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Volumn 20, Issue 4, 2008, Pages 1029-1039

Thylakoid membrane remodeling during state transitions in Arabidopsis

Author keywords

[No Author keywords available]

Indexed keywords

ARABIDOPSIS; ARABIDOPSIS THALIANA; CHLOROPHYTA; EMBRYOPHYTA;

EID: 48549104631     PISSN: 10404651     EISSN: 1532298X     Source Type: Journal    
DOI: 10.1105/tpc.107.055830     Document Type: Article
Times cited : (176)

References (58)
  • 1
    • 0026556851 scopus 로고
    • Protein-phosphorylation in regulation of photosynthesis
    • Allen, J.F. (1992a). Protein-phosphorylation in regulation of photosynthesis. Biochim. Biophys. Acta 1098: 275-335.
    • (1992) Biochim. Biophys. Acta , vol.1098 , pp. 275-335
    • Allen, J.F.1
  • 2
    • 0026513229 scopus 로고
    • How does protein phosphorylation regulate photosynthesis?
    • Allen, J.F. (1992b). How does protein phosphorylation regulate photosynthesis? Trends Biochem. Sci. 17: 12-17.
    • (1992) Trends Biochem. Sci , vol.17 , pp. 12-17
    • Allen, J.F.1
  • 3
    • 0035651544 scopus 로고    scopus 로고
    • Molecular recognition in thylakoid structure and function
    • Allen, J.F., and Forsberg, J. (2001). Molecular recognition in thylakoid structure and function. Trends Plant Sci. 6: 317-326.
    • (2001) Trends Plant Sci , vol.6 , pp. 317-326
    • Allen, J.F.1    Forsberg, J.2
  • 4
    • 0033385137 scopus 로고    scopus 로고
    • Insights into the consequences of grana stacking of thylakoid membranes in vascular plants: A personal perspective
    • Anderson, J.M. (1999). Insights into the consequences of grana stacking of thylakoid membranes in vascular plants: A personal perspective. Aust. J. Plant Physiol. 26: 625-639.
    • (1999) Aust. J. Plant Physiol , vol.26 , pp. 625-639
    • Anderson, J.M.1
  • 5
    • 0014962849 scopus 로고    scopus 로고
    • Arion, W.J., and Racker, E. (1970). Partial resolution of the enzymes catalyzing oxidative phosphorylation. 23. Preservation of energy coupling in submitochondrial particles lacking cytochrome oxidase. J. Biol. Chem. 245: 5186-5194.
    • Arion, W.J., and Racker, E. (1970). Partial resolution of the enzymes catalyzing oxidative phosphorylation. 23. Preservation of energy coupling in submitochondrial particles lacking cytochrome oxidase. J. Biol. Chem. 245: 5186-5194.
  • 6
    • 0037298310 scopus 로고    scopus 로고
    • Redox regulation of thylakoid protein phosphorylation
    • Aro, E.M., and Ohad, I. (2003). Redox regulation of thylakoid protein phosphorylation. Antioxid Redox Signal. 5: 55-67.
    • (2003) Antioxid Redox Signal , vol.5 , pp. 55-67
    • Aro, E.M.1    Ohad, I.2
  • 7
    • 0033377344 scopus 로고    scopus 로고
    • A model for the topology of the chloroplast thylakoid membrane
    • Arvidsson, P.O., and Sundby, C. (1999). A model for the topology of the chloroplast thylakoid membrane. Aust. J. Plant Physiol. 26: 687-694.
    • (1999) Aust. J. Plant Physiol , vol.26 , pp. 687-694
    • Arvidsson, P.O.1    Sundby, C.2
  • 8
    • 33847760762 scopus 로고    scopus 로고
    • Shape transitions in lipid membranes and protein mediated vesicle fusion and fission
    • Atilgan, E., and Sun, S.X. (2007). Shape transitions in lipid membranes and protein mediated vesicle fusion and fission. J. Chem. Phys. 126: 095102.
    • (2007) J. Chem. Phys , vol.126 , pp. 095102
    • Atilgan, E.1    Sun, S.X.2
  • 9
    • 84950058115 scopus 로고
    • An explanation for the relationship between salt-induced thylakoid stacking and the chlorophyll fluorescence changes associated with changes in spillover of energy from photosystem-II to photosystem-I
    • Barber, J. (1980). An explanation for the relationship between salt-induced thylakoid stacking and the chlorophyll fluorescence changes associated with changes in spillover of energy from photosystem-II to photosystem-I. FEBS Lett. 118: 1-10.
    • (1980) FEBS Lett , vol.118 , pp. 1-10
    • Barber, J.1
  • 10
    • 0001299286 scopus 로고
    • Influence of surface-charges on thylakoid structure and function
    • Barber, J. (1982). Influence of surface-charges on thylakoid structure and function. Annu. Rev. Plant Physiol. 33: 261-295.
    • (1982) Annu. Rev. Plant Physiol , vol.33 , pp. 261-295
    • Barber, J.1
  • 11
    • 0001153822 scopus 로고
    • Thylakoid protein phosphorylation during state 1-state 2 transitions in osmotically shocked pea chloroplasts
    • Bennett, J. (1983). Thylakoid protein phosphorylation during state 1-state 2 transitions in osmotically shocked pea chloroplasts. Biochim. Biophys. Acta 722: 176-181.
    • (1983) Biochim. Biophys. Acta , vol.722 , pp. 176-181
    • Bennett, J.1
  • 12
    • 0004207075 scopus 로고
    • Structural modifications in lamellar system of isolated Zea mays chloroplasts under different ionic conditions
    • Brangeon, J. (1974). Structural modifications in lamellar system of isolated Zea mays chloroplasts under different ionic conditions. J. Microsc. Oxford 21: 75-84.
    • (1974) J. Microsc. Oxford , vol.21 , pp. 75-84
    • Brangeon, J.1
  • 13
    • 0008763171 scopus 로고
    • Kinetics of cation-induced changes of photosystem-II fluorescence and of lateral distribution of the 2 photosystems in the thylakoid membranes of pea chloroplasts
    • Briantais, J.M., Vernotte, C., Olive, J., and Wollman, F.A. (1984). Kinetics of cation-induced changes of photosystem-II fluorescence and of lateral distribution of the 2 photosystems in the thylakoid membranes of pea chloroplasts. Biochim. Biophys. Acta 766: 1-8.
    • (1984) Biochim. Biophys. Acta , vol.766 , pp. 1-8
    • Briantais, J.M.1    Vernotte, C.2    Olive, J.3    Wollman, F.A.4
  • 14
    • 0034794143 scopus 로고    scopus 로고
    • Preparation and functional characterization of thylakoids from Arabidopsis thaliana
    • Casazza, A.P., Tarantino, D., and Soave, C. (2001). Preparation and functional characterization of thylakoids from Arabidopsis thaliana. Photosynth. Res. 68: 175-180.
    • (2001) Photosynth. Res , vol.68 , pp. 175-180
    • Casazza, A.P.1    Tarantino, D.2    Soave, C.3
  • 15
    • 0033381539 scopus 로고    scopus 로고
    • Grana formation: Entropy-assisted local order in chloroplasts?
    • Chow, W.S. (1999). Grana formation: Entropy-assisted local order in chloroplasts? Aust. J. Plant Physiol. 26: 641-647.
    • (1999) Aust. J. Plant Physiol , vol.26 , pp. 641-647
    • Chow, W.S.1
  • 16
    • 29144458149 scopus 로고    scopus 로고
    • Granal stacking of thylakoid membranes in higher plant chloroplasts: The physicochemical forces at work and the functional consequences that ensue
    • Chow, W.S., Kim, E.H., Horton, P., and Anderson, J.M. (2005). Granal stacking of thylakoid membranes in higher plant chloroplasts: The physicochemical forces at work and the functional consequences that ensue. Photochem. Photobiol. Sci. 4: 1081-1090.
    • (2005) Photochem. Photobiol. Sci , vol.4 , pp. 1081-1090
    • Chow, W.S.1    Kim, E.H.2    Horton, P.3    Anderson, J.M.4
  • 17
    • 11044234285 scopus 로고    scopus 로고
    • Supramolecular organization of thylakoid membrane proteins in green plants
    • Dekker, J.P., and Boekema, E.J. (2005). Supramolecular organization of thylakoid membrane proteins in green plants. Biochim. Biophys. Acta 1706: 12-39.
    • (2005) Biochim. Biophys. Acta , vol.1706 , pp. 12-39
    • Dekker, J.P.1    Boekema, E.J.2
  • 18
    • 0027489838 scopus 로고
    • Lateral diffusion of an integral nembrane protein - Monte Carlo analysis of the migration of phosphorylated light-harvesting complex-II in the thylakoid membrane
    • Drepper, F., Carlberg, I., Andersson, B., and Haehnel, W. (1993). Lateral diffusion of an integral nembrane protein - Monte Carlo analysis of the migration of phosphorylated light-harvesting complex-II in the thylakoid membrane. Biochemistry 32: 11915-11922.
    • (1993) Biochemistry , vol.32 , pp. 11915-11922
    • Drepper, F.1    Carlberg, I.2    Andersson, B.3    Haehnel, W.4
  • 19
    • 33646253458 scopus 로고    scopus 로고
    • FZL, an FZO-like protein in plants, is a determinant of thylakoid and chloroplast morphology
    • Gao, H., Sage, T.L., and Osteryoung, K.W. (2006). FZL, an FZO-like protein in plants, is a determinant of thylakoid and chloroplast morphology. Proc. Natl. Acad. Sci. USA 103: 6759-6764.
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , pp. 6759-6764
    • Gao, H.1    Sage, T.L.2    Osteryoung, K.W.3
  • 20
    • 84989674854 scopus 로고
    • Organization of pigment protein complexes into macrodomains in the thylakoid membranes of wild-type and chlorophyll-B-less mutant of barley as revealed by circular dichroism
    • Garab, G., Kieleczawa, J., Sutherland, J.C., Bustamante, C., and Hind, G. (1991). Organization of pigment protein complexes into macrodomains in the thylakoid membranes of wild-type and chlorophyll-B-less mutant of barley as revealed by circular dichroism. Photochem. Photobiol. 54: 273-281.
    • (1991) Photochem. Photobiol , vol.54 , pp. 273-281
    • Garab, G.1    Kieleczawa, J.2    Sutherland, J.C.3    Bustamante, C.4    Hind, G.5
  • 21
    • 1642586814 scopus 로고    scopus 로고
    • Role of LHCII-containing macrodomains in the structure, function and dynamics of grana
    • Garab, G., and Mustardy, L. (1999). Role of LHCII-containing macrodomains in the structure, function and dynamics of grana. Aust. J. Plant Physiol. 26: 649-658.
    • (1999) Aust. J. Plant Physiol , vol.26 , pp. 649-658
    • Garab, G.1    Mustardy, L.2
  • 22
    • 0028173557 scopus 로고
    • Release of a light thylakoid membrane fragment with high F-730/F-685 fluorescence emission ratio (77-K) by digitonin disruption from low-salt-destacked or phosphorylated thylakoids of pea
    • Georgakopoulos, J.H., and Argyroudi-Akoyunoglou, J.H. (1994). Release of a light thylakoid membrane fragment with high F-730/F-685 fluorescence emission ratio (77-K) by digitonin disruption from low-salt-destacked or phosphorylated thylakoids of pea. J. Photochem. Photobiol. B 26: 57-65.
    • (1994) J. Photochem. Photobiol. B , vol.26 , pp. 57-65
    • Georgakopoulos, J.H.1    Argyroudi-Akoyunoglou, J.H.2
  • 23
    • 0030831692 scopus 로고    scopus 로고
    • Implication of D1 degradation in phosphorylation-induced state transitions
    • Georgakopoulos, J.H., and Argyroudi-Akoyunoglou, J.H. (1997). Implication of D1 degradation in phosphorylation-induced state transitions. Photosynth. Res. 53: 185-195.
    • (1997) Photosynth. Res , vol.53 , pp. 185-195
    • Georgakopoulos, J.H.1    Argyroudi-Akoyunoglou, J.H.2
  • 24
    • 0000184562 scopus 로고
    • 63 Years since Kautsky - Chlorophyll-a fluorescence
    • Govindjee (1995). 63 Years since Kautsky - Chlorophyll-a fluorescence. Aust. J. Plant Physiol. 22: 131-160.
    • (1995) Aust. J. Plant Physiol , vol.22 , pp. 131-160
    • Govindjee1
  • 25
    • 0035653682 scopus 로고    scopus 로고
    • Balance of power: A view of the mechanism of photosynthetic state transitions
    • Haldrup, A., Jensen, P.E., Lunde, C., and Scheller, H.V. (2001). Balance of power: A view of the mechanism of photosynthetic state transitions. Trends Plant Sci. 6: 301-305.
    • (2001) Trends Plant Sci , vol.6 , pp. 301-305
    • Haldrup, A.1    Jensen, P.E.2    Lunde, C.3    Scheller, H.V.4
  • 26
    • 0020681368 scopus 로고
    • A comparison between cation and protein-phosphorylation effects on the fluorescence induction curve in chloroplasts treated with 3-(3,4-dichlorophenyl)-1,1-dimethylurea
    • Horton, P., and Black, M.T. (1983). A comparison between cation and protein-phosphorylation effects on the fluorescence induction curve in chloroplasts treated with 3-(3,4-dichlorophenyl)-1,1-dimethylurea. Biochim. Biophys. Acta 722: 214-218.
    • (1983) Biochim. Biophys. Acta , vol.722 , pp. 214-218
    • Horton, P.1    Black, M.T.2
  • 27
    • 0000400911 scopus 로고
    • Effect of salts and electron transport on conformation of isolated chloroplasts. 2. Electron microscopy
    • Izawa, S., and Good, N.E. (1966). Effect of salts and electron transport on conformation of isolated chloroplasts. 2. Electron microscopy. Plant Physiol. 41: 544-552.
    • (1966) Plant Physiol , vol.41 , pp. 544-552
    • Izawa, S.1    Good, N.E.2
  • 28
    • 0037112863 scopus 로고    scopus 로고
    • From chloroplasts to photosystems: In situ scanning force microscopy on intact thylakoid membranes
    • Kaftan, D., Brumfeld, V., Nevo, R., Scherz, A., and Reich, Z. (2002). From chloroplasts to photosystems: In situ scanning force microscopy on intact thylakoid membranes. EMBO J. 21: 6146-6153.
    • (2002) EMBO J , vol.21 , pp. 6146-6153
    • Kaftan, D.1    Brumfeld, V.2    Nevo, R.3    Scherz, A.4    Reich, Z.5
  • 31
    • 0034896388 scopus 로고    scopus 로고
    • Light-induced short-term adaptation mechanisms under redox control in the PSII-LHCII supercomplex: LHC II state transitions and PSII repair cycle
    • Kruse, O. (2001). Light-induced short-term adaptation mechanisms under redox control in the PSII-LHCII supercomplex: LHC II state transitions and PSII repair cycle. Naturwissenschaften 88: 284-292.
    • (2001) Naturwissenschaften , vol.88 , pp. 284-292
    • Kruse, O.1
  • 32
    • 0021103921 scopus 로고
    • Lateral mobility of the light-harvesting complex in chloroplast membranes controls excitation energy distribution in higher plants
    • Kyle, D.J., Staehelin, L.A., and Arntzen, C.J. (1983). Lateral mobility of the light-harvesting complex in chloroplast membranes controls excitation energy distribution in higher plants. Arch. Biochem. Biophys. 222: 527-541.
    • (1983) Arch. Biochem. Biophys , vol.222 , pp. 527-541
    • Kyle, D.J.1    Staehelin, L.A.2    Arntzen, C.J.3
  • 33
    • 0028467779 scopus 로고
    • Molecular-cloning of a chloroplastic protein associated with both the envelope and thylakoid membranes
    • Li, H.M., Kaneko, Y., and Keegstra, K. (1994). Molecular-cloning of a chloroplastic protein associated with both the envelope and thylakoid membranes. Plant Mol. Biol. 25: 619-632.
    • (1994) Plant Mol. Biol , vol.25 , pp. 619-632
    • Li, H.M.1    Kaneko, Y.2    Keegstra, K.3
  • 34
    • 29344434866 scopus 로고    scopus 로고
    • The relevance of mitochondrial membrane topology to mitochondrial function
    • Mannella, C.A. (2006). The relevance of mitochondrial membrane topology to mitochondrial function. Biochim. Biophys. Acta 1762: 140-147.
    • (2006) Biochim. Biophys. Acta , vol.1762 , pp. 140-147
    • Mannella, C.A.1
  • 35
    • 0034063592 scopus 로고    scopus 로고
    • Chlorophyll fluorescence - A practical guide
    • Maxwell, K., and Johnson, G.N. (2000). Chlorophyll fluorescence - A practical guide. J. Exp. Bot. 51: 659-668.
    • (2000) J. Exp. Bot , vol.51 , pp. 659-668
    • Maxwell, K.1    Johnson, G.N.2
  • 36
    • 0029168017 scopus 로고
    • Mitotic disassembly of the Golgi apparatus in vivo
    • Misteli, T., and Warren, G. (1995). Mitotic disassembly of the Golgi apparatus in vivo. J. Cell Sci. 108: 2715-2727.
    • (1995) J. Cell Sci , vol.108 , pp. 2715-2727
    • Misteli, T.1    Warren, G.2
  • 37
    • 33748433657 scopus 로고    scopus 로고
    • Differences in chloroplast ultrastructure of Phaeocystis antarctica in low and high light
    • Moisan, T.A., Ellisman, M.H., Buitenhuys, C.W., and Sosinsky, G.E. (2006). Differences in chloroplast ultrastructure of Phaeocystis antarctica in low and high light. Mar. Biol. 149: 1281-1290.
    • (2006) Mar. Biol , vol.149 , pp. 1281-1290
    • Moisan, T.A.1    Ellisman, M.H.2    Buitenhuys, C.W.3    Sosinsky, G.E.4
  • 38
    • 27644537088 scopus 로고    scopus 로고
    • Function and evolution of grana
    • Mullineaux, C.W. (2005). Function and evolution of grana. Trends Plant Sci. 10: 521-525.
    • (2005) Trends Plant Sci , vol.10 , pp. 521-525
    • Mullineaux, C.W.1
  • 39
    • 13944249560 scopus 로고    scopus 로고
    • State transitions: An example of acclimation to low-light stress
    • Mullineaux, C.W., and Emlyn-Jones, D. (2005). State transitions: An example of acclimation to low-light stress. J. Exp. Bot. 56: 389-393.
    • (2005) J. Exp. Bot , vol.56 , pp. 389-393
    • Mullineaux, C.W.1    Emlyn-Jones, D.2
  • 40
    • 0015116719 scopus 로고
    • Role of cations in organization of chloroplast membranes
    • Murakami, S., and Packer, L. (1971). Role of cations in organization of chloroplast membranes. Arch. Biochem. Biophys. 146: 337-347.
    • (1971) Arch. Biochem. Biophys , vol.146 , pp. 337-347
    • Murakami, S.1    Packer, L.2
  • 41
    • 0037712992 scopus 로고    scopus 로고
    • Granum revisited. A three-dimensional model where things fall into place
    • Mustardy, L., and Garab, G. (2003). Granum revisited. A three-dimensional model where things fall into place. Trends Plant Sci. 8: 117-122.
    • (2003) Trends Plant Sci , vol.8 , pp. 117-122
    • Mustardy, L.1    Garab, G.2
  • 42
    • 0015590205 scopus 로고
    • Chloroplast organization and ultrastructural localization of photosystems I and II
    • Nir, I., and Pease, D.C. (1973). Chloroplast organization and ultrastructural localization of photosystems I and II. J Ultrastruct Res. 42: 534-550.
    • (1973) J Ultrastruct Res , vol.42 , pp. 534-550
    • Nir, I.1    Pease, D.C.2
  • 43
    • 0041328335 scopus 로고    scopus 로고
    • Functional significance of the lipid-protein interface in photosynthetic membranes
    • Pali, T., Garab, G., Horvath, L.I., and Kota, Z. (2003). Functional significance of the lipid-protein interface in photosynthetic membranes. Cell. Mol. Life Sci. 60: 1591-1606.
    • (2003) Cell. Mol. Life Sci , vol.60 , pp. 1591-1606
    • Pali, T.1    Garab, G.2    Horvath, L.I.3    Kota, Z.4
  • 44
    • 26044440113 scopus 로고
    • Determination of accurate extinction coefficients and simultaneous equations for assaying chlorophyll a and chlorophyll b extracted with 4 different solvents - Verification of the concentration of chlorophyll standards by atomic-absorption spectroscopy
    • Porra, R.J., Thompson, W.A., and Kriedemann, P.E. (1989). Determination of accurate extinction coefficients and simultaneous equations for assaying chlorophyll a and chlorophyll b extracted with 4 different solvents - Verification of the concentration of chlorophyll standards by atomic-absorption spectroscopy. Biochim. Biophys. Acta 975: 384-394.
    • (1989) Biochim. Biophys. Acta , vol.975 , pp. 384-394
    • Porra, R.J.1    Thompson, W.A.2    Kriedemann, P.E.3
  • 45
    • 0030830941 scopus 로고    scopus 로고
    • Phosphorylation of light-harvesting complex II and photosystem II core proteins shows different irradiance-dependent regulation in vivo. Application of phosphothreonine antibodies to analysis of thylakoid phosphoproteins
    • Rintamaki, E., Salonen, M., Suoranta, U.M., Carlberg, I., Andersson, B., and Aro, E.M. (1997). Phosphorylation of light-harvesting complex II and photosystem II core proteins shows different irradiance-dependent regulation in vivo. Application of phosphothreonine antibodies to analysis of thylakoid phosphoproteins. J. Biol. Chem. 272: 30476-30482.
    • (1997) J. Biol. Chem , vol.272 , pp. 30476-30482
    • Rintamaki, E.1    Salonen, M.2    Suoranta, U.M.3    Carlberg, I.4    Andersson, B.5    Aro, E.M.6
  • 46
    • 34249887084 scopus 로고    scopus 로고
    • Role of thylakoid protein kinases in photosynthetic acclimation
    • Rochaix, J.D. (2007). Role of thylakoid protein kinases in photosynthetic acclimation. FEBS Lett. 581: 2768-2775.
    • (2007) FEBS Lett , vol.581 , pp. 2768-2775
    • Rochaix, J.D.1
  • 47
    • 0036194199 scopus 로고    scopus 로고
    • Rapid, reversible alterations in spinach thylakoid appression upon changes in light intensity
    • Rozak, P.R., Seiser, R.M., Wacholtz, W.F., and Wise, R.R. (2002). Rapid, reversible alterations in spinach thylakoid appression upon changes in light intensity. Plant Cell Environ. 25: 421-429.
    • (2002) Plant Cell Environ , vol.25 , pp. 421-429
    • Rozak, P.R.1    Seiser, R.M.2    Wacholtz, W.F.3    Wise, R.R.4
  • 48
    • 0020991649 scopus 로고
    • Freeze-fracture analysis of membrane appression and protein segregation in model membranes containing the chlorophyll-protein complexes from chloroplasts
    • Ryrie, I.J. (1983). Freeze-fracture analysis of membrane appression and protein segregation in model membranes containing the chlorophyll-protein complexes from chloroplasts. Eur. J. Biochem. 137: 205-213.
    • (1983) Eur. J. Biochem , vol.137 , pp. 205-213
    • Ryrie, I.J.1
  • 49
    • 33644687594 scopus 로고    scopus 로고
    • Three-dimensional organization of higher-plant chloroplast thylakoid membranes revealed by electron tomography
    • Shimoni, E., Rav-Hon, O., Ohad, I., Brumfeld, V., and Reich, Z. (2005). Three-dimensional organization of higher-plant chloroplast thylakoid membranes revealed by electron tomography. Plant Cell 17: 2580-2586.
    • (2005) Plant Cell , vol.17 , pp. 2580-2586
    • Shimoni, E.1    Rav-Hon, O.2    Ohad, I.3    Brumfeld, V.4    Reich, Z.5
  • 50
    • 0017190320 scopus 로고
    • Reversible particle movements associated with unstacking and restacking of chloroplast membranes in vitro
    • Staehelin, L.A. (1976). Reversible particle movements associated with unstacking and restacking of chloroplast membranes in vitro. J. Cell Biol. 71: 136-158.
    • (1976) J. Cell Biol , vol.71 , pp. 136-158
    • Staehelin, L.A.1
  • 51
    • 57749115510 scopus 로고    scopus 로고
    • Staehelin, L., and Van der staay, G. (1996). Structure, composition, functional organization and dynamic properties of thylakoid membranes. In Oxygenic Photosynthesis: The Light Reactions, D.R. Ort and C.F. Yocum, eds (Dordrecht, The Netherlands: Kluwer Academic Publishers), pp. 11-30.
    • Staehelin, L., and Van der staay, G. (1996). Structure, composition, functional organization and dynamic properties of thylakoid membranes. In Oxygenic Photosynthesis: The Light Reactions, D.R. Ort and C.F. Yocum, eds (Dordrecht, The Netherlands: Kluwer Academic Publishers), pp. 11-30.
  • 52
    • 0029177883 scopus 로고
    • Stacking and separation of photosystem I and photosystem II in plant thylakoid membranes: A physico-chemical view
    • Stys, D. (1995). Stacking and separation of photosystem I and photosystem II in plant thylakoid membranes: A physico-chemical view. Physiol. Plant. 95: 651-657.
    • (1995) Physiol. Plant , vol.95 , pp. 651-657
    • Stys, D.1
  • 53
    • 0344787506 scopus 로고
    • The cation-dependence of the degree of protein phosphorylation-induced unstacking of pea thylakoids
    • Telfer, A., Hodges, M., Millner, P.A., and Barber, J. (1984). The cation-dependence of the degree of protein phosphorylation-induced unstacking of pea thylakoids. Biochim. Biophys. Acta 766: 554-562.
    • (1984) Biochim. Biophys. Acta , vol.766 , pp. 554-562
    • Telfer, A.1    Hodges, M.2    Millner, P.A.3    Barber, J.4
  • 54
    • 33847199803 scopus 로고    scopus 로고
    • Sheets, ribbons and tubules - How organelles get their shape
    • Voeltz, G.K., and Prinz, W.A. (2007). Sheets, ribbons and tubules - How organelles get their shape. Nat. Rev. Mol. Cell Biol. 8: 258-264.
    • (2007) Nat. Rev. Mol. Cell Biol , vol.8 , pp. 258-264
    • Voeltz, G.K.1    Prinz, W.A.2
  • 55
    • 16544394373 scopus 로고    scopus 로고
    • Deletion of the chloroplast-localized thylakoid formation1 gene product in Arabidopsis leads to deficient thylakoid formation and variegated leaves
    • Wang, Q., Sullivan, R.W., Kight, A., Henry, R.L., Huang, J.R., Jones, A.M., and Korth, K.L. (2004). Deletion of the chloroplast-localized thylakoid formation1 gene product in Arabidopsis leads to deficient thylakoid formation and variegated leaves. Plant Physiol. 136: 3594-3604.
    • (2004) Plant Physiol , vol.136 , pp. 3594-3604
    • Wang, Q.1    Sullivan, R.W.2    Kight, A.3    Henry, R.L.4    Huang, J.R.5    Jones, A.M.6    Korth, K.L.7
  • 56
    • 0035898532 scopus 로고    scopus 로고
    • State transitions reveal the dynamics and flexibility of the photosynthetic apparatus
    • Wollman, F.A. (2001). State transitions reveal the dynamics and flexibility of the photosynthetic apparatus. EMBO J. 20: 3623-3630.
    • (2001) EMBO J , vol.20 , pp. 3623-3630
    • Wollman, F.A.1
  • 57
    • 0033529310 scopus 로고    scopus 로고
    • Regulation of thylakoid protein phosphorylation at the substrate level: Reversible light-induced conformational changes expose the phosphorylation site of the light-harvesting complex II
    • Zer, H., Vink, M., Keren, N., Dilly-Hartwig, H.G., Paulsen, H., Herrmann, R.G., Andersson, B., and Ohad, I. (1999). Regulation of thylakoid protein phosphorylation at the substrate level: Reversible light-induced conformational changes expose the phosphorylation site of the light-harvesting complex II. Proc. Natl. Acad. Sci. USA 96: 8277-8282.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 8277-8282
    • Zer, H.1    Vink, M.2    Keren, N.3    Dilly-Hartwig, H.G.4    Paulsen, H.5    Herrmann, R.G.6    Andersson, B.7    Ohad, I.8
  • 58
    • 0347579832 scopus 로고    scopus 로고
    • Light affects the accessibility of the thylakoid light harvesting complex II (LHCII) phosphorylation site to the membrane protein kinase(s)
    • Zer, H., Vink, M., Shochat, S., Herrmann, R.G., Andersson, B., and Ohad, I. (2003). Light affects the accessibility of the thylakoid light harvesting complex II (LHCII) phosphorylation site to the membrane protein kinase(s). Biochemistry. 42: 728-738.
    • (2003) Biochemistry , vol.42 , pp. 728-738
    • Zer, H.1    Vink, M.2    Shochat, S.3    Herrmann, R.G.4    Andersson, B.5    Ohad, I.6


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