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Volumn 10, Issue 2, 2004, Pages 147-151

In vivo turn-over of D1 reaction center core protein of photosystem II extends photosynthetic efficiency under light stress

Author keywords

[No Author keywords available]

Indexed keywords

EUGLENA;

EID: 4644262399     PISSN: 09715894     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Short Survey
Times cited : (2)

References (56)
  • 1
    • 0030471302 scopus 로고    scopus 로고
    • Protein stability and degradation in chloroplasts
    • Adam, Z. (1996). Protein stability and degradation in chloroplasts. Plant Mol. Biol., 32 : 773-783.
    • (1996) Plant Mol. Biol. , vol.32 , pp. 773-783
    • Adam, Z.1
  • 2
    • 0033865239 scopus 로고    scopus 로고
    • Chloroplast proteases: Possible regulators of gene expression?
    • Adam, Z. (2000). Chloroplast proteases: possible regulators of gene expression? Biochemie, 82 : 647-654.
    • (2000) Biochemie , vol.82 , pp. 647-654
    • Adam, Z.1
  • 3
    • 0003955248 scopus 로고    scopus 로고
    • Chloroplast proteases and their role in photosynthesis regulation
    • (Eds Eva-Mari and Andersson, B.) Kluwer Academic Publishers
    • Adam, Z. (2001). Chloroplast proteases and their role in photosynthesis regulation. In: Regulation of Photosynthesis, (Eds Eva-Mari and Andersson, B.) Kluwer Academic Publishers, pp 265-276.
    • (2001) Regulation of Photosynthesis , pp. 265-276
    • Adam, Z.1
  • 4
    • 0034866092 scopus 로고    scopus 로고
    • Degradation of unassembled and damaged thylakoid proteins
    • Adam, Z. and Ostersetzer, O. (2001). Degradation of unassembled and damaged thylakoid proteins. Biochem. Soc. Trans., 29 : 427-430.
    • (2001) Biochem. Soc. Trans. , vol.29 , pp. 427-430
    • Adam, Z.1    Ostersetzer, O.2
  • 5
    • 0029872716 scopus 로고    scopus 로고
    • Degradation of the light-stress protein is mediated by an ATP-independent, serine-type protease under low-light conditions
    • Adamska, I., Lindahl, M., Roobol-Boza, M. and Andersson, B. (1996). Degradation of the light-stress protein is mediated by an ATP-independent, serine-type protease under low-light conditions. Eur. J. Biochem., 236 : 591-599.
    • (1996) Eur. J. Biochem. , vol.236 , pp. 591-599
    • Adamska, I.1    Lindahl, M.2    Roobol-Boza, M.3    Andersson, B.4
  • 6
    • 0040842260 scopus 로고    scopus 로고
    • Proteolytic enzymes in the chloroplast related to light stress conditions
    • (Ed. Garab, G.), Kluwer Academic Publishers
    • Adamska, I. (1998). Proteolytic enzymes in the chloroplast related to light stress conditions. In: Photosynthesis: Mechanism and Effects III (Ed. Garab, G.), Kluwer Academic Publishers, pp. 2035-2038.
    • (1998) Photosynthesis: Mechanism and Effects III , pp. 2035-2038
    • Adamska, I.1
  • 7
    • 0030767058 scopus 로고    scopus 로고
    • Proteolytic activities and proteases of plant chloroplasts
    • Andersson, B. and Aro, E-M. (1997). Proteolytic activities and proteases of plant chloroplasts. Physiol. Plant., 100 : 780-793.
    • (1997) Physiol. Plant. , vol.100 , pp. 780-793
    • Andersson, B.1    Aro, E.-M.2
  • 8
    • 0031849102 scopus 로고    scopus 로고
    • Unifying model for the photoinhibition of photosystem II in vivo under steady-state photosynthesis
    • Anderson, J.M., Park, Y-I. and Chow, W.S. (1998). Unifying model for the photoinhibition of photosystem II in vivo under steady-state photosynthesis. Photosynth. Res., 56 : 1-13.
    • (1998) Photosynth. Res. , vol.56 , pp. 1-13
    • Anderson, J.M.1    Park, Y.-I.2    Chow, W.S.3
  • 9
    • 0027980297 scopus 로고
    • The CtpA gene encodes the C-terminal processing protease for the D1 protein of the PSII reaction center complex
    • Anubudurai, P.R., Mor, T.S., Ohad, I., Shestakov, S.V. and Pakrashi, H.B. (1994). The CtpA gene encodes the C-terminal processing protease for the D1 protein of the PSII reaction center complex. Proc. Natl. Acad. Sci., USA., 91 : 8082-8086.
    • (1994) Proc. Natl. Acad. Sci., USA , vol.91 , pp. 8082-8086
    • Anubudurai, P.R.1    Mor, T.S.2    Ohad, I.3    Shestakov, S.V.4    Pakrashi, H.B.5
  • 10
    • 0025034263 scopus 로고
    • In vitro studies on light-induced inhibition of photosystem II and D1 protein degradation at low temperatures
    • Aro, E-M., Hundal, T., Carlberg, I. and Andersson, B. (1990). In vitro studies on light-induced inhibition of photosystem II and D1 protein degradation at low temperatures. Biochem. Biophys. Acta, 1019 : 269-275.
    • (1990) Biochem. Biophys. Acta , vol.1019 , pp. 269-275
    • Aro, E.-M.1    Hundal, T.2    Carlberg, I.3    Andersson, B.4
  • 11
    • 0026542433 scopus 로고
    • ATP and light regulate D1 protein modification and degradation; role of D1* in photoinhibition
    • Aro, E-M., Kettunen, R. and Tyystjaarvi, E. (1992). ATP and light regulate D1 protein modification and degradation; role of D1* in photoinhibition. FEBS Lett., 297 : 29-33.
    • (1992) FEBS Lett. , vol.297 , pp. 29-33
    • Aro, E.-M.1    Kettunen, R.2    Tyystjaarvi, E.3
  • 12
    • 0027199986 scopus 로고
    • Photoinhibition of photosystem II: Inactivation, protein damage and turnover
    • Aro, E-M., Virgin, I. and Andersson, B. (1993). Photoinhibition of photosystem II: inactivation, protein damage and turnover. Biochem. Biophys. Acta, 1143 : 113-134.
    • (1993) Biochem. Biophys. Acta , vol.1143 , pp. 113-134
    • Aro, E.-M.1    Virgin, I.2    Andersson, B.3
  • 13
    • 0033513358 scopus 로고    scopus 로고
    • The water-water cycle in chloroplasts: Scavenging of active oxygen and dissipation of excess photons
    • Asada, K. (1999). The water-water cycle in chloroplasts: scavenging of active oxygen and dissipation of excess photons. Ann. Rev. Plant Physiol. Mol. Biol., 50 : 601-639.
    • (1999) Ann. Rev. Plant Physiol. Mol. Biol. , vol.50 , pp. 601-639
    • Asada, K.1
  • 14
    • 0015994609 scopus 로고
    • Protein synthesis in chloroplast; light driven synthesis of membrane protein by isolated pea chloroplast
    • Eaglesham, A.R.J. and Ellis, R.J. (1974). Protein synthesis in chloroplast; light driven synthesis of membrane protein by isolated pea chloroplast. Biochem. Biophys. Acta, 335 : 396-407.
    • (1974) Biochem. Biophys. Acta , vol.335 , pp. 396-407
    • Eaglesham, A.R.J.1    Ellis, R.J.2
  • 15
    • 0035852345 scopus 로고    scopus 로고
    • Fucntion of chloroplast SRP in thylakoid protein export
    • Eichaker, L.A. and Henry, R. (2001). Fucntion of chloroplast SRP in thylakoid protein export. Biochem. Biophys. Acta. 154 : 120-134.
    • (2001) Biochem. Biophys. Acta , vol.154 , pp. 120-134
    • Eichaker, L.A.1    Henry, R.2
  • 16
    • 0023429786 scopus 로고
    • Identification of a primary in vivo degradation product of the rapidly turning-over 32 kDa protein of PSII
    • Greenberg, B.M., Gaba, V., Mattoo, A.K. and Edelman, M. (1987). Identification of a primary in vivo degradation product of the rapidly turning-over 32 kDa protein of PSII. EMBO J., 6 : 2865-2869.
    • (1987) EMBO J. , vol.6 , pp. 2865-2869
    • Greenberg, B.M.1    Gaba, V.2    Mattoo, A.K.3    Edelman, M.4
  • 17
    • 0032510680 scopus 로고    scopus 로고
    • Chlorophyll availability affects psbA translation and D1 precursor processing in vivo in Synechocystis sp. PCC 6803
    • He, Q. and Vermass, W. (1998). Chlorophyll availability affects psbA translation and D1 precursor processing in vivo in Synechocystis sp. PCC 6803. Proc. Natl. Acad. Sci., USA, 95 : 5830-5835.
    • (1998) Proc. Natl. Acad. Sci., USA , vol.95 , pp. 5830-5835
    • He, Q.1    Vermass, W.2
  • 18
    • 0025283447 scopus 로고
    • Changes in the organization of PSII following light-induced D1-protein degradation
    • Hundal, T., Virgin, I., Styring, S. and andersson, B. (1990). Changes in the organization of PSII following light-induced D1-protein degradation. Biochem. Biophys. Acta, 1017 : 235-241.
    • (1990) Biochem. Biophys. Acta , vol.1017 , pp. 235-241
    • Hundal, T.1    Virgin, I.2    Styring, S.3    Andersson, B.4
  • 19
    • 0032724409 scopus 로고    scopus 로고
    • Turnover of the aggregates and cross-linked products of the D1 protein generated by acceptor-side photoinhibition of PSII
    • Ishikawa, Y., Nakatami, E., Henmi, T., Ferjani, A., Harada, A., Tamura, N. and Yamamoto, Y. (1999). Turnover of the aggregates and cross-linked products of the D1 protein generated by acceptor-side photoinhibition of PSII. Biochem. Biophys. Acta, 1413 : 147-158.
    • (1999) Biochem. Biophys. Acta , vol.1413 , pp. 147-158
    • Ishikawa, Y.1    Nakatami, E.2    Henmi, T.3    Ferjani, A.4    Harada, A.5    Tamura, N.6    Yamamoto, Y.7
  • 20
  • 21
    • 0023664103 scopus 로고
    • Control of gene expression during higher plant chloroplast biogenesis
    • Klein, P.R. and Mullet, J.E. (1987). Control of gene expression during higher plant chloroplast biogenesis. J. Biol. Chem., 262 : 4341-4348.
    • (1987) J. Biol. Chem. , vol.262 , pp. 4341-4348
    • Klein, P.R.1    Mullet, J.E.2
  • 22
    • 84989729970 scopus 로고
    • Photoinhibition of photosynthesis. An evaluation of damaging and protective mechanisms
    • Krause, G.H. (1988). Photoinhibition of photosynthesis. An evaluation of damaging and protective mechanisms. Physiol. Plant., 74 : 566-574.
    • (1988) Physiol. Plant. , vol.74 , pp. 566-574
    • Krause, G.H.1
  • 23
    • 0033214037 scopus 로고    scopus 로고
    • The C-terminal sequence encodes function in serine protease
    • Krem, M.M., Rose, T. and Cera, E.D. (1999). The C-terminal sequence encodes function in serine protease. J. Biol. Chem., 274 : 28063-28066.
    • (1999) J. Biol. Chem. , vol.274 , pp. 28063-28066
    • Krem, M.M.1    Rose, T.2    Cera, E.D.3
  • 24
    • 0001449340 scopus 로고
    • Membrane protein damage and repair. Selective loss of a quinone-protein function in chloroplast membrane
    • Kyle, D.J., Ohad, I. and Arntzen, C.J. (1984). Membrane protein damage and repair. Selective loss of a quinone-protein function in chloroplast membrane. Proc. Natl. Acad. Sci., USA, 81 : 4070-4074.
    • (1984) Proc. Natl. Acad. Sci., USA , vol.81 , pp. 4070-4074
    • Kyle, D.J.1    Ohad, I.2    Arntzen, C.J.3
  • 26
    • 0001294420 scopus 로고
    • Regulation of protein metabolism:coupling of photosynthetic electron transport and in vivo degradation of the rapidly metabolized 32-kDa protein of the chloroplast membranes
    • Mattoo, A.K., Hoffman-Folk, H., Marder, J.B. and Edelman, M. (1984). Regulation of protein metabolism:coupling of photosynthetic electron transport and in vivo degradation of the rapidly metabolized 32-kDa protein of the chloroplast membranes. Proc. Natl. Acad. Sci., USA, 81 : 1380-1384.
    • (1984) Proc. Natl. Acad. Sci., USA , vol.81 , pp. 1380-1384
    • Mattoo, A.K.1    Hoffman-Folk, H.2    Marder, J.B.3    Edelman, M.4
  • 27
    • 0023303085 scopus 로고
    • Intramembrane translocation and post-translational palmitoylation of the chloroplast 32-kDa herbicide binding protein
    • Mattoo, A.K. and Edelman, M. (1987). Intramembrane translocation and post-translational palmitoylation of the chloroplast 32-kDa herbicide binding protein. Proc. Natl. Acad. Sci., USA, 84 : 1497-1501.
    • (1987) Proc. Natl. Acad. Sci., USA , vol.84 , pp. 1497-1501
    • Mattoo, A.K.1    Edelman, M.2
  • 28
    • 0024979252 scopus 로고
    • Dynamics of the PSII reaction center
    • Mattoo, A.K. and Edelman, M. (1989). Dynamics of the PSII reaction center. Cell, 56 : 241-246.
    • (1989) Cell , vol.56 , pp. 241-246
    • Mattoo, A.K.1    Edelman, M.2
  • 29
    • 0029127671 scopus 로고
    • Specific degradation of D1 protein of PSII by treatment with hydrogen peroxide in darkness: Implication for the mechanism of degradation of the D1 protein under illumination
    • Miyao, M., Ikeuchi, M., Yamamoto, N. and Ono, T-A. (1995). Specific degradation of D1 protein of PSII by treatment with hydrogen peroxide in darkness: implication for the mechanism of degradation of the D1 protein under illumination. Biochemistry, 34 : 10019-10026.
    • (1995) Biochemistry , vol.34 , pp. 10019-10026
    • Miyao, M.1    Ikeuchi, M.2    Yamamoto, N.3    Ono, T.-A.4
  • 30
    • 0024978846 scopus 로고
    • psbA genes indicate common ancestry of prochlorophytes and chloroplasts
    • Morden, C.W. and Golden, S.S. (1989). psbA genes indicate common ancestry of prochlorophytes and chloroplasts. Nature, 337 : 382-385.
    • (1989) Nature , vol.337 , pp. 382-385
    • Morden, C.W.1    Golden, S.S.2
  • 31
    • 0025284693 scopus 로고
    • Chlorophyll regulates accumulation of the plastid-encoded chlorophyll apoproteins CP43 and D1 by increasing apoprotein stability
    • Mullet, I.E., Klein, P.G., and Klein, R.R. (1990). Chlorophyll regulates accumulation of the plastid-encoded chlorophyll apoproteins CP43 and D1 by increasing apoprotein stability. Proc. Natl. Acad. Sci., USA, 84 : 4038-4042.
    • (1990) Proc. Natl. Acad. Sci., USA , vol.84 , pp. 4038-4042
    • Mullet, I.E.1    Klein, P.G.2    Klein, R.R.3
  • 32
    • 0001505435 scopus 로고
    • Isolation of a PSII reaction center consisting of D1,D2 polypeptides and Cyt.b-559
    • Nanba, O. and Satoh, K. (1987). Isolation of a PSII reaction center consisting of D1,D2 polypeptides and Cyt.b-559. Proc. Natl. Acad. Sci., USA, 84 : 109-112.
    • (1987) Proc. Natl. Acad. Sci., USA , vol.84 , pp. 109-112
    • Nanba, O.1    Satoh, K.2
  • 33
    • 0033506468 scopus 로고    scopus 로고
    • Photoprotection revisited: Genetic and molecular approaches
    • Niyogi, K. (1999). Photoprotection revisited: genetic and molecular approaches. Ann. Rev. Plant Physiol. Plant Mol. Biol., 50 : 333-359.
    • (1999) Ann. Rev. Plant Physiol. Plant Mol. Biol. , vol.50 , pp. 333-359
    • Niyogi, K.1
  • 34
    • 0036809979 scopus 로고    scopus 로고
    • Dual role of triplet localization on the accessory chlorophyll in the PSII reaction center: Photoprotection and photodamage of the D1 protein
    • Noguchi, T. (2002). Dual role of triplet localization on the accessory chlorophyll in the PSII reaction center: photoprotection and photodamage of the D1 protein. Plant Cell Physiol. 43 : 1112-1116.
    • (2002) Plant Cell Physiol. , vol.43 , pp. 1112-1116
    • Noguchi, T.1
  • 35
    • 0021473380 scopus 로고
    • Membrane protein damage and repair: Removal and replacement of inactivated 32-kDa polypeptide in chloroplast membrane
    • Ohad, I., Kyle, D.J. and Arntzen, C.J. (1984). Membrane protein damage and repair: removal and replacement of inactivated 32-kDa polypeptide in chloroplast membrane. J. Cell Biol., 99 : 481-485.
    • (1984) J. Cell Biol. , vol.99 , pp. 481-485
    • Ohad, I.1    Kyle, D.J.2    Arntzen, C.J.3
  • 36
    • 0003050958 scopus 로고
    • Photoinhibition of photosynthesis induced by visible light
    • Powles, S.B. (1984). Photoinhibition of photosynthesis induced by visible light. Ann. Rev. Plant Physiol., 35 : 15-44.
    • (1984) Ann. Rev. Plant Physiol. , vol.35 , pp. 15-44
    • Powles, S.B.1
  • 37
    • 0000226607 scopus 로고
    • Dynamics of PSII:mechanism of photoinhibition and recovery process
    • Prasil, O., Adir, N. and Ohad, I. (1992). Dynamics of PSII:mechanism of photoinhibition and recovery process. Top Photosynth., 11 : 293-348.
    • (1992) Top Photosynth. , vol.11 , pp. 293-348
    • Prasil, O.1    Adir, N.2    Ohad, I.3
  • 38
    • 0022971952 scopus 로고
    • Amino acid sequences common to rapidly degraded proteins: The PEST hypothesis
    • Rogers, S., Wells, R. and Rechsteinner, M. (1986). Amino acid sequences common to rapidly degraded proteins: the PEST hypothesis. Science, 234 : 364-368.
    • (1986) Science , vol.234 , pp. 364-368
    • Rogers, S.1    Wells, R.2    Rechsteinner, M.3
  • 40
    • 0026043886 scopus 로고
    • Photoinduced degradation of the D1 polypeptide in isolated reaction centers of PSII: Evidence for an autoproteolytic process triggered by the oxidizing side of photosystem
    • Shipton, C.A. and Barber, J. (1991). Photoinduced degradation of the D1 polypeptide in isolated reaction centers of PSII: evidence for an autoproteolytic process triggered by the oxidizing side of photosystem. Proc. Natl. Acad. Sci., USA, 88 : 6691-6695.
    • (1991) Proc. Natl. Acad. Sci., USA , vol.88 , pp. 6691-6695
    • Shipton, C.A.1    Barber, J.2
  • 41
    • 0006658009 scopus 로고    scopus 로고
    • Photoinhibition of photosynthesis: Its molecular mechanism in higher plants
    • Singh, M. and Chaturvedi, R. (1997). Photoinhibition of photosynthesis: its molecular mechanism in higher plants. Agro's Ann. Rev. Plant Physiol., 3 : 72-90.
    • (1997) Agro's Ann. Rev. Plant Physiol. , vol.3 , pp. 72-90
    • Singh, M.1    Chaturvedi, R.2
  • 42
    • 0034529562 scopus 로고    scopus 로고
    • Turn-over of D1 protein encoded by psbA gene in higher plants and cynobacteria sustains photosynthetic efficiency to maintain plant productivity under photoinhibitory and non-photoinhibitory irradiance
    • Singh, M. (2000). Turn-over of D1 protein encoded by psbA gene in higher plants and cynobacteria sustains photosynthetic efficiency to maintain plant productivity under photoinhibitory and non-photoinhibitory irradiance. Photosynthetica, 38 : 161-169.
    • (2000) Photosynthetica , vol.38 , pp. 161-169
    • Singh, M.1
  • 43
    • 0034575031 scopus 로고    scopus 로고
    • Characterization of a phototolerant mutant of Synechocystis sp.PCC 6803 created by random mutagenesis of psbAII gene
    • Singh, M. and Satoh, K. (2000). Characterization of a phototolerant mutant of Synechocystis sp.PCC 6803 created by random mutagenesis of psbAII gene. Indian J Biochem. Biophys., 37 : 477-485.
    • (2000) Indian J Biochem. Biophys. , vol.37 , pp. 477-485
    • Singh, M.1    Satoh, K.2
  • 44
    • 0041883327 scopus 로고    scopus 로고
    • Site-specific mutations localized in D-E loop of D1 polypeptide affect phototolerancy in Synechocystis sp. PCC 6803 containing psbAII gene
    • Singh, M. and Satoh, K. (2003). Site-specific mutations localized in D-E loop of D1 polypeptide affect phototolerancy in Synechocystis sp. PCC 6803 containing psbAII gene. Indian J. Biochem. Biophys., 40 : 108-113.
    • (2003) Indian J. Biochem. Biophys. , vol.40 , pp. 108-113
    • Singh, M.1    Satoh, K.2
  • 45
    • 0039063875 scopus 로고    scopus 로고
    • Characterization of chloroplast proteases
    • (Ed. Garab, G.), Kluwer Academic Publishers
    • Sokolenko, A. and Hermann, R.G. (1998). Characterization of chloroplast proteases. In: Photosynthesis: Mechanisms and Effects III (Ed. Garab, G.), Kluwer Academic Publishers, pp. 2031-2034.
    • (1998) Photosynthesis: Mechanisms and Effects III , pp. 2031-2034
    • Sokolenko, A.1    Hermann, R.G.2
  • 47
    • 4644308165 scopus 로고    scopus 로고
    • Involement of GTP in the primary proteolysis of the D1 protein during photoinhibition of PSII
    • (Ed. Garab, G.), Kluwer Academic Publishers
    • Spetea, C., Hundal, T., Lohmann, F. and Andersson, B. (1998). Involement of GTP in the primary proteolysis of the D1 protein during photoinhibition of PSII. In: Photosynthesis: Mechanisms and Effects III (Ed. Garab, G.), Kluwer Academic Publishers, pp. 2019-2022.
    • (1998) Photosynthesis: Mechanisms and Effects III , pp. 2019-2022
    • Spetea, C.1    Hundal, T.2    Lohmann, F.3    Andersson, B.4
  • 48
    • 84961491017 scopus 로고
    • The three-dimensional structure of the herbicide-binding niche on the reaction center polypeptides of PSII
    • Trebst, A. (1986). The three-dimensional structure of the herbicide-binding niche on the reaction center polypeptides of PSII. Z. Naturforsch, 42C : 742-750.
    • (1986) Z. Naturforsch , vol.42 C , pp. 742-750
    • Trebst, A.1
  • 49
    • 0029921367 scopus 로고    scopus 로고
    • The rate constant of photoinhibition, measured in lincomycin-treated leaves is directly proportional to light intensity
    • Tyystjaarvi, E., and Aro, E-M. (1996). The rate constant of photoinhibition, measured in lincomycin-treated leaves is directly proportional to light intensity. Proc. Natl. Acad. Sci., USA, 93 : 2213-2218.
    • (1996) Proc. Natl. Acad. Sci., USA , vol.93 , pp. 2213-2218
    • Tyystjaarvi, E.1    Aro, E.-M.2
  • 50
    • 0011088692 scopus 로고    scopus 로고
    • Implication of a developmental stage dependent thylakoid-bound protease in the stabilization of the light-harvesting pigment-protein complex serving PSII during thylakoid biogenesis in red kidney bean
    • Tziveleka, L-A. and Argyroudi-Akoyunoglou, J.H. (1998). Implication of a developmental stage dependent thylakoid-bound protease in the stabilization of the light-harvesting pigment-protein complex serving PSII during thylakoid biogenesis in red kidney bean. Plant Physiol., 117 : 961-970.
    • (1998) Plant Physiol. , vol.117 , pp. 961-970
    • Tziveleka, L.-A.1    Argyroudi-Akoyunoglou, J.H.2
  • 51
    • 0026596487 scopus 로고
    • Spectroscopic characterization of photoinhibited PSII and kinetic resolution of the triggering of the D1 reaction center protein for degradation
    • Van Wijk, K.J., Andersson, B. and Styring, S. (1992). Spectroscopic characterization of photoinhibited PSII and kinetic resolution of the triggering of the D1 reaction center protein for degradation. Biochem. Biophys. Acta, 1100 : 207-215.
    • (1992) Biochem. Biophys. Acta , vol.1100 , pp. 207-215
    • Van Wijk, K.J.1    Andersson, B.2    Styring, S.3
  • 52
    • 0026604580 scopus 로고
    • Reversible and irreversible intermediates during photoinhibition of PSII: Stable reduced QA species promote chlorophyll triplet formation
    • Vass, I., Styring, S., Hundal, T., Koivuniemi, A., Aro, E-M. and Andersson, B. (1992). Reversible and irreversible intermediates during photoinhibition of PSII: stable reduced QA species promote chlorophyll triplet formation. Proc. Natl. Acad. Sci., USA, 89 : 1408-1412.
    • (1992) Proc. Natl. Acad. Sci., USA , vol.89 , pp. 1408-1412
    • Vass, I.1    Styring, S.2    Hundal, T.3    Koivuniemi, A.4    Aro, E.-M.5    Andersson, B.6
  • 53
    • 0025071018 scopus 로고
    • Light-induced D1 degradation in isolated PSII core complex
    • Virgin, I., Demetrios, F. and Andersson, B. (1990). Light-induced D1 degradation in isolated PSII core complex. FEBS Lett., 269 : 45-48.
    • (1990) FEBS Lett. , vol.269 , pp. 45-48
    • Virgin, I.1    Demetrios, F.2    Andersson, B.3
  • 54
    • 0008732737 scopus 로고
    • Degradation of the 32-kDa thylakoid-membrane polypeptide of Chlamydomonas reinhardi Y-1
    • Wettern, M. and Galling, G. (1985). Degradation of the 32-kDa thylakoid-membrane polypeptide of Chlamydomonas reinhardi Y-1. Planta, 166 : 474-482.
    • (1985) Planta , vol.166 , pp. 474-482
    • Wettern, M.1    Galling, G.2
  • 55
    • 0035083795 scopus 로고    scopus 로고
    • Quality control of photosystem II
    • Yamamoto, Y. (2001). Quality control of photosystem II. Plant Cell Physiol. 42 : 121-128.
    • (2001) Plant Cell Physiol. , vol.42 , pp. 121-128
    • Yamamoto, Y.1
  • 56
    • 0037070198 scopus 로고    scopus 로고
    • Synthesis, membrane insertion and assembly of the chloroplast encoded D1 protein into photosystem II
    • Zhang, L. and Aro, E-M. (2002). Synthesis, membrane insertion and assembly of the chloroplast encoded D1 protein into photosystem II. FEBS Lett., 512 : 13-18.
    • (2002) FEBS Lett. , vol.512 , pp. 13-18
    • Zhang, L.1    Aro, E.-M.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.