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Volumn 25, Issue C, 1997, Pages 297-337

The Molecular and Biochemical Basis of Pyrophosphate-Energized Proton Translocation at the Vacuolar Membrane

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EID: 77956734939     PISSN: 00652296     EISSN: None     Source Type: Book Series    
DOI: 10.1016/S0065-2296(08)60156-1     Document Type: Article
Times cited : (66)

References (93)
  • 2
    • 0001045812 scopus 로고
    • Inorganic pyrophosphate and inorganic pyrophosphatases
    • Ernster L. (Ed), Elsevier, Amsterdam
    • Baltscheffsky M., and Baltscheffsky H. Inorganic pyrophosphate and inorganic pyrophosphatases. In: Ernster L. (Ed). "Molecular Mechanisms in Bioenergetics" (1993), Elsevier, Amsterdam 331-348
    • (1993) "Molecular Mechanisms in Bioenergetics" , pp. 331-348
    • Baltscheffsky, M.1    Baltscheffsky, H.2
  • 4
    • 0027219384 scopus 로고
    • Differential sensitivity of membrane-associated pyrophosphatases to inhibition by diphosphonates and fluoride delineates two classes of enzyme
    • Baykov A.A., Dubnova E.B., Bakuleva N.P., Evtushenko O.A., Zhen R.-G., and Rea P.A. Differential sensitivity of membrane-associated pyrophosphatases to inhibition by diphosphonates and fluoride delineates two classes of enzyme. FEBS Letters 327 (1993) 199-202
    • (1993) FEBS Letters , vol.327 , pp. 199-202
    • Baykov, A.A.1    Dubnova, E.B.2    Bakuleva, N.P.3    Evtushenko, O.A.4    Zhen, R.-G.5    Rea, P.A.6
  • 11
    • 0000756080 scopus 로고
    • Localization in sucrose gradients of the pyrophosphate-dependent proton transport of maize root membranes
    • Chanson A., and Pilet P.E. Localization in sucrose gradients of the pyrophosphate-dependent proton transport of maize root membranes. Plant Physiology 84 (1987) 1431-1436
    • (1987) Plant Physiology , vol.84 , pp. 1431-1436
    • Chanson, A.1    Pilet, P.E.2
  • 12
    • 84969816364 scopus 로고
    • Target molecular size and sodium dodecyl sulfate polyacrylamide gel electrophoresis analysis of the ATP-dependent and pyrophosphate-dependent proton pumps from maize root tonoplast
    • Chanson A., and Pilet P.E. Target molecular size and sodium dodecyl sulfate polyacrylamide gel electrophoresis analysis of the ATP-dependent and pyrophosphate-dependent proton pumps from maize root tonoplast. Plant Physiology 90 (1989) 934-938
    • (1989) Plant Physiology , vol.90 , pp. 934-938
    • Chanson, A.1    Pilet, P.E.2
  • 13
    • 0025667013 scopus 로고
    • Floricaula: a homeotic gene required for flower development in Antirrhinum majus
    • Coen E.S., Romero J.M., Doyle S., Elliot R., Murphy G., and Carpenter R. Floricaula: a homeotic gene required for flower development in Antirrhinum majus. Cell 63 (1990) 1311-1322
    • (1990) Cell , vol.63 , pp. 1311-1322
    • Coen, E.S.1    Romero, J.M.2    Doyle, S.3    Elliot, R.4    Murphy, G.5    Carpenter, R.6
  • 14
    • 0020345921 scopus 로고
    • The mechanism of action of yeast inorganic pyrophosphatase
    • Cooperman B.S. The mechanism of action of yeast inorganic pyrophosphatase. Methods in Enzymology 87 (1982) 526-548
    • (1982) Methods in Enzymology , vol.87 , pp. 526-548
    • Cooperman, B.S.1
  • 15
    • 0015934615 scopus 로고
    • Yeast inorganic pyrophosphatase. I. New methods of purification, assay, and crystallization
    • Cooperman B.S., Chiu N.Y., Bruckmann R.H., Bunick G.J., and McKenna G.P. Yeast inorganic pyrophosphatase. I. New methods of purification, assay, and crystallization. Biochemistry 12 (1973) 1665-1669
    • (1973) Biochemistry , vol.12 , pp. 1665-1669
    • Cooperman, B.S.1    Chiu, N.Y.2    Bruckmann, R.H.3    Bunick, G.J.4    McKenna, G.P.5
  • 16
    • 0026628087 scopus 로고
    • Evolutionary conservation of the active site of the soluble inorganic pyrophosphatase
    • Cooperman B.S., Baykov A.A., and Lahti R. Evolutionary conservation of the active site of the soluble inorganic pyrophosphatase. Trends in Biochemical Sciences 17 (1992) 262-266
    • (1992) Trends in Biochemical Sciences , vol.17 , pp. 262-266
    • Cooperman, B.S.1    Baykov, A.A.2    Lahti, R.3
  • 17
    • 0024588364 scopus 로고
    • 2+] and its role in the hormonal regulation of mitochondrial matrix volume
    • 2+] and its role in the hormonal regulation of mitochondrial matrix volume. Biochemical Journal 258 (1989) 817-821
    • (1989) Biochemical Journal , vol.258 , pp. 817-821
    • Davidson, A.M.1    Halestrap, A.P.2
  • 19
    • 0000390119 scopus 로고
    • Fructose 6-phosphate metabolism in plants
    • Dennis D.T., and Greyson M.F. Fructose 6-phosphate metabolism in plants. Physiologia Plantarum 69 (1987) 395-404
    • (1987) Physiologia Plantarum , vol.69 , pp. 395-404
    • Dennis, D.T.1    Greyson, M.F.2
  • 20
    • 0028139560 scopus 로고
    • Light-stimulated proton transport into the vacuoles of leaf mesophyll cells does not require energization by the tonoplast pyrophosphatase
    • Ellebracht A., Heber U., and Sonnewald U. Light-stimulated proton transport into the vacuoles of leaf mesophyll cells does not require energization by the tonoplast pyrophosphatase. Planta 193 (1994) 203-207
    • (1994) Planta , vol.193 , pp. 203-207
    • Ellebracht, A.1    Heber, U.2    Sonnewald, U.3
  • 22
    • 34447112177 scopus 로고
    • Properties and purification of a proton translocating pyrophosphatase in tonoplast of Acer pseudoplatanus
    • Fraichard A., Magnin T., and Pugin A. Properties and purification of a proton translocating pyrophosphatase in tonoplast of Acer pseudoplatanus. Plant Physiology 96S (1991) 159
    • (1991) Plant Physiology , vol.96 S , pp. 159
    • Fraichard, A.1    Magnin, T.2    Pugin, A.3
  • 23
    • 0000969470 scopus 로고    scopus 로고
    • +-pumping inorganic pyrophosphatase: studies using ligand protection from covalent inhibitors
    • +-pumping inorganic pyrophosphatase: studies using ligand protection from covalent inhibitors. Plant Physiology 111 (1996) 195-202
    • (1996) Plant Physiology , vol.111 , pp. 195-202
    • Gordon-Weeks, R.1    Steele, S.H.2    Leigh, R.A.3
  • 24
    • 0019321186 scopus 로고
    • 18OJ]P, species during exchange with water. Application to exchanges catalyzed by yeast inorganic pyrophosphatase
    • 18OJ]P, species during exchange with water. Application to exchanges catalyzed by yeast inorganic pyrophosphatase. Journal of Biological Chemistry 255 (1980) 5320-5328
    • (1980) Journal of Biological Chemistry , vol.255 , pp. 5320-5328
    • Hackney, D.D.1
  • 25
    • 0018817999 scopus 로고
    • Oxygen-18 probes of enzymic reactions of phosphate compounds
    • Hackney D.D., Stempel K.E., and Boyer P.D. Oxygen-18 probes of enzymic reactions of phosphate compounds. Method? in Enzymology 64 (1980) 60-83
    • (1980) Method? in Enzymology , vol.64 , pp. 60-83
    • Hackney, D.D.1    Stempel, K.E.2    Boyer, P.D.3
  • 27
    • 0000786283 scopus 로고
    • A novel sucrose synthase pathway for sucrose degradation in cultured sycamore cells
    • Huber S.C., and Akazawa T. A novel sucrose synthase pathway for sucrose degradation in cultured sycamore cells. Plant Physiology 81 (1986) 1008-1013
    • (1986) Plant Physiology , vol.81 , pp. 1008-1013
    • Huber, S.C.1    Akazawa, T.2
  • 29
    • 0342444416 scopus 로고
    • GUS fusions: β-glucuronidase as a sensitive versatile gene fusion marker in higher plants
    • Jefferson R.A., Kavanagh T.A., and Bevan M.W. GUS fusions: β-glucuronidase as a sensitive versatile gene fusion marker in higher plants. EMBO Journal 6 (1987) 3901-3907
    • (1987) EMBO Journal , vol.6 , pp. 3901-3907
    • Jefferson, R.A.1    Kavanagh, T.A.2    Bevan, M.W.3
  • 30
    • 34249839467 scopus 로고
    • Inorganic pyrophosphatase content and metabolites in potato and tobacco plantsexpressing E. coli pyrophosphatase in their cytosol
    • Jelitto T., Sonnewald U., Willmitzer L., Hajirezeai M., and Stitt M. Inorganic pyrophosphatase content and metabolites in potato and tobacco plantsexpressing E. coli pyrophosphatase in their cytosol. Planta 188 (1992) 238-244
    • (1992) Planta , vol.188 , pp. 238-244
    • Jelitto, T.1    Sonnewald, U.2    Willmitzer, L.3    Hajirezeai, M.4    Stitt, M.5
  • 31
    • 0000914111 scopus 로고
    • 2+ in proton transport by the tonoplast prophosphatase in vacuoles
    • 2+ in proton transport by the tonoplast prophosphatase in vacuoles. Physiologia Plantarum 77 (1989) 326-331
    • (1989) Physiologia Plantarum , vol.77 , pp. 326-331
    • Johannes, E.1    Felle, H.2
  • 32
    • 0013594277 scopus 로고
    • Proton gradient across the tonoplast of Riccia fluitans as a result of the joint action of two electroenzymes
    • Johannes E., and Felle H. Proton gradient across the tonoplast of Riccia fluitans as a result of the joint action of two electroenzymes. Plant Physiology 93 (1990) 412-417
    • (1990) Plant Physiology , vol.93 , pp. 412-417
    • Johannes, E.1    Felle, H.2
  • 33
    • 0028211273 scopus 로고
    • A model recognition approach to the prediction of alpha-helical membrane protein structure and topology
    • Jones D.T., Taylor W.R., and Thornton J.M. A model recognition approach to the prediction of alpha-helical membrane protein structure and topology. Biochemistry 33 (1994) 3038-3049
    • (1994) Biochemistry , vol.33 , pp. 3038-3049
    • Jones, D.T.1    Taylor, W.R.2    Thornton, J.M.3
  • 34
    • 0026497327 scopus 로고
    • In and out and up and down with Lac permease
    • Kaback H.R. In and out and up and down with Lac permease. International Reviews of Cytology 137A (1992) 97-125
    • (1992) International Reviews of Cytology , vol.137 A , pp. 97-125
    • Kaback, H.R.1
  • 36
    • 0028278224 scopus 로고
    • Heterologous expression of plant vacuolar pyrophosphatase in yeast demonstrates sufficiency of the substrate-binding subunit for proton transport
    • Kim E.J., Zhen R.-G., and Rea P.A. Heterologous expression of plant vacuolar pyrophosphatase in yeast demonstrates sufficiency of the substrate-binding subunit for proton transport. Proceedings of the National Academy of Sciences of the USA 91 (1994) 6128-6132
    • (1994) Proceedings of the National Academy of Sciences of the USA , vol.91 , pp. 6128-6132
    • Kim, E.J.1    Zhen, R.-G.2    Rea, P.A.3
  • 38
    • 0030096580 scopus 로고    scopus 로고
    • Cold calcium signaling in Arabidopsis involves two cellular pools and a change in calcium signature after acclimation
    • Knight H., Trewavas A.J., and Knight M.R. Cold calcium signaling in Arabidopsis involves two cellular pools and a change in calcium signature after acclimation. Plant Cell 8 (1996) 489-503
    • (1996) Plant Cell , vol.8 , pp. 489-503
    • Knight, H.1    Trewavas, A.J.2    Knight, M.R.3
  • 39
    • 0023775270 scopus 로고
    • Cloning, molecular characterization, and chromosome localization of the inorganic pyrophosphatase (PPA) gene from S. cerevisiae
    • Kolakowski L.F., Schloesser M., and Cooperman B.S. Cloning, molecular characterization, and chromosome localization of the inorganic pyrophosphatase (PPA) gene from S. cerevisiae. Nucleic Acid Research 16 (1988) 441-452
    • (1988) Nucleic Acid Research , vol.16 , pp. 441-452
    • Kolakowski, L.F.1    Schloesser, M.2    Cooperman, B.S.3
  • 40
    • 11944253488 scopus 로고
    • Peroxidase-induced wilting in transgenic tobacco plants
    • Lagrimini L.M., Bradford S., and Rothstein S. Peroxidase-induced wilting in transgenic tobacco plants. The Plant Cell 2 (1990) 7-18
    • (1990) The Plant Cell , vol.2 , pp. 7-18
    • Lagrimini, L.M.1    Bradford, S.2    Rothstein, S.3
  • 41
    • 0024233964 scopus 로고
    • Cloning and characterization of the gene encoding inorganic pyrophosphatase of Escherichia coli K-12
    • Lahti R., Pitkaranta T., Valve E., Ilta I., Kukko-Kalske E., and Heinonen J. Cloning and characterization of the gene encoding inorganic pyrophosphatase of Escherichia coli K-12. Journal of Bacteriology 170 (1988) 5901-5907
    • (1988) Journal of Bacteriology , vol.170 , pp. 5901-5907
    • Lahti, R.1    Pitkaranta, T.2    Valve, E.3    Ilta, I.4    Kukko-Kalske, E.5    Heinonen, J.6
  • 42
    • 11944268830 scopus 로고
    • +-pyrophosphatase: the roles of magnesium, pyrophosphate, and their complexes as substrates, activators, and inhibitors
    • +-pyrophosphatase: the roles of magnesium, pyrophosphate, and their complexes as substrates, activators, and inhibitors. Plant Physiology 100 (1992) 1698-1705
    • (1992) Plant Physiology , vol.100 , pp. 1698-1705
    • Leigh, R.A.1    Pope, A.J.2    Jennings, I.R.3    Sanders, D.4
  • 43
    • 0029410822 scopus 로고
    • Molecular cloning and expression analysis of isoforms encoding tonoplast-bound proton-translocating inorganic pyrophosphatase in tobacco
    • Lerchl J., Konig S., and Sonnewald U. Molecular cloning and expression analysis of isoforms encoding tonoplast-bound proton-translocating inorganic pyrophosphatase in tobacco. Plant Molecular Biology 29 (1995) 833-840
    • (1995) Plant Molecular Biology , vol.29 , pp. 833-840
    • Lerchl, J.1    Konig, S.2    Sonnewald, U.3
  • 44
    • 0025912666 scopus 로고
    • Yeast PPA2 gene encodes a mitochondrial inorganic pyrophosphatase that is essential for mitochondrial function
    • Lundin M., Baltscheffsky H., and Ronne H. Yeast PPA2 gene encodes a mitochondrial inorganic pyrophosphatase that is essential for mitochondrial function. Journal of Biological Chemistry 266 (1991) 12168-12172
    • (1991) Journal of Biological Chemistry , vol.266 , pp. 12168-12172
    • Lundin, M.1    Baltscheffsky, H.2    Ronne, H.3
  • 45
    • 0017199756 scopus 로고
    • A critical evaluation of the analysis of membrane proteins by polyacrylamide gel electrophoresis in the presence of dodecyl sulphate
    • Maddy A.H. A critical evaluation of the analysis of membrane proteins by polyacrylamide gel electrophoresis in the presence of dodecyl sulphate. Journal of Theoretical Biology 62 (1976) 315-326
    • (1976) Journal of Theoretical Biology , vol.62 , pp. 315-326
    • Maddy, A.H.1
  • 47
    • 0026071909 scopus 로고
    • 2+, and immunological comparison with other inorganic pyrophosphatases
    • 2+, and immunological comparison with other inorganic pyrophosphatases. European Journal of Biochemistry 196 (1991) 11-17
    • (1991) European Journal of Biochemistry , vol.196 , pp. 11-17
    • Maeshima, M.1
  • 48
    • 0024306480 scopus 로고
    • Purification and properties of vacuolar membrane proton-translocating inorganic pyrophosphatase from mung bean
    • Maeshima M., and Yoshida S. Purification and properties of vacuolar membrane proton-translocating inorganic pyrophosphatase from mung bean. Journal of Biological Chemistry 264 (1989) 20068-20073
    • (1989) Journal of Biological Chemistry , vol.264 , pp. 20068-20073
    • Maeshima, M.1    Yoshida, S.2
  • 50
    • 0023650983 scopus 로고
    • The pea mitchondrial ATPase subunit 9 gene is located upstream of the ATPase a-subunit gene
    • Morikama A., and Nakamura K. The pea mitchondrial ATPase subunit 9 gene is located upstream of the ATPase a-subunit gene. Nucleic Acids Research 15 (1987) 4692
    • (1987) Nucleic Acids Research , vol.15 , pp. 4692
    • Morikama, A.1    Nakamura, K.2
  • 52
    • 13144267671 scopus 로고
    • Inhibition of photosynthetic sucrose synthesis by imidodiphosphate, an analog of inorganic pyrophosphate
    • Neuhaus H.E., and Stitt M. Inhibition of photosynthetic sucrose synthesis by imidodiphosphate, an analog of inorganic pyrophosphate. Plant Science 76 (1991) 49-55
    • (1991) Plant Science , vol.76 , pp. 49-55
    • Neuhaus, H.E.1    Stitt, M.2
  • 54
    • 0025752365 scopus 로고
    • Proton pumping /VjW-dicyclohexylcar-bodiimide-sensitive inorganic pyrophosphate synthase from Rhodospirillum rubrum: purification, characterization, and reconstitution
    • Nyren P., Nore B.F., and Strid A. Proton pumping /VjW-dicyclohexylcar-bodiimide-sensitive inorganic pyrophosphate synthase from Rhodospirillum rubrum: purification, characterization, and reconstitution. Biochemistry 30 (1991) 2883-2887
    • (1991) Biochemistry , vol.30 , pp. 2883-2887
    • Nyren, P.1    Nore, B.F.2    Strid, A.3
  • 57
    • 0002893533 scopus 로고
    • Some characteristics of anion transport at the tonoplast of oat roots, determined from the effects of anions on pyrophosphate-dependent proton transport
    • Pope A.J., and Leigh R.A. Some characteristics of anion transport at the tonoplast of oat roots, determined from the effects of anions on pyrophosphate-dependent proton transport. Planta 172 (1987) 91-100
    • (1987) Planta , vol.172 , pp. 91-100
    • Pope, A.J.1    Leigh, R.A.2
  • 59
    • 58149372868 scopus 로고
    • Fluoride leads to an increase of inorganic pyrophosphate and an inhibition of photosynthetic sucrose synthesis in spinach leaves
    • Quick W.P., Neuhaus H.E., Feil R., and Stitt M. Fluoride leads to an increase of inorganic pyrophosphate and an inhibition of photosynthetic sucrose synthesis in spinach leaves. Biochimica et Biophysica Acta 973 (1989) 263-271
    • (1989) Biochimica et Biophysica Acta , vol.973 , pp. 263-271
    • Quick, W.P.1    Neuhaus, H.E.2    Feil, R.3    Stitt, M.4
  • 60
    • 0000088438 scopus 로고
    • +-translocating ATPase of higher plant tonoplast
    • +-translocating ATPase of higher plant tonoplast. Plant Physiology 81 (1986) 126-129
    • (1986) Plant Physiology , vol.81 , pp. 126-129
    • Rea, P.A.1    Poole, R.J.2
  • 62
    • 0011599499 scopus 로고
    • Tonoplast adenosine triphosphatase and inorganic pyrophosphatase
    • Rea P.A., and Turner J.C. Tonoplast adenosine triphosphatase and inorganic pyrophosphatase. Methods in Plant Biochemistry 3 (1990) 385-405
    • (1990) Methods in Plant Biochemistry , vol.3 , pp. 385-405
    • Rea, P.A.1    Turner, J.C.2
  • 63
    • 0000695380 scopus 로고
    • +-transIocating inorganic pyrophosphatase of higher plant cells
    • +-transIocating inorganic pyrophosphatase of higher plant cells. Plant Physiology 100 (1992) 723-732
    • (1992) Plant Physiology , vol.100 , pp. 723-732
    • Rea, P.A.1    Britten, C.J.2    Sarafian, V.3
  • 67
    • 0002900649 scopus 로고
    • +-translocating inorganic pyrophosphatase from vacuole membranes of red beet
    • +-translocating inorganic pyrophosphatase from vacuole membranes of red beet. Plant Physiology 91 (1989) 34-38
    • (1989) Plant Physiology , vol.91 , pp. 34-38
    • Sarafian, V.1    Poole, R.J.2
  • 68
    • 0026512325 scopus 로고
    • Molecular cloning and sequence of cDNA encoding the pyrophosphate-energized vacuolar membrane proton pump of Arabidopsis thaliana
    • Sarafian V., Kim Y., Poole R.J., and Rea P.A. Molecular cloning and sequence of cDNA encoding the pyrophosphate-energized vacuolar membrane proton pump of Arabidopsis thaliana. Proceedings of the National Academy of Sciences of the USA 89 (1992) 1775-1779
    • (1992) Proceedings of the National Academy of Sciences of the USA , vol.89 , pp. 1775-1779
    • Sarafian, V.1    Kim, Y.2    Poole, R.J.3    Rea, P.A.4
  • 72
    • 0027264995 scopus 로고
    • Predicting the topology of eukaryotic membrane proteins
    • Sipos L., and von Heijne G. Predicting the topology of eukaryotic membrane proteins. European Journal of Biochemistry 213 (1993) 1333-1340
    • (1993) European Journal of Biochemistry , vol.213 , pp. 1333-1340
    • Sipos, L.1    von Heijne, G.2
  • 74
    • 0026893738 scopus 로고
    • Expression of E. coli inorganic pyrophosphatase in transgenic plants alters photoassimilate partitioning
    • Sonnewald U. Expression of E. coli inorganic pyrophosphatase in transgenic plants alters photoassimilate partitioning. Plant Journal 2 (1992) 571-581
    • (1992) Plant Journal , vol.2 , pp. 571-581
    • Sonnewald, U.1
  • 75
    • 0019889782 scopus 로고
    • Thermodynamics, kinetics, and mechanism in yeast inorganic pyrophosphatase catalysis of inorganic pyrophosphate: inorganic phosphate equilibration
    • Springs B., Welsh K.M., and Cooperman B.S. Thermodynamics, kinetics, and mechanism in yeast inorganic pyrophosphatase catalysis of inorganic pyrophosphate: inorganic phosphate equilibration. Biochemistry 20 (1981) 6384-6391
    • (1981) Biochemistry , vol.20 , pp. 6384-6391
    • Springs, B.1    Welsh, K.M.2    Cooperman, B.S.3
  • 76
    • 0022554097 scopus 로고
    • Refinements in oxygen-18 methodology for the study of phosphorylation mechanisms
    • Stempel K.E., and Boyer P.D. Refinements in oxygen-18 methodology for the study of phosphorylation mechanisms. Methods in Enzymology 126 (1986) 618-639
    • (1986) Methods in Enzymology , vol.126 , pp. 618-639
    • Stempel, K.E.1    Boyer, P.D.2
  • 78
    • 0024978052 scopus 로고
    • Determination of the inorganic pyrophosphate level and its subcellular localization in Chara corallina
    • Takeshige K., and Tazawa M. Determination of the inorganic pyrophosphate level and its subcellular localization in Chara corallina. Journal of Biological Chemistry 264 (1989) 3262-3266
    • (1989) Journal of Biological Chemistry , vol.264 , pp. 3262-3266
    • Takeshige, K.1    Tazawa, M.2
  • 79
    • 0027170407 scopus 로고
    • Molecular cloning of cDNA for vacuolar membrane proton-translocating inorganic pyrophosphatase in Hordeum vulgare
    • Tanaka Y., Chiba K., Maeda M., and Maeshima M. Molecular cloning of cDNA for vacuolar membrane proton-translocating inorganic pyrophosphatase in Hordeum vulgare. Biochemical and Biophysical Research Communications 190 (1993) 962-967
    • (1993) Biochemical and Biophysical Research Communications , vol.190 , pp. 962-967
    • Tanaka, Y.1    Chiba, K.2    Maeda, M.3    Maeshima, M.4
  • 81
    • 0024212768 scopus 로고
    • Antisense genes in plants: an overview
    • van der Krol A.R., Mol J.N.M., and Stuitje A.R. Antisense genes in plants: an overview. Gene 72 (1988) 45-50
    • (1988) Gene , vol.72 , pp. 45-50
    • van der Krol, A.R.1    Mol, J.N.M.2    Stuitje, A.R.3
  • 82
    • 0025940840 scopus 로고
    • Construction of a functional lactose permease devoid of cysteine residues
    • van Iwaarden P., Pastore J.C., Konings W.N., and Kaback H.R. Construction of a functional lactose permease devoid of cysteine residues. Biochemistry 30 (1991) 9595-9600
    • (1991) Biochemistry , vol.30 , pp. 9595-9600
    • van Iwaarden, P.1    Pastore, J.C.2    Konings, W.N.3    Kaback, H.R.4
  • 84
    • 0000651660 scopus 로고
    • The distribution of positively charged residues in bacterial inner membrane proteins correlates with the transmembrane topology
    • von Heijne G. The distribution of positively charged residues in bacterial inner membrane proteins correlates with the transmembrane topology. EMBO Journal 5 (1994) 3021-3027
    • (1994) EMBO Journal , vol.5 , pp. 3021-3027
    • von Heijne, G.1
  • 85
    • 0026716643 scopus 로고
    • Membrane protein structure prediction. Hydrophobicity analysis and the positive-inside rule
    • von Heijne G. Membrane protein structure prediction. Hydrophobicity analysis and the positive-inside rule. Journal of Molecular Biology 225 (1992) 487-494
    • (1992) Journal of Molecular Biology , vol.225 , pp. 487-494
    • von Heijne, G.1
  • 86
    • 0000703574 scopus 로고
    • 2+-dependent, cation-stimulated inorganic pyrophosphatase associated with vacuoles of red beet (Beta vulgaris L.)
    • 2+-dependent, cation-stimulated inorganic pyrophosphatase associated with vacuoles of red beet (Beta vulgaris L.). Planta 153 (1981) 150-155
    • (1981) Planta , vol.153 , pp. 150-155
    • Walker, R.R.1    Leigh, R.A.2
  • 88
    • 0001197431 scopus 로고
    • Subcellular compartmentation of pyrophosphatase and alkaline pyrophosphatase in leaves
    • Weiner H., Stitt M., and Heldt H.W. Subcellular compartmentation of pyrophosphatase and alkaline pyrophosphatase in leaves. Biochimica et Biophysica Acta 893 (1987) 13-21
    • (1987) Biochimica et Biophysica Acta , vol.893 , pp. 13-21
    • Weiner, H.1    Stitt, M.2    Heldt, H.W.3
  • 90
    • 0025362525 scopus 로고
    • Role of vacuolar acidification in protein sorting and zymogen activation: a genetic analysis of the yeast vacuolar proton-translocating ATPase
    • Yamashiro C.T., Kane P.M., Wolczyk D.F., Preston R.A., and Stevens T.H. Role of vacuolar acidification in protein sorting and zymogen activation: a genetic analysis of the yeast vacuolar proton-translocating ATPase. Molecular and Cellular Biology 10 (1990) 3737-3749
    • (1990) Molecular and Cellular Biology , vol.10 , pp. 3737-3749
    • Yamashiro, C.T.1    Kane, P.M.2    Wolczyk, D.F.3    Preston, R.A.4    Stevens, T.H.5
  • 91
    • 77956718972 scopus 로고
    • +- PPase discloses potential coupling and DCCD-binding sites
    • +- PPase discloses potential coupling and DCCD-binding sites. Plant Physiology 108S (1995) 21
    • (1995) Plant Physiology , vol.108 S , pp. 21
    • Zhen, R.G.1    Rea, P.A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.