메뉴 건너뛰기




Volumn 5, Issue 4, 2004, Pages 282-295

Biology, structure and mechanism of P-type ATPases

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATASE; AMINO ACID DERIVATIVE; CADMIUM; CALCIUM CHANNEL P TYPE; COPPER; MEMBRANE PROTEIN; METAL DERIVATIVE; PROTEIN DERIVATIVE; ZINC;

EID: 3242701547     PISSN: 14710072     EISSN: None     Source Type: Journal    
DOI: 10.1038/nrm1354     Document Type: Review
Times cited : (479)

References (104)
  • 1
    • 0001409028 scopus 로고
    • The influence of some cations on an adenosine triphosphatase from peripheral nerves
    • +-ATPase. A paper worth a Nobel prize 40 years later.
    • (1957) Biochim. Biophys. Acta , vol.23 , pp. 394-401
    • Skou, J.C.1
  • 2
    • 72949126637 scopus 로고
    • Die Calciumpumpe der Erschlaffungsgrana des Muskels und ihre Abhängigkeit von der ATP-Spaltung
    • Hasselbach, W. & Makinose, M. Die Calciumpumpe der Erschlaffungsgrana des Muskels und ihre Abhängigkeit von der ATP-Spaltung. Eur J. Biochem. 333, 518-528 (1961).
    • (1961) Eur J. Biochem. , vol.333 , pp. 518-528
    • Hasselbach, W.1    Makinose, M.2
  • 3
    • 0014953793 scopus 로고
    • Correlated changes in membrane potential and ATP concentrations in Neurospora
    • Slayman, C. L, Lu, C. Y. & Shane, L. Correlated changes in membrane potential and ATP concentrations in Neurospora. Nature 226, 274-276 (1970).
    • (1970) Nature , vol.226 , pp. 274-276
    • Slayman, C.L.1    Lu, C.Y.2    Shane, L.3
  • 4
    • 0016786376 scopus 로고
    • +)-ATPase V. Conformational changes in the enzyme. Transitions between the Na-form and the K-form studied with tryptic digestion as a tool
    • +)-ATPase V. Conformational changes in the enzyme. Transitions between the Na-form and the K-form studied with tryptic digestion as a tool. Biochim. Biophys. Acta 401, 399-415 (1975).
    • (1975) Biochim. Biophys. Acta , vol.401 , pp. 399-415
    • Jorgensen, P.L.1
  • 5
    • 0024358181 scopus 로고
    • Utilization of binding energy and coupling rules for active transport and other coupled vectorial processes
    • Jencks, W. P. Utilization of binding energy and coupling rules for active transport and other coupled vectorial processes. Methods Enzymol. 171, 145-164 (1989).
    • (1989) Methods Enzymol. , vol.171 , pp. 145-164
    • Jencks, W.P.1
  • 6
    • 0029940235 scopus 로고    scopus 로고
    • Structural organization, ion transport, and energy transduction of P-type ATPases
    • Moller, J. V., Juul, B. & le Maire, M. Structural organization, ion transport, and energy transduction of P-type ATPases. Biochim. Biophys. Acta 1, 1-51 (1996).
    • (1996) Biochim. Biophys. Acta , vol.1 , pp. 1-51
    • Moller, J.V.1    Juul, B.2    Le Maire, M.3
  • 7
    • 0031964372 scopus 로고    scopus 로고
    • Evolution of substrate specificities in the P-type ATPase superfamily
    • Axelsen, K. B. & Palmgren, M. G. Evolution of substrate specificities in the P-type ATPase superfamily. J. Mol. Evol. 46, 84-101 (1998). A thorough analysis of the sequence homology among P-type ATPases.
    • (1998) J. Mol. Evol. , vol.46 , pp. 84-101
    • Axelsen, K.B.1    Palmgren, M.G.2
  • 8
    • 16044367245 scopus 로고    scopus 로고
    • Complete genome sequence of the methanogenic archaeon, Methanococcus jannaschii
    • Bult, C. J. et al. Complete genome sequence of the methanogenic archaeon, Methanococcus jannaschii. Science 273, 1058-1073 (1996).
    • (1996) Science , vol.273 , pp. 1058-1073
    • Bult, C.J.1
  • 9
    • 0032129962 scopus 로고    scopus 로고
    • The inventory of all ion and drug ATPases encoded by the yeast genome
    • Goffeau, A. The inventory of all ion and drug ATPases encoded by the yeast genome. Acta Physiol. Scand. 643, 297-300 (1998).
    • (1998) Acta Physiol. Scand. , vol.643 , pp. 297-300
    • Goffeau, A.1
  • 10
    • 0034976968 scopus 로고    scopus 로고
    • Inventory of the superfamily of P-type ion pumps in Arabidopsis
    • Axelsen, K. B. & Palmgren, M. G. Inventory of the superfamily of P-type ion pumps in Arabidopsis. Plant Physiol. 126, 696-706 (2001).
    • (2001) Plant Physiol. , vol.126 , pp. 696-706
    • Axelsen, K.B.1    Palmgren, M.G.2
  • 11
    • 0042931216 scopus 로고    scopus 로고
    • P-type ATPases in Caenorhabditis and Drosophila: Implications for evolution of the P-type ATPase subunit families with special references to the Na,K-ATPase and H,K-ATPase subgroup
    • Okamura, H., Yasuhara, J. C., Fambrough, D. M. & Takeyasu, K. P-type ATPases in Caenorhabditis and Drosophila: implications for evolution of the P-type ATPase subunit families with special references to the Na,K-ATPase and H,K-ATPase subgroup. J. Membr. Biol. 191, 13-24 (2002).
    • (2002) J. Membr. Biol. , vol.191 , pp. 13-24
    • Okamura, H.1    Yasuhara, J.C.2    Fambrough, D.M.3    Takeyasu, K.4
  • 13
    • 0031689027 scopus 로고    scopus 로고
    • Structure and function of the Kdp-ATPase of Escherichia coli
    • Altendorf, K. et al. Structure and function of the Kdp-ATPase of Escherichia coli. Acta Physiol. Scand. 643, 137-146 (1998).
    • (1998) Acta Physiol. Scand. , vol.643 , pp. 137-146
    • Altendorf, K.1
  • 15
    • 0344132580 scopus 로고    scopus 로고
    • Expression and mutagenesis of ZntA, a zinc-transporting P-type ATPase from Escherichia coli
    • Okkeri, J. & Haltia, T. Expression and mutagenesis of ZntA, a zinc-transporting P-type ATPase from Escherichia coli. Biochemistry 38, 14109-14116 (1999).
    • (1999) Biochemistry , vol.38 , pp. 14109-14116
    • Okkeri, J.1    Haltia, T.2
  • 16
    • 0036850783 scopus 로고    scopus 로고
    • Transport and detoxification systems for transition metals, heavy metals and metalloids in eukaryotic and prokaryotic microbes
    • Rosen, B. P. Transport and detoxification systems for transition metals, heavy metals and metalloids in eukaryotic and prokaryotic microbes. Comp. Biochem. Physiol., Part A Mol. Integr. Physiol. 133, 689-693 (2002).
    • (2002) Comp. Biochem. Physiol., Part A Mol. Integr. Physiol. , vol.133 , pp. 689-693
    • Rosen, B.P.1
  • 17
    • 0033575729 scopus 로고    scopus 로고
    • Metal ion transporters and homeostasis
    • Nelson, N. Metal ion transporters and homeostasis. EMBO J. 18, 4361-4371 (1999).
    • (1999) EMBO J. , vol.18 , pp. 4361-4371
    • Nelson, N.1
  • 18
    • 0037802583 scopus 로고    scopus 로고
    • Function and regulation of the mammalian copper-transporting ATPases: Insights from biochemical and cell biological approaches
    • Lutsenko, S. & Petris, M. J. Function and regulation of the mammalian copper-transporting ATPases: insights from biochemical and cell biological approaches. J. Membr. Biol. 191, 1-12 (2003).
    • (2003) J. Membr. Biol. , vol.191 , pp. 1-12
    • Lutsenko, S.1    Petris, M.J.2
  • 19
    • 0027364961 scopus 로고
    • The Wilson disease gene is a copper transporting ATPase with homology to the Menkes disease gene
    • Tanzi, R. E. et al. The Wilson disease gene is a copper transporting ATPase with homology to the Menkes disease gene. Nature Genet. 5, 344-350 (1993).
    • (1993) Nature Genet. , vol.5 , pp. 344-350
    • Tanzi, R.E.1
  • 20
    • 0027288228 scopus 로고
    • Primary structure of two P-type ATPases involved in copper homeostasis in Enterococcus hirae
    • Odermatt, A., Suter, H., Krapf, R. & Solioz, M. Primary structure of two P-type ATPases involved in copper homeostasis in Enterococcus hirae. J. Biol. Chem. 268, 12775-12779 (1993).
    • (1993) J. Biol. Chem. , vol.268 , pp. 12775-12779
    • Odermatt, A.1    Suter, H.2    Krapf, R.3    Solioz, M.4
  • 21
    • 0027452091 scopus 로고
    • The Wilson disease gene is a putative copper transporting P-type ATPase similar to the Menkes gene
    • Bull, P. C., Thomas, G. R., Rommens, J. M., Forbes, J. R. & Cox, D. W. The Wilson disease gene is a putative copper transporting P-type ATPase similar to the Menkes gene. Nature Genet. 5, 327-337 (1993).
    • (1993) Nature Genet. , vol.5 , pp. 327-337
    • Bull, P.C.1    Thomas, G.R.2    Rommens, J.M.3    Forbes, J.R.4    Cox, D.W.5
  • 22
    • 0142218366 scopus 로고    scopus 로고
    • Regulation of transbilayer plasma membrane phospholipd asymmetry
    • Daleke, D. L. Regulation of transbilayer plasma membrane phospholipd asymmetry. J. Lipid Res. 44, 233-242 (2003).
    • (2003) J. Lipid Res. , vol.44 , pp. 233-242
    • Daleke, D.L.1
  • 23
    • 0037345029 scopus 로고    scopus 로고
    • Drs2p-related-type ATPases Dnf1p and Dnf2p are required for phospholipid translocation across the yeast plasma membrane and serve a role in endocytosis
    • Pomorski, T, et al. Drs2p-related-type ATPases Dnf1p and Dnf2p are required for phospholipid translocation across the yeast plasma membrane and serve a role in endocytosis. Mol. Biol. Cell 14, 1240-1254 (2003).
    • (2003) Mol. Biol. Cell , vol.14 , pp. 1240-1254
    • Pomorski, T.1
  • 24
    • 0024573741 scopus 로고
    • Erythrocyte morphology reflects the transbilayer distribution of incorporated phospholipids
    • Daleke, D. L. & Huestis, W. H. Erythrocyte morphology reflects the transbilayer distribution of incorporated phospholipids. J. Cell Biol. 108, 1375-1385 (1989).
    • (1989) J. Cell Biol. , vol.108 , pp. 1375-1385
    • Daleke, D.L.1    Huestis, W.H.2
  • 25
    • 0036667745 scopus 로고    scopus 로고
    • A calcium pump made visible
    • Lee, A. G. A calcium pump made visible. Curr. Opin. Struct. Biol. 12, 547-554 (2002).
    • (2002) Curr. Opin. Struct. Biol. , vol.12 , pp. 547-554
    • Lee, A.G.1
  • 27
    • 0034621834 scopus 로고    scopus 로고
    • Crystal structure of the calcium pump of sarcoplasmic reticulum at 2.6 Å resolution
    • Toyoshima, C., Nakasako, M., Nomura, H. & Ogawa, H. Crystal structure of the calcium pump of sarcoplasmic reticulum at 2.6 Å resolution. Nature 405, 647-655 (2000). The first X-ray structure of a P-type ATPase defines the four principal domains, and highlights a surprisingly long distance between the ion-translocation site in the membrane and the cytoplasmic phosphorylation site.
    • (2000) Nature , vol.405 , pp. 647-655
    • Toyoshima, C.1    Nakasako, M.2    Nomura, H.3    Ogawa, H.4
  • 28
    • 0037043709 scopus 로고    scopus 로고
    • Structural changes in the calcium pump accompanying the dissociation of calcium
    • 2+ release to the outside medium.
    • (2002) Nature , vol.418 , pp. 605-611
    • Toyoshima, C.1    Nomura, H.2
  • 30
    • 0038412004 scopus 로고    scopus 로고
    • Junctional membrane structure and store operated calcium entry in muscle cells
    • Ma, J. J. & Pan, Z. Junctional membrane structure and store operated calcium entry in muscle cells. Front. Biosci. 8, D242-D255 (2003).
    • (2003) Front. Biosci. , vol.8
    • Ma, J.J.1    Pan, Z.2
  • 31
    • 0035213374 scopus 로고    scopus 로고
    • Dissecting calcium oscillators in plant cells
    • Harper, J. F. Dissecting calcium oscillators in plant cells. Trends Plant Sci. 6, 395-397 (2001).
    • (2001) Trends Plant Sci. , vol.6 , pp. 395-397
    • Harper, J.F.1
  • 32
    • 0035781086 scopus 로고    scopus 로고
    • +-ATPases: Powerhouses for nutrient uptake
    • +-ATPases: powerhouses for nutrient uptake. Annu. Rev. Plant Physiol. Mol. Biol. 52, 817-845 (2001). All there is to know about the plant proton pump - an excellent, comprehensive review.
    • (2001) Annu. Rev. Plant Physiol. Mol. Biol. , vol.52 , pp. 817-845
    • Palmgren, M.G.1
  • 34
    • 0035997378 scopus 로고    scopus 로고
    • Biochemistry of Na,K-ATPase
    • Kaplan, J. H. Biochemistry of Na,K-ATPase. Annu. Rev. Biochem. 71, 511-535 (2002).
    • (2002) Annu. Rev. Biochem. , vol.71 , pp. 511-535
    • Kaplan, J.H.1
  • 35
  • 36
    • 0037031285 scopus 로고    scopus 로고
    • Extracellular domains, transmembrane segments, and intracellular domains interact to determine the cation selectivity of Na,K- and gastric H,K-ATPase
    • Mense, M., Rajendran, V, Blostein, R. & Caplan, M. J. Extracellular domains, transmembrane segments, and intracellular domains interact to determine the cation selectivity of Na,K- and gastric H,K-ATPase. Biochemistry 41, 9803-9812 (2002).
    • (2002) Biochemistry , vol.41 , pp. 9803-9812
    • Mense, M.1    Rajendran, V.2    Blostein, R.3    Caplan, M.J.4
  • 38
    • 0028074994 scopus 로고
    • Fungal plasma membrane proton pumps as promising new antifungal targets
    • Monk, B. C. & Perlin, D. S. Fungal plasma membrane proton pumps as promising new antifungal targets. Crit. Rev. Microbiol. 20, 209-223 (1994).
    • (1994) Crit. Rev. Microbiol. , vol.20 , pp. 209-223
    • Monk, B.C.1    Perlin, D.S.2
  • 39
    • 0027464932 scopus 로고
    • +,K(+)-adenosinetriphosphatase
    • +,K(+)-adenosinetriphosphatase. Biochemistry 32, 2345-2355 (1993).
    • (1993) Biochemistry , vol.32 , pp. 2345-2355
    • Besancon, M.1
  • 40
    • 0034773778 scopus 로고    scopus 로고
    • The functional role of β subunits in oligomeric P-type ATPases
    • Geering, K. The functional role of β subunits in oligomeric P-type ATPases. J. Bioenerg. Biomembr. 33, 425-438 (2001).
    • (2001) J. Bioenerg. Biomembr. , vol.33 , pp. 425-438
    • Geering, K.1
  • 41
    • 0034779892 scopus 로고    scopus 로고
    • Molecular and functional studies of the γ subunit of the sodium pump
    • Therien, A. G., Pu, H. X., Karlish, S. J. & Blostein, R. Molecular and functional studies of the γ subunit of the sodium pump. J. Bioenerg. Biomembr. 33,407-414 (2001).
    • (2001) J. Bioenerg. Biomembr. , vol.33 , pp. 407-414
    • Therien, A.G.1    Pu, H.X.2    Karlish, S.J.3    Blostein, R.4
  • 42
    • 0038578770 scopus 로고    scopus 로고
    • FXYD proteins: New tissue- and isoform-specific regulators of Na,K-ATPase
    • Gearing, K. et al. FXYD proteins: new tissue- and isoform-specific regulators of Na,K-ATPase. Ann. NY Acad. Sci. 986, 388-394 (2003).
    • (2003) Ann. NY Acad. Sci. , vol.986 , pp. 388-394
    • Gearing, K.1
  • 43
    • 0037119411 scopus 로고    scopus 로고
    • Characterization of a hyperthermophilic P-type ATPase from Methanococcus jannaschii expressed in yeast
    • Morsomme, P. et al. Characterization of a hyperthermophilic P-type ATPase from Methanococcus jannaschii expressed in yeast. J. Biol. Chem. 277, 29608-29616 (2002).
    • (2002) J. Biol. Chem. , vol.277 , pp. 29608-29616
    • Morsomme, P.1
  • 44
    • 0023657967 scopus 로고
    • Activation of yeast plasma membrane ATPase by acid pH during growth
    • Eraso, P. & Gancedo, C. Activation of yeast plasma membrane ATPase by acid pH during growth. FEBS Lett. 224, 187-192 (1987).
    • (1987) FEBS Lett. , vol.224 , pp. 187-192
    • Eraso, P.1    Gancedo, C.2
  • 46
    • 0020580035 scopus 로고
    • 2+-ATPase vesicles treated with vanadate
    • 2+-ATPase vesicles treated with vanadate. J. Biol. Chem. 258, 2599-2603 (1983).
    • (1983) J. Biol. Chem. , vol.258 , pp. 2599-2603
    • Dux, L.1    Martonosi, A.2
  • 47
    • 0022627265 scopus 로고
    • Crystallization of the gastric H,K-ATPase
    • Rabon, E., Wilke, M., Sachs, G. & Zampighi, G. Crystallization of the gastric H,K-ATPase. J. Mol. Biol. 261, 1434-1439 (1986).
    • (1986) J. Mol. Biol. , vol.261 , pp. 1434-1439
    • Rabon, E.1    Wilke, M.2    Sachs, G.3    Zampighi, G.4
  • 49
    • 0035035788 scopus 로고    scopus 로고
    • 2+-ATPase in E1 and E2 states
    • 2+-ATPase in the E2-P state.
    • (2001) Biophys. J. , vol.80 , pp. 2187-2197
    • Rice, W.J.1
  • 51
    • 0035368086 scopus 로고    scopus 로고
    • +-ATPase
    • +-ATPase. J. Mol. Biol. 309, 465-476 (2001).
    • (2001) J. Mol. Biol. , vol.309 , pp. 465-476
    • Jahn, T.1
  • 52
    • 0032560170 scopus 로고    scopus 로고
    • Structure of the calcium pump from sarcoplasmic reticulum at 8 Å resolution
    • Zhang, P., Toyoshima, C., Yonekura, K., Green, N. M. & Stokes, D. L. Structure of the calcium pump from sarcoplasmic reticulum at 8 Å resolution. Nature 392, 835-839 (1998).
    • (1998) Nature , vol.392 , pp. 835-839
    • Zhang, P.1    Toyoshima, C.2    Yonekura, K.3    Green, N.M.4    Stokes, D.L.5
  • 53
    • 0242585345 scopus 로고    scopus 로고
    • The pentacovalent phosphorus intermediate of a phosphoryl transfer reaction
    • Lahiri, S. D., Zhang, G., Dunaway-Mariano, D. & Allen, K. N. The pentacovalent phosphorus intermediate of a phosphoryl transfer reaction. Science 299, 2067-2071 (2003). The 1.2-Å structure of a close homologue of the P-type-ATPase P-domain shows the crucial Asp residue in the process of being phosphorylated.
    • (2003) Science , vol.299 , pp. 2067-2071
    • Lahiri, S.D.1    Zhang, G.2    Dunaway-Mariano, D.3    Allen, K.N.4
  • 54
    • 0038442766 scopus 로고    scopus 로고
    • ATP-induced conformational changes of the nucleotide-binding domain of Na,K-ATPase
    • Hilge, M. et al. ATP-induced conformational changes of the nucleotide-binding domain of Na,K-ATPase. Nature Struct. Biol. 10, 468-474 (2003). The solution NMR structure of a recombinant N-domain shows the triphosphate of ATP protruding from the nucleotide-binding pocket.
    • (2003) Nature Struct. Biol. , vol.10 , pp. 468-474
    • Hilge, M.1
  • 57
    • 0031970010 scopus 로고    scopus 로고
    • The catalytic domain of the P-type ATPase has the haloacid dehalogenase fold
    • Aravind, L., Galperin, M. Y. & Koonin, E. V. The catalytic domain of the P-type ATPase has the haloacid dehalogenase fold. Trends Biochem. Sci. 23, 127-129 (1998).
    • (1998) Trends Biochem. Sci. , vol.23 , pp. 127-129
    • Aravind, L.1    Galperin, M.Y.2    Koonin, E.V.3
  • 58
    • 0028168416 scopus 로고
    • Amino acids Lys-Asp-Asp-Lys-Pro-Val402 in the Ca(2+)-ATPase of cardiac sarcoplasmic reticulum are critical for functional association with phospholamban
    • Toyofuku, T., Kurzydlowski, K., Tada, M. & MacLennan, D. H. Amino acids Lys-Asp-Asp-Lys-Pro-Val402 in the Ca(2+)-ATPase of cardiac sarcoplasmic reticulum are critical for functional association with phospholamban. J. Biol. Chem. 269, 22929-22932 (1994).
    • (1994) J. Biol. Chem. , vol.269 , pp. 22929-22932
    • Toyofuku, T.1    Kurzydlowski, K.2    Tada, M.3    MacLennan, D.H.4
  • 60
    • 0031974775 scopus 로고    scopus 로고
    • Solution structure of the fourth metal-binding domain from the Menkes copper-transporting ATPase
    • Gitschier, J., Moffat, B., Reilly, D., Wood, W. I. & Fairbrother, W. J. Solution structure of the fourth metal-binding domain from the Menkes copper-transporting ATPase. Nature Struct. Biol. 5, 47-54 (1998).
    • (1998) Nature Struct. Biol. , vol.5 , pp. 47-54
    • Gitschier, J.1    Moffat, B.2    Reilly, D.3    Wood, W.I.4    Fairbrother, W.J.5
  • 61
    • 0036431502 scopus 로고    scopus 로고
    • A new zinc-protein coordination site in intracellular metal trafficking: Solution structure of the Apo and Zn(II) forms of ZntA(46-118)
    • Banci, L. et al. A new zinc-protein coordination site in intracellular metal trafficking: solution structure of the Apo and Zn(II) forms of ZntA(46-118). J. Mol. Biol. 323, 883-897 (2002).
    • (2002) J. Mol. Biol. , vol.323 , pp. 883-897
    • Banci, L.1
  • 62
    • 0036968784 scopus 로고    scopus 로고
    • Sequence conservation in families whose members have little or no sequence similarity: The four-helical cytokines and cytochromes
    • Hill, E. E., Morea, V. & Chothia, C. Sequence conservation in families whose members have little or no sequence similarity: the four-helical cytokines and cytochromes. J. Mol. Biol. 322, 205-233 (2002).
    • (2002) J. Mol. Biol. , vol.322 , pp. 205-233
    • Hill, E.E.1    Morea, V.2    Chothia, C.3
  • 63
    • 0027506471 scopus 로고
    • The probable arrangement of the helices in G protein-coupled receptors
    • Baldwin, J. M. The probable arrangement of the helices in G protein-coupled receptors. EMBO J. 12, 1693-1703 (1993).
    • (1993) EMBO J. , vol.12 , pp. 1693-1703
    • Baldwin, J.M.1
  • 64
    • 0034671503 scopus 로고    scopus 로고
    • +-ATPase by substitution of a conserved aspartyl residue in transmembrane segment 6
    • +-ATPase by substitution of a conserved aspartyl residue in transmembrane segment 6. J. Biol. Chem. 275, 39167-39173 (2000).
    • (2000) J. Biol. Chem. , vol.275 , pp. 39167-39173
    • Buch-Pedersen, M.J.1
  • 65
    • 0038381484 scopus 로고    scopus 로고
    • Conserved Asp684 in transmembrane segment M6 of the plant plasma membrane P-type proton pump AHA2 is a molecular determinant of proton translocation
    • Buch-Pedersen, M. J. & Palmgren, M. G. Conserved Asp684 in transmembrane segment M6 of the plant plasma membrane P-type proton pump AHA2 is a molecular determinant of proton translocation. J. Biol. Chem. 278, 17845-17851 (2003).
    • (2003) J. Biol. Chem. , vol.278 , pp. 17845-17851
    • Buch-Pedersen, M.J.1    Palmgren, M.G.2
  • 66
    • 0035815396 scopus 로고    scopus 로고
    • A putative proton binding site of plasma membrane H(+)-ATPase identified through homology modelling
    • Bukrinsky, J. T., Buch-Pedersen, M. J., Larsen, S. & Palmgren, M. G. A putative proton binding site of plasma membrane H(+)-ATPase identified through homology modelling. FEBS Lett. 494, 6-10 (2001).
    • (2001) FEBS Lett. , vol.494 , pp. 6-10
    • Bukrinsky, J.T.1    Buch-Pedersen, M.J.2    Larsen, S.3    Palmgren, M.G.4
  • 68
    • 0021274142 scopus 로고
    • Role of divalent cation bound to phosphoenzyme intermediate of sarcoplasmic reticulum ATPase
    • Wakabayashi, S. & Shigekawa, M. Role of divalent cation bound to phosphoenzyme intermediate of sarcoplasmic reticulum ATPase. J. Biol. Chem. 259, 4427-4436 (1984).
    • (1984) J. Biol. Chem. , vol.259 , pp. 4427-4436
    • Wakabayashi, S.1    Shigekawa, M.2
  • 69
    • 0034033869 scopus 로고    scopus 로고
    • Modeling a dehalogenase fold into the 8-Å density map for Ca(2+)-ATPase defines a new domain structure
    • Stokes, D. L. & Green, N. M. Modeling a dehalogenase fold into the 8-Å density map for Ca(2+)-ATPase defines a new domain structure. Biophys. J. 78, 1765-1776 (2000).
    • (2000) Biophys. J. , vol.78 , pp. 1765-1776
    • Stokes, D.L.1    Green, N.M.2
  • 70
    • 0033982453 scopus 로고    scopus 로고
    • Regulation of plasma membrene H(+)-ATPase in fungi and plants
    • Portillo, F. Regulation of plasma membrene H(+)-ATPase in fungi and plants. Biochim. Biophys. Acta 1469, 31-42 (2000).
    • (2000) Biochim. Biophys. Acta , vol.1469 , pp. 31-42
    • Portillo, F.1
  • 71
    • 0029909937 scopus 로고    scopus 로고
    • Ligand-regulated transport of the Menkes copper P-type ATPase efflux pump from the Golgi apparatus to the plasma membrane: A novel mechanism of regulated trafficking
    • Petris, M. J. et al. Ligand-regulated transport of the Menkes copper P-type ATPase efflux pump from the Golgi apparatus to the plasma membrane: a novel mechanism of regulated trafficking. EMBO J. 15, 6084-6095 (1996).
    • (1996) EMBO J. , vol.15 , pp. 6084-6095
    • Petris, M.J.1
  • 72
    • 0034455768 scopus 로고    scopus 로고
    • Sarco(endo)plasmic reticulum calcium pumps: Recent advances in our understanding of structure/function and biology
    • East, J. M. Sarco(endo)plasmic reticulum calcium pumps: recent advances in our understanding of structure/function and biology. Mol. Membr. Biol. 17, 189-200 (2000).
    • (2000) Mol. Membr. Biol. , vol.17 , pp. 189-200
    • East, J.M.1
  • 73
    • 0038464639 scopus 로고    scopus 로고
    • Phospholamban: A crucial regulator of cardiac contractility
    • MacLennan, D. H. & Kranias, E. G. Phospholamban: a crucial regulator of cardiac contractility. Nature Rev. Mol. Cell Biol. 4, 566-577 (2003).
    • (2003) Nature Rev. Mol. Cell Biol. , vol.4 , pp. 566-577
    • MacLennan, D.H.1    Kranias, E.G.2
  • 75
    • 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, 993-1002 (1994).
    • (1994) FASEB J. , vol.8 , pp. 993-1002
    • Carafoli, E.1
  • 76
    • 0034730505 scopus 로고    scopus 로고
    • Autoinhibition of a calmodulin-dependent calcium pump involves a structure in the stalk that connects the transmembrane domain to the ATPase catalytic domain
    • Curran, A. C. et al. Autoinhibition of a calmodulin-dependent calcium pump involves a structure in the stalk that connects the transmembrane domain to the ATPase catalytic domain. J. Biol. Chem. 275, 30301-30308 (2000).
    • (2000) J. Biol. Chem. , vol.275 , pp. 30301-30308
    • Curran, A.C.1
  • 78
    • 0025841745 scopus 로고
    • Identification of an autoinhibitory domain in the C-terminal region of the plant plasma membrane H(+)-ATPase
    • Palmgren, M. G., Sommarin, M., Serrano, R. & Larsson, C. Identification of an autoinhibitory domain in the C-terminal region of the plant plasma membrane H(+)-ATPase. J. Biol. Chem. 266, 20470-20475 (1991).
    • (1991) J. Biol. Chem. , vol.266 , pp. 20470-20475
    • Palmgren, M.G.1    Sommarin, M.2    Serrano, R.3    Larsson, C.4
  • 81
    • 0034634727 scopus 로고    scopus 로고
    • Mutagenic study of the structure, function and biogenesis of the yeast plasma membrane H(+)-ATPase
    • Morsomme, P., Slayman, C. W. & Goffeau, A. Mutagenic study of the structure, function and biogenesis of the yeast plasma membrane H(+)-ATPase. Biochim. Biophys. Acta 1469, 133-157 (2000).
    • (2000) Biochim. Biophys. Acta , vol.1469 , pp. 133-157
    • Morsomme, P.1    Slayman, C.W.2    Goffeau, A.3
  • 82
    • 0030879911 scopus 로고    scopus 로고
    • Topology of the fusicoccin-binding 14-3-3 homologs of Commelina communis
    • Oecking, C., Piotrowski, M., Hagemeier, J. & Hagemann, K. Topology of the fusicoccin-binding 14-3-3 homologs of Commelina communis. Plant J. 12, 441-453 (1997).
    • (1997) Plant J. , vol.12 , pp. 441-453
    • Oecking, C.1    Piotrowski, M.2    Hagemeier, J.3    Hagemann, K.4
  • 83
    • 0033579441 scopus 로고    scopus 로고
    • Binding of 14-3-3 protein to the plasma membrane H(+)-ATPase AHA2 involves the three C-terminal residues Tyr(946)-Thr-Val and requires phosphorylation of Thr(947)
    • Fuglsang, A. T. et al. Binding of 14-3-3 protein to the plasma membrane H(+)-ATPase AHA2 involves the three C-terminal residues Tyr(946)-Thr-Val and requires phosphorylation of Thr(947). J. Biol. Chem. 274, 36774-36780 (1999).
    • (1999) J. Biol. Chem. , vol.274 , pp. 36774-36780
    • Fuglsang, A.T.1
  • 84
    • 0028836587 scopus 로고
    • Fussicoccin receptors: Perception and transduction of the fusicoccin-signal
    • Aducci, P., Marra, M., Fogliano, V. & Fullone M. R. Fussicoccin receptors: perception and transduction of the fusicoccin-signal. J. Exp. Bot. 48, 1463-1478 (1995).
    • (1995) J. Exp. Bot. , vol.48 , pp. 1463-1478
    • Aducci, P.1    Marra, M.2    Fogliano, V.3    Fullone, M.R.4
  • 87
    • 0025742857 scopus 로고
    • +-ATPase by directed mutagenesis and intragenic suppression
    • +-ATPase by directed mutagenesis and intragenic suppression. FEBS Lett. 287, 71-74 (1991).
    • (1991) FEBS Lett. , vol.287 , pp. 71-74
    • Portillo, F.1    Eraso, P.2    Serrano, R.3
  • 88
    • 0027999624 scopus 로고
    • Tertiary conformational changes of the Neurospora crassa plasma membrane H(+)-ATPase monitored by hydrogen/deuterium exchange kinetics. A Fourier transformed infrared spectroscopy approach
    • Goormaghtigh, E., Vigneron, L., Scarborough, G. A. & Ruysschaert, J. M. Tertiary conformational changes of the Neurospora crassa plasma membrane H(+)-ATPase monitored by hydrogen/deuterium exchange kinetics. A Fourier transformed infrared spectroscopy approach. J. Biol. Chem. 269, 27409-27413 (1994).
    • (1994) J. Biol. Chem. , vol.269 , pp. 27409-27413
    • Goormaghtigh, E.1    Vigneron, L.2    Scarborough, G.A.3    Ruysschaert, J.M.4
  • 89
    • 0037099293 scopus 로고    scopus 로고
    • Domain movements of plasma membrane H(+)-ATPase: 3D structures of two states by electron cryo-microscopy
    • Rhee, K. H., Scarborough, G. A. & Henderson, R. Domain movements of plasma membrane H(+)-ATPase: 3D structures of two states by electron cryo-microscopy. EMBO J. 21, 3582-3589 (2002).
    • (2002) EMBO J. , vol.21 , pp. 3582-3589
    • Rhee, K.H.1    Scarborough, G.A.2    Henderson, R.3
  • 92
    • 0024435744 scopus 로고
    • The photosynthetic reaction centre from the purple bacterium Rhodopseudomonas viridis
    • Deisenhofer, J. & Michel, H. The photosynthetic reaction centre from the purple bacterium Rhodopseudomonas viridis. Biosci. Rep. 9, 383-419 (1989).
    • (1989) Biosci. Rep. , vol.9 , pp. 383-419
    • Deisenhofer, J.1    Michel, H.2
  • 94
    • 0032478818 scopus 로고    scopus 로고
    • + conduction and selectivity
    • + conduction and selectivity. Science 280, 69-77 (1998).
    • (1998) Science , vol.280 , pp. 69-77
    • Doyle, D.A.1
  • 95
    • 0038076054 scopus 로고    scopus 로고
    • + channel
    • + channel. Nature 423, 33-41 (2003).
    • (2003) Nature , vol.423 , pp. 33-41
    • Jiang, Y.1
  • 96
    • 0000770960 scopus 로고
    • Biochemical aspects of active transport
    • Albers, R. Biochemical aspects of active transport. Annu. Rev. Biochem. 36, 727-756 (1967).
    • (1967) Annu. Rev. Biochem. , vol.36 , pp. 727-756
    • Albers, R.1
  • 97
    • 0015523849 scopus 로고
    • Activation by adenosine triphosphate in the phosphorylation kinetics of sodium and potassium ion transport adenosine triphosphatase
    • Post, R. L., Hegyvary, C. & Kume, S. Activation by adenosine triphosphate in the phosphorylation kinetics of sodium and potassium ion transport adenosine triphosphatase. J. Biol. Chem. 247, 6530-6540 (1972).
    • (1972) J. Biol. Chem. , vol.247 , pp. 6530-6540
    • Post, R.L.1    Hegyvary, C.2    Kume, S.3
  • 98
    • 0025292355 scopus 로고
    • Model for the structure of bacteriorhodopsin based on high-resolution electron cryo-microscopy
    • Henderson, R. et al. Model for the structure of bacteriorhodopsin based on high-resolution electron cryo-microscopy J. Mol. Biol. 213, 899-929 (1990).
    • (1990) J. Mol. Biol. , vol.213 , pp. 899-929
    • Henderson, R.1
  • 99
    • 0028147508 scopus 로고
    • Atomic model of plant light-harvesting complex by electron crystallography
    • Kühlbrandt, W., Wang, D. N. & Fujiyoshi, Y. Atomic model of plant light-harvesting complex by electron crystallography. Nature 367, 614-621 (1994).
    • (1994) Nature , vol.367 , pp. 614-621
    • Kühlbrandt, W.1    Wang, D.N.2    Fujiyoshi, Y.3
  • 100
    • 0038112088 scopus 로고    scopus 로고
    • Structure and gating mechanism of the acetylcholine receptor pore
    • Miyazawa, A., Fujiyoshi, Y. & Unwin, N. Structure and gating mechanism of the acetylcholine receptor pore. Nature 423, 949-955 (2003).
    • (2003) Nature , vol.423 , pp. 949-955
    • Miyazawa, A.1    Fujiyoshi, Y.2    Unwin, N.3
  • 101
    • 0022706389 scopus 로고
    • The relation between the divergence of sequence and structure in proteins
    • Chothia, C. & Lesk, A. M. The relation between the divergence of sequence and structure in proteins. EMBO J. 5, 823-826 (1986).
    • (1986) EMBO J. , vol.5 , pp. 823-826
    • Chothia, C.1    Lesk, A.M.2
  • 102
    • 0030801002 scopus 로고    scopus 로고
    • Gapped BLAST and PSI-BLAST: A new generation of protein database search programs
    • Altschul, S. F. et al. Gapped BLAST and PSI-BLAST: a new generation of protein database search programs. Nucleic Acids Res. 25, 3389-3402 (1997).
    • (1997) Nucleic Acids Res. , vol.25 , pp. 3389-3402
    • Altschul, S.F.1
  • 103
    • 0027968068 scopus 로고
    • CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • Thompson, J. D., Higgins, D. G. & Gibson, T. J. CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic Acids Res. 22, 4673-4680 (1994).
    • (1994) Nucleic Acids Res. , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 104
    • 0027136282 scopus 로고
    • Comparative protein modelling by satisfaction of spatial restraints
    • Sali, A. & Blundell, T. L. Comparative protein modelling by satisfaction of spatial restraints. J. Mol. Biol. 234, 779-815 (1993).
    • (1993) J. Mol. Biol. , vol.234 , pp. 779-815
    • Sali, A.1    Blundell, T.L.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.