메뉴 건너뛰기




Volumn 287, Issue 34, 2012, Pages 28336-28348

Ca2+ induces spontaneous dephosphorylation of a novel P5A-type ATPase

Author keywords

[No Author keywords available]

Indexed keywords

ARABIDOPSIS THALIANA; ATPASES; BIOCHEMICAL FUNCTIONS; CATALYTIC RESIDUE; CYTOSOLIC; DEPHOSPHORYLATIONS; ENDOPLASMIC RETICULUM; EUKARYOTIC GENOME; ION PUMPS; KNOCKOUT MUTANT; P-TYPE; PHOSPHOENZYME; PLANT NUTRIENTS; PUTATIVE BINDING SITES; REACTION CYCLES;

EID: 84865262163     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M112.387191     Document Type: Article
Times cited : (15)

References (58)
  • 1
    • 0031964372 scopus 로고    scopus 로고
    • Evolution of substrate specificities in the P-type ATPase superfamily
    • DOI 10.1007/PL00006286
    • Axelsen, K. B., and Palmgren, M. G. (1998) Evolution of substrate specificities in the P-type ATPase superfamily. J. Mol. Evol. 46, 84-101 (Pubitemid 28047242)
    • (1998) Journal of Molecular Evolution , vol.46 , Issue.1 , pp. 84-101
    • Axelsen, K.B.1    Palmgren, M.G.2
  • 2
    • 39149124100 scopus 로고    scopus 로고
    • Phylogenetic analysis of P5 P-type ATPases, a eukaryotic lineage of secretory pathway pumps
    • Møller, A. B., Asp, T., Holm, P. B., and Palmgren, M. G. (2008) Phylogenetic analysis of P5 P-type ATPases, a eukaryotic lineage of secretory pathway pumps. Mol. Phylogenet. Evol. 46, 619-634
    • (2008) Mol. Phylogenet. Evol. , vol.46 , pp. 619-634
    • Møller, A.B.1    Asp, T.2    Holm, P.B.3    Palmgren, M.G.4
  • 4
    • 21444440293 scopus 로고    scopus 로고
    • Characterization of a novel cation transporter ATPase gene (ATP13A4) interrupted by 3q25-q29 inversion in an individual with language delay
    • DOI 10.1016/j.ygeno.2005.04.002, PII S0888754305000947
    • Kwasnicka-Crawford, D. A., Carson, A. R., Roberts, W., Summers, A. M., Rehnström, K., Järvelä, I., and Scherer, S. W. (2005) Characterization of a novel cation transporter ATPase gene (ATP13A4) interrupted by 3q25-q29 inversion in an individual with language delay. Genomics 86, 182-194 (Pubitemid 40917223)
    • (2005) Genomics , vol.86 , Issue.2 , pp. 182-194
    • Kwasnicka-Crawford, D.A.1    Carson, A.R.2    Roberts, W.3    Summers, A.M.4    Rehnstrom, K.5    Jarvela, I.6    Scherer, S.W.7
  • 5
    • 0037160521 scopus 로고    scopus 로고
    • Cloning the AFURS1 gene which is up-regulated in senescent human parenchymal kidney cells
    • DOI 10.1016/S0378-1119(01)00881-2, PII S0378111901008812
    • Habtemichael, N., and Kovacs, G. (2002) Cloning the AFURS1 gene, which is up-regulated in senescent human parenchymal kidney cells. Gene 283, 271-275 (Pubitemid 34178531)
    • (2002) Gene , vol.283 , Issue.1-2 , pp. 271-275
    • Habtemichael, N.1    Kovacs, G.2
  • 6
    • 3242701547 scopus 로고    scopus 로고
    • Biology, structure, and mechanism of P-type ATPases
    • Kühlbrandt, W. (2004) Biology, structure, and mechanism of P-type ATPases. Nat. Rev. Mol. Cell Biol. 5, 282-295
    • (2004) Nat. Rev. Mol. Cell Biol. , vol.5 , pp. 282-295
    • Kühlbrandt, W.1
  • 9
    • 79951681214 scopus 로고    scopus 로고
    • The sarcoplasmic Ca2+-ATPase. Design of a perfect chemi-osmotic pump
    • Møller, J. V., Olesen, C., Winther, A. M., and Nissen, P. (2010) The sarcoplasmic Ca2+-ATPase. Design of a perfect chemi-osmotic pump. Q. Rev. Biophys. 43, 501-566
    • (2010) Q. Rev. Biophys. , vol.43 , pp. 501-566
    • Møller, J.V.1    Olesen, C.2    Winther, A.M.3    Nissen, P.4
  • 11
    • 0034611014 scopus 로고    scopus 로고
    • Regulation of HMG-CoA reductase degradation requires the P-type ATPase Cod1p/Spf1p
    • Cronin, S. R., Khoury, A., Ferry, D. K., and Hampton, R. Y. (2000) Regulation of HMG-CoA reductase degradation requires the P-type ATPase Cod1p/Spf1p. J. Cell Biol. 148, 915-924
    • (2000) J. Cell Biol. , vol.148 , pp. 915-924
    • Cronin, S.R.1    Khoury, A.2    Ferry, D.K.3    Hampton, R.Y.4
  • 12
    • 0037054541 scopus 로고    scopus 로고
    • 2+ homeostasis
    • DOI 10.1083/jcb.200203052
    • Cronin, S. R., Rao, R., and Hampton, R. Y. (2002) Cod1p/Spf1p is a P-type ATPase involved in ER function and Ca2+ homeostasis. J. Cell Biol. 157, 1017-1028 (Pubitemid 34839776)
    • (2002) Journal of Cell Biology , vol.157 , Issue.6 , pp. 1017-1028
    • Cronin, S.R.1    Rao, R.2    Hampton, R.Y.3
  • 13
    • 27744488764 scopus 로고    scopus 로고
    • Pollen development and fertilization in Arabidopsis is dependent on the MALE GAMETOGENESIS IMPAIRED ANTHERS gene encoding a Type V P-type ATPase
    • DOI 10.1101/gad.357305
    • Jakobsen, M. K., Poulsen, L. R., Schulz, A., Fleurat-Lessard, P., Møller, A., Husted, S., Schiøtt, M., Amtmann, A., and Palmgren, M. G. (2005) Pollen development and fertilization in Arabidopsis is dependent on the MALE GAMETOGENESIS IMPAIRED ANTHERS gene encoding a type V Ptype ATPase. Genes Dev. 19, 2757-2769 (Pubitemid 41627941)
    • (2005) Genes and Development , vol.19 , Issue.22 , pp. 2757-2769
    • Jakobsen, M.K.1    Poulsen, L.R.2    Schulz, A.3    Fleurat-Lessard, P.4    Moller, A.5    Husted, S.6    Schiott, M.7    Amtmann, A.8    Palmgren, M.G.9
  • 14
    • 1842832344 scopus 로고    scopus 로고
    • Two distinctly localized P-type ATPases collaborate to maintain organelle homeostasis required for glycoprotein processing and quality control
    • DOI 10.1091/mbc.02-06-0090
    • Vashist, S., Frank, C. G., Jakob, C. A., and Ng, D. T. (2002) Two distinctly localized P-type ATPases collaborate to maintain organelle homeostasis required for glycoprotein processing and quality control. Mol. Biol. Cell 13, 3955-3966 (Pubitemid 35398562)
    • (2002) Molecular Biology of the Cell , vol.13 , Issue.11 , pp. 3955-3966
    • Vashist, S.1    Frank, C.G.2    Jakob, C.A.3    Ng, D.T.W.4
  • 15
    • 0037054553 scopus 로고    scopus 로고
    • The endoplasmic reticulum cation P-type ATPase Cta4p is required for control of cell shape and microtubule dynamics
    • Façanha, A. L., Appelgren, H., Tabish, M., Okorokov, L., and Ekwall, K. (2002) The endoplasmic reticulum cation P-type ATPase Cta4p is required for control of cell shape and microtubule dynamics. J. Cell Biol. 157, 1029-1039
    • (2002) J. Cell Biol. , vol.157 , pp. 1029-1039
    • Façanha, A.L.1    Appelgren, H.2    Tabish, M.3    Okorokov, L.4    Ekwall, K.5
  • 17
    • 0036223875 scopus 로고    scopus 로고
    • Yeast genes controlling responses to topogenic signals in a model transmembrane protein
    • DOI 10.1091/mbc.01-10-0488
    • Tipper, D. J., and Harley, C. A. (2002) Yeast genes controlling responses to topogenic signals in a model transmembrane protein. Mol. Biol. Cell 13, 1158-1174 (Pubitemid 34309613)
    • (2002) Molecular Biology of the Cell , vol.13 , Issue.4 , pp. 1158-1174
    • Tipper, D.J.1    Harley, C.A.2
  • 18
    • 0033011212 scopus 로고    scopus 로고
    • P-type ATPase spf1 mutants show a novel resistance mechanism for the killer toxin SMKT
    • DOI 10.1046/j.1365-2958.1999.01400.x
    • Suzuki, C., and Shimma, Y. I. (1999) P-type ATPase spf1 mutants show a novel resistance mechanism for the killer toxin SMKT. Mol. Microbiol. 32, 813-823 (Pubitemid 29241521)
    • (1999) Molecular Microbiology , vol.32 , Issue.4 , pp. 813-823
    • Suzuki, C.1    Shimma, Y.-I.2
  • 19
    • 0035697185 scopus 로고    scopus 로고
    • Interaction of SMKT, a killer toxin produced by Pichia farinosa, with the yeast cell membranes
    • DOI 10.1002/yea.791
    • Suzuki, C., Ando, Y., and Machida, S. (2001) Interaction of SMKT, a killer toxin produced by Pichia farinosa, with the yeast cell membranes. Yeast 18, 1471-1478 (Pubitemid 34083127)
    • (2001) Yeast , vol.18 , Issue.16 , pp. 1471-1478
    • Suzuki, C.1    Ando, Y.2    Machida, S.3
  • 20
    • 0035523645 scopus 로고    scopus 로고
    • Immunochemical and mutational analyses of P-type ATPase Spf1p involved in the yeast secretory pathway
    • Suzuki, C. (2001) Immunochemical and mutational analyses of P-type ATPase Spf1p involved in the yeast secretory pathway. Biosci. Biotechnol. Biochem. 65, 2405-2411
    • (2001) Biosci. Biotechnol. Biochem. , vol.65 , pp. 2405-2411
    • Suzuki, C.1
  • 22
    • 0032447801 scopus 로고    scopus 로고
    • Floral dip. A simplified method for Agrobacterium-mediated transformation of Arabidopsis thaliana
    • Clough, S. J., and Bent, A. F. (1998) Floral dip. A simplified method for Agrobacterium-mediated transformation of Arabidopsis thaliana. Plant J. 16, 735-743
    • (1998) Plant J. , vol.16 , pp. 735-743
    • Clough, S.J.1    Bent, A.F.2
  • 23
    • 84982358134 scopus 로고
    • A revised medium for rapid growth and bioassays with tobacco tissue cultures
    • Murashige, T., and Skoog, F. (1962) A revised medium for rapid growth and bioassays with tobacco tissue cultures. Physiol. Plant. 15, 473-497
    • (1962) Physiol. Plant. , vol.15 , pp. 473-497
    • Murashige, T.1    Skoog, F.2
  • 24
    • 0142245636 scopus 로고    scopus 로고
    • A Gateway Cloning Vector Set for High-Throughput Functional Analysis of Genes in Planta
    • DOI 10.1104/pp.103.027979
    • Curtis, M. D., and Grossniklaus, U. (2003)Agateway cloning vector set for high throughput functional analysis of genes in planta. Plant Physiol. 133, 462-469 (Pubitemid 37325657)
    • (2003) Plant Physiology , vol.133 , Issue.2 , pp. 462-469
    • Curtis, M.D.1    Grossniklaus, U.2
  • 25
    • 29344456761 scopus 로고    scopus 로고
    • Photoactivation of GFP reveals protein dynamics within the endoplasmic reticulum membrane
    • DOI 10.1093/jxb/eri289
    • Runions, J., Brach, T., Kühner, S., and Hawes, C. (2006) Photoactivation of GFP reveals protein dynamics within the endoplasmic reticulum membrane. J. Exp. Bot. 57, 43-50 (Pubitemid 43007126)
    • (2006) Journal of Experimental Botany , vol.57 , Issue.1 , pp. 43-50
    • Runions, J.1    Brach, T.2    Kuhner, S.3    Hawes, C.4
  • 26
    • 0020529962 scopus 로고
    • Transformation of intact yeast cells treated with alkali cations
    • Ito, H., Fukuda, Y., Murata, K., and Kimura, A. (1983) Transformation of intact yeast-cells treated with alkali cations. J. Bacteriol. 153, 163-168 (Pubitemid 13119852)
    • (1983) Journal of Bacteriology , vol.153 , Issue.1 , pp. 163-168
    • Ito, H.1    Fukuda, Y.2    Murata, K.3    Kimura, A.4
  • 27
    • 0022978478 scopus 로고
    • Molecular characterization of the in situ red cell membrane calcium pump by limited proteolysis
    • Sarkadi, B., Enyedi, A., Földes-Papp, Z., and Gárdos, G. (1986) Molecular characterization of the in situ red cell membrane calcium pump by limited proteolysis. J. Biol. Chem. 261, 9552-9557 (Pubitemid 17218248)
    • (1986) Journal of Biological Chemistry , vol.261 , Issue.20 , pp. 9552-9557
    • Sarkadi, B.1    Enyedi, A.2    Foldes-Papp, Z.3    Gardos, G.4
  • 28
    • 0032483082 scopus 로고    scopus 로고
    • 2+-ATPase affects cation binding from both sides of the membrane and destabilizes the occluded enzyme forms
    • DOI 10.1021/bi9802925, PII S000629609800292X
    • Vilsen, B., and Andersen, J. P. (1998) Mutation to the glutamate in the fourth membrane segment of Na+,K+-ATPase and Ca2+-ATPase affects cation binding from both sides of the membrane and destabilizes the occluded enzyme forms. Biochemistry 37, 10961-10971 (Pubitemid 28368920)
    • (1998) Biochemistry , vol.37 , Issue.31 , pp. 10961-10971
    • Vilsen, B.1    Andersen, J.P.2
  • 30
    • 0026653810 scopus 로고
    • Functional expression of plant plasma membrane H+-ATPase in yeast endoplasmic reticulum
    • Villalba, J. M., Palmgren, M. G., Berberián, G. E., Ferguson, C., and Serrano, R. (1992) Functional expression of plant plasma membrane H+-ATPase in yeast endoplasmic reticulum. J. Biol. Chem. 267, 12341-12349
    • (1992) J. Biol. Chem. , vol.267 , pp. 12341-12349
    • Villalba, J.M.1    Palmgren, M.G.2    Berberián, G.E.3    Ferguson, C.4    Serrano, R.5
  • 31
    • 33644864126 scopus 로고    scopus 로고
    • The plant plasma membrane Ca2+ pump ACA8 contains overlapping as well as physically separated autoinhibitory and calmodulin-binding domains
    • Baekgaard, L., Luoni, L., De Michelis, M. I., and Palmgren, M. G. (2006) The plant plasma membrane Ca2+ pump ACA8 contains overlapping as well as physically separated autoinhibitory and calmodulin-binding domains. J. Biol. Chem. 281, 1058-1065
    • (2006) J. Biol. Chem. , vol.281 , pp. 1058-1065
    • Baekgaard, L.1    Luoni, L.2    De Michelis, M.I.3    Palmgren, M.G.4
  • 32
    • 37249060052 scopus 로고    scopus 로고
    • Crystal structure of the plasma membrane proton pump
    • DOI 10.1038/nature06417, PII NATURE06417
    • Pedersen, B. P., Buch-Pedersen, M. J., Morth, J. P., Palmgren, M. G., and Nissen, P. (2007) Crystal structure of the plasma membrane proton pump. Nature 450, 1111-1114 (Pubitemid 350273616)
    • (2007) Nature , vol.450 , Issue.7172 , pp. 1111-1114
    • Pedersen, B.P.1    Buch-Pedersen, M.J.2    Preben, M.J.3    Palmgren, M.G.4    Nissen, P.5
  • 33
    • 30044436319 scopus 로고    scopus 로고
    • The thioredoxin system protects ribosomes against stress-induced aggregation
    • DOI 10.1091/mbc.E05-06-0520
    • Rand, J. D., and Grant, C. M. (2006) The thioredoxin system protects ribosomes against stress-induced aggregation. Mol. Biol. Cell 17, 387-401 (Pubitemid 43049491)
    • (2006) Molecular Biology of the Cell , vol.17 , Issue.1 , pp. 387-401
    • Rand, J.D.1    Grant, C.M.2
  • 34
    • 23044466035 scopus 로고    scopus 로고
    • Cooperative function of the CHD5-like protein Mdm39p with a P-type ATPase Spf1p in the maintenance of ER homeostasis in Saccharomyces cerevisiae
    • DOI 10.1007/s00438-005-1153-6
    • Ando, A., and Suzuki, C. (2005) Cooperative function of the CHD5-like protein Mdm39p with a P-type ATPase Spf1p in the maintenance of ER homeostasis in Saccharomyces cerevisiae. Mol. Genet. Genomics 273, 497-506 (Pubitemid 41073970)
    • (2005) Molecular Genetics and Genomics , vol.273 , Issue.6 , pp. 497-506
    • Ando, A.1    Suzuki, C.2
  • 35
    • 65049087704 scopus 로고    scopus 로고
    • Cd2+,Mn2+, Ni2+, and Se2+ toxicity to Saccharomyces cerevisiae lacking YPK9p the orthologue of human ATP13A2
    • Schmidt, K., Wolfe, D. M., Stiller, B., and Pearce, D. A. (2009) Cd2+,Mn2+, Ni2+, and Se2+ toxicity to Saccharomyces cerevisiae lacking YPK9p the orthologue of human ATP13A2. Biochem. Biophys. Res. Commun. 383, 198-202
    • (2009) Biochem. Biophys. Res. Commun. , vol.383 , pp. 198-202
    • Schmidt, K.1    Wolfe, D.M.2    Stiller, B.3    Pearce, D.A.4
  • 36
    • 0028866670 scopus 로고
    • Organization of P-type ATPases. Significance of structural diversity
    • Lutsenko, S., and Kaplan, J. H. (1995) Organization of P-type ATPases. Significance of structural diversity. Biochemistry 34, 15607-15613
    • (1995) Biochemistry , vol.34 , pp. 15607-15613
    • Lutsenko, S.1    Kaplan, J.H.2
  • 37
    • 0023461605 scopus 로고
    • Replacement of the promoter of the yeast plasma membrane ATPase gene by a galactose-dependent promoter and its physiological consequences
    • Cid, A., Perona, R., and Serrano, R. (1987) Replacement of the promoter of the yeast plasma membrane ATPase gene by a galactose-dependent promoter and its physiological consequences. Curr. Genet. 12, 105-110
    • (1987) Curr. Genet. , vol.12 , pp. 105-110
    • Cid, A.1    Perona, R.2    Serrano, R.3
  • 38
    • 0015867369 scopus 로고
    • Evidence for an aspartyl phosphate residue at the active site of sodium and potassium ion transport adenosine triphosphatase
    • Post, R. L., and Kume, S. (1973) Evidence for an aspartyl phosphate residue at the active site of sodium and potassium ion transport adenosine triphosphatase. J. Biol. Chem. 248, 6993-7000
    • (1973) J. Biol. Chem. , vol.248 , pp. 6993-7000
    • Post, R.L.1    Kume, S.2
  • 39
    • 0020479815 scopus 로고
    • Partial purification and properties of the proton-translocating ATPase of plant plasma membranes
    • Vara, F., and Serrano, R. (1982) Partial purification and properties of the proton-translocating ATPase of plant plasma membranes. J. Biol. Chem. 257, 12826-12830
    • (1982) J. Biol. Chem. , vol.257 , pp. 12826-12830
    • Vara, F.1    Serrano, R.2
  • 40
    • 0035781086 scopus 로고    scopus 로고
    • Plant plasma membrane H+-ATPases. Powerhouses for nutrient uptake
    • Palmgren, M. G. (2001) Plant plasma membrane H+-ATPases. Powerhouses for nutrient uptake. Annu. Rev. Plant Physiol. Plant Mol. Biol. 52, 817-845
    • (2001) Annu. Rev. Plant Physiol. Plant Mol. Biol. , vol.52 , pp. 817-845
    • Palmgren, M.G.1
  • 41
    • 0019315398 scopus 로고
    • Role of water, hydrogen ion, and temperature on the synthesis of adenosine triphosphate by the sarcoplasmic reticulum adenosine triphosphatase in the absence of a calcium ion gradient
    • de Meis, L., Martins, O. B., and Alves, E. W. (1980) Role of water, hydrogen ion, and temperature on the synthesis of adenosine triphosphate by the sarcoplasmic reticulum adenosine triphosphatase in the absence of a calcium ion gradient. Biochemistry 19, 4252-4261
    • (1980) Biochemistry , vol.19 , pp. 4252-4261
    • De Meis, L.1    Martins, O.B.2    Alves, E.W.3
  • 42
    • 0034621834 scopus 로고    scopus 로고
    • Crystal structure of the calcium pump of sarcoplasmic reticulum at 2.6 Å resolution
    • DOI 10.1038/35015017
    • Toyoshima, C., Nakasako, M., Nomura, H., and Ogawa, H. (2000) Crystal structure of the calcium pump of sarcoplasmic reticulum at 2.6 Å resolution. Nature 405, 647-655 (Pubitemid 30428644)
    • (2000) Nature , vol.405 , Issue.6787 , pp. 647-655
    • Toyoshima, C.1    Nakasako, M.2    Nomura, H.3    Ogawa, H.4
  • 44
    • 81455144649 scopus 로고    scopus 로고
    • P5A-type ATPase Cta4p is essential for Ca2+ transport in the endoplasmic reticulum of Schizosaccharomyces pombe
    • Lustoza, A. C., Palma, L. M., Façanha, A. R., Okorokov, L. A., and Okorokova-Façanha, A. L. (2011) P5A-type ATPase Cta4p is essential for Ca2+ transport in the endoplasmic reticulum of Schizosaccharomyces pombe. PLoS One 6, e27843
    • (2011) PLoS One , vol.6
    • Lustoza, A.C.1    Palma, L.M.2    Façanha, A.R.3    Okorokov, L.A.4    Okorokova-Façanha, A.L.5
  • 45
    • 0037221305 scopus 로고    scopus 로고
    • Amiodarone induces a caffeine-inhibited, MID1-depedent rise in free cytoplasmic calcium in Saccharomyces cerevisiae
    • DOI 10.1046/j.1365-2958.2003.03291.x
    • Courchesne, W. E., and Ozturk, S. (2003) Amiodarone induces a caffeine-inhibited, MID1-dependent rise in free cytoplasmic calcium in Saccharomyces cerevisiae. Mol. Microbiol. 47, 223-234 (Pubitemid 36051336)
    • (2003) Molecular Microbiology , vol.47 , Issue.1 , pp. 223-234
    • Courchesne, W.E.1    Ozturk, S.2
  • 47
    • 0028887443 scopus 로고
    • Cytosolic concentration of Ca2+ regulates the plasma membrane H+-ATPase in guard cells of fava bean
    • Kinoshita, T., Nishimura, M., and Shimazaki, K. (1995) Cytosolic concentration of Ca2+ regulates the plasma membrane H+-ATPase in guard cells of fava bean. Plant Cell 7, 1333-1342
    • (1995) Plant Cell , vol.7 , pp. 1333-1342
    • Kinoshita, T.1    Nishimura, M.2    Shimazaki, K.3
  • 48
    • 0033199505 scopus 로고    scopus 로고
    • 2+ in the yeast endoplasmic reticulum reaches only 10 microM and is mainly controlled by the secretory pathway pump Pmr1
    • DOI 10.1093/emboj/18.17.4733
    • Strayle, J., Pozzan, T., and Rudolph, H. K. (1999) Steady-state free Ca2+ in the yeast endoplasmic reticulum reaches only 10 microM and is mainly controlled by the secretory pathway pump pmr1. EMBO J. 18, 4733-4743 (Pubitemid 29415527)
    • (1999) EMBO Journal , vol.18 , Issue.17 , pp. 4733-4743
    • Strayle, J.1    Pozzan, T.2    Rudolph, H.K.3
  • 49
    • 0030611178 scopus 로고    scopus 로고
    • 2+-ATPase in yeast Golgi, has properties distinct from sarco/endoplasmic reticulum and plasma membrane calcium pumps
    • DOI 10.1074/jbc.272.15.9895
    • Sorin, A., Rosas, G., and Rao, R. (1997) PMR1, a Ca2+-ATPase in yeast Golgi, has properties distinct from sarco/endoplasmic reticulum and plasma membrane calcium pumps. J. Biol. Chem. 272, 9895-9901 (Pubitemid 27171658)
    • (1997) Journal of Biological Chemistry , vol.272 , Issue.15 , pp. 9895-9901
    • Sorin, A.1    Rosas, G.2    Rao, R.3
  • 50
    • 0041706252 scopus 로고    scopus 로고
    • Antifungal activity of amiodarone is mediated by disruption of calcium homeostasis
    • DOI 10.1074/jbc.M303300200
    • Gupta, S. S., Ton, V. K., Beaudry, V., Rulli, S., Cunningham, K., and Rao, R. (2003) Antifungal activity of amiodarone is mediated by disruption of calcium homeostasis. J. Biol. Chem. 278, 28831-28839 (Pubitemid 36935793)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.31 , pp. 28831-28839
    • Gupta, S.S.1    Ton, V.-K.2    Beaudry, V.3    Rulli, S.4    Cunningham, K.5    Rao, R.6
  • 53
    • 39649119621 scopus 로고    scopus 로고
    • The pH of the secretory pathway: Measurement, determinants, and regulation
    • Paroutis, P., Touret, N., and Grinstein, S. (2004) The pH of the secretory pathway. Measurement, determinants, and regulation. Physiology 19, 207-215 (Pubitemid 39481936)
    • (2004) Physiology , Issue.4 , pp. 207-215
    • Paroutis, P.1    Touret, N.2    Grinstein, S.3
  • 54
    • 67650516832 scopus 로고    scopus 로고
    • Cdc50p plays a vital role in the ATPase reaction cycle of the putative aminophospholipid transporter Drs2p
    • Lenoir, G., Williamson, P., Puts, C. F., and Holthuis, J. C. (2009) Cdc50p plays a vital role in the ATPase reaction cycle of the putative aminophospholipid transporter Drs2p. J. Biol. Chem. 284, 17956-17967
    • (2009) J. Biol. Chem. , vol.284 , pp. 17956-17967
    • Lenoir, G.1    Williamson, P.2    Puts, C.F.3    Holthuis, J.C.4
  • 58
    • 77951883450 scopus 로고    scopus 로고
    • The physiological significance of the cardiotonic steroid/ouabain-binding site of the Na,K-ATPase
    • Lingrel, J. B. (2010) The physiological significance of the cardiotonic steroid/ouabain-binding site of the Na,K-ATPase. Annu. Rev. Physiol. 72, 395-412
    • (2010) Annu. Rev. Physiol. , vol.72 , pp. 395-412
    • Lingrel, J.B.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.