메뉴 건너뛰기




Volumn 98, Issue 5, 2010, Pages 922-931

Effect of antenna-depletion in photosystem II on excitation energy transfer in Arabidopsis thaliana

Author keywords

[No Author keywords available]

Indexed keywords

ARABIDOPSIS; ARABIDOPSIS THALIANA;

EID: 77749292432     PISSN: 00063495     EISSN: 15420086     Source Type: Journal    
DOI: 10.1016/j.bpj.2009.11.012     Document Type: Article
Times cited : (90)

References (50)
  • 1
    • 2642511792 scopus 로고    scopus 로고
    • Light-harvesting in Photosystem II
    • B. R. Green and W. W. Parson, editors. Kluwer Academic Publishers, Dordrecht
    • van Amerongen, H., and J. P. Dekker. 2003. Light-harvesting in Photosystem II. In Light-Harvesting Antennas in Photosynthesis. B. R. Green and W. W. Parson, editors. Kluwer Academic Publishers, Dordrecht. 219-251.
    • (2003) Light-Harvesting Antennas in Photosynthesis , pp. 219-251
    • van Amerongen, H.1    Dekker, J.P.2
  • 3
    • 33947363865 scopus 로고    scopus 로고
    • Functional heterogeneity of photosystem II in domain specific regions of the thylakoid membrane of spinach (Spinacia oleracea L.)
    • Veerman, J., M. D. McConnell, ..., D. Bruce. 2007. Functional heterogeneity of photosystem II in domain specific regions of the thylakoid membrane of spinach (Spinacia oleracea L.). Biochemistry. 46:3443-3453.
    • (2007) Biochemistry , vol.46 , pp. 3443-3453
    • Veerman, J.1    McConnell, M.D.2    Bruce, D.3
  • 4
    • 13444261972 scopus 로고    scopus 로고
    • The effect of outer antenna complexes on the photochemical trapping rate in barley thylakoid Photosystem II
    • Engelmann, E. C. M., G. Zucchelli, ..., R. C. Jennings. 2005. The effect of outer antenna complexes on the photochemical trapping rate in barley thylakoid Photosystem II. Biochim. Biophys. Acta. 1706:276-286.
    • (2005) Biochim. Biophys. Acta , vol.1706 , pp. 276-286
    • Engelmann, E.C.M.1    Zucchelli, G.2    Jennings, R.C.3
  • 5
    • 34247576821 scopus 로고    scopus 로고
    • The structure of a plant photosystem I supercomplex at 3.4 A resolution
    • Amunts, A., O. Drory, and N. Nelson. 2007. The structure of a plant photosystem I supercomplex at 3.4 A resolution. Nature. 447:58-63.
    • (2007) Nature , vol.447 , pp. 58-63
    • Amunts, A.1    Drory, O.2    Nelson, N.3
  • 6
    • 30744445692 scopus 로고    scopus 로고
    • Towards complete cofactor arrangement in the 3.0 A resolution structure of photosystem II
    • Loll, B., J. Kern, ..., J. Biesiadka. 2005. Towards complete cofactor arrangement in the 3.0 A resolution structure of photosystem II. Nature. 438:1040-1044.
    • (2005) Nature , vol.438 , pp. 1040-1044
    • Loll, B.1    Kern, J.2    Biesiadka, J.3
  • 7
    • 1642602038 scopus 로고    scopus 로고
    • Crystal structure of spinach major light-harvesting complex at 2.72 A resolution
    • Liu, Z. F., H. Yan, ..., W.Chang. 2004. Crystal structure of spinach major light-harvesting complex at 2.72 A resolution. Nature. 428:287-292.
    • (2004) Nature , vol.428 , pp. 287-292
    • Liu, Z.F.1    Yan, H.2    Chang, W.3
  • 8
    • 20344401549 scopus 로고    scopus 로고
    • Excitation dynamics in the LHCII complex of higher plants: Modeling based on the 2.72 Angstrom crystal structure
    • Novoderezhkin, V. I., M. A. Palacios, ..., R. van Grondelle. 2005. Excitation dynamics in the LHCII complex of higher plants: modeling based on the 2.72 Angstrom crystal structure. J. Phys. Chem. B. 109:10493-10504.
    • (2005) J. Phys. Chem. B , vol.109 , pp. 10493-10504
    • Novoderezhkin, V.I.1    Palacios, M.A.2    van Grondelle, R.3
  • 9
    • 0033679186 scopus 로고    scopus 로고
    • Primary charge separation in Photosystem II
    • Dekker, J. P., and R. Van Grondelle. 2000. Primary charge separation in Photosystem II. Photosynth. Res. 63:195-208.
    • (2000) Photosynth. Res , vol.63 , pp. 195-208
    • Dekker, J.P.1    Van Grondelle, R.2
  • 10
    • 24144496800 scopus 로고    scopus 로고
    • Comparison of the light-harvesting networks of plant and cyanobacterial photosystem I
    • Şener, M. K., C. Jolley, ..., K. Schulten. 2005. Comparison of the light-harvesting networks of plant and cyanobacterial photosystem I. Biophys. J. 89:1630-1642.
    • (2005) Biophys. J , vol.89 , pp. 1630-1642
    • Şener, M.K.1    Jolley, C.2    Schulten, K.3
  • 11
    • 11044234285 scopus 로고    scopus 로고
    • Supramolecular organization of thylakoid membrane proteins in green plants
    • Dekker, J. P., and E. J. Boekema. 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
  • 12
    • 0032512418 scopus 로고    scopus 로고
    • Barzda, V., E. J. G. Peterman, ..., H. vanAmerongen. 1998. The influence of aggregation on triplet formation in light-harvesting chlorophyll a/b pigment-protein complex II of green plants. Biochemistry. 37:546-551.
    • Barzda, V., E. J. G. Peterman, ..., H. vanAmerongen. 1998. The influence of aggregation on triplet formation in light-harvesting chlorophyll a/b pigment-protein complex II of green plants. Biochemistry. 37:546-551.
  • 13
    • 44449172118 scopus 로고    scopus 로고
    • Photoprotection in the antenna complexes of photosystem II: Role of individual xanthophylls in chlorophyll triplet quenching
    • Mozzo, M., L. Dall'Osto, ., R. Croce. 2008. Photoprotection in the antenna complexes of photosystem II: role of individual xanthophylls in chlorophyll triplet quenching. J. Biol. Chem. 283:6184-6192.
    • (2008) J. Biol. Chem , vol.283 , pp. 6184-6192
    • Mozzo, M.1    Dall'Osto, L.2    Croce, R.3
  • 14
    • 34250767369 scopus 로고    scopus 로고
    • The Arabidopsis aba4-1 mutant reveals a specific function for neoxanthin in protection against photooxidative stress
    • Dall'Osto, L., S. Cazzaniga, ..., R. Bassi. 2007. The Arabidopsis aba4-1 mutant reveals a specific function for neoxanthin in protection against photooxidative stress. Plant Cell. 19:1048-1064.
    • (2007) Plant Cell , vol.19 , pp. 1048-1064
    • Dall'Osto, L.1    Cazzaniga, S.2    Bassi, R.3
  • 15
    • 44049086448 scopus 로고    scopus 로고
    • Architecture of a charge-transfer state regulating light harvesting in a plant antenna protein
    • Ahn, T. K., T. J. Avenson, ..., G. R. Fleming. 2008. Architecture of a charge-transfer state regulating light harvesting in a plant antenna protein. Science. 320:794-797.
    • (2008) Science , vol.320 , pp. 794-797
    • Ahn, T.K.1    Avenson, T.J.2    Fleming, G.R.3
  • 16
    • 36549023939 scopus 로고    scopus 로고
    • Identification of a mechanism of photoprotective energy dissipation in higher plants
    • Ruban, A. V., R. Berera, ..., R. van Grondelle. 2007. Identification of a mechanism of photoprotective energy dissipation in higher plants. Nature. 450:575-578.
    • (2007) Nature , vol.450 , pp. 575-578
    • Ruban, A.V.1    Berera, R.2    van Grondelle, R.3
  • 18
    • 33751232344 scopus 로고    scopus 로고
    • Excitation energy transfer and charge separation in photosystem II membranes revisited
    • Broess, K., G. Trinkunas, ., H. van Amerongen. 2006. Excitation energy transfer and charge separation in photosystem II membranes revisited. Biophys. J. 91:3776-3786.
    • (2006) Biophys. J , vol.91 , pp. 3776-3786
    • Broess, K.1    Trinkunas, G.2    van Amerongen, H.3
  • 19
    • 43049158093 scopus 로고    scopus 로고
    • Determination of the excitation migration time in Photosystem II consequences for the membrane organization and charge separation parameters
    • Broess, K., G. Trinkunas, ., H. van Amerongen. 2008. Determination of the excitation migration time in Photosystem II consequences for the membrane organization and charge separation parameters. Biochim. Biophys. Acta. 1777:404-409.
    • (2008) Biochim. Biophys. Acta , vol.1777 , pp. 404-409
    • Broess, K.1    Trinkunas, G.2    van Amerongen, H.3
  • 20
    • 0026710549 scopus 로고
    • Global target analysis of picosecond chlorophyll fluorescence kinetics from pea chloroplasts: A new approach to the characterization of the primary processes in photosystem II α- and β-units
    • Roelofs, T. A., C.-H. Lee, and A. R. Holzwarth. 1992. Global target analysis of picosecond chlorophyll fluorescence kinetics from pea chloroplasts: a new approach to the characterization of the primary processes in photosystem II α- and β-units. Biophys. J. 61:1147-1163.
    • (1992) Biophys. J , vol.61 , pp. 1147-1163
    • Roelofs, T.A.1    Lee, C.-H.2    Holzwarth, A.R.3
  • 21
    • 0032125846 scopus 로고    scopus 로고
    • Nearest-neighbor analysis of a photosystem II complex from Marchantia polymorpha L. (liverwort), which contains reaction center and antenna proteins
    • Harrer, R., R. Bassi, ..., C. Schäfer. 1998. Nearest-neighbor analysis of a photosystem II complex from Marchantia polymorpha L. (liverwort), which contains reaction center and antenna proteins. Eur. J. Biochem. 255:196-205.
    • (1998) Eur. J. Biochem , vol.255 , pp. 196-205
    • Harrer, R.1    Bassi, R.2    Schäfer, C.3
  • 22
    • 0037469152 scopus 로고    scopus 로고
    • The structure of photosystem II in Arabidopsis: Localization of the CP26 and CP29 antenna complexes
    • Yakushevska, A. E., W. Keegstra, ..., P. Horton. 2003. The structure of photosystem II in Arabidopsis: localization of the CP26 and CP29 antenna complexes. Biochemistry. 42:608-613.
    • (2003) Biochemistry , vol.42 , pp. 608-613
    • Yakushevska, A.E.1    Keegstra, W.2    Horton, P.3
  • 23
    • 48549086564 scopus 로고    scopus 로고
    • de Bianchi, S., L. Dall'Osto, ..., R. Bassi. 2008. Minor antenna proteins CP24 and CP26 affect the interactions between photosystem II subunits and the electron transport rate in grana membranes of Arabidopsis. Plant Cell. 20:1012-1028.
    • de Bianchi, S., L. Dall'Osto, ..., R. Bassi. 2008. Minor antenna proteins CP24 and CP26 affect the interactions between photosystem II subunits and the electron transport rate in grana membranes of Arabidopsis. Plant Cell. 20:1012-1028.
  • 24
    • 33845740676 scopus 로고    scopus 로고
    • Lack of the light-harvesting complex CP24 affects the structure and function of the grana membranes of higher plant chloroplasts
    • Kovács, L., J. Damkjaer, ..., P. Horton. 2006. Lack of the light-harvesting complex CP24 affects the structure and function of the grana membranes of higher plant chloroplasts. Plant Cell. 18:3106-3120.
    • (2006) Plant Cell , vol.18 , pp. 3106-3120
    • Kovács, L.1    Damkjaer, J.2    Horton, P.3
  • 25
    • 0042768158 scopus 로고    scopus 로고
    • Genome-wide insertional mutagenesis of Arabidopsis thaliana
    • Alonso, J. M., A. N. Stepanova, ..., J. R. Ecker. 2003. Genome-wide insertional mutagenesis of Arabidopsis thaliana. Science. 301:653-657.
    • (2003) Science , vol.301 , pp. 653-657
    • Alonso, J.M.1    Stepanova, A.N.2    Ecker, J.R.3
  • 26
    • 0035020030 scopus 로고    scopus 로고
    • Antisense inhibition of the photosynthetic antenna proteins CP29 and CP26: Implications for the mechanism of protective energy dissipation
    • Andersson, J., R. G. Walters, ..., S. Jansson. 2001. Antisense inhibition of the photosynthetic antenna proteins CP29 and CP26: implications for the mechanism of protective energy dissipation. Plant Cell. 13:1193-1204.
    • (2001) Plant Cell , vol.13 , pp. 1193-1204
    • Andersson, J.1    Walters, R.G.2    Jansson, S.3
  • 27
    • 0034794143 scopus 로고    scopus 로고
    • Preparation and functional characterization of thylakoids from Arabidopsis thaliana
    • Casazza, A. P., D. Tarantino, and C. Soave. 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
  • 28
    • 0037062584 scopus 로고    scopus 로고
    • Chromophore organization in the higher-plant photosystem II antenna protein CP26
    • Croce, R., G. Canino, ..., R. Bassi. 2002. Chromophore organization in the higher-plant photosystem II antenna protein CP26. Biochemistry. 41:7334-7343.
    • (2002) Biochemistry , vol.41 , pp. 7334-7343
    • Croce, R.1    Canino, G.2    Bassi, R.3
  • 29
    • 0023472472 scopus 로고
    • Tricine-sodium dodecyl sulfatepolyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa
    • Schägger, H., and G. von Jagow. 1987. Tricine-sodium dodecyl sulfatepolyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa. Anal. Biochem. 166:368-379.
    • (1987) Anal. Biochem , vol.166 , pp. 368-379
    • Schägger, H.1    von Jagow, G.2
  • 30
    • 45549109763 scopus 로고    scopus 로고
    • An original adaptation of photosynthesis in the marine green alga Ostreococcus
    • Cardol, P., B. Bailleul, ..., G. Finazzi. 2008. An original adaptation of photosynthesis in the marine green alga Ostreococcus. Proc. Natl. Acad. Sci. USA. 105:7881-7886.
    • (2008) Proc. Natl. Acad. Sci. USA , vol.105 , pp. 7881-7886
    • Cardol, P.1    Bailleul, B.2    Finazzi, G.3
  • 31
    • 18644377743 scopus 로고    scopus 로고
    • Effects of refractive index and viscosity on fluorescence and anisotropy decays of enhanced cyan and yellow fluorescent proteins
    • Borst, J. W., M. A. Hink, ..., A. J. Visser. 2005. Effects of refractive index and viscosity on fluorescence and anisotropy decays of enhanced cyan and yellow fluorescent proteins. J. Fluoresc. 15:153-160.
    • (2005) J. Fluoresc , vol.15 , pp. 153-160
    • Borst, J.W.1    Hink, M.A.2    Visser, A.J.3
  • 32
    • 0022130969 scopus 로고
    • Artefact and distortion sources in time correlated single photon counting
    • van Hoek, A., and A. J. W. G. Visser. 1985. Artefact and distortion sources in time correlated single photon counting. Anal. Instrum. 14:359-378.
    • (1985) Anal. Instrum , vol.14 , pp. 359-378
    • van Hoek, A.1    Visser, A.J.W.G.2
  • 33
    • 0032823422 scopus 로고    scopus 로고
    • Thermal stability of a flavoprotein assessed from associative analysis of polarized timeresolved fluorescence spectroscopy
    • Digris, A. V., V. V. Skakoun, ..., A. J. Visser. 1999. Thermal stability of a flavoprotein assessed from associative analysis of polarized timeresolved fluorescence spectroscopy. Eur. Biophys. J. 28:526-531.
    • (1999) Eur. Biophys. J , vol.28 , pp. 526-531
    • Digris, A.V.1    Skakoun, V.V.2    Visser, A.J.3
  • 34
    • 58749095136 scopus 로고    scopus 로고
    • Picosecond fluorescence of intact and dissolved PSI-LHCI crystals
    • van Oort, B., A. Amunts, ..., R. Croce. 2008. Picosecond fluorescence of intact and dissolved PSI-LHCI crystals. Biophys. J. 95:5851-5861.
    • (2008) Biophys. J , vol.95 , pp. 5851-5861
    • van Oort, B.1    Amunts, A.2    Croce, R.3
  • 35
    • 0036788599 scopus 로고    scopus 로고
    • Pigment organization and energy transfer dynamics in isolated photosystem I (PSI) complexes from Arabidopsis thaliana depleted of the PSI-G, PSI-K, PSI-L, or PSI-N subunit
    • Ihalainen, J. A., P. E. Jensen, ..., J. P. Dekker. 2002. Pigment organization and energy transfer dynamics in isolated photosystem I (PSI) complexes from Arabidopsis thaliana depleted of the PSI-G, PSI-K, PSI-L, or PSI-N subunit. Biophys. J. 83:2190-2201.
    • (2002) Biophys. J , vol.83 , pp. 2190-2201
    • Ihalainen, J.A.1    Jensen, P.E.2    Dekker, J.P.3
  • 36
    • 24044445567 scopus 로고    scopus 로고
    • Excitation energy trapping in photosystem I complexes depleted in Lhca1 and Lhca4
    • Ihalainen, J. A., F. Klimmek, ..., J. P. Dekker. 2005. Excitation energy trapping in photosystem I complexes depleted in Lhca1 and Lhca4. FEBS Lett. 579:4787-4791.
    • (2005) FEBS Lett , vol.579 , pp. 4787-4791
    • Ihalainen, J.A.1    Klimmek, F.2    Dekker, J.P.3
  • 37
    • 13444291522 scopus 로고    scopus 로고
    • Kinetics of excitation trapping in intact Photosystem I of Chlamydomonas reinhardtii and Arabidopsis thaliana
    • Ihalainen, J. A., I. H. M. van Stokkum,., J. P. Dekker. 2005. Kinetics of excitation trapping in intact Photosystem I of Chlamydomonas reinhardtii and Arabidopsis thaliana. Biochim. Biophys. Acta. 1706:267-275.
    • (2005) Biochim. Biophys. Acta , vol.1706 , pp. 267-275
    • Ihalainen, J.A.1    van Stokkum, I.H.M.2    Dekker, J.P.3
  • 39
    • 34447271037 scopus 로고    scopus 로고
    • Aggregation of light-harvesting complex II leads to formation of efficient excitation energy traps in monomeric and trimeric complexes
    • van Oort, B., A. van Hoek, ..., H. van Amerongen. 2007. Aggregation of light-harvesting complex II leads to formation of efficient excitation energy traps in monomeric and trimeric complexes. FEBS Lett. 581:3528-3532.
    • (2007) FEBS Lett , vol.581 , pp. 3528-3532
    • van Oort, B.1    van Hoek, A.2    van Amerongen, H.3
  • 40
    • 0032317945 scopus 로고    scopus 로고
    • Higher plants light harvesting proteins. Structure and function as revealed by mutation analysis of either protein or chromophore moieties
    • Sandonà, D., R. Croce, ..., R. Bassi. 1998. Higher plants light harvesting proteins. Structure and function as revealed by mutation analysis of either protein or chromophore moieties. Biochim. Biophys. Acta. 1365:207-214.
    • (1998) Biochim. Biophys. Acta , vol.1365 , pp. 207-214
    • Sandonà, D.1    Croce, R.2    Bassi, R.3
  • 41
    • 33749373006 scopus 로고    scopus 로고
    • Biochemical and structural analyses of a higher plant photosystem II supercomplex of a photosystem I-less mutant of barley. Consequences of a chronic over-reduction of the plastoquinone pool
    • Morosinotto, T., R. Bassi, ..., J. Barber. 2006. Biochemical and structural analyses of a higher plant photosystem II supercomplex of a photosystem I-less mutant of barley. Consequences of a chronic over-reduction of the plastoquinone pool. FEBS J. 273:4616-4630.
    • (2006) FEBS J , vol.273 , pp. 4616-4630
    • Morosinotto, T.1    Bassi, R.2    Barber, J.3
  • 42
    • 0035210531 scopus 로고    scopus 로고
    • Supermolecular organization of photosystem II and its associated light-harvesting antenna in Arabidopsis thaliana
    • Yakushevska, A. E., P. E. Jensen, ..., J. P. Dekker. 2001. Supermolecular organization of photosystem II and its associated light-harvesting antenna in Arabidopsis thaliana. Eur. J. Biochem. 268:6020-6028.
    • (2001) Eur. J. Biochem , vol.268 , pp. 6020-6028
    • Yakushevska, A.E.1    Jensen, P.E.2    Dekker, J.P.3
  • 43
    • 0028346592 scopus 로고
    • Three-dimensional structure of the higher-plant photosystem II reaction centre and evidence for its dimeric organization in vivo
    • Santini, C., V. Tidu, ..., R. Bassi. 1994. Three-dimensional structure of the higher-plant photosystem II reaction centre and evidence for its dimeric organization in vivo. Eur. J. Biochem. 221:307-315.
    • (1994) Eur. J. Biochem , vol.221 , pp. 307-315
    • Santini, C.1    Tidu, V.2    Bassi, R.3
  • 45
    • 0035940523 scopus 로고    scopus 로고
    • Time-resolved fluorescence analysis of the photosystem II antenna proteins in detergent micelles and liposomes
    • Moya, I., M. Silvestri, ..., R. Bassi. 2001. Time-resolved fluorescence analysis of the photosystem II antenna proteins in detergent micelles and liposomes. Biochemistry. 40:12552-12561.
    • (2001) Biochemistry , vol.40 , pp. 12552-12561
    • Moya, I.1    Silvestri, M.2    Bassi, R.3
  • 46
    • 0037030843 scopus 로고    scopus 로고
    • Super-radiance and exciton (de)localization in light-harvesting complex II from green plants?
    • Palacios, M. A., F. L. de Weerd, ..., H. van Amerongen. 2002. Super-radiance and exciton (de)localization in light-harvesting complex II from green plants? J. Phys. Chem. B. 106:5782-5787.
    • (2002) J. Phys. Chem. B , vol.106 , pp. 5782-5787
    • Palacios, M.A.1    de Weerd, F.L.2    van Amerongen, H.3
  • 47
    • 34447254542 scopus 로고    scopus 로고
    • Equilibrium between quenched and nonquenched conformations of the major plant light-harvesting complex studied with high-pressure time-resolved fluorescence
    • van Oort, B., A. van Hoek, ..., H. van Amerongen. 2007. Equilibrium between quenched and nonquenched conformations of the major plant light-harvesting complex studied with high-pressure time-resolved fluorescence. J. Phys. Chem. B. 111:7631-7637.
    • (2007) J. Phys. Chem. B , vol.111 , pp. 7631-7637
    • van Oort, B.1    van Hoek, A.2    van Amerongen, H.3
  • 48
    • 21844453924 scopus 로고    scopus 로고
    • Molecular basis of photoprotection and control of photosynthetic light-harvesting
    • Pascal, A. A., Z. F. Liu, ..., A. Ruban. 2005. Molecular basis of photoprotection and control of photosynthetic light-harvesting. Nature. 436:134-137.
    • (2005) Nature , vol.436 , pp. 134-137
    • Pascal, A.A.1    Liu, Z.F.2    Ruban, A.3
  • 49
    • 53949088888 scopus 로고    scopus 로고
    • Far-red fluorescence: A direct spectroscopic marker for LHCII oligomer formation in non-photochemical quenching
    • Miloslavina, Y., A. Wehner, ..., A. R. Holzwarth. 2008. Far-red fluorescence: a direct spectroscopic marker for LHCII oligomer formation in non-photochemical quenching. FEBS Lett. 582:3625-3631.
    • (2008) FEBS Lett , vol.582 , pp. 3625-3631
    • Miloslavina, Y.1    Wehner, A.2    Holzwarth, A.R.3
  • 50
    • 70350565366 scopus 로고    scopus 로고
    • Functional architecture of higher plant photosystem II supercomplexes
    • Caffarri, S., R. Kouril, ..., R. Croce. 2009. Functional architecture of higher plant photosystem II supercomplexes. EMBO J. 28:3052-3063.
    • (2009) EMBO J , vol.28 , pp. 3052-3063
    • Caffarri, S.1    Kouril, R.2    Croce, R.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.