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Volumn 8, Issue 2, 2013, Pages

Oxidized Amino Acid Residues in the Vicinity of QA and PheoD1 of the Photosystem II Reaction Center: Putative Generation Sites of Reducing-Side Reactive Oxygen Species

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID; CYTOCHROME B559; CYTOCHROME B559 ALPHA SUBUNIT; CYTOCHROME B559 BETA SUBUNIT; REACTIVE OXYGEN METABOLITE; UNCLASSIFIED DRUG;

EID: 84874569527     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0058042     Document Type: Article
Times cited : (26)

References (54)
  • 2
    • 33745936562 scopus 로고    scopus 로고
    • Structure and function of Photosystems I and II
    • Nelson N, Yocum CF, (2006) Structure and function of Photosystems I and II. Ann Rev Plant Biol 57: 521-565.
    • (2006) Ann Rev Plant Biol , vol.57 , pp. 521-565
    • Nelson, N.1    Yocum, C.F.2
  • 3
    • 0035825682 scopus 로고    scopus 로고
    • Crystal structure of Photosystem II from Synechococcus elongatus at 3.8 Å resolution
    • Zouni A, Witt H-T, Kern J, Fromme P, Krauss N, et al. (2001) Crystal structure of Photosystem II from Synechococcus elongatus at 3.8 Å resolution. Nature 409: 739-743.
    • (2001) Nature , vol.409 , pp. 739-743
    • Zouni, A.1    Witt, H.-T.2    Kern, J.3    Fromme, P.4    Krauss, N.5
  • 4
    • 0037422557 scopus 로고    scopus 로고
    • Crystal structure of oxygen-evolving Photosystem II from Thermosynechococcus vulcanus at 3.7 Å resolution
    • Kamiya N, Shen J-R, (2003) Crystal structure of oxygen-evolving Photosystem II from Thermosynechococcus vulcanus at 3.7 Å resolution. Proc Natl Sci Acad (USA) 100: 98-103.
    • (2003) Proc Natl Sci Acad (USA) , vol.100 , pp. 98-103
    • Kamiya, N.1    Shen, J.-R.2
  • 6
    • 30744445692 scopus 로고    scopus 로고
    • Towards complete cofactor arrangement in the 3.0 Å resolution structure of Photosystem II
    • Loll B, Kern N, Saenger W, Zouni A, Biesiadka J, (2006) Towards complete cofactor arrangement in the 3.0 Å resolution structure of Photosystem II. Nature 438: 1040-1044.
    • (2006) Nature , vol.438 , pp. 1040-1044
    • Loll, B.1    Kern, N.2    Saenger, W.3    Zouni, A.4    Biesiadka, J.5
  • 7
    • 62049085169 scopus 로고    scopus 로고
    • Cyanobacterial photosystem II at 2.9 Å resolution and the roles of quinones, lipids, channels and chloride
    • Guskov A, Kern J, Gabdulkhakov A, Broser M, Zouni A, et al. (2009) Cyanobacterial photosystem II at 2.9 Å resolution and the roles of quinones, lipids, channels and chloride. Nat Struct Mol Biol 16: 334-342.
    • (2009) Nat Struct Mol Biol , vol.16 , pp. 334-342
    • Guskov, A.1    Kern, J.2    Gabdulkhakov, A.3    Broser, M.4    Zouni, A.5
  • 8
    • 85028099698 scopus 로고    scopus 로고
    • Crystal structure of oxygen-evolving Photosystem II at a resolution of 1.9 Å
    • Umena Y, Kawakami K, Shen J-R, Kamiya N, (2011) Crystal structure of oxygen-evolving Photosystem II at a resolution of 1.9 Å. Nature. 473: 55-60.
    • (2011) Nature , vol.473 , pp. 55-60
    • Umena, Y.1    Kawakami, K.2    Shen, J.-R.3    Kamiya, N.4
  • 10
    • 0031853225 scopus 로고    scopus 로고
    • The structure and function of the 33 kDa extrinsic protein of Photosystem II. A critical review
    • Bricker TM, Frankel LK, (1998) The structure and function of the 33 kDa extrinsic protein of Photosystem II. A critical review. Photosyn Res 56: 157-173.
    • (1998) Photosyn Res , vol.56 , pp. 157-173
    • Bricker, T.M.1    Frankel, L.K.2
  • 11
    • 34547839673 scopus 로고    scopus 로고
    • The extrinsic proteins of Photosystem II
    • Roose J, Wegener K, Pakrasi H, (2007) The extrinsic proteins of Photosystem II. Photosyn Res 92: 369-387.
    • (2007) Photosyn Res , vol.92 , pp. 369-387
    • Roose, J.1    Wegener, K.2    Pakrasi, H.3
  • 12
    • 73449135829 scopus 로고    scopus 로고
    • Documentation of significant electron transport defects on the reducing side of Photosystem II upon removal of the PsbP and PsbQ extrinsic proteins
    • Roose JL, Frankel LK, Bricker TM, (2010) Documentation of significant electron transport defects on the reducing side of Photosystem II upon removal of the PsbP and PsbQ extrinsic proteins. Biochemistry 49: 36-41.
    • (2010) Biochemistry , vol.49 , pp. 36-41
    • Roose, J.L.1    Frankel, L.K.2    Bricker, T.M.3
  • 13
    • 79957984587 scopus 로고    scopus 로고
    • Auxiliary functions of the PsbO, PsbP and PsbQ proteins of higher plant Photosystem II: A critical analysis
    • Bricker TM, Frankel LK, (2011) Auxiliary functions of the PsbO, PsbP and PsbQ proteins of higher plant Photosystem II: A critical analysis. J Photochem Photobiol B: Biol 104: 165-178.
    • (2011) J Photochem Photobiol B: Biol , vol.104 , pp. 165-178
    • Bricker, T.M.1    Frankel, L.K.2
  • 14
    • 0000223633 scopus 로고    scopus 로고
    • Introduction to oxygen evolution and the oxygen-evolving complex
    • Dordrecht: Kluwer Academic Publishers, In: Ort DR, Yocum CF, editors
    • Bricker TM, Ghanotakis DF (1996) Introduction to oxygen evolution and the oxygen-evolving complex. In: Ort DR, Yocum CF, editors. Oxygenic Photosynthesis: The Light Reactions. Dordrecht: Kluwer Academic Publishers. 113-136.
    • (1996) Oxygenic Photosynthesis: The Light Reactions , pp. 113-136
    • Bricker, T.M.1    Ghanotakis, D.F.2
  • 16
    • 67649948825 scopus 로고    scopus 로고
    • Production of reactive oxygen species by Photosystem II
    • Pospíšil P, (2009) Production of reactive oxygen species by Photosystem II. Biochim Biophys Acta 1787: 1151-1160.
    • (2009) Biochim Biophys Acta , vol.1787 , pp. 1151-1160
    • Pospíšil, P.1
  • 17
    • 0025336206 scopus 로고
    • Characterization of triplet-states in isolated Photosystem II reaction centres - oxygen quenching as a mechanism for photodamage
    • Durrant JR, Giorgi LB, Barber J, Klug DR, Porter G, (1990) Characterization of triplet-states in isolated Photosystem II reaction centres - oxygen quenching as a mechanism for photodamage. Biochim Biophys Acta 1017: 166-175.
    • (1990) Biochim Biophys Acta , vol.1017 , pp. 166-175
    • Durrant, J.R.1    Giorgi, L.B.2    Barber, J.3    Klug, D.R.4    Porter, G.5
  • 18
    • 0027217043 scopus 로고
    • Direct detection of singlet oxygen from isolated Photosystem II reaction centres
    • Macpherson AN, Telfer A, Truscott TG, Barber J, (1993) Direct detection of singlet oxygen from isolated Photosystem II reaction centres. Biochim Biophys Acta 1143: 301-309.
    • (1993) Biochim Biophys Acta , vol.1143 , pp. 301-309
    • Macpherson, A.N.1    Telfer, A.2    Truscott, T.G.3    Barber, J.4
  • 19
    • 0028010410 scopus 로고
    • Singlet oxygen production in thylakoid membranes during photoinhibition as detected by EPR spectroscopy
    • Hideg E, Spetea C, Vass I, (1994) Singlet oxygen production in thylakoid membranes during photoinhibition as detected by EPR spectroscopy. Photosyn Res 39: 191-199.
    • (1994) Photosyn Res , vol.39 , pp. 191-199
    • Hideg, E.1    Spetea, C.2    Vass, I.3
  • 20
    • 84865152482 scopus 로고    scopus 로고
    • Identification of oxidized amino acid residues in the vicinity of the Mn4CaO5 cluster of Photosystem II: Implications for the identification of oxygen channels within the photosystem
    • Frankel LK, Sallans L, Limbach PA, Bricker TM, (2012) Identification of oxidized amino acid residues in the vicinity of the Mn4CaO5 cluster of Photosystem II: Implications for the identification of oxygen channels within the photosystem. Biochemistry 51: 6371-6377.
    • (2012) Biochemistry , vol.51 , pp. 6371-6377
    • Frankel, L.K.1    Sallans, L.2    Limbach, P.A.3    Bricker, T.M.4
  • 22
    • 84864442260 scopus 로고    scopus 로고
    • Light-induced oxidative stress, N-formylkynurenine, and oxygenic photosynthesis
    • Dreaden Kasson TM, Rexroth S, Barry BA, (2012) Light-induced oxidative stress, N-formylkynurenine, and oxygenic photosynthesis. Plos One 7: e42220.
    • (2012) Plos One , vol.7
    • Dreaden Kasson, T.M.1    Rexroth, S.2    Barry, B.A.3
  • 23
    • 79959342657 scopus 로고    scopus 로고
    • N-Formylkynurenine as a marker of high light stress in photosynthesis
    • Dreaden TM, Chen J, Rexroth S, Barry BA, (2011) N-Formylkynurenine as a marker of high light stress in photosynthesis. J Biol Chem 286: 22632-22641.
    • (2011) J Biol Chem , vol.286 , pp. 22632-22641
    • Dreaden, T.M.1    Chen, J.2    Rexroth, S.3    Barry, B.A.4
  • 24
    • 0001449340 scopus 로고
    • Membrane protein damage and repair: selective loss of a quinone-protein function in chloroplast membranes
    • Kyle DJ, Ohad I, Arntzen CJ, (1984) Membrane protein damage and repair: selective loss of a quinone-protein function in chloroplast membranes. 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
  • 25
    • 0027947679 scopus 로고
    • The photoproduction of superoxide radicals and the superoxide dismutase activity of Photosystem II, The possible involvement of cytochrome b559
    • Ananyev GM, Renger G, Wacker U, Klimov V (1994) The photoproduction of superoxide radicals and the superoxide dismutase activity of Photosystem II. The possible involvement of cytochrome b559. Photosyn Res: 327-338.
    • (1994) Photosyn Res , pp. 327-338
    • Ananyev, G.M.1    Renger, G.2    Wacker, U.3    Klimov, V.4
  • 26
    • 3242890310 scopus 로고    scopus 로고
    • Superoxide, hydrogen peroxide and hydroxyl radical in D1/D2/cytochrome b559 Photosystem II reaction center complex
    • Liu K, Sun J, Song YG, Liu B, Xu YK, et al. (2004) Superoxide, hydrogen peroxide and hydroxyl radical in D1/D2/cytochrome b559 Photosystem II reaction center complex. Photosyn Res 81: 41-47.
    • (2004) Photosyn Res , vol.81 , pp. 41-47
    • Liu, K.1    Sun, J.2    Song, Y.G.3    Liu, B.4    Xu, Y.K.5
  • 27
    • 0000337384 scopus 로고    scopus 로고
    • Form and function of cytochrome b559
    • In: Ort DR, Yocum CF, editors, Dordrech: Kluwer Academic Publishers
    • Whitmarsh J, Pakrasi HB (1996) Form and function of cytochrome b559. In: Ort DR, Yocum CF, editors. Oxygenic Photosynthesis: The Light Reactions. Dordrech: Kluwer Academic Publishers. 249-264.
    • (1996) Oxygenic Photosynthesis: The Light Reactions , pp. 249-264
    • Whitmarsh, J.1    Pakrasi, H.B.2
  • 28
    • 0343618724 scopus 로고    scopus 로고
    • Dark reoxidation of the plastoquinone-pool is mediated by the low-potential form of cytochrome b559 in spinach thylakoids
    • Kruk J, Strzałka K, (1999) Dark reoxidation of the plastoquinone-pool is mediated by the low-potential form of cytochrome b559 in spinach thylakoids. Photosyn Res 62: 273-279.
    • (1999) Photosyn Res , vol.62 , pp. 273-279
    • Kruk, J.1    Strzałka, K.2
  • 29
    • 0031466276 scopus 로고    scopus 로고
    • Purification and determination of intact molecular mass by electrospray ionization mass spectrometry of the photosystem II reaction center subunits
    • Sharma J, Panico M, Barber J, Morris HR, (1997) Purification and determination of intact molecular mass by electrospray ionization mass spectrometry of the photosystem II reaction center subunits. J Biol Chem 272: 33153-33157.
    • (1997) J Biol Chem , vol.272 , pp. 33153-33157
    • Sharma, J.1    Panico, M.2    Barber, J.3    Morris, H.R.4
  • 30
    • 4444329125 scopus 로고    scopus 로고
    • Characterization of a digested protein complex with quantitative aspects: An approach based on accurate mass chromatographic analysis with Fourier transform-ion cyclotron resonance mass spectrometry
    • Nakamura T, Dohmae N, Takio K, (2004) Characterization of a digested protein complex with quantitative aspects: An approach based on accurate mass chromatographic analysis with Fourier transform-ion cyclotron resonance mass spectrometry. Proteomics 4: 2558-2566.
    • (2004) Proteomics , vol.4 , pp. 2558-2566
    • Nakamura, T.1    Dohmae, N.2    Takio, K.3
  • 31
    • 57449108112 scopus 로고    scopus 로고
    • Low-oxygen induction of normally cryptic psbA genes in cyanobacteria
    • Summerfield TC, Toepel J, Sherman LA, (2008) Low-oxygen induction of normally cryptic psbA genes in cyanobacteria. Biochemistry 47: 12939-12941.
    • (2008) Biochemistry , vol.47 , pp. 12939-12941
    • Summerfield, T.C.1    Toepel, J.2    Sherman, L.A.3
  • 32
    • 77956899459 scopus 로고    scopus 로고
    • Functional characterization and quantification of the alternative PsbA copies in Thermosynechococcus elongatus and their role in photoprotection
    • Sander J, Nowaczyk M, Buchta J, Dau H, Vass I, et al. (2010) Functional characterization and quantification of the alternative PsbA copies in Thermosynechococcus elongatus and their role in photoprotection. J Biol Chem 285: 29851-29856.
    • (2010) J Biol Chem , vol.285 , pp. 29851-29856
    • Sander, J.1    Nowaczyk, M.2    Buchta, J.3    Dau, H.4    Vass, I.5
  • 33
    • 0032534935 scopus 로고    scopus 로고
    • Modulation of quantum yield of primary radical pair formation in photosystem II by site-directed mutagenesis affecting radical cations and anions
    • Merry SAP, Nixon PJ, Barter LMC, Schilstra M, Porter G, et al. (1998) Modulation of quantum yield of primary radical pair formation in photosystem II by site-directed mutagenesis affecting radical cations and anions. Biochemistry 37: 17439-17447.
    • (1998) Biochemistry , vol.37 , pp. 17439-17447
    • Merry, S.A.P.1    Nixon, P.J.2    Barter, L.M.C.3    Schilstra, M.4    Porter, G.5
  • 34
    • 0035933845 scopus 로고    scopus 로고
    • High field EPR study of the pheophytin anion radical in wild type and D1-E130 mutants of Photosystem II in Chlamydomonas reinhardtii
    • Dorlet P, Xiong L, Sayre RT, Un S, (2001) High field EPR study of the pheophytin anion radical in wild type and D1-E130 mutants of Photosystem II in Chlamydomonas reinhardtii. J Biol Chem 276: 22313-22316.
    • (2001) J Biol Chem , vol.276 , pp. 22313-22316
    • Dorlet, P.1    Xiong, L.2    Sayre, R.T.3    Un, S.4
  • 35
    • 0021114712 scopus 로고
    • Penetration of dioxygen into proteins studied by quenching of phosphorescence and fluorescence
    • W
    • Calhoun DB, Vanderkooi JM, Woodrow III GV, Englander S, (1983) W (1983) Penetration of dioxygen into proteins studied by quenching of phosphorescence and fluorescence. Biochemistry 22: 1526-1532.
    • (1983) Biochemistry , vol.22 , pp. 1526-1532
    • Calhoun, D.B.1    Vanderkooi, J.M.2    Woodrow III, G.V.3    Englander, S.4
  • 36
    • 0031468625 scopus 로고    scopus 로고
    • Primary structure characterization of the Photosystem II D1 and D2 subunits
    • Sharma J, Panico M, Shipton CA, Nilsson F, Morris HR, et al. (1997) Primary structure characterization of the Photosystem II D1 and D2 subunits. J Biol Chem 272: 33158-33166.
    • (1997) J Biol Chem , vol.272 , pp. 33158-33166
    • Sharma, J.1    Panico, M.2    Shipton, C.A.3    Nilsson, F.4    Morris, H.R.5
  • 37
    • 34249813112 scopus 로고    scopus 로고
    • Dark production of reactive oxygen species in photosystem II membrane particles at elevated temperature: EPR spin-trapping study
    • Pospíšil P, Šnyrychova? S, Nauš J, (2007) Dark production of reactive oxygen species in photosystem II membrane particles at elevated temperature: EPR spin-trapping study. Biochim Biophys Acta 1767: 854-859.
    • (2007) Biochim Biophys Acta , vol.1767 , pp. 854-859
    • Pospíšil, P.1    Šnyrychova, S.2    Nauš, J.3
  • 38
    • 57649114596 scopus 로고    scopus 로고
    • Quality control of Photosystem II: reactive oxygen species are responsible for the damage to Photosystem II under moderate heat stress
    • Yamashita A, Nijo N, Pospíšil P, Morita N, Takenaka D, et al. (2008) Quality control of Photosystem II: reactive oxygen species are responsible for the damage to Photosystem II under moderate heat stress. J Biol Chem 283: 28380-28391.
    • (2008) J Biol Chem , vol.283 , pp. 28380-28391
    • Yamashita, A.1    Nijo, N.2    Pospíšil, P.3    Morita, N.4    Takenaka, D.5
  • 39
    • 13944284179 scopus 로고    scopus 로고
    • Singlet oxygen production in photosynthesis
    • Krieger-Liszkay A, (2005) Singlet oxygen production in photosynthesis. J Exp Bot 56: 337-346.
    • (2005) J Exp Bot , vol.56 , pp. 337-346
    • Krieger-Liszkay, A.1
  • 40
    • 0034033915 scopus 로고    scopus 로고
    • Identification of peptide oxidation by tandem mass spectrometry
    • Schey KL, Finley EL, (2000) Identification of peptide oxidation by tandem mass spectrometry. Acc Chem Res 33: 299-306.
    • (2000) Acc Chem Res , vol.33 , pp. 299-306
    • Schey, K.L.1    Finley, E.L.2
  • 41
    • 33749522859 scopus 로고    scopus 로고
    • Mass spectrometry of protein modifications by reactive oxygen and nitrogen species
    • Schöneich C, Sharov VS, (2006) Mass spectrometry of protein modifications by reactive oxygen and nitrogen species. Free Rad Biol Med 41: 1507-1520.
    • (2006) Free Rad Biol Med , vol.41 , pp. 1507-1520
    • Schöneich, C.1    Sharov, V.S.2
  • 42
    • 0027331576 scopus 로고
    • Turnover of the Photosystem II D1 protein in higher plants under photoinhibitory and nonphotoinhibitory irradiance
    • Sundby C, McCaffery S, Anderson JM, (1993) Turnover of the Photosystem II D1 protein in higher plants under photoinhibitory and nonphotoinhibitory irradiance. J Biol Chem 268: 25476-25482.
    • (1993) J Biol Chem , vol.268 , pp. 25476-25482
    • Sundby, C.1    McCaffery, S.2    Anderson, J.M.3
  • 43
    • 0000075484 scopus 로고
    • A highly resolved oxygen-evolving Photosystem II preparation from spinach thylakoid membranes
    • Berthold DA, Babcock GT, Yocum CF, (1981) A highly resolved oxygen-evolving Photosystem II preparation from spinach thylakoid membranes. FEBS Lett 134: 231-234.
    • (1981) FEBS Lett , vol.134 , pp. 231-234
    • Berthold, D.A.1    Babcock, G.T.2    Yocum, C.F.3
  • 44
    • 0020563680 scopus 로고
    • Hydroxylamine as an inhibitor between Z and P680 in Photosystem II
    • Ghanotakis DF, Babcock GT, (1983) Hydroxylamine as an inhibitor between Z and P680 in Photosystem II. FEBS Lett 153: 231-234.
    • (1983) FEBS Lett , vol.153 , pp. 231-234
    • Ghanotakis, D.F.1    Babcock, G.T.2
  • 45
    • 0000995767 scopus 로고
    • Lithium dodecyl sulfate/polyacrylamide gel electrophoresis of thylakoid membranes at 4°C: Characterizations of two additional chlorophyll a-protein complexes
    • Delepelaire P, Chua N, (1979) Lithium dodecyl sulfate/polyacrylamide gel electrophoresis of thylakoid membranes at 4°C: Characterizations of two additional chlorophyll a-protein complexes. Proc Natl Acad Sci (USA) 76: 111-115.
    • (1979) Proc Natl Acad Sci (USA) , vol.76 , pp. 111-115
    • Delepelaire, P.1    Chua, N.2
  • 46
    • 0029078506 scopus 로고
    • Micropreparative one- and two-dimensional electrophoresis: Improvement with new photopolymerization systems
    • Rabilloud T, Vincon M, Garin J, (1995) Micropreparative one- and two-dimensional electrophoresis: Improvement with new photopolymerization systems. Electrophoresis 16: 1414-1422.
    • (1995) Electrophoresis , vol.16 , pp. 1414-1422
    • Rabilloud, T.1    Vincon, M.2    Garin, J.3
  • 47
    • 2342613564 scopus 로고    scopus 로고
    • Prevention of artifactual protein oxidation generated during sodium dodecyl sulfate-gel electrophoresis
    • Sun G, Anderson VE, (2004) Prevention of artifactual protein oxidation generated during sodium dodecyl sulfate-gel electrophoresis. Electrophoresis 25: 959-965.
    • (2004) Electrophoresis , vol.25 , pp. 959-965
    • Sun, G.1    Anderson, V.E.2
  • 48
    • 34249094851 scopus 로고    scopus 로고
    • A mass accuracy sensitive probability based scoring algorithm for database searching of tandem mass spectrometry data
    • Xu H, Freitas MA, (2007) A mass accuracy sensitive probability based scoring algorithm for database searching of tandem mass spectrometry data. BMC Bioinform 8: 133-137.
    • (2007) BMC Bioinform , vol.8 , pp. 133-137
    • Xu, H.1    Freitas, M.A.2
  • 49
    • 63049105321 scopus 로고    scopus 로고
    • MassMatrix: A database search program for rapid characterization of proteins and peptides from tandem mass spectrometry data
    • Xu H, Freitas MA, (2009) MassMatrix: A database search program for rapid characterization of proteins and peptides from tandem mass spectrometry data. Proteomics 9: 1548-1555.
    • (2009) Proteomics , vol.9 , pp. 1548-1555
    • Xu, H.1    Freitas, M.A.2
  • 50
    • 33745041235 scopus 로고    scopus 로고
    • Radiolytic protein footprinting with mass spectrometry to probe the structure of macromolecular complexes
    • Takamoto K, Chance MR, (2006) Radiolytic protein footprinting with mass spectrometry to probe the structure of macromolecular complexes. Ann Rev Biophys Biomol Struct 35: 251-276.
    • (2006) Ann Rev Biophys Biomol Struct , vol.35 , pp. 251-276
    • Takamoto, K.1    Chance, M.R.2
  • 51
    • 34547640455 scopus 로고    scopus 로고
    • Mass spectrometry-based approaches for structural studies on protein complexes at low-resolution
    • Renzone G, Salzano AM, Arena S, D'Ambrosio C, Scaloni A, (2007) Mass spectrometry-based approaches for structural studies on protein complexes at low-resolution. Curr Proteom 4: 1-16.
    • (2007) Curr Proteom , vol.4 , pp. 1-16
    • Renzone, G.1    Salzano, A.M.2    Arena, S.3    D'Ambrosio, C.4    Scaloni, A.5
  • 52
    • 24044513966 scopus 로고    scopus 로고
    • Comparative evaluation of mass spectrometry platforms used in large-scale proteomics investigations
    • Elias JE, Haas W, Faherty BK, Gygi SP, (2005) Comparative evaluation of mass spectrometry platforms used in large-scale proteomics investigations. Nat Meth 2: 667-675.
    • (2005) Nat Meth , vol.2 , pp. 667-675
    • Elias, J.E.1    Haas, W.2    Faherty, B.K.3    Gygi, S.P.4
  • 53
    • 84874561398 scopus 로고    scopus 로고
    • Software The PyMOL Molecular Graphics System, Version 1.4 Schrödinger, LLC
    • Software The PyMOL Molecular Graphics System, Version 1.4 Schrödinger, LLC.


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