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Volumn 1465, Issue 1-2, 2000, Pages 307-323

Solute pores, ion channels, and metabolite transporters in the outer and inner envelope membranes of higher plant plastids

Author keywords

Channel; Plastid envelope membrane; Porin; Transport protein

Indexed keywords

CARRIER PROTEIN; ION CHANNEL; MEMBRANE PROTEIN; OUTER MEMBRANE PROTEIN; PORIN;

EID: 0034193582     PISSN: 00052736     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0005-2736(00)00146-2     Document Type: Review
Times cited : (90)

References (116)
  • 1
    • 0025224152 scopus 로고
    • Biochemistry and function of the plastid envelope
    • Douce R., Joyard J. Biochemistry and function of the plastid envelope. Annu. Rev. Cell Biol. 6:1990;173-216.
    • (1990) Annu. Rev. Cell Biol. , vol.6 , pp. 173-216
    • Douce, R.1    Joyard, J.2
  • 2
    • 0029328453 scopus 로고
    • Nitrate nutrient and signal for plant growth
    • Crawford N.M. Nitrate nutrient and signal for plant growth. Plant Cell. 7:1995;859-868.
    • (1995) Plant Cell , vol.7 , pp. 859-868
    • Crawford, N.M.1
  • 3
    • 0000307632 scopus 로고
    • Sulfur metabolism in plants
    • Anderson J.W. Sulfur metabolism in plants. Biochem. Plants. 00:1990;328-375.
    • (1990) Biochem. Plants , vol.0 , pp. 328-375
    • Anderson, J.W.1
  • 4
    • 0026704801 scopus 로고
    • Single channel recording in the chloroplast envelope
    • Pottosin I.I. Single channel recording in the chloroplast envelope. FEBS Lett. 308:1992;87-90.
    • (1992) FEBS Lett. , vol.308 , pp. 87-90
    • Pottosin, I.I.1
  • 5
    • 0002595586 scopus 로고
    • Pore forming activity in the outer membrane of the chloroplast envelope
    • Flügge U.I., Benz R. Pore forming activity in the outer membrane of the chloroplast envelope. FEBS Lett. 169:1984;85-89.
    • (1984) FEBS Lett. , vol.169 , pp. 85-89
    • Flügge, U.I.1    Benz, R.2
  • 7
    • 0028341536 scopus 로고
    • Permeation of hydrophilic solutes through mitochondrial outer membranes review on mitochondrial porins
    • Benz R. Permeation of hydrophilic solutes through mitochondrial outer membranes review on mitochondrial porins. Biochim. Biophys. Acta. 1197:1994;167-196.
    • (1994) Biochim. Biophys. Acta , vol.1197 , pp. 167-196
    • Benz, R.1
  • 8
    • 0027771708 scopus 로고
    • Transport across the bacterial outer membrane
    • Nikaido H. Transport across the bacterial outer membrane. J. Bioenerg. Biomembr. 25:1993;581-589.
    • (1993) J. Bioenerg. Biomembr. , vol.25 , pp. 581-589
    • Nikaido, H.1
  • 9
    • 0028946962 scopus 로고
    • Structural basis for sugar translocation through maltoporin channels at 3.1A resolution
    • Schirmer T., Keller T.A., Wang Y.F., Rosenbusch J.P. Structural basis for sugar translocation through maltoporin channels at 3.1A resolution. Science. 267:1995;512-514.
    • (1995) Science , vol.267 , pp. 512-514
    • Schirmer, T.1    Keller, T.A.2    Wang, Y.F.3    Rosenbusch, J.P.4
  • 10
    • 0030926805 scopus 로고    scopus 로고
    • Ligand-specific opening of a gated-porin channel in the outer membrane of living bacteria
    • Jiang X., Payne M.A., Cao Z., Foster S.B., Feix J.B., Newton S.M., Klebba P.E. Ligand-specific opening of a gated-porin channel in the outer membrane of living bacteria. Science. 276:1997;1261-1264.
    • (1997) Science , vol.276 , pp. 1261-1264
    • Jiang, X.1    Payne, M.A.2    Cao, Z.3    Foster, S.B.4    Feix, J.B.5    Newton, S.M.6    Klebba, P.E.7
  • 11
    • 0031464541 scopus 로고    scopus 로고
    • Reconstitution of a chloroplast protein import channel
    • Hinnah S.C., Hill K., Wagner R., Schlicher T., Soll J. Reconstitution of a chloroplast protein import channel. EMBO J. 16:1997;7351-7360.
    • (1997) EMBO J. , vol.16 , pp. 7351-7360
    • Hinnah, S.C.1    Hill, K.2    Wagner, R.3    Schlicher, T.4    Soll, J.5
  • 12
    • 0030787877 scopus 로고    scopus 로고
    • Isolation and characterization of an amino acid-selective channel protein present in the chloroplastic outer envelope membrane
    • Pohlmeyer K., Soll J., Steinkamp T., Hinnah S., Wagner R. Isolation and characterization of an amino acid-selective channel protein present in the chloroplastic outer envelope membrane. Proc. Natl. Acad. Sci. USA. 94:1997;9504-9509.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 9504-9509
    • Pohlmeyer, K.1    Soll, J.2    Steinkamp, T.3    Hinnah, S.4    Wagner, R.5
  • 13
    • 0032125382 scopus 로고    scopus 로고
    • A high-conductance solute channel in the chloroplastic outer envelope from pea
    • Pohlmeyer K., Soll J., Grimm R., Hill K., Wagner R. A high-conductance solute channel in the chloroplastic outer envelope from pea. Plant Cell. 10:1998;1207-1216.
    • (1998) Plant Cell , vol.10 , pp. 1207-1216
    • Pohlmeyer, K.1    Soll, J.2    Grimm, R.3    Hill, K.4    Wagner, R.5
  • 14
    • 0032563173 scopus 로고    scopus 로고
    • Voltage gating is a fundamental feature of porin and toxin beta-barrel membrane channels
    • Bainbridge G., Gokce I., Lakey J.H. Voltage gating is a fundamental feature of porin and toxin beta-barrel membrane channels. FEBS Lett. 431:1998;305-308.
    • (1998) FEBS Lett. , vol.431 , pp. 305-308
    • Bainbridge, G.1    Gokce, I.2    Lakey, J.H.3
  • 15
    • 0028025336 scopus 로고
    • Porins and specific diffusion channels in bacterial outer membranes
    • Nikaido H. Porins and specific diffusion channels in bacterial outer membranes. J. Biol. Chem. 269:1994;3905-3908.
    • (1994) J. Biol. Chem. , vol.269 , pp. 3905-3908
    • Nikaido, H.1
  • 16
    • 0014477179 scopus 로고
    • PH changes in the inner phase of the thylakoids during photosynthesis
    • Rumberg B., Siggel U. pH changes in the inner phase of the thylakoids during photosynthesis. Naturwissenschaften. 56:1969;130-132.
    • (1969) Naturwissenschaften , vol.56 , pp. 130-132
    • Rumberg, B.1    Siggel, U.2
  • 17
    • 0015904985 scopus 로고
    • Alkalization of the chloroplast stroma caused by light dependent proton flux into the thylakoid space
    • Heldt H.W., Werdan K., Milovancev M., Geller G. Alkalization of the chloroplast stroma caused by light dependent proton flux into the thylakoid space. Biochim. Biophys. Acta. 314:1973;224-241.
    • (1973) Biochim. Biophys. Acta , vol.314 , pp. 224-241
    • Heldt, H.W.1    Werdan, K.2    Milovancev, M.3    Geller, G.4
  • 18
    • 0012718461 scopus 로고
    • 2+, and an amine anesthetic on stromal pH and photosynthesis
    • 2+, and an amine anesthetic on stromal pH and photosynthesis. Plant Physiol. 95:1991;1229-1236.
    • (1991) Plant Physiol. , vol.95 , pp. 1229-1236
    • Peters, J.S.1    Berkowitz, G.A.2
  • 19
    • 0027324802 scopus 로고
    • Ion channels in the thylakoid membrane (A patch clamp study)
    • Enz C., Steinkamp T., Wagner R. Ion channels in the thylakoid membrane (A patch clamp study). Biochim. Biophys. Acta. 1143:1993;67-76.
    • (1993) Biochim. Biophys. Acta , vol.1143 , pp. 67-76
    • Enz, C.1    Steinkamp, T.2    Wagner, R.3
  • 20
    • 0009796007 scopus 로고
    • + concentrations. I. Light induced cation uptake into intact chloroplasts is driven by an electrical potential difference
    • + concentrations. I. Light induced cation uptake into intact chloroplasts is driven by an electrical potential difference. Plant Physiol. 73:1983;169-174.
    • (1983) Plant Physiol. , vol.73 , pp. 169-174
    • Demming, B.1    Gimmler, H.2
  • 22
    • 0008584460 scopus 로고
    • + flux across the chloroplast envelope are associated with regulation of stromal pH and photosynthesis
    • + flux across the chloroplast envelope are associated with regulation of stromal pH and photosynthesis. Plant Physiol. 97:1991;580-587.
    • (1991) Plant Physiol. , vol.97 , pp. 580-587
    • Wu, W.H.1    Peters, J.2    Berkowitz, G.A.3
  • 25
    • 0028152342 scopus 로고
    • +-stimulated ATPase in pea chloroplasts inner envelope vesicles
    • +-stimulated ATPase in pea chloroplasts inner envelope vesicles. Plant Physiol. 106:1994;731-737.
    • (1994) Plant Physiol. , vol.106 , pp. 731-737
    • Shingles, R.1    McCarty, R.E.2
  • 27
    • 0009773326 scopus 로고
    • Effects of magnesium on intact chloroplast. I. Evidence of activation of (sodium) potassium/proton exchange across the chloroplast envelope
    • Huber S.C., Maury J. Effects of magnesium on intact chloroplast. I. Evidence of activation of (sodium) potassium/proton exchange across the chloroplast envelope. Plant Physiol. 65:1980;350-354.
    • (1980) Plant Physiol. , vol.65 , pp. 350-354
    • Huber, S.C.1    Maury, J.2
  • 28
    • 0343612113 scopus 로고
    • Effect of magnesium on intact chloroplast. II. Cation specificity and involvement of the envelope ATPase in (sodium) potassium/proton exchange across the envelope
    • Maury W.J., Huber S.C., Moreland D.E. Effect of magnesium on intact chloroplast. II. Cation specificity and involvement of the envelope ATPase in (sodium) potassium/proton exchange across the envelope. Plant Physiol. 69:1981;719-728.
    • (1981) Plant Physiol. , vol.69 , pp. 719-728
    • Maury, W.J.1    Huber, S.C.2    Moreland, D.E.3
  • 29
    • 0039919932 scopus 로고
    • Lidocaine and ATPase inhibitor interaction with the chloroplast envelope
    • Wu W.H., Berkowitz G.A. Lidocaine and ATPase inhibitor interaction with the chloroplast envelope. Plant Physiol. 97:1991;1551-1557.
    • (1991) Plant Physiol. , vol.97 , pp. 1551-1557
    • Wu, W.H.1    Berkowitz, G.A.2
  • 30
    • 0000546107 scopus 로고
    • + exchange through chloroplast envelope ion channels
    • + exchange through chloroplast envelope ion channels. Plant Physiol. 98:1992;666-672.
    • (1992) Plant Physiol. , vol.98 , pp. 666-672
    • Wu, W.H.1    Berkowitz, G.A.2
  • 32
    • 0001226199 scopus 로고    scopus 로고
    • Direct measurement of calcium transport across chloroplast inner-envelope vesicles
    • Roh M.H., Shingles R., Cleveland M.J., McCarty R.E. Direct measurement of calcium transport across chloroplast inner-envelope vesicles. Plant Physiol. 118:1998;1447-1454.
    • (1998) Plant Physiol. , vol.118 , pp. 1447-1454
    • Roh, M.H.1    Shingles, R.2    Cleveland, M.J.3    McCarty, R.E.4
  • 35
    • 1642549595 scopus 로고
    • Light-dependent hydrogen ion fluxes are compensated by chloride-fluxes
    • in: N. Murata (Ed.), Kluwer, Dordrecht
    • G. Schönknecht, M. Thaler, W. Simonis, Light-dependent hydrogen ion fluxes are compensated by chloride-fluxes, in: N. Murata (Ed.), Research on Photosynthesis, Kluwer, Dordrecht, 1992, pp. 777-780.
    • (1992) Research on Photosynthesis , pp. 777-780
    • Schönknecht, G.1    Thaler, M.2    Simonis, W.3
  • 36
    • 0028912359 scopus 로고
    • A voltage-dependent porin-like channel in the inner membrane of plant chloroplasts
    • Fuks B., Homble F. A voltage-dependent porin-like channel in the inner membrane of plant chloroplasts. J. Biol. Chem. 270:1995;9947-9952.
    • (1995) J. Biol. Chem. , vol.270 , pp. 9947-9952
    • Fuks, B.1    Homble, F.2
  • 38
    • 0041111565 scopus 로고
    • Biosynthesis of starch: ADPglucose pyrophosphorylase, the regulatory enzyme of starch synthesis structure-function relationships
    • Preiss J. Biosynthesis of starch: ADPglucose pyrophosphorylase, the regulatory enzyme of starch synthesis structure-function relationships. Denpun Kagaku. 40:1993;117-131.
    • (1993) Denpun Kagaku , vol.40 , pp. 117-131
    • Preiss, J.1
  • 39
    • 0017851328 scopus 로고
    • Specific transport of inorganic phosphate, 3-phosphoglycerate and triose phosphates across the inner membrane of the envelope in spinach chloroplasts
    • Fliege R., Flügge U.I., Werdan K., Heldt H.W. Specific transport of inorganic phosphate, 3-phosphoglycerate and triose phosphates across the inner membrane of the envelope in spinach chloroplasts. Biochim. Biophys. Acta. 502:1978;232-247.
    • (1978) Biochim. Biophys. Acta , vol.502 , pp. 232-247
    • Fliege, R.1    Flügge, U.I.2    Werdan, K.3    Heldt, H.W.4
  • 40
    • 0024574552 scopus 로고
    • The triose phosphate-3-phosphoglycerate-phosphate translocator from spinach chloroplasts: Nucleic acid sequence of a full length cDNA clone
    • Flügge U.I., Fischer K., Gross A., Sebald W., Lottspeich F., Eckerskorn C. The triose phosphate-3-phosphoglycerate-phosphate translocator from spinach chloroplasts: nucleic acid sequence of a full length cDNA clone. EMBO J. 8:1989;39-46.
    • (1989) EMBO J. , vol.8 , pp. 39-46
    • Flügge, U.I.1    Fischer, K.2    Gross, A.3    Sebald, W.4    Lottspeich, F.5    Eckerskorn, C.6
  • 41
    • 0028371131 scopus 로고
    • Cloning and in vivo expression of functional triose phosphate/phosphate translocarors from C3- And C4-plants: Evidence for the putative participation of specific amino acid residues in the recognition of phosphoenolpyruvate
    • Fischer K., Arbinger B., Kammerer B., Busch C., Brink S., Wallmeier H., Sauer N., Eckerskorn C., Flügge U.I. Cloning and in vivo expression of functional triose phosphate/phosphate translocarors from C3- and C4-plants: evidence for the putative participation of specific amino acid residues in the recognition of phosphoenolpyruvate. Plant J. 5:1994;215-226.
    • (1994) Plant J. , vol.5 , pp. 215-226
    • Fischer, K.1    Arbinger, B.2    Kammerer, B.3    Busch, C.4    Brink, S.5    Wallmeier, H.6    Sauer, N.7    Eckerskorn, C.8    Flügge, U.I.9
  • 42
    • 0028155460 scopus 로고
    • A rapid method for measuring organelle-specific substrate transport in homogenates from plant tissues
    • Flügge U.I., Weber A. A rapid method for measuring organelle-specific substrate transport in homogenates from plant tissues. Planta. 194:1994;181-185.
    • (1994) Planta , vol.194 , pp. 181-185
    • Flügge, U.I.1    Weber, A.2
  • 43
    • 0000227641 scopus 로고
    • The phosphate-triose phosphate-phosphoglycerate translocator of the chloroplast
    • Flügge U.I., Heldt H.W. The phosphate-triose phosphate-phosphoglycerate translocator of the chloroplast. Trends Biochem. Sci. 9:1984;530-533.
    • (1984) Trends Biochem. Sci. , vol.9 , pp. 530-533
    • Flügge, U.I.1    Heldt, H.W.2
  • 45
    • 0031885634 scopus 로고    scopus 로고
    • Energy supply for the ATP-synthase deficient chloroplasts of Chlamydomonas reinhardii
    • Boschetti A., Schmid K. Energy supply for the ATP-synthase deficient chloroplasts of Chlamydomonas reinhardii. Plant Cell Physiol. 39:1998;160-168.
    • (1998) Plant Cell Physiol. , vol.39 , pp. 160-168
    • Boschetti, A.1    Schmid, K.2
  • 46
    • 0023972404 scopus 로고
    • Restoration of photosynthetic growth in a mutant of Chlamydomonas reinhardtii in which the chloroplast atpB gene of the ATP synthase has a deletion: An example of mitochondrial dependent photosynthesis
    • Lemaire C., Wollman F.A., Bennoun A. Restoration of photosynthetic growth in a mutant of Chlamydomonas reinhardtii in which the chloroplast atpB gene of the ATP synthase has a deletion: An example of mitochondrial dependent photosynthesis. Proc. Natl. Acad. Sci. USA. 85:1988;1344-1348.
    • (1988) Proc. Natl. Acad. Sci. USA , vol.85 , pp. 1344-1348
    • Lemaire, C.1    Wollman, F.A.2    Bennoun, A.3
  • 47
    • 0000939796 scopus 로고
    • Molecular cloning and structural analysis of the phosphate translocator from pea chloroplasts and its comparison to the spinach phosphate translocator
    • Willey D.L., Fischer K., Wachter E., Link T.A., Flügge U.I. Molecular cloning and structural analysis of the phosphate translocator from pea chloroplasts and its comparison to the spinach phosphate translocator. Planta. 183:1991;451-461.
    • (1991) Planta , vol.183 , pp. 451-461
    • Willey, D.L.1    Fischer, K.2    Wachter, E.3    Link, T.A.4    Flügge, U.I.5
  • 48
    • 0037482189 scopus 로고
    • Hydrodynamic properties of the Triton X-100-solubilized chloroplast phosphate translocator
    • Flügge U.I. Hydrodynamic properties of the Triton X-100-solubilized chloroplast phosphate translocator. Biochim. Biophys. Acta. 815:1985;299-305.
    • (1985) Biochim. Biophys. Acta , vol.815 , pp. 299-305
    • Flügge, U.I.1
  • 49
    • 0023118165 scopus 로고
    • Solute carriers involved in energy transfer of mitochondria from a homologous protein family
    • Aquila H., Link T.A., Klingenberg M. Solute carriers involved in energy transfer of mitochondria from a homologous protein family. FEBS Lett. 212:1987;1-9.
    • (1987) FEBS Lett. , vol.212 , pp. 1-9
    • Aquila, H.1    Link, T.A.2    Klingenberg, M.3
  • 50
    • 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. J. Mol. Biol. 225:1992;487-494.
    • (1992) J. Mol. Biol. , vol.225 , pp. 487-494
    • Von Heijne, G.1
  • 51
    • 0001160047 scopus 로고
    • Different in vitro and in vivo targeting properties of the transit peptide of a chloroplast envelope inner membrane protein
    • Silva-Filho M.C., Wieërs M., Flügge U.I., Chaumont F., Boutry M. Different in vitro and in vivo targeting properties of the transit peptide of a chloroplast envelope inner membrane protein. J. Biol. Chem. 272:1987;15264-15266.
    • (1987) J. Biol. Chem. , vol.272 , pp. 15264-15266
    • Silva-Filho, M.C.1    Wieërs, M.2    Flügge, U.I.3    Chaumont, F.4    Boutry, M.5
  • 52
    • 0029360523 scopus 로고
    • The N-terminal hydrophobic region of the mature phosphate translocator is sufficient for targeting to the chloroplast inner envelope membrane
    • Knight J.S., Gray J.C. The N-terminal hydrophobic region of the mature phosphate translocator is sufficient for targeting to the chloroplast inner envelope membrane. Plant Cell. 7:1995;1421-1432.
    • (1995) Plant Cell , vol.7 , pp. 1421-1432
    • Knight, J.S.1    Gray, J.C.2
  • 53
    • 0027411773 scopus 로고
    • Expression of the functional mature chloroplast triose phosphate translocator in yeast and purification of the histidin-tagged protein by a single step chromatography step
    • Loddenkötter B., Kammerer B., Fischer K., Flügge U.I. Expression of the functional mature chloroplast triose phosphate translocator in yeast and purification of the histidin-tagged protein by a single step chromatography step. Proc. Natl. Acad. Sci. USA. 90:1993;2155-2159.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 2155-2159
    • Loddenkötter, B.1    Kammerer, B.2    Fischer, K.3    Flügge, U.I.4
  • 54
    • 0000713345 scopus 로고
    • Capacities of pea chloroplasts to catalyse the oxidative pentose phosphate pathway and glycolysis
    • Stitt M., ap Rees T. Capacities of pea chloroplasts to catalyse the oxidative pentose phosphate pathway and glycolysis. Phytochemistry. 18:1979;1905-1911.
    • (1979) Phytochemistry , vol.18 , pp. 1905-1911
    • Stitt, M.1    Ap Rees, T.2
  • 57
    • 0028813444 scopus 로고
    • Molecular organization of the shikimate pathway in higher plants
    • Schmid J., Amrhein N. Molecular organization of the shikimate pathway in higher plants. Phytochemistry. 39:1995;737-749.
    • (1995) Phytochemistry , vol.39 , pp. 737-749
    • Schmid, J.1    Amrhein, N.2
  • 58
    • 0028794939 scopus 로고
    • Biosynthesis of branched chain amino acids: From test tubes to field
    • Singh B.K., Shaner D.L. Biosynthesis of branched chain amino acids: From test tubes to field. Plant Cell. 7:1995;935-944.
    • (1995) Plant Cell , vol.7 , pp. 935-944
    • Singh, B.K.1    Shaner, D.L.2
  • 59
    • 0031105611 scopus 로고    scopus 로고
    • A new class of plastidic phosphate translocator a putative link between primary and secondary metabolism by the phosphoenolpyruvate/phosphate antiporter
    • Fischer K., Kammerer B., Gutensohn M., Arbinger B., Weber A., Häusler R., Flügge U.I. A new class of plastidic phosphate translocator a putative link between primary and secondary metabolism by the phosphoenolpyruvate/phosphate antiporter. Plant Cell. 9:1997;543-562.
    • (1997) Plant Cell , vol.9 , pp. 543-562
    • Fischer, K.1    Kammerer, B.2    Gutensohn, M.3    Arbinger, B.4    Weber, A.5    Häusler, R.6    Flügge, U.I.7
  • 60
    • 0025162804 scopus 로고
    • Lack of fructose-1,6-bisphosphatase in a range of higher plants that store starch
    • Entwistle G., ap Rees T. Lack of fructose-1,6-bisphosphatase in a range of higher plants that store starch. Biochem. J. 271:1990;467-472.
    • (1990) Biochem. J. , vol.271 , pp. 467-472
    • Entwistle, G.1    Ap Rees, T.2
  • 61
    • 0031464334 scopus 로고    scopus 로고
    • Metabolism and transport in non-photosynthetic plastids
    • Emes M.J., Neuhaus H.E. Metabolism and transport in non-photosynthetic plastids. J. Exp. Bot. 48:1998;1995-2005.
    • (1998) J. Exp. Bot. , vol.48 , pp. 1995-2005
    • Emes, M.J.1    Neuhaus, H.E.2
  • 62
    • 0001552084 scopus 로고
    • Nitrite reduction and carbohydrate metabolism in plastids purified from roots of Pisum sativum L.
    • Bowsher C.G., Hucklesby D.P., Emes M.J. Nitrite reduction and carbohydrate metabolism in plastids purified from roots of Pisum sativum L. Planta. 177:1989;359-366.
    • (1989) Planta , vol.177 , pp. 359-366
    • Bowsher, C.G.1    Hucklesby, D.P.2    Emes, M.J.3
  • 63
    • 0001802996 scopus 로고
    • Starch synthesis by isolated amyloplasts from wheat endosperm
    • Tyson R.H., ap Rees T. Starch synthesis by isolated amyloplasts from wheat endosperm. Planta. 175:1988;33-38.
    • (1988) Planta , vol.175 , pp. 33-38
    • Tyson, R.H.1    Ap Rees, T.2
  • 64
    • 0028093886 scopus 로고
    • Starch synthesis and carbohydrate oxidation in amyloplasts from developing wheat endosperm
    • Tetlow I.J., Blisset K.J., Emes M.J. Starch synthesis and carbohydrate oxidation in amyloplasts from developing wheat endosperm. Planta. 194:1994;454-460.
    • (1994) Planta , vol.194 , pp. 454-460
    • Tetlow, I.J.1    Blisset, K.J.2    Emes, M.J.3
  • 65
    • 0029982947 scopus 로고    scopus 로고
    • Reconstitution of the hexose phosphate translocator from the envelope membranes of wheat endoperm amyloplasts
    • Tetlow I.J., Bowsher C.G., Emes M.J. Reconstitution of the hexose phosphate translocator from the envelope membranes of wheat endoperm amyloplasts. Biochem. J. 319:1996;717-723.
    • (1996) Biochem. J. , vol.319 , pp. 717-723
    • Tetlow, I.J.1    Bowsher, C.G.2    Emes, M.J.3
  • 66
    • 0002113153 scopus 로고
    • Evidence that glucose 6-phosphate is imported as the substrate for starch synthesis by the plastids of developing pea embryos
    • Hill L.M., Smith A.M. Evidence that glucose 6-phosphate is imported as the substrate for starch synthesis by the plastids of developing pea embryos. Planta. 185:1991;91-96.
    • (1991) Planta , vol.185 , pp. 91-96
    • Hill, L.M.1    Smith, A.M.2
  • 67
    • 0001578389 scopus 로고
    • Characterization of glucose-6-phosphate incorporation into starch by isolated intact cauliflower-bud plastids
    • Neuhaus H.E., Henrichs G., Scheibe R. Characterization of glucose-6-phosphate incorporation into starch by isolated intact cauliflower-bud plastids. Plant Physiol. 101:1993;573-578.
    • (1993) Plant Physiol. , vol.101 , pp. 573-578
    • Neuhaus, H.E.1    Henrichs, G.2    Scheibe, R.3
  • 68
    • 0001325327 scopus 로고
    • Specific transport of inorganic phosphate, glucose 6-phosphate, dihydroxyacetone phosphate and 3-phosphoglycerate into amyloplasts
    • Borchert S., Große H., Heldt H.W. Specific transport of inorganic phosphate, glucose 6-phosphate, dihydroxyacetone phosphate and 3-phosphoglycerate into amyloplasts. FEBS Lett. 253:1989;183-186.
    • (1989) FEBS Lett. , vol.253 , pp. 183-186
    • Borchert, S.1    Große, H.2    Heldt, H.W.3
  • 69
    • 0031834277 scopus 로고    scopus 로고
    • Molecular characterisation of a carbon transporter in plastids from heterotrophic tissues the glucose 6-phosphate/phosphate antiporter
    • Kammerer B., Fischer K., Hilpert B., Schubert S., Gutensohn M., Weber A., Flügge U.I. Molecular characterisation of a carbon transporter in plastids from heterotrophic tissues the glucose 6-phosphate/phosphate antiporter. Plant Cell. 10:1998;105-117.
    • (1998) Plant Cell , vol.10 , pp. 105-117
    • Kammerer, B.1    Fischer, K.2    Hilpert, B.3    Schubert, S.4    Gutensohn, M.5    Weber, A.6    Flügge, U.I.7
  • 70
    • 0000600563 scopus 로고
    • Reductant for glutamate synthase is generated by the oxidative pentose phosphate pathway in non-photosynthetic root plastids
    • Bowsher C.G., Boulton E.L., Rose J., Nayagam S., Emes M.J. Reductant for glutamate synthase is generated by the oxidative pentose phosphate pathway in non-photosynthetic root plastids. Plant J. 2:1992;894-898.
    • (1992) Plant J. , vol.2 , pp. 894-898
    • Bowsher, C.G.1    Boulton, E.L.2    Rose, J.3    Nayagam, S.4    Emes, M.J.5
  • 71
    • 0028815182 scopus 로고
    • Coupled movements of glucose 6-phosphate and triose phosphate across the envelopes of plastids from developing embryos of pea (Pisum sativum L.)
    • Hill L.M., Smith A.M. Coupled movements of glucose 6-phosphate and triose phosphate across the envelopes of plastids from developing embryos of pea (Pisum sativum L.). J. Plant Physiol. 146:1995;411-417.
    • (1995) J. Plant Physiol. , vol.146 , pp. 411-417
    • Hill, L.M.1    Smith, A.M.2
  • 72
    • 0000023327 scopus 로고
    • Comparison of the kinetic properties, inhibition and labelling of the phosphate translocators from maize and spinach mesophyll chloroplasts
    • Gross A., Brückner G., Heldt H.W., Flügge U.I. Comparison of the kinetic properties, inhibition and labelling of the phosphate translocators from maize and spinach mesophyll chloroplasts. Planta. 180:1990;262-271.
    • (1990) Planta , vol.180 , pp. 262-271
    • Gross, A.1    Brückner, G.2    Heldt, H.W.3    Flügge, U.I.4
  • 73
    • 0003025740 scopus 로고
    • The regulation and control of photosynthetic carbon assimilation
    • in: C.H. Foyer, P.W. Quick (Eds.), Taylor and Francis, London
    • P.W. Quick, H.E. Neuhaus, The regulation and control of photosynthetic carbon assimilation, in: C.H. Foyer, P.W. Quick (Eds.), A Molecular Approach to Primary Metabolism in Plants, Taylor and Francis, London, 1995, pp. 41-61.
    • (1995) A Molecular Approach to Primary Metabolism in Plants , pp. 41-61
    • Quick, P.W.1    Neuhaus, H.E.2
  • 74
    • 0012477911 scopus 로고
    • Alterations in growth, photosynthesis and respiration in a starchless mutant of Arabidopsis thaliana deficient in chloroplast phosphoglucose mutase activity
    • Casper T., Huber S.C., Somerville C.R. Alterations in growth, photosynthesis and respiration in a starchless mutant of Arabidopsis thaliana deficient in chloroplast phosphoglucose mutase activity. Plant Physiol. 79:1986;1-7.
    • (1986) Plant Physiol. , vol.79 , pp. 1-7
    • Casper, T.1    Huber, S.C.2    Somerville, C.R.3
  • 76
    • 0001186989 scopus 로고
    • Glucose transport into spinach chloroplasts
    • Schäfer G., Heber U., Heldt H.W. Glucose transport into spinach chloroplasts. Plant Physiol. 60:1977;286-289.
    • (1977) Plant Physiol. , vol.60 , pp. 286-289
    • Schäfer, G.1    Heber, U.2    Heldt, H.W.3
  • 77
    • 0001983884 scopus 로고
    • Accumulation of maltose during photosynthesis in protoplasts isolated from spinach leaves treated with mannose
    • Herold A., Leegood R., McNeil P.H., Robinson S.P. Accumulation of maltose during photosynthesis in protoplasts isolated from spinach leaves treated with mannose. Plant Physiol. 67:1981;85-88.
    • (1981) Plant Physiol. , vol.67 , pp. 85-88
    • Herold, A.1    Leegood, R.2    McNeil, P.H.3    Robinson, S.P.4
  • 78
    • 0030573165 scopus 로고    scopus 로고
    • The chloroplasts envelope is permeable for maltose but not for maltodextrins
    • Rost S., Frank C., Beck E. The chloroplasts envelope is permeable for maltose but not for maltodextrins. Biochim. Biophys. Acta. 1291:1997;221-227.
    • (1997) Biochim. Biophys. Acta , vol.1291 , pp. 221-227
    • Rost, S.1    Frank, C.2    Beck, E.3
  • 79
    • 0029168324 scopus 로고
    • Starch degradation in intact amyloplasts from cauliflower buds (Brassica oleracea L.)
    • Neuhaus H.E., Henrichs G., Scheibe R. Starch degradation in intact amyloplasts from cauliflower buds (Brassica oleracea L.). Planta. 195:1995;496-504.
    • (1995) Planta , vol.195 , pp. 496-504
    • Neuhaus, H.E.1    Henrichs, G.2    Scheibe, R.3
  • 81
    • 0027978717 scopus 로고
    • A mutant of Arabidopsis thaliana lacking the ability to transport glucose across the chloroplast envelope
    • Trethewey R.N., ap Rees T. A mutant of Arabidopsis thaliana lacking the ability to transport glucose across the chloroplast envelope. Biochem. J. 301:1994;449-454.
    • (1994) Biochem. J. , vol.301 , pp. 449-454
    • Trethewey, R.N.1    Ap Rees, T.2
  • 82
    • 0028084170 scopus 로고
    • Reduction of the chloroplastic fructose-1,6-bisphosphatase in transgenic potato plants impairs photosynthesis and plant growth
    • Koßmann J., Sonnewald U., Willmitzer L. Reduction of the chloroplastic fructose-1,6-bisphosphatase in transgenic potato plants impairs photosynthesis and plant growth. Plant J. 6:1994;637-650.
    • (1994) Plant J. , vol.6 , pp. 637-650
    • Koßmann, J.1    Sonnewald, U.2    Willmitzer, L.3
  • 83
    • 0041538843 scopus 로고    scopus 로고
    • Compensation of decreased triose phosphate/phosphate translocator activity by accelerated starch turnover and glucose transport in transgenic tobacco
    • Häusler R., Schlieben N.H., Schulz B., Flügge U.I. Compensation of decreased triose phosphate/phosphate translocator activity by accelerated starch turnover and glucose transport in transgenic tobacco. Planta. 204:1998;366-376.
    • (1998) Planta , vol.204 , pp. 366-376
    • Häusler, R.1    Schlieben, N.H.2    Schulz, B.3    Flügge, U.I.4
  • 84
    • 0017862824 scopus 로고
    • Dicarboxylate transport across the inner membrane of the chloroplasts envelope
    • Lehner K., Heldt H.W. Dicarboxylate transport across the inner membrane of the chloroplasts envelope. Biochim. Biophys. Acta. 501:1978;531-544.
    • (1978) Biochim. Biophys. Acta , vol.501 , pp. 531-544
    • Lehner, K.1    Heldt, H.W.2
  • 85
    • 0000796160 scopus 로고
    • A two-translocator model for the transport of 2-oxoglutarate and glutamate in chloroplasts during ammonia assimilation in the light
    • Woo K.C., Flügge U.I., Heldt H.W. A two-translocator model for the transport of 2-oxoglutarate and glutamate in chloroplasts during ammonia assimilation in the light. Plant Physiol. 84:1987;624-632.
    • (1987) Plant Physiol. , vol.84 , pp. 624-632
    • Woo, K.C.1    Flügge, U.I.2    Heldt, H.W.3
  • 86
    • 84995036286 scopus 로고
    • Light/dark modulation: Regulation of chloroplast metabolism in a new light
    • Scheibe R. Light/dark modulation: Regulation of chloroplast metabolism in a new light. Bot. Acta. 103:1990;327-334.
    • (1990) Bot. Acta , vol.103 , pp. 327-334
    • Scheibe, R.1
  • 87
    • 0002026724 scopus 로고
    • A specific translocator for oxaloacetate transport in chloroplasts
    • Hatch M.D., Dröscher L., Flügge U.I., Heldt H.W. A specific translocator for oxaloacetate transport in chloroplasts. FEBS Lett. 178:1984;15-19.
    • (1984) FEBS Lett. , vol.178 , pp. 15-19
    • Hatch, M.D.1    Dröscher, L.2    Flügge, U.I.3    Heldt, H.W.4
  • 88
    • 0025766501 scopus 로고
    • Molecular aspects of plastid envelope biochemistry
    • Joyard J., Block M.A., Douce R. Molecular aspects of plastid envelope biochemistry. Eur. J. Biochem. 199:1991;489-509.
    • (1991) Eur. J. Biochem. , vol.199 , pp. 489-509
    • Joyard, J.1    Block, M.A.2    Douce, R.3
  • 89
    • 0027474355 scopus 로고
    • Purification and functional reconstitution of the 2-oxoglutarate/malate translocator from spinach chloroplasts
    • Menzlaff E., Flügge U.I. Purification and functional reconstitution of the 2-oxoglutarate/malate translocator from spinach chloroplasts. Biochim. Biophys. Acta. 1147:1993;13-18.
    • (1993) Biochim. Biophys. Acta , vol.1147 , pp. 13-18
    • Menzlaff, E.1    Flügge, U.I.2
  • 90
    • 0003269891 scopus 로고
    • A mutant of Arabidopsis deficient in chloroplasts dicarboxylate transport is missing an envelope protein
    • Somerville S.C., Somerville C.R. A mutant of Arabidopsis deficient in chloroplasts dicarboxylate transport is missing an envelope protein. Plant Sci. Lett. 37:1985;317-320.
    • (1985) Plant Sci. Lett. , vol.37 , pp. 317-320
    • Somerville, S.C.1    Somerville, C.R.2
  • 91
    • 0028917799 scopus 로고
    • The 2-oxoglutarate/malate translocator of the chloroplasts envelope membranes: Molecular cloning of a transporter containing 12-helix motif and expression of the functional protein in yeast cells
    • Weber A., Menzlaff E., Arbinger B., Gutensohn M., Eckerskorn C., Flügge U.I. The 2-oxoglutarate/malate translocator of the chloroplasts envelope membranes: Molecular cloning of a transporter containing 12-helix motif and expression of the functional protein in yeast cells. Biochemistry. 34:1995;2621-2627.
    • (1995) Biochemistry , vol.34 , pp. 2621-2627
    • Weber, A.1    Menzlaff, E.2    Arbinger, B.3    Gutensohn, M.4    Eckerskorn, C.5    Flügge, U.I.6
  • 92
    • 0031397428 scopus 로고    scopus 로고
    • Evidence that a malate/inorganic phosphate translocator imports carbon across the leucoplast envelope for fatty acid synthesis in developing castor seed endosperm
    • Eastmond P.J., Dennis D.T., Rawsthorne S. Evidence that a malate/inorganic phosphate translocator imports carbon across the leucoplast envelope for fatty acid synthesis in developing castor seed endosperm. Plant Physiol. 114:1997;851-856.
    • (1997) Plant Physiol. , vol.114 , pp. 851-856
    • Eastmond, P.J.1    Dennis, D.T.2    Rawsthorne, S.3
  • 93
    • 0001080443 scopus 로고
    • Malate- And pyruvate-dependent fatty acid synthesis in leucoplasts from developing castor endosperm
    • Smith R.G., Gauthier D.A., Dennis D.T., Turpin D.H. Malate- and pyruvate-dependent fatty acid synthesis in leucoplasts from developing castor endosperm. Plant Physiol. 98:1992;1233-1238.
    • (1992) Plant Physiol. , vol.98 , pp. 1233-1238
    • Smith, R.G.1    Gauthier, D.A.2    Dennis, D.T.3    Turpin, D.H.4
  • 94
    • 0024600466 scopus 로고
    • Molecular aspects of adenine nucleotide carrier from mitochondria
    • Klingenberg M. Molecular aspects of adenine nucleotide carrier from mitochondria. Arch. Biochem. Biophys. 270:1989;1-14.
    • (1989) Arch. Biochem. Biophys. , vol.270 , pp. 1-14
    • Klingenberg, M.1
  • 95
    • 0026505331 scopus 로고
    • Topography of glycosylation reactions in the endoplasmic reticulum
    • Abeijon C., Hirschberg C.B. Topography of glycosylation reactions in the endoplasmic reticulum. Trends Biol. Sci. 17:1992;32-36.
    • (1992) Trends Biol. Sci. , vol.17 , pp. 32-36
    • Abeijon, C.1    Hirschberg, C.B.2
  • 97
    • 0026209190 scopus 로고
    • Nucleotide sequence of two cDNAs encoding the adenine nucleotide translocator from Zea mays L.
    • Winning B.M., Day C.D., Sarah C.J., Leaver C.J. Nucleotide sequence of two cDNAs encoding the adenine nucleotide translocator from Zea mays L. Plant Mol. Biol. 17:1991;305-307.
    • (1991) Plant Mol. Biol. , vol.17 , pp. 305-307
    • Winning, B.M.1    Day, C.D.2    Sarah, C.J.3    Leaver, C.J.4
  • 98
    • 0002552053 scopus 로고
    • Adenine nucleotide translocation in spinach chloroplasts
    • Heldt H.W. Adenine nucleotide translocation in spinach chloroplasts. FEBS Lett. 5:1969;11-14.
    • (1969) FEBS Lett. , vol.5 , pp. 11-14
    • Heldt, H.W.1
  • 99
    • 0029742096 scopus 로고    scopus 로고
    • Starch degradation in chloroplasts isolated from C3 or CAM induced Mesembryanthemum crystallinum L.
    • Neuhaus H.E., Schulte N. Starch degradation in chloroplasts isolated from C3 or CAM induced Mesembryanthemum crystallinum L. Biochem. J. 318:1996;945-953.
    • (1996) Biochem. J. , vol.318 , pp. 945-953
    • Neuhaus, H.E.1    Schulte, N.2
  • 100
    • 0002910808 scopus 로고
    • Inhibitors of the adenine nucleotide translocase
    • Stubbs M. Inhibitors of the adenine nucleotide translocase. Int. Encycl. Pharm. Ther. 107:1981;283-304.
    • (1981) Int. Encycl. Pharm. Ther. , vol.107 , pp. 283-304
    • Stubbs, M.1
  • 101
    • 0001313742 scopus 로고
    • ATP/ADP translocator from pea root plastids. Comparison with translocators from spinach chloroplasts and pea leaf mitochondria
    • Schünemann D., Borchert S., Flügge U.I., Heldt H.W. ATP/ADP translocator from pea root plastids. Comparison with translocators from spinach chloroplasts and pea leaf mitochondria. Plant Physiol. 103:1993;131-137.
    • (1993) Plant Physiol. , vol.103 , pp. 131-137
    • Schünemann, D.1    Borchert, S.2    Flügge, U.I.3    Heldt, H.W.4
  • 102
    • 0031036197 scopus 로고    scopus 로고
    • Characterization of a novel ATP/ADP transporter from Arabidopsis thaliana L.
    • Neuhaus H.E., Thom E., Möhlmann T., Steup M., Kampfenkel K. Characterization of a novel ATP/ADP transporter from Arabidopsis thaliana L. Plant J. 11:1997;73-82.
    • (1997) Plant J. , vol.11 , pp. 73-82
    • Neuhaus, H.E.1    Thom, E.2    Möhlmann, T.3    Steup, M.4    Kampfenkel, K.5
  • 103
    • 0028822675 scopus 로고
    • Molecular characterization of an Arabidopsis thaliana cDNA encoding a novel putative adenylate translocator of higher plants
    • Kampfenkel K., Möhlmann T., Batz O., van Montagu M., Inzé D., Neuhaus H.E. Molecular characterization of an Arabidopsis thaliana cDNA encoding a novel putative adenylate translocator of higher plants. FEBS Lett. 374:1995;351-355.
    • (1995) FEBS Lett. , vol.374 , pp. 351-355
    • Kampfenkel, K.1    Möhlmann, T.2    Batz, O.3    Van Montagu, M.4    Inzé, D.5    Neuhaus, H.E.6
  • 104
    • 0024456846 scopus 로고
    • Nucleotide sequence of the Rickettsia prowazekii ATP/ADP translocase-encoding gene
    • Williamson L.R., Plano G.V., Winkler H.H., Krause D.C., Wood D.O. Nucleotide sequence of the Rickettsia prowazekii ATP/ADP translocase-encoding gene. Gene. 80:1989;269-278.
    • (1989) Gene , vol.80 , pp. 269-278
    • Williamson, L.R.1    Plano, G.V.2    Winkler, H.H.3    Krause, D.C.4    Wood, D.O.5
  • 105
    • 0017230491 scopus 로고
    • Rickettsial permeability: An ADP-ATP transport system
    • Winkler H.H. Rickettsial permeability: an ADP-ATP transport system. J. Biol. Chem. 251:1976;389-396.
    • (1976) J. Biol. Chem. , vol.251 , pp. 389-396
    • Winkler, H.H.1
  • 106
    • 0020266408 scopus 로고
    • Adenine nucleotide and lysine transport in Chlamydia psittaci
    • Hatch T.P., Al-Hossainy E., Silverman J.A. Adenine nucleotide and lysine transport in Chlamydia psittaci. J. Bacteriol. 150:1982;662-670.
    • (1982) J. Bacteriol. , vol.150 , pp. 662-670
    • Hatch, T.P.1    Al-Hossainy, E.2    Silverman, J.A.3
  • 107
    • 0033030228 scopus 로고    scopus 로고
    • Two nucleotide transport proteins in Chlamydia trachomatis. One for net nucleoside triphosphate uptake and the other for the transport of energy
    • Tjaden J., van der Laan M., Schwöppe C., Möhlmann T., Winkler H.H., Neuhaus H.E. Two nucleotide transport proteins in Chlamydia trachomatis. One for net nucleoside triphosphate uptake and the other for the transport of energy. J. Bacteriol. 181:1999;1196-1202.
    • (1999) J. Bacteriol. , vol.181 , pp. 1196-1202
    • Tjaden, J.1    Van Der Laan, M.2    Schwöppe, C.3    Möhlmann, T.4    Winkler, H.H.5    Neuhaus, H.E.6
  • 108
    • 0030593468 scopus 로고    scopus 로고
    • Over-production of proteins in Escherichia coli: Mutant hosts that allow synthesis of some membrane proteins and globular proteins at high levels
    • Miroux B., Walker J.E. Over-production of proteins in Escherichia coli: mutant hosts that allow synthesis of some membrane proteins and globular proteins at high levels. J. Mol. Biol. 260:1996;289-298.
    • (1996) J. Mol. Biol. , vol.260 , pp. 289-298
    • Miroux, B.1    Walker, J.E.2
  • 109
    • 2642673614 scopus 로고    scopus 로고
    • Expression of a plastidic ATP/ADP transporter gene in Escherichia coli leads to a functional adenine nucleotide transport system in the bacterial cytoplasmic membrane
    • Tjaden J., Schwöppe C., Möhlmann T., Neuhaus H.E. Expression of a plastidic ATP/ADP transporter gene in Escherichia coli leads to a functional adenine nucleotide transport system in the bacterial cytoplasmic membrane. J. Biol. Chem. 273:1998;9630-9636.
    • (1998) J. Biol. Chem. , vol.273 , pp. 9630-9636
    • Tjaden, J.1    Schwöppe, C.2    Möhlmann, T.3    Neuhaus, H.E.4
  • 110
    • 0032521666 scopus 로고    scopus 로고
    • Occurrence of two plastidic ATP/ADP transporters in Arabidopsis thaliana: Molecular characterisation and comparative structural analysis of homologous ATP/ADP translocators from plastids and Rickettsia prowazekii
    • Möhlmann T., Tjaden J., Schwöppe C., Winkler H.H., Kampfenkel K., Neuhaus H.E. Occurrence of two plastidic ATP/ADP transporters in Arabidopsis thaliana: Molecular characterisation and comparative structural analysis of homologous ATP/ADP translocators from plastids and Rickettsia prowazekii. Eur. J. Biochem. 252:1998;353-359.
    • (1998) Eur. J. Biochem. , vol.252 , pp. 353-359
    • Möhlmann, T.1    Tjaden, J.2    Schwöppe, C.3    Winkler, H.H.4    Kampfenkel, K.5    Neuhaus, H.E.6
  • 111
    • 0028190781 scopus 로고
    • Starch and fatty acid synthesis in plastids from developing embryos of oilseed rape (Brassica napus L.)
    • Kang F., Rawsthorne S. Starch and fatty acid synthesis in plastids from developing embryos of oilseed rape (Brassica napus L.). Plant J. 6:1994;795-805.
    • (1994) Plant J. , vol.6 , pp. 795-805
    • Kang, F.1    Rawsthorne, S.2
  • 112
    • 0028118987 scopus 로고
    • Interaction between starch synthesis and fatty-acid synthesis in isolated cauliflower-bud amyloplasts
    • Möhlmann T., Scheibe R., Neuhaus H.E. Interaction between starch synthesis and fatty-acid synthesis in isolated cauliflower-bud amyloplasts. Planta. 194:1994;492-497.
    • (1994) Planta , vol.194 , pp. 492-497
    • Möhlmann, T.1    Scheibe, R.2    Neuhaus, H.E.3
  • 113
    • 0006233414 scopus 로고    scopus 로고
    • Analysis of the precursor and effector dependency of lipid synthesis in amyloplasts isolated from developing wheat- Or maize-endosperm tissue
    • Möhlmann T., Neuhaus H.E. Analysis of the precursor and effector dependency of lipid synthesis in amyloplasts isolated from developing wheat- or maize-endosperm tissue. J. Cereal Sci. 26:1997;161-167.
    • (1997) J. Cereal Sci. , vol.26 , pp. 161-167
    • Möhlmann, T.1    Neuhaus, H.E.2
  • 114
    • 0032439289 scopus 로고    scopus 로고
    • Altered plastidic ATP/ADP-transporter activity influences potato (Solanum tuberosum) morphology, amount and composition of tuber starch, and tuber morphology
    • Tjaden J., Möhlmann T., Kampfenkel K., Henrichs G., Neuhaus H.E. Altered plastidic ATP/ADP-transporter activity influences potato (Solanum tuberosum) morphology, amount and composition of tuber starch, and tuber morphology. Plant J. 16:1998;531-540.
    • (1998) Plant J. , vol.16 , pp. 531-540
    • Tjaden, J.1    Möhlmann, T.2    Kampfenkel, K.3    Henrichs, G.4    Neuhaus, H.E.5
  • 116
    • 0029328417 scopus 로고
    • Starch biosynthesis
    • Martin C., Smith A.M. Starch biosynthesis. Plant Cell. 7:1995;971-985.
    • (1995) Plant Cell , vol.7 , pp. 971-985
    • Martin, C.1    Smith, A.M.2


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