메뉴 건너뛰기




Volumn 135, Issue 1-3, 2018, Pages 125-139

Erratum to: Interaction of the signaling state analog and the apoprotein form of the orange carotenoid protein with the fluorescence recovery protein (Photosynthesis Research, (2018), 135, 1-3, (125-139), 10.1007/s11120-017-0346-2);Interaction of the signaling state analog and the apoprotein form of the orange carotenoid protein with the fluorescence recovery protein

Author keywords

Fluorescein maleimide; Fluorescence correlation spectroscopy; Fluorescence recovery protein; Mass spectroscopy; Orange carotenoid protein; Site specific fluorescence labeling

Indexed keywords

APOPROTEIN; BACTERIAL PROTEIN; CYSTEINE; THIOL DERIVATIVE;

EID: 85013832143     PISSN: 01668595     EISSN: 15735079     Source Type: Journal    
DOI: 10.1007/s11120-017-0445-0     Document Type: Erratum
Times cited : (28)

References (45)
  • 2
    • 52949146331 scopus 로고    scopus 로고
    • Occurrence and function of the orange carotenoid protein in photoprotective mechanisms in various cyanobacteria
    • COI: 1:CAS:528:DC%2BD1cXhtFylsrnI, PID: 18694721
    • Boulay C, Abasova L, Six C, Vass I, Kirilovsky D (2008) Occurrence and function of the orange carotenoid protein in photoprotective mechanisms in various cyanobacteria. Biochim Biophys Acta 1777(10):1344–1354. doi:10.1016/j.bbabio.2008.07.002
    • (2008) Biochim Biophys Acta , vol.1777 , Issue.10 , pp. 1344-1354
    • Boulay, C.1    Abasova, L.2    Six, C.3    Vass, I.4    Kirilovsky, D.5
  • 3
    • 77954925946 scopus 로고    scopus 로고
    • Identification of a protein required for recovery of full antenna capacity in OCP-related photoprotective mechanism in cyanobacteria
    • COI: 1:CAS:528:DC%2BC3cXot1eksbg%3D, PID: 20534537
    • Boulay C, Wilson A, D’Haene S, Kirilovsky D (2010) Identification of a protein required for recovery of full antenna capacity in OCP-related photoprotective mechanism in cyanobacteria. Proc Natl Acad Sci USA 107(25):11620–11625. doi:10.1073/pnas.1002912107
    • (2010) Proc Natl Acad Sci USA , vol.107 , Issue.25 , pp. 11620-11625
    • Boulay, C.1    Wilson, A.2    D’Haene, S.3    Kirilovsky, D.4
  • 5
    • 84924787561 scopus 로고    scopus 로고
    • Biosynthesis of soluble carotenoid holoproteins in Escherichia coli
    • de Carbon CB, Thurotte A, Wilson A, Perreau F, Kirilovsky D (2015) Biosynthesis of soluble carotenoid holoproteins in Escherichia coli. Sci Rep 5:9085. doi:10.1038/srep09085
    • (2015) Sci Rep , vol.5 , pp. 9085
    • de Carbon, C.B.1    Thurotte, A.2    Wilson, A.3    Perreau, F.4    Kirilovsky, D.5
  • 6
    • 0001938338 scopus 로고    scopus 로고
    • The role of xanthophyll cycle carotenoids in the protection of photosynthesis
    • Demmig-Adams B, Adams WW (1996) The role of xanthophyll cycle carotenoids in the protection of photosynthesis. Trends Plant Sci 1(1):21–26. doi:10.1016/S1360-1385(96)80019-7
    • (1996) Trends Plant Sci , vol.1 , Issue.1 , pp. 21-26
    • Demmig-Adams, B.1    Adams, W.W.2
  • 7
    • 84899506373 scopus 로고    scopus 로고
    • Non-photochemical quenching and energy dissipation in plants, algae and cyanobacteria, Vol 40
    • Springer, Dordrecht
    • Demmig-Adams B, Garab G, Adams WW III, Govindjee (eds) (2014) Non-photochemical quenching and energy dissipation in plants, algae and cyanobacteria, Vol 40. Advances in photosynthesis and respiration, Springer, Dordrecht
    • (2014) Advances in photosynthesis and respiration
    • Demmig-Adams, B.1    Garab, G.2    Adams, W.W.I.I.I.3
  • 8
    • 81155139746 scopus 로고    scopus 로고
    • A kinetic model of non-photochemical quenching in cyanobacteria
    • COI: 1:CAS:528:DC%2BC3MXhsVKgsbfN, PID: 21907180
    • Gorbunov MY, Kuzminov FI, Fadeev VV, Kim JD, Falkowski PG (2011) A kinetic model of non-photochemical quenching in cyanobacteria. Biochim Biophys Acta 1807(12):1591–1599. doi:10.1016/j.bbabio.2011.08.009
    • (2011) Biochim Biophys Acta , vol.1807 , Issue.12 , pp. 1591-1599
    • Gorbunov, M.Y.1    Kuzminov, F.I.2    Fadeev, V.V.3    Kim, J.D.4    Falkowski, P.G.5
  • 9
    • 84858681266 scopus 로고    scopus 로고
    • Adventures with Cyanobacteria: a personal perspective
    • Govindjee, Shevela D (2011) Adventures with Cyanobacteria: a personal perspective. Front Plant Sci 2(28):1–17. doi:10.3389/fpls.2011.00028
    • (2011) Front Plant Sci , vol.2 , Issue.28 , pp. 1-17
    • Govindjee, S.D.1
  • 11
    • 80051943328 scopus 로고    scopus 로고
    • In vitro reconstitution of the cyanobacterial photoprotective mechanism mediated by the orange carotenoid protein in Synechocystis PCC 6803
    • COI: 1:CAS:528:DC%2BC3MXhtFeqsL7F, PID: 21764991
    • Gwizdala M, Wilson A, Kirilovsky D (2011) In vitro reconstitution of the cyanobacterial photoprotective mechanism mediated by the orange carotenoid protein in Synechocystis PCC 6803. Plant Cell 23(7):2631–2643. doi:10.1105/tpc.111.086884
    • (2011) Plant Cell , vol.23 , Issue.7 , pp. 2631-2643
    • Gwizdala, M.1    Wilson, A.2    Kirilovsky, D.3
  • 12
    • 84872116028 scopus 로고    scopus 로고
    • Characterization of the Synechocystis PCC 6803 fluorescence recovery protein involved in photoprotection
    • COI: 1:CAS:528:DC%2BC3sXitlaju78%3D, PID: 23159727
    • Gwizdala M, Wilson A, Omairi-Nasser A, Kirilovsky D (2013) Characterization of the Synechocystis PCC 6803 fluorescence recovery protein involved in photoprotection. Biochim Biophys Acta 1827(3):348–354. doi:10.1016/j.bbabio.2012.11.001
    • (2013) Biochim Biophys Acta , vol.1827 , Issue.3 , pp. 348-354
    • Gwizdala, M.1    Wilson, A.2    Omairi-Nasser, A.3    Kirilovsky, D.4
  • 13
    • 0019819335 scopus 로고
    • A carotenoid protein from cyanobacteria
    • Holt TK, Krogmann DW (1981) A carotenoid protein from cyanobacteria. Biochim Biophys Acta (637):408–414. doi:10.1016/0005-2728(81)90045-1
    • (1981) Biochim Biophys Acta , vol.637 , pp. 408-414
    • Holt, T.K.1    Krogmann, D.W.2
  • 14
    • 85034714756 scopus 로고    scopus 로고
    • Monitoring the diffusion behavior of Na, K-ATPase by fluorescence correlation spectroscopy (FCS) upon fluorescence labelling with eGFP or Dreiklang. Optofluid
    • Junghans C, Schmitt F-J, Vukojević V, Friedrich T (2015) Monitoring the diffusion behavior of Na, K-ATPase by fluorescence correlation spectroscopy (FCS) upon fluorescence labelling with eGFP or Dreiklang. Optofluid. Microfluid Nanofluid 2:1–13. doi:10.1515/optof-2016-0001
    • (2015) Microfluid Nanofluid , vol.2 , pp. 1-13
    • Junghans, C.1    Schmitt, F.-J.2    Vukojević, V.3    Friedrich, T.4
  • 17
    • 80755179274 scopus 로고    scopus 로고
    • The orange carotenoid protein in photoprotection of photosystem II in cyanobacteria
    • COI: 1:CAS:528:DC%2BC3MXhsFOgur%2FE, PID: 21565162
    • Kirilovsky D, Kerfeld CA (2012) The orange carotenoid protein in photoprotection of photosystem II in cyanobacteria. Biochim Biophys Acta 1817(1):158–166. doi:10.1016/j.bbabio.2011.04.013
    • (2012) Biochim Biophys Acta , vol.1817 , Issue.1 , pp. 158-166
    • Kirilovsky, D.1    Kerfeld, C.A.2
  • 19
    • 84896893249 scopus 로고    scopus 로고
    • Structural and functional modularity of the orange carotenoid protein: distinct roles for the N- and C-terminal domains in cyanobacterial photoprotection
    • COI: 1:CAS:528:DC%2BC2cXks1SnsL4%3D, PID: 24399299
    • Leverenz RL, Jallet D, Li MD, Mathies RA, Kirilovsky D, Kerfeld CA (2014) Structural and functional modularity of the orange carotenoid protein: distinct roles for the N- and C-terminal domains in cyanobacterial photoprotection. Plant Cell 26(1):426–437. doi:10.1105/tpc.113.118588
    • (2014) Plant Cell , vol.26 , Issue.1 , pp. 426-437
    • Leverenz, R.L.1    Jallet, D.2    Li, M.D.3    Mathies, R.A.4    Kirilovsky, D.5    Kerfeld, C.A.6
  • 21
    • 84908218510 scopus 로고    scopus 로고
    • Mass spectrometry footprinting reveals the structural rearrangements of cyanobacterial orange carotenoid protein upon light activation
    • COI: 1:CAS:528:DC%2BC2cXhs1Gnu7nI, PID: 25256653
    • Liu H, Zhang H, King j D, Wolf NR, Prado M, Gross ML, Blankenship RE (2014) Mass spectrometry footprinting reveals the structural rearrangements of cyanobacterial orange carotenoid protein upon light activation. Biochim Biophys Acta 1837(12):1955–1963. doi:10.1016/j.bbabio.2014.09.004
    • (2014) Biochim Biophys Acta , vol.1837 , Issue.12 , pp. 1955-1963
    • Liu, H.1    Zhang, H.2    King j, D.3    Wolf, N.R.4    Prado, M.5    Gross, M.L.6    Blankenship, R.E.7
  • 22
    • 84959364862 scopus 로고    scopus 로고
    • Dramatic domain rearrangements of the cyanobacterial orange carotenoid protein upon photoactivation
    • COI: 1:CAS:528:DC%2BC28XitVSlsb4%3D, PID: 26848988
    • Liu H, Zhang H, Orf GS, Lu Y, Jiang J, King JD, Wolf NR, Gross ML, Blankenship RE (2016) Dramatic domain rearrangements of the cyanobacterial orange carotenoid protein upon photoactivation. Biochemistry 55(7):1003–1009. doi:10.1021/acs.biochem.6b00013
    • (2016) Biochemistry , vol.55 , Issue.7 , pp. 1003-1009
    • Liu, H.1    Zhang, H.2    Orf, G.S.3    Lu, Y.4    Jiang, J.5    King, J.D.6    Wolf, N.R.7    Gross, M.L.8    Blankenship, R.E.9
  • 23
    • 0016366591 scopus 로고
    • Fluorescence correlation spectroscopy. II. An experimental realization
    • COI: 1:CAS:528:DyaE2cXnsVKnsg%3D%3D, PID: 4818131
    • Magde D, Elson EL, Webb WW (1974) Fluorescence correlation spectroscopy. II. An experimental realization. Biopolymers 13(1):29–61. doi:10.1002/bip.1974.360130103
    • (1974) Biopolymers , vol.13 , Issue.1 , pp. 29-61
    • Magde, D.1    Elson, E.L.2    Webb, W.W.3
  • 24
    • 84896743395 scopus 로고    scopus 로고
    • Characterization of the fluorescence correlation spectroscopy (FCS) standard rhodamine 6G and calibration of its diffusion coefficient in aqueous solutions
    • COI: 1:STN:280:DC%2BC2crhsFCluw%3D%3D, PID: 24606354
    • Majer G, Melchior JP (2014) Characterization of the fluorescence correlation spectroscopy (FCS) standard rhodamine 6G and calibration of its diffusion coefficient in aqueous solutions. J Chem Phys 140(9):094201. doi:10.1063/1.4867096
    • (2014) J Chem Phys , vol.140 , Issue.9 , pp. 94201
    • Majer, G.1    Melchior, J.P.2
  • 25
    • 84906306744 scopus 로고    scopus 로고
    • The time course of non-photochemical quenching in phycobilisomes of Synechocystis sp. PCC6803 as revealed by picosecond time-resolved fluorimetry
    • COI: 1:CAS:528:DC%2BC2cXkvV2msLw%3D, PID: 24463052
    • Maksimov EG, Schmitt FJ, Shirshin EA, Svirin MD, Elanskaya IV, Friedrich T, Fadeev VV, Paschenko VZ, Rubin AB (2014) The time course of non-photochemical quenching in phycobilisomes of Synechocystis sp. PCC6803 as revealed by picosecond time-resolved fluorimetry. Biochim Biophys Acta 1837(9):1540–1547. doi:10.1016/j.bbabio.2014.01.010
    • (2014) Biochim Biophys Acta , vol.1837 , Issue.9 , pp. 1540-1547
    • Maksimov, E.G.1    Schmitt, F.J.2    Shirshin, E.A.3    Svirin, M.D.4    Elanskaya, I.V.5    Friedrich, T.6    Fadeev, V.V.7    Paschenko, V.Z.8    Rubin, A.B.9
  • 26
    • 84931569539 scopus 로고    scopus 로고
    • Features of temporal behavior of fluorescence recovery in Synechocystis sp. PCC6803
    • COI: 1:CAS:528:DC%2BC2MXltVSgtbg%3D, PID: 25800518
    • Maksimov EG, Klementiev KE, Shirshin EA, Tsoraev GV, Elanskaya IV, Paschenko VZ (2015a) Features of temporal behavior of fluorescence recovery in Synechocystis sp. PCC6803. Photosynth Res 125(1–2):167–178. doi:10.1007/s11120-015-0124-y
    • (2015) Photosynth Res , vol.125 , Issue.1-2 , pp. 167-178
    • Maksimov, E.G.1    Klementiev, K.E.2    Shirshin, E.A.3    Tsoraev, G.V.4    Elanskaya, I.V.5    Paschenko, V.Z.6
  • 30
    • 84931567169 scopus 로고    scopus 로고
    • Primary electron transfer processes in photosynthetic reaction centers from oxygenic organisms
    • COI: 1:CAS:528:DC%2BC2MXitFOrsL8%3D, PID: 25648636
    • Mamedov M, Govindjee, Nadtochenko V, Semenov A (2015) Primary electron transfer processes in photosynthetic reaction centers from oxygenic organisms. Photosynth Res 125(1):51–63. doi:10.1007/s11120-015-0088-y
    • (2015) Photosynth Res , vol.125 , Issue.1 , pp. 51-63
    • Mamedov, M.1    Govindjee2    Nadtochenko, V.3    Semenov, A.4
  • 31
    • 85010715780 scopus 로고    scopus 로고
    • Light absorption and energy transfer in the antenna complexes of photosynthetic organisms
    • COI: 1:CAS:528:DC%2BC28XhtFyit7vI, PID: 27428615
    • Mirkovic T, Ostroumov EE, Anna JM, van Grondelle R, Govindjee, Scholes GD (2017) Light absorption and energy transfer in the antenna complexes of photosynthetic organisms. Chem Rev 117(2):249–293. doi:10.1021/acs.chemrev.6b00002
    • (2017) Chem Rev , vol.117 , Issue.2 , pp. 249-293
    • Mirkovic, T.1    Ostroumov, E.E.2    Anna, J.M.3    van Grondelle, R.4    Govindjee5    Scholes, G.D.6
  • 32
    • 0035028317 scopus 로고    scopus 로고
    • Non-photochemical quenching. a response to excess light energy
    • PID: 11299337
    • Müller P, Li X-P, Niyogi KK (2001) Non-photochemical quenching. a response to excess light energy. Plant Physiol 125(4):1558–1566. doi:10.1104/pp.125.4.1558
    • (2001) Plant Physiol , vol.125 , Issue.4 , pp. 1558-1566
    • Müller, P.1    Li, X.-P.2    Niyogi, K.K.3
  • 33
    • 84878984467 scopus 로고    scopus 로고
    • Evolution of flexible non-photochemical quenching mechanisms that regulate light harvesting in oxygenic photosynthesis
    • COI: 1:CAS:528:DC%2BC3sXlvV2rtrs%3D, PID: 23583332
    • Niyogi KK, Truong TB (2013) Evolution of flexible non-photochemical quenching mechanisms that regulate light harvesting in oxygenic photosynthesis. Curr Opin Plant Biol 16(3):307–314. doi:10.1016/j.pbi.2013.03.011
    • (2013) Curr Opin Plant Biol , vol.16 , Issue.3 , pp. 307-314
    • Niyogi, K.K.1    Truong, T.B.2
  • 34
    • 61549113770 scopus 로고    scopus 로고
    • Influence of zeaxanthin and echinenone binding on the activity of the orange carotenoid protein
    • COI: 1:CAS:528:DC%2BD1MXivVeltrk%3D, PID: 19366615
    • Punginelli C, Wilson A, Routaboul JM, Kirilovsky D (2009) Influence of zeaxanthin and echinenone binding on the activity of the orange carotenoid protein. Biochim Biophys Acta 1787(4):280–288. doi:10.1016/j.bbabio.2009.01.011
    • (2009) Biochim Biophys Acta , vol.1787 , Issue.4 , pp. 280-288
    • Punginelli, C.1    Wilson, A.2    Routaboul, J.M.3    Kirilovsky, D.4
  • 35
    • 0001764437 scopus 로고
    • Fluorescence correlation spectroscopy and application to the study of brownian motion of biopolymers
    • COI: 1:CAS:528:DyaE1MXkslSjt7o%3D
    • Rigler R, Grasselli P, Ehrenberg M (1979) Fluorescence correlation spectroscopy and application to the study of brownian motion of biopolymers. Phys Scr 19:486–490. doi:10.1088/0031-8949/19/4/030
    • (1979) Phys Scr , vol.19 , pp. 486-490
    • Rigler, R.1    Grasselli, P.2    Ehrenberg, M.3
  • 36
    • 84901400843 scopus 로고    scopus 로고
    • The cyanobacterial photoactive orange carotenoid protein is an excellent singlet oxygen quencher
    • COI: 1:CAS:528:DC%2BC2cXpslSjs78%3D, PID: 24748041
    • Sedoud A, Lopez-Igual R, Ur Rehman A, Wilson A, Perreau F, Boulay C, Vass I, Krieger-Liszkay A, Kirilovsky D (2014) The cyanobacterial photoactive orange carotenoid protein is an excellent singlet oxygen quencher. Plant Cell 26(4):1781–1791. doi:10.1105/tpc.114.123802
    • (2014) Plant Cell , vol.26 , Issue.4 , pp. 1781-1791
    • Sedoud, A.1    Lopez-Igual, R.2    Ur Rehman, A.3    Wilson, A.4    Perreau, F.5    Boulay, C.6    Vass, I.7    Krieger-Liszkay, A.8    Kirilovsky, D.9
  • 37
    • 85054611489 scopus 로고    scopus 로고
    • Oxygenic photosynthesis in cyanobacteria
    • Srivastava AK, Rai AN, Neilan BA, (eds), Taylor & Francis, Boca Raton, London, New York
    • Shevela D, Pishchalinikov RY, Eichacker LA, Govindjee (2013) Oxygenic photosynthesis in cyanobacteria. In: Srivastava AK, Rai AN, Neilan BA (eds) Stress biology of cyanobacteria. Taylor & Francis, Boca Raton, London, New York
    • (2013) Stress biology of cyanobacteria
    • Shevela, D.1    Pishchalinikov, R.Y.2    Eichacker, L.A.3    Govindjee4
  • 38
    • 84992195231 scopus 로고    scopus 로고
    • The purple Trp288Ala mutant of Synechocystis OCP persistently quenches phycobilisome fluorescence and tightly interacts with FRP
    • COI: 1:CAS:528:DC%2BC28XhslSit7jI, PID: 27755972
    • Sluchanko NN, Klementiev KE, Shirshin EA, Tsoraev GV, Friedrich T, Maksimov EG (2017) The purple Trp288Ala mutant of Synechocystis OCP persistently quenches phycobilisome fluorescence and tightly interacts with FRP. Biochim Biophys Acta 1858:1–11. doi:10.1016/j.bbabio.2016.10.005
    • (2017) Biochim Biophys Acta , vol.1858 , pp. 1-11
    • Sluchanko, N.N.1    Klementiev, K.E.2    Shirshin, E.A.3    Tsoraev, G.V.4    Friedrich, T.5    Maksimov, E.G.6
  • 39
    • 84878986302 scopus 로고    scopus 로고
    • Crystal structure of the FRP and identification of the active site for modulation of OCP-mediated photoprotection in cyanobacteria
    • COI: 1:CAS:528:DC%2BC3sXhtFOls7bF, PID: 23716688
    • Sutter M, Wilson A, Leverenz RL, Lopez-Igual R, Thurotte A, Salmeen AE, Kirilovsky D, Kerfeld CA (2013) Crystal structure of the FRP and identification of the active site for modulation of OCP-mediated photoprotection in cyanobacteria. Proc Natl Acad Sci USA 110(24):10022–10027. doi:10.1073/pnas.1303673110
    • (2013) Proc Natl Acad Sci USA , vol.110 , Issue.24 , pp. 10022-10027
    • Sutter, M.1    Wilson, A.2    Leverenz, R.L.3    Lopez-Igual, R.4    Thurotte, A.5    Salmeen, A.E.6    Kirilovsky, D.7    Kerfeld, C.A.8
  • 40
    • 57449085362 scopus 로고    scopus 로고
    • Quantitative single-molecule imaging by confocal laser scanning microscopy
    • COI: 1:CAS:528:DC%2BD1cXhsVOmsb%2FI, PID: 19011092
    • Vukojevic V, Heidkamp M, Ming Y, Johansson B, Terenius L, Rigler R (2008) Quantitative single-molecule imaging by confocal laser scanning microscopy. Proc Natl Acad Sci USA 105(47):18176–18181. doi:10.1073/pnas.0809250105
    • (2008) Proc Natl Acad Sci USA , vol.105 , Issue.47 , pp. 18176-18181
    • Vukojevic, V.1    Heidkamp, M.2    Ming, Y.3    Johansson, B.4    Terenius, L.5    Rigler, R.6
  • 41
    • 77749239764 scopus 로고    scopus 로고
    • Quantitative study of synthetic Hox transcription factor-DNA interactions in live cells
    • PID: 20147626
    • Vukojevic V, Papadopoulos DK, Terenius L, Gehring W, Rigler R (2010) Quantitative study of synthetic Hox transcription factor-DNA interactions in live cells. Proc Natl Acad Sci USA 107:4087–4092. doi:10.1073/pnas.0914612107
    • (2010) Proc Natl Acad Sci USA , vol.107 , pp. 4087-4092
    • Vukojevic, V.1    Papadopoulos, D.K.2    Terenius, L.3    Gehring, W.4    Rigler, R.5
  • 42
    • 33745445226 scopus 로고    scopus 로고
    • A soluble carotenoid protein involved in phycobilisome-related energy dissipation in cyanobacteria
    • COI: 1:CAS:528:DC%2BD28Xjslaksbg%3D, PID: 16531492
    • Wilson A, Ajlani G, Verbavatz J-M, Vass I, Kerfeld CA, Kirilovsky D (2006) A soluble carotenoid protein involved in phycobilisome-related energy dissipation in cyanobacteria. Plant Cell 18(4):992–1007. doi:10.1105/tpc.105.040121
    • (2006) Plant Cell , vol.18 , Issue.4 , pp. 992-1007
    • Wilson, A.1    Ajlani, G.2    Verbavatz, J.-M.3    Vass, I.4    Kerfeld, C.A.5    Kirilovsky, D.6
  • 44
    • 78650936291 scopus 로고    scopus 로고
    • Essential role of two tyrosines and two tryptophans on the photoprotection activity of the orange carotenoid protein
    • COI: 1:CAS:528:DC%2BC3MXhsFygur8%3D, PID: 21172302
    • Wilson A, Punginelli C, Couturier M, Perreau F, Kirilovsky D (2011) Essential role of two tyrosines and two tryptophans on the photoprotection activity of the orange carotenoid protein. Biochim Biophys Acta 1807(3):293–301. doi:10.1016/j.bbabio.2010.12.009
    • (2011) Biochim Biophys Acta , vol.1807 , Issue.3 , pp. 293-301
    • Wilson, A.1    Punginelli, C.2    Couturier, M.3    Perreau, F.4    Kirilovsky, D.5
  • 45
    • 0030687617 scopus 로고    scopus 로고
    • The orange carotenoid protein of Synechocystis PCC 6803
    • COI: 1:CAS:528:DyaK2sXntF2mtrk%3D, PID: 9398074
    • Wu YP, Krogmann DW (1997) The orange carotenoid protein of Synechocystis PCC 6803. Biochim Biophys Acta 1322(1):1–7. doi:10.1016/S0005-2728(97)00067-4
    • (1997) Biochim Biophys Acta , vol.1322 , Issue.1 , pp. 1-7
    • Wu, Y.P.1    Krogmann, D.W.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.