelet activation
    • Dean WL, Whiteheart SW. Plasma membrane Ca(2+)-ATPase (PMCA) translocates to filopodia during platelet activation. Thromb Haemost. 91, 2004, 325-333.
    • (2004) Thromb Haemost , vol.91 , pp. 325-333
    • Dean, W.L.1    Whiteheart, S.W.2
  • 35
    • 0037155343 scopus 로고    scopus 로고
    • Plasma membrane Ca2+ ATPase isoform 2b interacts preferentially with Na+/H +exchanger regulatory factor 2 in apical plasma membranes
    • DeMarco SJ, Chicka MC, Strehler EE. Plasma membrane Ca2+ ATPase isoform 2b interacts preferentially with Na+/H +exchanger regulatory factor 2 in apical plasma membranes. J Biol Chem. 277, 2002, 10506-10511.
    • (2002) J Biol Chem , vol.277 , pp. 10506-10511
    • DeMarco, S.J.1    Chicka, M.C.2    Strehler, E.E.3
  • 36
    • 0035877655 scopus 로고    scopus 로고
    • Plasma membrane Ca2+-atpase isoforms 2b and 4b interact promiscuously and selectively with members of the membrane-associated guanylate kinase family of PDZ (PSD95/Dlg/ZO-1) domain-containing proteins
    • DeMarco SJ, Strehler EE. Plasma membrane Ca2+-atpase isoforms 2b and 4b interact promiscuously and selectively with members of the membrane-associated guanylate kinase family of PDZ (PSD95/Dlg/ZO-1) domain-containing proteins. J Biol Chem. 276, 2001, 21594-21600.
    • (2001) J Biol Chem , vol.276 , pp. 21594-21600
    • DeMarco, S.J.1    Strehler, E.E.2
  • 37
    • 0348111468 scopus 로고    scopus 로고
    • Dissection of the functional differences between sarco(endo)plasmic reticulum Ca2+-ATPase (SERCA) 1 and 2 isoforms and characterization of Darier disease (SERCA2) mutants by steady-state and transient kinetic analyses
    • Dode L, Andersen JP, Leslie N, Dhitavat J, Vilsen B, Hovnanian A. Dissection of the functional differences between sarco(endo)plasmic reticulum Ca2+-ATPase (SERCA) 1 and 2 isoforms and characterization of Darier disease (SERCA2) mutants by steady-state and transient kinetic analyses. J Biol Chem. 278, 2003, 47877-47889.
    • (2003) J Biol Chem , vol.278 , pp. 47877-47889
    • Dode, L.1    Andersen, J.P.2    Leslie, N.3    Dhitavat, J.4    Vilsen, B.5    Hovnanian, A.6
  • 38
    • 28244490516 scopus 로고    scopus 로고
    • Functional comparison between secretory pathway Ca2+/Mn2+-ATPase (SPCA) 1 and sarcoplasmic reticulum Ca2+-ATPase (SERCA) 1 isoforms by steady-state and transient kinetic analyses
    • Dode L, Andersen JP, Raeymaekers L, Missiaen L, Vilsen B, Wuytack F. Functional comparison between secretory pathway Ca2+/Mn2+-ATPase (SPCA) 1 and sarcoplasmic reticulum Ca2+-ATPase (SERCA) 1 isoforms by steady-state and transient kinetic analyses. J Biol Chem. 280, 2005, 39124-39134.
    • (2005) J Biol Chem , vol.280 , pp. 39124-39134
    • Dode, L.1    Andersen, J.P.2    Raeymaekers, L.3    Missiaen, L.4    Vilsen, B.5    Wuytack, F.6
  • 39
    • 33645633094 scopus 로고    scopus 로고
    • Dissection of the functional differences between human secretory pathway Ca2+/Mn2+-ATPase (SPCA) 1 and 2 isoenzymes by steady-state and transient kinetic analyses
    • Dode L, Andersen JP, Vanoevelen J, Raeymaekers L, Missiaen L, Vilsen B, Wuytack F. Dissection of the functional differences between human secretory pathway Ca2+/Mn2+-ATPase (SPCA) 1 and 2 isoenzymes by steady-state and transient kinetic analyses. J Biol Chem. 281, 2006, 3182-3189.
    • (2006) J Biol Chem , vol.281 , pp. 3182-3189
    • Dode, L.1    Andersen, J.P.2    Vanoevelen, J.3    Raeymaekers, L.4    Missiaen, L.5    Vilsen, B.6    Wuytack, F.7
  • 40
    • 2342614190 scopus 로고    scopus 로고
    • Drastic reduction of sarcalumenin in Dp427 (dystrophin of 427 kDa)-deficient fibres indicates that abnormal calcium handling plays a key role in muscular dystrophy
    • Dowling P, Doran P, Ohlendieck K. Drastic reduction of sarcalumenin in Dp427 (dystrophin of 427 kDa)-deficient fibres indicates that abnormal calcium handling plays a key role in muscular dystrophy. Biochem J. 379, 2004, 479-488.
    • (2004) Biochem J , vol.379 , pp. 479-488
    • Dowling, P.1    Doran, P.2    Ohlendieck, K.3
  • 41
    • 7444225717 scopus 로고    scopus 로고
    • Anti-apoptotic protein Bcl-2 interacts with and destabilizes the sarcoplasmic/ endoplasmic reticulum Ca2+-ATPase (SERCA)
    • Dremina ES, Sharov VS, Kumar K, Zaidi A, Michaelis EK, Schoneich C. Anti-apoptotic protein Bcl-2 interacts with and destabilizes the sarcoplasmic/ endoplasmic reticulum Ca2+-ATPase (SERCA). Biochem J. 383, 2004, 361-370.
    • (2004) Biochem J , vol.383 , pp. 361-370
    • Dremina, E.S.1    Sharov, V.S.2    Kumar, K.3    Zaidi, A.4    Michaelis, E.K.5    Schoneich, C.6
  • 43
    • 36949077764 scopus 로고
    • Removal of calcium and relaxation in actomyosin systems
    • Ebashi F, Ebashi S. Removal of calcium and relaxation in actomyosin systems. Nature. 194, 1962, 378-379.
    • (1962) Nature , vol.194 , pp. 378-379
    • Ebashi, F.1    Ebashi, S.2
  • 45
    • 0030610570 scopus 로고    scopus 로고
    • Plasma membrane Ca2+pump isoforms 2a and 2b are unusually responsive to calmodulin and Ca2+
    • Elwess NL, Filoteo AG, Enyedi A, Penniston JT. Plasma membrane Ca2+pump isoforms 2a and 2b are unusually responsive to calmodulin and Ca2+. J Biol Chem. 272, 1997, 17981-17986.
    • (1997) J Biol Chem , vol.272 , pp. 17981-17986
    • Elwess, N.L.1    Filoteo, A.G.2    Enyedi, A.3    Penniston, J.T.4
  • 46
    • 0025922159 scopus 로고
    • The plasma membrane Ca2+ pump contains a site that interacts with its calmodulin-binding domain
    • Falchetto R, Vorherr T, Brunner J, Carafoli E. The plasma membrane Ca2+ pump contains a site that interacts with its calmodulin-binding domain. J Biol Chem. 266, 1991, 2930-2936.
    • (1991) J Biol Chem , vol.266 , pp. 2930-2936
    • Falchetto, R.1    Vorherr, T.2    Brunner, J.3    Carafoli, E.4
  • 47
    • 0027069575 scopus 로고
    • The calmodulin-binding site of the plasma membrane Ca2+ pump interacts with the transduction domain of the enzyme
    • Falchetto R, Vorherr T, Carafoli E. The calmodulin-binding site of the plasma membrane Ca2+ pump interacts with the transduction domain of the enzyme. Protein Sci. 1, 1992, 1613-1621.
    • (1992) Protein Sci , vol.1 , pp. 1613-1621
    • Falchetto, R.1    Vorherr, T.2    Carafoli, E.3
  • 48
    • 0028898297 scopus 로고
    • Eosin a potent inhibitor of the plasma membrane Ca pump, does not inhibit the cardiac Na-Ca exchanger
    • Gatto C, Hale CC, Xu W, Milanick MA. Eosin, a potent inhibitor of the plasma membrane Ca pump, does not inhibit the cardiac Na-Ca exchanger. Biochemistry. 34, 1995, 965-972.
    • (1995) Biochemistry , vol.34 , pp. 965-972
    • Gatto, C.1    Hale, C.C.2    Xu, W.3    Milanick, M.A.4
  • 49
    • 0037418696 scopus 로고    scopus 로고
    • Identification of a new SERCA2 splice variant regulated during monocytic differentiation
    • Gelebart P, Martin V, Enouf J, Papp B. Identification of a new SERCA2 splice variant regulated during monocytic differentiation. Biochem Biophys Res Commun. 303, 2003, 676-684.
    • (2003) Biochem Biophys Res Commun , vol.303 , pp. 676-684
    • Gelebart, P.1    Martin, V.2    Enouf, J.3    Papp, B.4
  • 50
    • 0037564426 scopus 로고    scopus 로고
    • Characterization of PISP, a novel single-PDZ protein that binds to all plasma membrane Ca2+-ATPase b-splice variants
    • Goellner GM, DeMarco SJ, Strehler EE. Characterization of PISP, a novel single-PDZ protein that binds to all plasma membrane Ca2+-ATPase b-splice variants. Ann N Y Acad Sci. 986, 2003, 461-471.
    • (2003) Ann N Y Acad Sci , vol.986 , pp. 461-471
    • Goellner, G.M.1    DeMarco, S.J.2    Strehler, E.E.3
  • 51
    • 0017670545 scopus 로고
    • Phosphodiesterase protein activatormimics red blood cell cytoplasmic activator of (Ca2+-Mg2+)ATPase
    • Gopinath RM, Vincenzi FF. Phosphodiesterase protein activatormimics red blood cell cytoplasmic activator of (Ca2+-Mg2+)ATPase. Biochem Biophys Res Commun. 77, 1977, 1203-1209.
    • (1977) Biochem Biophys Res Commun , vol.77 , pp. 1203-1209
    • Gopinath, R.M.1    Vincenzi, F.F.2
  • 52
    • 46249123354 scopus 로고    scopus 로고
    • SERCA pump activity is physiologically regulated by presenilin and regulates amyloid beta production
    • Green KN, Demuro A, Akbari Y, Hitt BD, Smith IF, Parker I, LaFerla FM. SERCA pump activity is physiologically regulated by presenilin and regulates amyloid beta production. J Cell Biol. 181, 2008, 1107-1116.
    • (2008) J Cell Biol , vol.181 , pp. 1107-1116
    • Green, K.N.1    Demuro, A.2    Akbari, Y.3    Hitt, B.D.4    Smith, I.F.5    Parker, I.6    LaFerla, F.M.7
  • 54
    • 0000605334 scopus 로고    scopus 로고
    • The Calcium Pumps
    • In: Carafoli E, Klee C, editors. Oxford, UK: Oxford University Press
    • Guerini D, Carafoli, E. The Calcium Pumps. In: Carafoli E, Klee C, editors. Calcium as A Cellular Regulators. Oxford, UK: Oxford University Press, 1999, pp. 249-278, Vol. 10.
    • (1999) Calcium as A Cellular Regulators , vol.10 , pp. 249-278
    • Guerini, D.1    Carafoli, E.2
  • 55
    • 0021771056 scopus 로고
    • Stimulation of the purified erythrocyte Ca2+-ATPase by tryptic fragments of calmodulin
    • Guerini D, Krebs J, Carafoli E. Stimulation of the purified erythrocyte Ca2+-ATPase by tryptic fragments of calmodulin. J Biol Chem. 259, 1984, 15172-15177.
    • (1984) J Biol Chem , vol.259 , pp. 15172-15177
    • Guerini, D.1    Krebs, J.2    Carafoli, E.3
  • 56
    • 0034613260 scopus 로고    scopus 로고
    • Single amino acid mutations in transmembrane domain 5 confer to the plasma membrane Ca2+ pump properties typical of the Ca2+ pump of endo(sarco)plasmic reticulum
    • Guerini D, Zecca-Mazza A, Carafoli E. Single amino acid mutations in transmembrane domain 5 confer to the plasma membrane Ca2+ pump properties typical of the Ca2+ pump of endo(sarco)plasmic reticulum. J Biol Chem. 275, 2000, 31361-31368.
    • (2000) J Biol Chem , vol.275 , pp. 31361-31368
    • Guerini, D.1    Zecca-Mazza, A.2    Carafoli, E.3
  • 57
    • 0026786270 scopus 로고
    • Molecular cloning and tissue distribution of alternatively spliced mRNAs encoding possible mammalian homologues of the yeast secretory pathway calcium pump
    • Gunteski-Hamblin AM, Clarke DM, Shull GE. Molecular cloning and tissue distribution of alternatively spliced mRNAs encoding possible mammalian homologues of the yeast secretory pathway calcium pump. Biochemistry. 31, 1992, 7600-7608.
    • (1992) Biochemistry , vol.31 , pp. 7600-7608
    • Gunteski-Hamblin, A.M.1    Clarke, D.M.2    Shull, G.E.3
  • 58
    • 0028174326 scopus 로고
    • Ca2+/H +countertransport and electrogenicity in proteoliposomes containing erythrocyte plasma membrane Ca-ATPase and exogenous lipids
    • Hao L, Rigaud JL, Inesi G. Ca2+/H +countertransport and electrogenicity in proteoliposomes containing erythrocyte plasma membrane Ca-ATPase and exogenous lipids. J Biol Chem. 269, 1994, 14268-14275.
    • (1994) J Biol Chem , vol.269 , pp. 14268-14275
    • Hao, L.1    Rigaud, J.L.2    Inesi, G.3
  • 59
    • 72949126637 scopus 로고
    • [The calcium pump of the" relaxing granules" of muscle and its dependence on ATP-splitting]
    • Hasselbach W, Makinose M. [The calcium pump of the" relaxing granules" of muscle and its dependence on ATP-splitting.]. Biochem Z. 333, 1961, 518-528.
    • (1961) Biochem Z , vol.333 , pp. 518-528
    • Hasselbach, W.1    Makinose, M.2
  • 60
    • 0028080919 scopus 로고
    • Sarcoplasmic reticulum calcium pump in cardiac and slow twitch skeletal muscle but not fast twitch skeletal muscle undergoes phosphorylation by endogenous and exogenous Ca2+/calmodulin-dependent protein kinase Characterization of optimal conditions for calcium pump phosphorylation
    • Hawkins C, XuA, Narayanan N. Sarcoplasmic reticulum calcium pump in cardiac and slow twitch skeletal muscle but not fast twitch skeletal muscle undergoes phosphorylation by endogenous and exogenous Ca2+/calmodulin-dependent protein kinase. Characterization of optimal conditions for calcium pump phosphorylation. J Biol Chem. 269, 1994, 31198-31206.
    • (1994) J Biol Chem , vol.269 , pp. 31198-31206
    • Hawkins, C.1    Xu, A.2    Narayanan, N.3
  • 61
    • 0029935911 scopus 로고    scopus 로고
    • In vitro binding of clathrin adaptors to sorting signals correlates with endocytosis and basolateral sorting
    • Heilker R, Manning-Krieg U, Zuber JF, Spiess M. In vitro binding of clathrin adaptors to sorting signals correlates with endocytosis and basolateral sorting. EMBO J. 15, 1996, 2893-2899.
    • (1996) EMBO J , vol.15 , pp. 2893-2899
    • Heilker, R.1    Manning-Krieg, U.2    Zuber, J.F.3    Spiess, M.4
  • 62
    • 0028116583 scopus 로고
    • Cloning and expression of isoform 2 of the human plasma membrane Ca2+ ATPase Functional properties of the enzyme and its splicing products
    • Hilfiker H, Guerini D, Carafoli E. Cloning and expression of isoform 2 of the human plasma membrane Ca2+ ATPase. Functional properties of the enzyme and its splicing products. J Biol Chem. 269, 1994, 26178-26183.
    • (1994) J Biol Chem , vol.269 , pp. 26178-26183
    • Hilfiker, H.1    Guerini, D.2    Carafoli, E.3
  • 63
    • 0027231703 scopus 로고
    • The C-terminal domain of the plasma membrane Ca2+ pump contains three high affinity Ca2+ binding sites
    • Hofmann F, James P, Vorherr T, Carafoli E. The C-terminal domain of the plasma membrane Ca2+ pump contains three high affinity Ca2+ binding sites. J Biol Chem. 268, 1993, 10252-10259.
    • (1993) J Biol Chem , vol.268 , pp. 10252-10259
    • Hofmann, F.1    James, P.2    Vorherr, T.3    Carafoli, E.4
  • 65
    • 12244255136 scopus 로고    scopus 로고
    • A structural model of the complex formed by phospholamban and the calcium pump of sarcoplasmic reticulum obtained by molecular mechanics
    • Hutter MC, Krebs J, Meiler J, Griesinger C, Carafoli E, Helms V. A structural model of the complex formed by phospholamban and the calcium pump of sarcoplasmic reticulum obtained by molecular mechanics. Chembiochem. 3, 2002, 1200-1208.
    • (2002) Chembiochem , vol.3 , pp. 1200-1208
    • Hutter, M.C.1    Krebs, J.2    Meiler, J.3    Griesinger, C.4    Carafoli, E.5    Helms, V.6
  • 66
    • 0024429640 scopus 로고
    • Nature and site of phospholamban regulation of the Ca2+ pump of sarcoplasmic reticulum
    • James P, Inui M, Tada M, ChiesiM, Carafoli E. Nature and site of phospholamban regulation of the Ca2+ pump of sarcoplasmic reticulum. Nature. 342, 1989, 90-92.
    • (1989) Nature , vol.342 , pp. 90-92
    • James, P.1    Inui, M.2    Tada, M.3    Chiesi, M.4    Carafoli, E.5
  • 67
    • 0023872238 scopus 로고
    • Identification and primary structure of a calmodulin binding domain of the Ca2+ pump of human erythrocytes
    • James P, Maeda M, Fischer R, Verma AK, Krebs J, Penniston JT, Carafoli E. Identification and primary structure of a calmodulin binding domain of the Ca2+ pump of human erythrocytes. J Biol Chem. 263, 1988, 2905-2910.
    • (1988) J Biol Chem , vol.263 , pp. 2905-2910
    • James, P.1    Maeda, M.2    Fischer, R.3    Verma, A.K.4    Krebs, J.5    Penniston, J.T.6    Carafoli, E.7
  • 69
    • 0017622160 scopus 로고
    • Partial purification of the Ca2+-Mg2+ ATPase activator from human erythrocytes: its similarity to the activator of 3':5 - cyclic nucleotide phosphodiesterase
    • Jarrett HW, Penniston JT. Partial purification of the Ca2+-Mg2+ ATPase activator from human erythrocytes: its similarity to the activator of 3':5 - cyclic nucleotide phosphodiesterase. Biochem Biophys Res Commun. 77, 1977, 1210-1216.
    • (1977) Biochem Biophys Res Commun , vol.77 , pp. 1210-1216
    • Jarrett, H.W.1    Penniston, J.T.2
  • 70
    • 0032563599 scopus 로고    scopus 로고
    • Differential modulation of SERCA2 isoforms by calreticulin
    • John LM, Lechleiter JD, Camacho P. Differential modulation of SERCA2 isoforms by calreticulin. J Cell Biol. 142, 1998, 963-973.
    • (1998) J Cell Biol , vol.142 , pp. 963-973
    • John, L.M.1    Lechleiter, J.D.2    Camacho, P.3
  • 71
    • 0030032378 scopus 로고    scopus 로고
    • Cardiac-specific overexpression of phospholamban alters calcium kinetics and resultant cardiomyocyte mechanics in transgenic mice
    • Kadambi VJ, Ponniah S, Harrer JM, Hoit BD, Dorn GW, II, Walsh RA, Kranias EG. Cardiac-specific overexpression of phospholamban alters calcium kinetics and resultant cardiomyocyte mechanics in transgenic mice. J Clin Invest. 97, 1996, 533-539.
    • (1996) J Clin Invest , vol.97 , pp. 533-539
    • Kadambi, V.J.1    Ponniah, S.2    Harrer, J.M.3    Hoit, B.D.4    Dorn II, G.W.5    Walsh, R.A.6    Kranias, E.G.7
  • 73
    • 0028040761 scopus 로고
    • Depletion of manganese within the secretory pathway inhibits O-linked glycosylation in mammalian cells
    • Kaufman RJ, Swaroop M, Murtha-Riel P. Depletion of manganese within the secretory pathway inhibits O-linked glycosylation in mammalian cells. Biochemistry. 33, 1994, 9813-9819.
    • (1994) Biochemistry , vol.33 , pp. 9813-9819
    • Kaufman, R.J.1    Swaroop, M.2    Murtha-Riel, P.3
  • 74
    • 0027407886 scopus 로고
    • Alternative splicing of exons encoding the calmodulin-binding domains and C termini of plasma membrane Ca(2+)-ATPase isoforms 1 2 3 and 4
    • Keeton TP, Burk SE, Shull GE. Alternative splicing of exons encoding the calmodulin-binding domains and C termini of plasma membrane Ca(2+)-ATPase isoforms 1, 2, 3, and 4. J Biol Chem. 268, 1993, 2740-2748.
    • (1993) J Biol Chem , vol.268 , pp. 2740-2748
    • Keeton, T.P.1    Burk, S.E.2    Shull, G.E.3
  • 76
    • 0030989981 scopus 로고    scopus 로고
    • Phospholamban inhibitory function is activated by depolymerization
    • Kimura Y, Kurzydlowski K, TadaM, MacLennan DH. Phospholamban inhibitory function is activated by depolymerization. J Biol Chem. 272, 1997, 15061-15064.
    • (1997) J Biol Chem , vol.272 , pp. 15061-15064
    • Kimura, Y.1    Kurzydlowski, K.2    Tada, M.3    MacLennan, D.H.4
  • 78
    • 2542535432 scopus 로고    scopus 로고
    • Islet secretory defect in insulin receptor substrate 1 null mice is linked with reduced calcium signaling and expression of sarco(endo)plasmic reticulum Ca2+-ATPase (SERCA)-2b and -3
    • Kulkarni RN, Roper MG, Dahlgren G, Shih DQ, Kauri LM, Peters JL, Stoffel M, Kennedy RT. Islet secretory defect in insulin receptor substrate 1 null mice is linked with reduced calcium signaling and expression of sarco(endo)plasmic reticulum Ca2+-ATPase (SERCA)-2b and -3. Diabetes. 53, 2004, 1517-1525.
    • (2004) Diabetes , vol.53 , pp. 1517-1525
    • Kulkarni, R.N.1    Roper, M.G.2    Dahlgren, G.3    Shih, D.Q.4    Kauri, L.M.5    Peters, J.L.6    Stoffel, M.7    Kennedy, R.T.8
  • 79
    • 0032532213 scopus 로고    scopus 로고
    • Modulation of endoplasmic reticulum calcium pump by Bcl-2
    • Kuo TH, Kim HR, Zhu L, Yu Y, Lin HM, Tsang W. Modulation of endoplasmic reticulum calcium pump by Bcl-2. Oncogene. 17, 1998, 1903-1910.
    • (1998) Oncogene , vol.17 , pp. 1903-1910
    • Kuo, T.H.1    Kim, H.R.2    Zhu, L.3    Yu, Y.4    Lin, H.M.5    Tsang, W.6
  • 81
    • 0028889152 scopus 로고
    • Mutations in PMR1 suppress oxidative damage in yeast cells lacking superoxide dismutase
    • Lapinskas PJ, Cunningham KW, Liu XF, Fink GR, Culotta VC. Mutations in PMR1 suppress oxidative damage in yeast cells lacking superoxide dismutase. Mol Cell Biol. 15, 1995, 1382-1388.
    • (1995) Mol Cell Biol , vol.15 , pp. 1382-1388
    • Lapinskas, P.J.1    Cunningham, K.W.2    Liu, X.F.3    Fink, G.R.4    Culotta, V.C.5
  • 82
    • 0031019426 scopus 로고    scopus 로고
    • Rat liver Golgi apparatus contains a protein kinase similar to the casein kinase of lactating mammary gland
    • Lasa M, Marin O, Pinna LA. Rat liver Golgi apparatus contains a protein kinase similar to the casein kinase of lactating mammary gland. Eur J Biochem. 243, 1997, 719-725.
    • (1997) Eur J Biochem , vol.243 , pp. 719-725
    • Lasa, M.1    Marin, O.2    Pinna, L.A.3
  • 83
    • 67649391254 scopus 로고    scopus 로고
    • Cyclopiazonic acid is complexed to a divalent metal ion when bound to the sarcoplasmic reticulum Ca2+-ATPase
    • Laursen M, Bublitz M, Moncoq K, Olesen C, Moller JV, Young HS, Nissen P, Morth JP. Cyclopiazonic acid is complexed to a divalent metal ion when bound to the sarcoplasmic reticulum Ca2+-ATPase. J Biol Chem. 284, 2009, 13513-13518.
    • (2009) J Biol Chem , vol.284 , pp. 13513-13518
    • Laursen, M.1    Bublitz, M.2    Moncoq, K.3    Olesen, C.4    Moller, J.V.5    Young, H.S.6    Nissen, P.7    Morth, J.P.8
  • 84
    • 0347753252 scopus 로고    scopus 로고
    • Ca2+-dependent redox modulation of SERCA 2b by ERp57
    • Li Y, Camacho P. Ca2+-dependent redox modulation of SERCA 2b by ERp57. J Cell Biol. 164, 2004, 35-46.
    • (2004) J Cell Biol , vol.164 , pp. 35-46
    • Li, Y.1    Camacho, P.2
  • 86
    • 43449113547 scopus 로고    scopus 로고
    • Inhibitory interaction of the 14-3-3 proteins with ubiquitous (PMCA1) and tissue-specific (PMCA3) isoforms of the plasma membrane Ca2+ pump
    • Linde CI, Di Leva F, Domi T, Tosatto SC, Brini M, Carafoli E. Inhibitory interaction of the 14-3-3 proteins with ubiquitous (PMCA1) and tissue-specific (PMCA3) isoforms of the plasma membrane Ca2+ pump. Cell Calcium. 43, 2008, 550-561.
    • (2008) Cell Calcium , vol.43 , pp. 550-561
    • Linde, C.I.1    Di Leva, F.2    Domi, T.3    Tosatto, S.C.4    Brini, M.5    Carafoli, E.6
  • 87
    • 77952710840 scopus 로고    scopus 로고
    • Unique characteristics of Ca2+ homeostasis of the trans-Golgi compartment
    • Lissandron V, Podini P, Pizzo P, Pozzan T. Unique characteristics of Ca2+ homeostasis of the trans-Golgi compartment. Proc Natl Acad Sci U S A. 107, 2010, 9198-9203.
    • (2010) Proc Natl Acad Sci U S A , vol.107 , pp. 9198-9203
    • Lissandron, V.1    Podini, P.2    Pizzo, P.3    Pozzan, T.4
  • 89
    • 0027932798 scopus 로고
    • Targeted ablation of the phospholamban gene is associated with markedly enhanced myocardial contractility and loss of beta-agonist stimulation
    • LuoW, Grupp IL, Harrer J, Ponniah S, Grupp G, Duffy JJ, Doetschman T, Kranias EG. Targeted ablation of the phospholamban gene is associated with markedly enhanced myocardial contractility and loss of beta-agonist stimulation. Circ Res. 75, 1994, 401-409.
    • (1994) Circ Res , vol.75 , pp. 401-409
    • Luo, W.1    Grupp, I.L.2    Harrer, J.3    Ponniah, S.4    Grupp, G.5    Duffy, J.J.6    Doetschman, T.7    Kranias, E.G.8
  • 90
    • 0026691835 scopus 로고
    • Functional comparisons between isoforms of the sarcoplasmic or endoplasmic reticulum family of calcium pumps
    • Lytton J, Westlin M, Burk SE, Shull GE, MacLennan DH. Functional comparisons between isoforms of the sarcoplasmic or endoplasmic reticulum family of calcium pumps. J Biol Chem. 267, 1992, 14483-14489.
    • (1992) J Biol Chem , vol.267 , pp. 14483-14489
    • Lytton, J.1    Westlin, M.2    Burk, S.E.3    Shull, G.E.4    MacLennan, D.H.5
  • 91
    • 0026050850 scopus 로고
    • Thapsigargin inhibits the sarcoplasmic or endoplasmic reticulum Ca-ATPase family of calcium pumps
    • Lytton J, Westlin M, Hanley MR. Thapsigargin inhibits the sarcoplasmic or endoplasmic reticulum Ca-ATPase family of calcium pumps. J Biol Chem. 266, 1991, 17067-17071.
    • (1991) J Biol Chem , vol.266 , pp. 17067-17071
    • Lytton, J.1    Westlin, M.2    Hanley, M.R.3
  • 92
    • 0024549111 scopus 로고
    • Molecular cloning of the mammalian smooth muscle sarco(endo)plasmic reticulum Ca2+-ATPase
    • Lytton J, Zarain-HerzbergA, PeriasamyM, MacLennan DH. Molecular cloning of the mammalian smooth muscle sarco(endo)plasmic reticulum Ca2+-ATPase. J Biol Chem. 264, 1989, 7059-7065.
    • (1989) J Biol Chem , vol.264 , pp. 7059-7065
    • Lytton, J.1    Zarain-Herzberg, A.2    Periasamy, M.3    MacLennan, D.H.4
  • 93
    • 0033598739 scopus 로고    scopus 로고
    • Overlapping effects of S3 stalk segment mutations on the affinity of Ca2+-ATPase (SERCA) for thapsigargin and cyclopiazonic acid
    • Ma H, Zhong L, Inesi G, Fortea I, Soler F, Fernandez-Belda F. Overlapping effects of S3 stalk segment mutations on the affinity of Ca2+-ATPase (SERCA) for thapsigargin and cyclopiazonic acid. Biochemistry. 38, 1999, 15522-15527.
    • (1999) Biochemistry , vol.38 , pp. 15522-15527
    • Ma, H.1    Zhong, L.2    Inesi, G.3    Fortea, I.4    Soler, F.5    Fernandez-Belda, F.6
  • 94
    • 0014940130 scopus 로고
    • Purification and properties of an adenosine triphosphatase from sarcoplasmic reticulum
    • MacLennan DH. Purification and properties of an adenosine triphosphatase from sarcoplasmic reticulum. J Biol Chem. 245, 1970, 4508-4518.
    • (1970) J Biol Chem , vol.245 , pp. 4508-4518
    • MacLennan, D.H.1
  • 95
    • 0022371456 scopus 로고
    • Amino-acid sequence of a Ca2++Mg2+-dependent ATPase from rabbit muscle sarcoplasmic reticulum, deduced from its complementary DNA sequence
    • MacLennan DH, Brandl CJ, Korczak B, Green NM. Amino-acid sequence of a Ca2++Mg2+-dependent ATPase from rabbit muscle sarcoplasmic reticulum, deduced from its complementary DNA sequence. Nature. 316, 1985, 696-700.
    • (1985) Nature , vol.316 , pp. 696-700
    • MacLennan, D.H.1    Brandl, C.J.2    Korczak, B.3    Green, N.M.4
  • 97
    • 34248162457 scopus 로고    scopus 로고
    • The molecular basis for cyclopiazonic acid inhibition of the sarcoplasmic reticulum calcium pump
    • Moncoq K, Trieber CA, Young HS. The molecular basis for cyclopiazonic acid inhibition of the sarcoplasmic reticulum calcium pump. J Biol Chem. 282, 2007, 9748-9757.
    • (2007) J Biol Chem , vol.282 , pp. 9748-9757
    • Moncoq, K.1    Trieber, C.A.2    Young, H.S.3
  • 98
    • 0029563492 scopus 로고
    • The plasma membrane calcium pump-a physiological perspective on its regulation
    • Monteith GR, Roufogalis BD. The plasma membrane calcium pump-a physiological perspective on its regulation. Cell Calcium. 18, 1995, 459-470.
    • (1995) Cell Calcium , vol.18 , pp. 459-470
    • Monteith, G.R.1    Roufogalis, B.D.2
  • 100
    • 0034306417 scopus 로고    scopus 로고
    • Phospholamban remains associated with the Ca2+- andMg2+-dependent ATPase following phosphorylation by cAMP-dependent protein kinase
    • Negash S, Yao Q, Sun H, Li J, Bigelow DJ, Squier TC. Phospholamban remains associated with the Ca2+- andMg2+-dependent ATPase following phosphorylation by cAMP-dependent protein kinase. Biochem J. 351, 2000, 195-205.
    • (2000) Biochem J , vol.351 , pp. 195-205
    • Negash, S.1    Yao, Q.2    Sun, H.3    Li, J.4    Bigelow, D.J.5    Squier, T.C.6
  • 101
    • 0019828884 scopus 로고
    • ATP-dependent calcium transport by a Golgi-enriched membrane fraction from mouse mammary gland
    • Neville MC, Selker F, Semple K, Watters C. ATP-dependent calcium transport by a Golgi-enriched membrane fraction from mouse mammary gland. J Membr Biol. 61, 1981, 97-105.
    • (1981) J Membr Biol , vol.61 , pp. 97-105
    • Neville, M.C.1    Selker, F.2    Semple, K.3    Watters, C.4
  • 102
    • 0019822476 scopus 로고
    • Acidic phospholipids, unsaturated fatty acids, and limited proteolysis mimic the effect of calmodulin on the purified erythrocyte Ca2+-ATPase
    • Niggli V, Adunyah ES, Carafoli E. Acidic phospholipids, unsaturated fatty acids, and limited proteolysis mimic the effect of calmodulin on the purified erythrocyte Ca2+-ATPase. J Biol Chem. 256, 1981, 8588-8592.
    • (1981) J Biol Chem , vol.256 , pp. 8588-8592
    • Niggli, V.1    Adunyah, E.S.2    Carafoli, E.3
  • 103
    • 0019876575 scopus 로고
    • (Ca2+-Mg2+)-ATPase of the erythrocyte membrane Reconstitution and effect of calmodulin and phospholipids
    • Purified
    • Niggli V, Adunyah ES, Penniston JT, Carafoli E. Purified (Ca2+-Mg2+)-ATPase of the erythrocyte membrane. Reconstitution and effect of calmodulin and phospholipids. J Biol Chem. 256, 1981, 395-401.
    • (1981) J Biol Chem , vol.256 , pp. 395-401
    • Niggli, V.1    Adunyah, E.S.2    Penniston, J.T.3    Carafoli, E.4
  • 104
    • 0018654140 scopus 로고
    • Purification of the (Ca2+-Mg2+)-ATPase from human erythrocytemembranes using a calmodulin affinity column
    • Niggli V, Penniston JT, Carafoli E. Purification of the (Ca2+-Mg2+)-ATPase from human erythrocytemembranes using a calmodulin affinity column. J Biol Chem. 254, 1979, 9955-9958.
    • (1979) J Biol Chem , vol.254 , pp. 9955-9958
    • Niggli, V.1    Penniston, J.T.2    Carafoli, E.3
  • 105
    • 0020000695 scopus 로고
    • The purified Ca2+ pump of human erythrocyte membranes catalyzes an electroneutral Ca2+-H+ exchange in reconstituted liposomal systems
    • Niggli V, Sigel E, Carafoli E. The purified Ca2+ pump of human erythrocyte membranes catalyzes an electroneutral Ca2+-H+ exchange in reconstituted liposomal systems. J Biol Chem. 257, 1982, 2350-2356.
    • (1982) J Biol Chem , vol.257 , pp. 2350-2356
    • Niggli, V.1    Sigel, E.2    Carafoli, E.3
  • 106
    • 0026801231 scopus 로고
    • Calcium depletion blocks proteolytic cleavages of plasma protein precursors which occur at the Golgi and/or trans-Golgi network Possible involvement of Ca(2+)-dependent Golgi endoproteases
    • Oda K. Calcium depletion blocks proteolytic cleavages of plasma protein precursors which occur at the Golgi and/or trans-Golgi network. Possible involvement of Ca(2+)-dependent Golgi endoproteases.J Biol Chem. 267, 1992, 17465-17471.
    • (1992) iol Chem , vol.267 , pp. 17465-17471
    • Oda, K.1
  • 107
    • 0032524664 scopus 로고    scopus 로고
    • Sarcolipin regulates the activity of SERCA1, the fast-twitch skeletal muscle sarcoplasmic reticulum Ca2+-ATPase
    • Odermatt A, Becker S, Khanna VK, Kurzydlowski K, Leisner E, Pette D, MacLennan DH. Sarcolipin regulates the activity of SERCA1, the fast-twitch skeletal muscle sarcoplasmic reticulum Ca2+-ATPase. J Biol Chem. 273, 1998, 12360-12369.
    • (1998) J Biol Chem , vol.273 , pp. 12360-12369
    • Odermatt, A.1    Becker, S.2    Khanna, V.K.3    Kurzydlowski, K.4    Leisner, E.5    Pette, D.6    MacLennan, D.H.7
  • 108
    • 0029666260 scopus 로고    scopus 로고
    • The vmax of the Ca2+-ATPase of cardiac sarcoplasmic reticulum (SERCA2a) is not altered by Ca2+/calmodulin-dependent phosphorylation or by interaction with phospholamban
    • Odermatt A, KurzydlowskiK, MacLennan DH. The vmax of the Ca2+-ATPase of cardiac sarcoplasmic reticulum (SERCA2a) is not altered by Ca2+/calmodulin-dependent phosphorylation or by interaction with phospholamban. J Biol Chem. 271, 1996, 14206-14213.
    • (1996) J Biol Chem , vol.271 , pp. 14206-14213
    • Odermatt, A.1    Kurzydlowski, K.2    MacLennan, D.H.3
  • 109
    • 0025038977 scopus 로고
    • 5-Di-(tert-butyl)-1,4-benzohydroquinone mobilizes inositol 1,4 5-trisphosphate-sensitive and -insensitive Ca2+ stores
    • Oldershaw KA, Taylor CW. 2,5-Di-(tert-butyl)-1,4-benzohydroquinone mobilizes inositol 1,4,5-trisphosphate-sensitive and -insensitive Ca2+ stores. FEBS Lett. 274, 1990, 214-216.
    • (1990) FEBS Lett , vol.274 , pp. 214-216
    • Oldershaw, K.A.1    Taylor, C.W.2
  • 110
    • 34547120747 scopus 로고    scopus 로고
    • The plasma membrane calcium pump
    • In: Krebs J, Michalak M, editors. Oxford, UK: Elsevier
    • Ortega C, Ortolano, S, Carafoli, E. The plasma membrane calcium pump. In: Krebs J, Michalak M, editors. Calcium: A Matter of Life or Death, Oxford, UK: Elsevier, 2007, pp. 179-197, Vol. 41.
    • (2007) Calcium: A Matter of Life or Death , vol.41 , pp. 179-197
    • Ortega, C.1    Ortolano, S.2    Carafoli, E.3
  • 111
    • 33847025691 scopus 로고    scopus 로고
    • The role of phosphorylation on the structure and dynamics of phospholamban: a model from molecular simulations
    • Pantano S, Carafoli E. The role of phosphorylation on the structure and dynamics of phospholamban: a model from molecular simulations. Proteins. 66, 2007, 930-940.
    • (2007) Proteins , vol.66 , pp. 930-940
    • Pantano, S.1    Carafoli, E.2
  • 112
    • 33646830005 scopus 로고
    • Ion motive ATPases. I. Ubiquity, properties, and significance to cell function
    • Pedersen P, Carafoli, E. Ion motive ATPases. I. Ubiquity, properties, and significance to cell function. Trends Biochem Sci. 12, 1987, 146-150.
    • (1987) Trends Biochem Sci , vol.12 , pp. 146-150
    • Pedersen, P.1    Carafoli, E.2
  • 113
    • 0032530540 scopus 로고    scopus 로고
    • Modulation of the plasma membrane Ca2+ pump
    • Penniston JT, Enyedi A. Modulation of the plasma membrane Ca2+ pump. J Membr Biol. 165, 1998, 101-109.
    • (1998) J Membr Biol , vol.165 , pp. 101-109
    • Penniston, J.T.1    Enyedi, A.2
  • 114
    • 0030003266 scopus 로고    scopus 로고
    • Expression and functional characterization of isoforms 4 of the plasma membrane calcium pump
    • Preiano BS, Guerini D, Carafoli E. Expression and functional characterization of isoforms 4 of the plasma membrane calcium pump. Biochemistry. 35, 1996, 7946-7953.
    • (1996) Biochemistry , vol.35 , pp. 7946-7953
    • Preiano, B.S.1    Guerini, D.2    Carafoli, E.3
  • 115
    • 0347988217 scopus 로고    scopus 로고
    • Characterization of Cos-7 cells overexpressing the rat secretory pathway Ca2+-ATPase
    • Reinhardt TA, Horst RL, Waters WR. Characterization of Cos-7 cells overexpressing the rat secretory pathway Ca2+-ATPase. Am J Physiol Cell Physiol. 286, 2004, C164-C169.
    • (2004) Am J Physiol Cell Physiol , vol.286
    • Reinhardt, T.A.1    Horst, R.L.2    Waters, W.R.3
  • 116
    • 27744510789 scopus 로고    scopus 로고
    • Inhibitory interaction of the 14-3-3{epsilon} protein with isoform 4 of the plasma membrane Ca(2+)-ATPase pump
    • Rimessi A, Coletto L, Pinton P, Rizzuto R, Brini M, Carafoli E. Inhibitory interaction of the 14-3-3{epsilon} protein with isoform 4 of the plasma membrane Ca(2+)-ATPase pump. J Biol Chem. 280, 2005, 37195-37203.
    • (2005) J Biol Chem , vol.280 , pp. 37195-37203
    • Rimessi, A.1    Coletto, L.2    Pinton, P.3    Rizzuto, R.4    Brini, M.5    Carafoli, E.6
  • 117
    • 0034640960 scopus 로고    scopus 로고
    • Cytosolic phosphorylation of calnexin controls intracellular Ca(2+) oscillations via an interaction with SERCA2b
    • Roderick HL, Lechleiter JD, Camacho P. Cytosolic phosphorylation of calnexin controls intracellular Ca(2+) oscillations via an interaction with SERCA2b. J Cell Biol. 149, 2000, 1235-1248.
    • (2000) J Cell Biol , vol.149 , pp. 1235-1248
    • Roderick, H.L.1    Lechleiter, J.D.2    Camacho, P.3
  • 119
    • 0026708121 scopus 로고
    • Inesi G. Characterization of the inhibition of intracellular Ca2+ transport ATPases by thapsigargin
    • Sagara Y, Fernandez-Belda F, de Meis L, Inesi G. Characterization of the inhibition of intracellular Ca2+ transport ATPases by thapsigargin. J Biol Chem. 267, 1992, 12606-12613.
    • (1992) J Biol Chem , vol.267 , pp. 12606-12613
    • Sagara, Y.1    Fernandez-Belda F2    de Meis L3
  • 120
    • 0025737973 scopus 로고
    • Inhibition of the sarcoplasmic reticulum Ca2+transport ATPase by thapsigargin at subnanomolar concentrations
    • Sagara Y, Inesi G. Inhibition of the sarcoplasmic reticulum Ca2+transport ATPase by thapsigargin at subnanomolar concentrations. J Biol Chem. 266, 1991, 13503-13506.
    • (1991) J Biol Chem , vol.266 , pp. 13503-13506
    • Sagara, Y.1    Inesi, G.2
  • 122
    • 0014016755 scopus 로고
    • ATP-dependent Ca++-extrusion from human red cells
    • Schatzmann HJ. ATP-dependent Ca++-extrusion from human red cells. Experientia. 22, 1966, 364-365.
    • (1966) Experientia , vol.22 , pp. 364-365
    • Schatzmann, H.J.1
  • 124
    • 0038322052 scopus 로고    scopus 로고
    • Interaction of the plasma membrane Ca2+pump 4b/CI with the Ca2+/calmodulindependent membrane-associated kinase CASK
    • Schuh K, Uldrijan S, Gambaryan S, Roethlein N, Neyses L. Interaction of the plasma membrane Ca2+pump 4b/CI with the Ca2+/calmodulindependent membrane-associated kinase CASK. J Biol Chem. 278, 2003, 9778-9783.
    • (2003) JBiol Chem , vol.278 , pp. 9778-9783
    • Schuh, K.1    Uldrijan, S.2    Gambaryan, S.3    Roethlein, N.4    Neyses, L.5
  • 125
    • 0024427497 scopus 로고
    • Cyclopiazonic acid is a specific inhibitor of the Ca2+-ATPase of sarcoplasmic reticulum
    • Seidler NW, Jona I, Vegh M, Martonosi A. Cyclopiazonic acid is a specific inhibitor of the Ca2+-ATPase of sarcoplasmic reticulum. J Biol Chem. 264, 1989, 17816-17823.
    • (1989) J Biol Chem , vol.264 , pp. 17816-17823
    • Seidler, N.W.1    Jona, I.2    Vegh, M.3    Martonosi, A.4
  • 127
    • 0023874795 scopus 로고
    • Molecular cloning of two isoforms of the plasma membrane Ca2+-transporting ATPase from rat brain. Structural and functional domains exhibit similarity to Na+, K+- and other cation transport ATPases
    • Shull GE, Greeb J. Molecular cloning of two isoforms of the plasma membrane Ca2+-transporting ATPase from rat brain. Structural and functional domains exhibit similarity to Na+, K+- and other cation transport ATPases. J Biol Chem. 263, 1988, 8646-8657.
    • (1988) J Biol Chem , vol.263 , pp. 8646-8657
    • Shull, G.E.1    Greeb, J.2
  • 128
    • 0035137205 scopus 로고    scopus 로고
    • Role of alternative splicing in generating isoform diversity among plasma membrane calcium pumps
    • Strehler EE, Zacharias DA. Role of alternative splicing in generating isoform diversity among plasma membrane calcium pumps. Physiol Rev. 81, 2001, 21-50.
    • (2001) Physiol Rev , vol.81 , pp. 21-50
    • Strehler, E.E.1    Zacharias, D.A.2
  • 130
    • 0018166809 scopus 로고
    • Effects of lanthanum on calcium-dependent phenomena in human red cells
    • Szasz I, Sarkadi B, Schubert A, Gardos G. Effects of lanthanum on calcium-dependent phenomena in human red cells. Biochim Biophys Acta. 512, 1978, 331-340.
    • (1978) Biochim Biophys Acta , vol.512 , pp. 331-340
    • Szasz, I.1    Sarkadi, B.2    Schubert, A.3    Gardos, G.4
  • 131
    • 42049103001 scopus 로고    scopus 로고
    • Caloxins: a novel class of selective plasma membrane Ca2+ pump inhibitors obtained using biotechnology
    • SzewczykMM, Pande J, Grover AK. Caloxins: a novel class of selective plasma membrane Ca2+ pump inhibitors obtained using biotechnology. Pflugers Arch. 456, 2008, 255-266.
    • (2008) Pflugers Arch , vol.456 , pp. 255-266
    • Szewczyk, M.M.1    Pande, J.2    Grover, A.K.3
  • 132
    • 34347247711 scopus 로고    scopus 로고
    • Interdomain communication in calcium pump as revealed in the crystal structures with transmembrane inhibitors
    • TakahashiM, Kondou Y, Toyoshima C. Interdomain communication in calcium pump as revealed in the crystal structures with transmembrane inhibitors. Proc Natl Acad Sci U S A. 104, 2007, 5800-5805.
    • (2007) Proc Natl Acad Sci U S A , vol.104 , pp. 5800-5805
    • Takahashi, M.1    Kondou, Y.2    Toyoshima, C.3
  • 133
    • 0030822623 scopus 로고    scopus 로고
    • Characterization of the Golgi complex cleared of proteins in transit and examination of calcium uptake activities
    • Taylor RS, Jones SM, Dahl RH, Nordeen MH, Howell KE. Characterization of the Golgi complex cleared of proteins in transit and examination of calcium uptake activities. Mol Biol Cell. 8, 1997, 1911-1931.
    • (1997) Mol Biol Cell , vol.8 , pp. 1911-1931
    • Taylor, R.S.1    Jones, S.M.2    Dahl, R.H.3    Nordeen, M.H.4    Howell, K.E.5
  • 134
    • 0025332577 scopus 로고
    • Thapsigargin, a tumor promoter, discharges intracellular Ca2+ stores by specific inhibition of the endoplasmic reticulum Ca2(+)-ATPase
    • Thastrup O, Cullen PJ, Drobak BK, Hanley MR, Dawson AP. Thapsigargin, a tumor promoter, discharges intracellular Ca2+ stores by specific inhibition of the endoplasmic reticulum Ca2(+)-ATPase. Proc Natl Acad Sci U S A. 87, 1990, 2466-2470.
    • (1990) Proc Natl Acad Sci U S A , vol.87 , pp. 2466-2470
    • Thastrup, O.1    Cullen, P.J.2    Drobak, B.K.3    Hanley, M.R.4    Dawson, A.P.5
  • 135
    • 58349111168 scopus 로고    scopus 로고
    • The plasma membrane calcium ATPase (PMCA) of neurones is electroneutral and exchanges 2 H+ for each Ca2+ or Ba2+ ion extruded
    • Thomas RC. The plasma membrane calcium ATPase (PMCA) of neurones is electroneutral and exchanges 2 H+ for each Ca2+ or Ba2+ ion extruded. J Physiol. 587, 2009, 315-327.
    • (2009) J Physiol , vol.587 , pp. 315-327
    • Thomas, R.C.1
  • 136
    • 0027405626 scopus 로고
    • Identification of regions in the Ca(2+)-ATPase of sarcoplasmic reticulum that affect functional association with phospholamban
    • Toyofuku T, Kurzydlowski K, Tada M, MacLennan DH. Identification of regions in the Ca(2+)-ATPase of sarcoplasmic reticulum that affect functional association with phospholamban. J Biol Chem. 268, 1993, 2809-2815.
    • (1993) J Biol Chem , vol.268 , pp. 2809-2815
    • Toyofuku, T.1    Kurzydlowski, K.2    Tada, M.3    MacLennan, D.H.4
  • 137
    • 47049101464 scopus 로고    scopus 로고
    • Structural aspects of ion pumping by Ca2+-ATPase of sarcoplasmic reticulum
    • Toyoshima C. Structural aspects of ion pumping by Ca2+-ATPase of sarcoplasmic reticulum. Arch Biochem Biophys. 476, 2008, 3-11.
    • (2008) Arch Biochem Biophys , vol.476 , pp. 3-11
    • Toyoshima, C.1
  • 138
    • 47049101464 scopus 로고    scopus 로고
    • Structural aspects of ion pumping by Ca(2+)-ATPase of sarcoplasmic reticulum
    • Toyoshima C. Structural aspects of ion pumping by Ca(2+)-ATPase of sarcoplasmic reticulum. Arch Biochem Biophys. 476, 2008, 3-11.
    • (2008) Arch Biochem Biophys , vol.476 , pp. 3-11
    • Toyoshima, C.1
  • 140
    • 0034621834 scopus 로고    scopus 로고
    • Crystal structure of the calcium pump of sarcoplasmic reticulum at 2 6 A resolution
    • Toyoshima C, Nakasako M, Nomura H, Ogawa H. Crystal structure of the calcium pump of sarcoplasmic reticulum at 2.6 A resolution. Nature. 405, 2000, 647-655.
    • (2000) Nature , vol.405 , pp. 647-655
    • Toyoshima, C.1    Nakasako, M.2    Nomura, H.3    Ogawa, H.4
  • 141
    • 0037043709 scopus 로고    scopus 로고
    • Structural changes in the calcium pump accompanying the dissociation of calcium
    • Toyoshima C, Nomura H. Structural changes in the calcium pump accompanying the dissociation of calcium. Nature. 418, 2002, 605-611.
    • (2002) Nature , vol.418 , pp. 605-611
    • Toyoshima, C.1    Nomura, H.2
  • 146
    • 0031976097 scopus 로고    scopus 로고
    • Factors controlling the glycosylation potential of the Golgi apparatus
    • Varki A. Factors controlling the glycosylation potential of the Golgi apparatus. Trends Cell Biol. 8, 1998, 34-40.
    • (1998) Trends Cell Biol , vol.8 , pp. 34-40
    • Varki, A.1
  • 147
    • 0035955750 scopus 로고    scopus 로고
    • Replacement of the muscle-specific sarcoplasmic reticulum Ca(2+)-ATPase isoform SERCA2a by the nonmuscle SERCA2b homologue causes mild concentric hypertrophy and impairs contraction-relaxation of the heart
    • Ver Heyen M, Heymans S, Antoons G, Reed T, Periasamy M, Awede B, Lebacq J, Vangheluwe P, Dewerchin M, Collen D, Sipido K, Carmeliet P, Wuytack F. Replacement of the muscle-specific sarcoplasmic reticulum Ca(2+)-ATPase isoform SERCA2a by the nonmuscle SERCA2b homologue causes mild concentric hypertrophy and impairs contraction-relaxation of the heart. Circ Res. 89, 2001, 838-846.
    • (2001) Circ Res , vol.89 , pp. 838-846
    • Ver Heyen, M.1    Heymans, S.2    Antoons, G.3    Reed, T.4    Periasamy, M.5    Awede, B.6    Lebacq, J.7    Vangheluwe, P.8    Dewerchin, M.9    Collen, D.10    Sipido, K.11    Carmeliet, P.12    Wuytack, F.13
  • 148
    • 0026794257 scopus 로고
    • Functional difference between SERCA2a and SERCA2b Ca2+ pumps and their modulation by phospholamban
    • Verboomen H, Wuytack F, De Smedt H, Himpens B, Casteels R. Functional difference between SERCA2a and SERCA2b Ca2+ pumps and their modulation by phospholamban. Biochem J 286 (Pt 2): 591-595, 1992.
    • (1992) Biochem J , vol.286 , Issue.PART 2 , pp. 591-595
    • Verboomen, H.1    Wuytack, F.2    De Smedt, H.3    Himpens, B.4    Casteels, R.5
  • 149
    • 0028116070 scopus 로고
    • The functional importance of the extreme C-terminal tail in the gene 2 organellar Ca(2+)-transport ATPase (SERCA2a/b)
    • Verboomen H, Wuytack F, Van den Bosch L, Mertens L, Casteels R. The functional importance of the extreme C-terminal tail in the gene 2 organellar Ca(2+)-transport ATPase (SERCA2a/b). Biochem J 303 (Pt 3): 979-984, 1994.
    • (1994) Biochem J , vol.303 , Issue.PART 3 , pp. 979-984
    • Verboomen, H.1    Wuytack, F.2    Van den Bosch, L.3    Mertens, L.4    Casteels, R.5
  • 151
    • 0021894412 scopus 로고
    • Ca2+ transport and Ca2+-dependent ATP hydrolysis by Golgi vesicles from lactating rat mammary glands
    • Virk SS, Kirk CJ, Shears SB. Ca2+ transport and Ca2+-dependent ATP hydrolysis by Golgi vesicles from lactating rat mammary glands. Biochem J. 226, 1985, 741-748.
    • (1985) Biochem J , vol.226 , pp. 741-748
    • Virk, S.S.1    Kirk, C.J.2    Shears, S.B.3
  • 152
    • 0033134009 scopus 로고    scopus 로고
    • Human calumenin localizes to the secretory pathway and is secreted to the medium
    • Vorum H, Hager H, Christensen BM, Nielsen S, Honore B. Human calumenin localizes to the secretory pathway and is secreted to the medium. Exp Cell Res. 248, 1999, 473-481.
    • (1999) Exp Cell Res , vol.248 , pp. 473-481
    • Vorum, H.1    Hager, H.2    Christensen, B.M.3    Nielsen, S.4    Honore, B.5
  • 153
    • 2442561408 scopus 로고    scopus 로고
    • Mint-3 regulates the retrieval of the internalized membrane-type matrix metalloproteinase, MT5-MMP, to the plasma membrane by binding to its carboxyl end motif EWV
    • Wang P, Wang X, PeiD. Mint-3 regulates the retrieval of the internalized membrane-type matrix metalloproteinase, MT5-MMP, to the plasma membrane by binding to its carboxyl end motif EWV. J Biol Chem. 279, 2004, 20461-20470.
    • (2004) J Biol Chem , vol.279 , pp. 20461-20470
    • Wang, P.1    Wang, X.2    Pei, D.3
  • 154
    • 0021646760 scopus 로고
    • Ca2+-stimulated adenosine triphosphatase in Golgienriched membranes of lactating murine mammary tissue
    • Watters CD. A Ca2+-stimulated adenosine triphosphatase in Golgienriched membranes of lactating murine mammary tissue. Biochem J. 224, 1984, 39-45.
    • (1984) Biochem J , vol.224 , pp. 39-45
    • Watters, C.D.A.1
  • 155
    • 0034604602 scopus 로고    scopus 로고
    • Phenotypic screening of mutations in Pmr1, the yeast secretory pathway Ca2+/Mn2+-ATPase, reveals residues critical for ion selectivity and transport
    • Wei Y, Chen J, Rosas G, Tompkins DA, Holt PA, Rao R. Phenotypic screening of mutations in Pmr1, the yeast secretory pathway Ca2+/Mn2+-ATPase, reveals residues critical for ion selectivity and transport. J Biol Chem. 275, 2000, 23927-23932.
    • (2000) J Biol Chem , vol.275 , pp. 23927-23932
    • Wei, Y.1    Chen, J.2    Rosas, G.3    Tompkins, D.A.4    Holt, P.A.5    Rao, R.6
  • 156
    • 0033517785 scopus 로고    scopus 로고
    • An N-terminal EF hand-like motif modulates ion transport by Pmr1, the yeast Golgi Ca(2+)/Mn(2+)-ATPase
    • Wei Y, Marchi V, Wang R, Rao R. An N-terminal EF hand-like motif modulates ion transport by Pmr1, the yeast Golgi Ca(2+)/Mn(2+)-ATPase. Biochemistry. 38, 1999, 14534-14541.
    • (1999) Biochemistry , vol.38 , pp. 14534-14541
    • Wei, Y.1    Marchi, V.2    Wang, R.3    Rao, R.4
  • 157
    • 0019461644 scopus 로고
    • Energy-dependent calcium sequestration activity in a Golgi apparatus fraction derived from lactating rat mammary glands
    • West DW. Energy-dependent calcium sequestration activity in a Golgi apparatus fraction derived from lactating rat mammary glands. Biochim Biophys Acta. 673, 1981, 374-386.
    • (1981) Biochim Biophys Acta , vol.673 , pp. 374-386
    • West, D.W.1
  • 158
    • 0021325903 scopus 로고
    • Casein kinase activity in rat mammary gland Golgi vesicles Demonstration of latency and requirement for a transmembrane ATP carrier.
    • West DW, Clegg RA. Casein kinase activity in rat mammary gland Golgi vesicles. Demonstration of latency and requirement for a transmembrane ATP carrier. Biochem J. 219, 1984, 181-187.
    • (1984) Biochem J , vol.219 , pp. 181-187
    • West, D.W.1    Clegg, R.A.2
  • 161
    • 15744398885 scopus 로고    scopus 로고
    • A novel isoform of the secretory pathway Ca2+, Mn(2+)-ATPase, hSPCA2, has unusual properties and is expressed in the brain
    • Xiang M, Mohamalawari D, Rao R. A novel isoform of the secretory pathway Ca2+, Mn(2+)-ATPase, hSPCA2, has unusual properties and is expressed in the brain. J Biol Chem. 280, 2005, 11608-11614.
    • (2005) J Biol Chem , vol.280 , pp. 11608-11614
    • Xiang, M.1    Mohamalawari, D.2    Rao, R.3
  • 162
    • 0027468913 scopus 로고
    • Phosphorylation and activation of the Ca(2+)-pumping ATPase of cardiac sarcoplasmic reticulum by Ca2+/calmodulin-dependent protein kinase
    • Xu A, Hawkins C, Narayanan N. Phosphorylation and activation of the Ca(2+)-pumping ATPase of cardiac sarcoplasmic reticulum by Ca2+/calmodulin-dependent protein kinase. J Biol Chem. 268, 1993, 8394-8397.
    • (1993) J Biol Chem , vol.268 , pp. 8394-8397
    • Xu, A.1    Hawkins, C.2    Narayanan, N.3
  • 163
    • 0034610307 scopus 로고    scopus 로고
    • Insulin regulation of beta-cell function involves a feedback loop on SERCA gene expression, Ca(2+) homeostasis, and insulin expression and secretion
    • Xu GG, Gao ZY, Borge PD, Jr., Jegier PA, Young RA, Wolf BA. Insulin regulation of beta-cell function involves a feedback loop on SERCA gene expression, Ca(2+) homeostasis, and insulin expression and secretion. Biochemistry. 39, 2000, 14912-14919.
    • (2000) Biochemistry , vol.39 , pp. 14912-14919
    • Xu, G.G.1    Gao, Z.Y.2    Borge Jr., P.D.3    Jegier, P.A.4    Young, R.A.5    Wolf, B.A.6
  • 164
    • 0032488978 scopus 로고    scopus 로고
    • Specific substitutions at amino acid 256 of the sarcoplasmic/endoplasmic reticulum Ca2+ transport ATPase mediate resistance to thapsigargin in thapsigargin-resistant hamster cells
    • Yu M, Zhong L, Rishi AK, Khadeer M, Inesi G, Hussain A. Specific substitutions at amino acid 256 of the sarcoplasmic/endoplasmic reticulum Ca2+ transport ATPase mediate resistance to thapsigargin in thapsigargin-resistant hamster cells. J Biol Chem. 273, 1998, 3542-3546.
    • (1998) J Biol Chem , vol.273 , pp. 3542-3546
    • Yu, M.1    Zhong, L.2    Rishi, A.K.3    Khadeer, M.4    Inesi, G.5    Hussain, A.6
  • 165
    • 0027266757 scopus 로고
    • H+ countertransport and electrogenicity of the sarcoplasmic reticulum Ca2+ pump in reconstituted proteoliposomes
    • Yu X, Carroll S, Rigaud JL, Inesi G. H+ countertransport and electrogenicity of the sarcoplasmic reticulum Ca2+ pump in reconstituted proteoliposomes. Biophys J. 64, 1993, 1232-1242.
    • (1993) Biophys J , vol.64 , pp. 1232-1242
    • Yu, X.1    Carroll, S.2    Rigaud, J.L.3    Inesi, G.4
  • 166
    • 0024996453 scopus 로고
    • Mapping of functional domains in the plasma membrane Ca2+ pump using trypsin proteolysis
    • Zvaritch E, James P, Vorherr T, Falchetto R, Modyanov N, Carafoli E. Mapping of functional domains in the plasma membrane Ca2+ pump using trypsin proteolysis. Biochemistry. 29, 1990, 8070-8076.
    • (1990) Biochemistry , vol.29 , pp. 8070-8076
    • Zvaritch, E.1    James, P.2    Vorherr, T.3    Falchetto, R.4    Modyanov, N.5    Carafoli, E.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.