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Volumn 7, Issue 6, 2012, Pages

On the structure and function of the phytoene desaturase CRTI from pantoea ananatis, a membrane-peripheral and FAD-dependent oxidase/isomerase

Author keywords

[No Author keywords available]

Indexed keywords

AMINE OXIDASE (FLAVIN CONTAINING); CAROTENE ISOMERASE; FLAVINE ADENINE NUCLEOTIDE; ISOMERASE; OXIDOREDUCTASE; OXYGEN; PHOSPHATIDYLCHOLINE; PROTEIN CRTI; PROTOPORPHYRINOGEN OXIDASE; QUINONE DERIVATIVE; UNCLASSIFIED DRUG;

EID: 84862667142     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0039550     Document Type: Article
Times cited : (76)

References (60)
  • 2
    • 84858301666 scopus 로고    scopus 로고
    • The path from β-carotene to carlactone, a strigolactone-like plant hormone
    • Alder A, Jamil M, Marzorati M, Bruno M, Vermathen M, et al. (2012) The path from β-carotene to carlactone, a strigolactone-like plant hormone. Science 16 335(6074): 1348-51.
    • (2012) Science , vol.16 , Issue.6074 , pp. 1348-1351
    • Alder, A.1    Jamil, M.2    Marzorati, M.3    Bruno, M.4    Vermathen, M.5
  • 3
    • 77955642541 scopus 로고    scopus 로고
    • Colors with functions: elucidating the biochemical and molecular basis of carotenoid metabolism
    • von Lintig, J (2010) Colors with functions: elucidating the biochemical and molecular basis of carotenoid metabolism. Annu. Rev. Nutr. 30: 35-56.
    • (2010) Annu. Rev. Nutr , vol.30 , pp. 35-56
    • von Lintig, J.1
  • 4
    • 1542315589 scopus 로고    scopus 로고
    • The biosynthesis and nutritional uses of carotenoids
    • Fraser PD, Bramley PM, (2004) The biosynthesis and nutritional uses of carotenoids. Prog. Lipid Res. 43: 228-265.
    • (2004) Prog. Lipid Res , vol.43 , pp. 228-265
    • Fraser, P.D.1    Bramley, P.M.2
  • 5
    • 0024728612 scopus 로고
    • Molecular oxygen and the state of geometric isomerism of intermediates are essential in the carotene desaturation and cyclization reactions in daffodil chromoplasts
    • Beyer P, Mayer M, Kleinig H, (1989) Molecular oxygen and the state of geometric isomerism of intermediates are essential in the carotene desaturation and cyclization reactions in daffodil chromoplasts. Eur. J. Biochem. 184: 141-150.
    • (1989) Eur. J. Biochem , vol.184 , pp. 141-150
    • Beyer, P.1    Mayer, M.2    Kleinig, H.3
  • 6
    • 0033555264 scopus 로고    scopus 로고
    • Two Arabidopsis thaliana carotene desaturases, phytoene desaturase and zeta-carotene desaturase, expressed in Escherichia coli, catalyze a poly-cis pathway to yield pro-lycopene
    • Bartley GE, Scolnik PA, Beyer P, (1999) Two Arabidopsis thaliana carotene desaturases, phytoene desaturase and zeta-carotene desaturase, expressed in Escherichia coli, catalyze a poly-cis pathway to yield pro-lycopene. Eur. J. Biochem. 259: 396-403.
    • (1999) Eur. J. Biochem , vol.259 , pp. 396-403
    • Bartley, G.E.1    Scolnik, P.A.2    Beyer, P.3
  • 7
    • 34250791177 scopus 로고    scopus 로고
    • Maize Y9 encodes a product essential for 15-cis-zeta-carotene isomerization
    • Li F, Murillo C, Wurtzel ET, (2007) Maize Y9 encodes a product essential for 15-cis-zeta-carotene isomerization. Plant Physiol. 144: 1181-1189.
    • (2007) Plant Physiol , vol.144 , pp. 1181-1189
    • Li, F.1    Murillo, C.2    Wurtzel, E.T.3
  • 8
    • 77952005971 scopus 로고    scopus 로고
    • Isolation and characterization of the Z-ISO gene encoding a missing component of carotenoid biosynthesis in plants
    • Chen Y, Li F, Wurtzel ET, (2010) Isolation and characterization of the Z-ISO gene encoding a missing component of carotenoid biosynthesis in plants. Plant Physiol. 153: 66-79.
    • (2010) Plant Physiol , vol.153 , pp. 66-79
    • Chen, Y.1    Li, F.2    Wurtzel, E.T.3
  • 9
    • 0036009770 scopus 로고    scopus 로고
    • Cloning of tangerine from tomato reveals a carotenoid isomerase essential for the production of β -carotene and xanthophylls in plants
    • Isaacson T, Ronen G, Zamir D, Hirschberg J, (2002) Cloning of tangerine from tomato reveals a carotenoid isomerase essential for the production of β-carotene and xanthophylls in plants. Plant Cell 14: 333-342.
    • (2002) Plant Cell , vol.14 , pp. 333-342
    • Isaacson, T.1    Ronen, G.2    Zamir, D.3    Hirschberg, J.4
  • 10
    • 0036009771 scopus 로고    scopus 로고
    • Identification of the carotenoid isomerase provides insight into carotenoid biosynthesis, prolamellar body formation, and photomorphogenesis
    • Park H, Kreunen SS, Cuttriss AJ, Dellapenna D, Pogson BJ, (2002) Identification of the carotenoid isomerase provides insight into carotenoid biosynthesis, prolamellar body formation, and photomorphogenesis. Plant Cell 14: 321-332.
    • (2002) Plant Cell , vol.14 , pp. 321-332
    • Park, H.1    Kreunen, S.S.2    Cuttriss, A.J.3    Dellapenna, D.4    Pogson, B.J.5
  • 11
    • 79953136756 scopus 로고    scopus 로고
    • Plant carotene cis-trans isomerase CRTISO: a new member of the FADred-dependent flavoproteins catalyzing non-redox reactions
    • Yu Q, Ghisla S, Hirschberg J, Mann V, Beyer P, (2011) Plant carotene cis-trans isomerase CRTISO: a new member of the FADred-dependent flavoproteins catalyzing non-redox reactions. J. Biol. Chem. 286: 8666-8676.
    • (2011) J. Biol. Chem , vol.286 , pp. 8666-8676
    • Yu, Q.1    Ghisla, S.2    Hirschberg, J.3    Mann, V.4    Beyer, P.5
  • 12
    • 0025325851 scopus 로고
    • Quinone compounds are able to replace molecular oxygen as terminal electron acceptor in phytoene desaturation in chromoplasts of Narcissus pseudonarcissus L
    • Mayer MP, Beyer P, Kleinig H, (1990) Quinone compounds are able to replace molecular oxygen as terminal electron acceptor in phytoene desaturation in chromoplasts of Narcissus pseudonarcissus L. Eur. J. Biochem. 191: 359-363.
    • (1990) Eur. J. Biochem , vol.191 , pp. 359-363
    • Mayer, M.P.1    Beyer, P.2    Kleinig, H.3
  • 13
    • 0029556712 scopus 로고
    • Genetic dissection of carotenoid synthesis in Arabidopsis defines plastoquinone as an essential component of phytoene desaturation
    • Norris SR, Barrette TR, DellaPenna D, (1995) Genetic dissection of carotenoid synthesis in Arabidopsis defines plastoquinone as an essential component of phytoene desaturation. Plant Cell 7: 2139-2149.
    • (1995) Plant Cell , vol.7 , pp. 2139-2149
    • Norris, S.R.1    Barrette, T.R.2    DellaPenna, D.3
  • 14
    • 0035211544 scopus 로고    scopus 로고
    • A plastid terminal oxidase comes to light: implications for carotenoid biosynthesis and chlororespiration
    • Carol P, Kuntz M, (2001) A plastid terminal oxidase comes to light: implications for carotenoid biosynthesis and chlororespiration.Trends Plant Sci. 6: 31-36.
    • (2001) Trends Plant Sci , vol.6 , pp. 31-36
    • Carol, P.1    Kuntz, M.2
  • 16
    • 62349132057 scopus 로고    scopus 로고
    • Evolution of carotene desaturation: the complication of a simple pathway
    • Sandmann G, (2009) Evolution of carotene desaturation: the complication of a simple pathway. Arch. Biochem.Biophys. 483: 169-174.
    • (2009) Arch. Biochem.Biophys , vol.483 , pp. 169-174
    • Sandmann, G.1
  • 17
    • 0033983338 scopus 로고    scopus 로고
    • Engineering the provitamin A (beta-carotene) biosynthetic pathway into (carotenoid-free) rice endosperm
    • Ye X, Al-Babili S, Klöti A, Zhang J, Lucca P, et al. (2000) Engineering the provitamin A (beta-carotene) biosynthetic pathway into (carotenoid-free) rice endosperm. Science 287: 303-305.
    • (2000) Science , vol.287 , pp. 303-305
    • Ye, X.1    Al-Babili, S.2    Klöti, A.3    Zhang, J.4    Lucca, P.5
  • 18
    • 23644440517 scopus 로고    scopus 로고
    • Improving the nutritional value of Golden Rice through increased pro-vitamin A content
    • Paine JA, Shipton CA, Chaggar S, Howells RM, Kennedy MJ, et al. (2005) Improving the nutritional value of Golden Rice through increased pro-vitamin A content. Nat. Biotechno. 23: 482-487.
    • (2005) Nat. Biotechno , vol.23 , pp. 482-487
    • Paine, J.A.1    Shipton, C.A.2    Chaggar, S.3    Howells, R.M.4    Kennedy, M.J.5
  • 19
    • 57449119110 scopus 로고    scopus 로고
    • Combinatorial genetic transformation generates a library of metabolic phenotypes for the carotenoid pathway in maize
    • Zhu C, Naqvia S, Breitenbach J, Sandmann G, Christou P, et al. (2008) Combinatorial genetic transformation generates a library of metabolic phenotypes for the carotenoid pathway in maize. Proc. Natl. Acad. Sci. USA 105: 18232-18237.
    • (2008) Proc. Natl. Acad. Sci USA , vol.105 , pp. 18232-18237
    • Zhu, C.1    Naqvia, S.2    Breitenbach, J.3    Sandmann, G.4    Christou, P.5
  • 21
    • 34548415299 scopus 로고    scopus 로고
    • Metabolic engineering of potato carotenoid content through tuber-specific overexpression of a bacterial mini-pathway
    • Diretto G, Al-Babili S, Tavazza R, Papacchioli V, Beyer P, et al. (2007) Metabolic engineering of potato carotenoid content through tuber-specific overexpression of a bacterial mini-pathway. PLoS ONE 4, e350.
    • (2007) PLoS ONE , vol.4
    • Diretto, G.1    Al-Babili, S.2    Tavazza, R.3    Papacchioli, V.4    Beyer, P.5
  • 22
    • 0027689316 scopus 로고
    • Functional expression of the Erwinia uredovora carotenoid biosynthesis gene crtI in transgenic plants showing an increase of β-carotene biosynthesis
    • Misawa N, Yamano S, Linden H, de Felipe MR, Lucas M, et al. (1993) Functional expression of the Erwinia uredovora carotenoid biosynthesis gene crtI in transgenic plants showing an increase of β-carotene biosynthesis. Plant J. 4: 833-840.
    • (1993) Plant J , vol.4 , pp. 833-840
    • Misawa, N.1    Yamano, S.2    Linden, H.3    de Felipe, M.R.4    Lucas, M.5
  • 23
    • 20444384767 scopus 로고    scopus 로고
    • Carotenoids as modulators of lipid membrane physical properties
    • Gruszecki WI, Strzałka K, (2005) Carotenoids as modulators of lipid membrane physical properties. Biochim. Biophys. Acta 1740: 108-115.
    • (2005) Biochim. Biophys. Acta , vol.1740 , pp. 108-115
    • Gruszecki, W.I.1    Strzałka, K.2
  • 24
    • 77951240773 scopus 로고    scopus 로고
    • The lycopene cyclase CrtY from Pantoea ananatis (formerly Erwinia uredovora) catalyzes an FADred-dependent non-redox reaction
    • Yu Q, Schaub P, Ghisla S, Al-Babili S, Krieger-Liszkay A, et al. (2010) The lycopene cyclase CrtY from Pantoea ananatis (formerly Erwinia uredovora) catalyzes an FADred-dependent non-redox reaction. J. Biol. Chem. 285: 12109-12120.
    • (2010) J. Biol. Chem , vol.285 , pp. 12109-12120
    • Yu, Q.1    Schaub, P.2    Ghisla, S.3    Al-Babili, S.4    Krieger-Liszkay, A.5
  • 25
    • 0017366794 scopus 로고
    • One-and two-electron redox chemistry of 1-carba-1-deazariboflavin
    • Spencer R, Fisher J, Walsh C, (1977) One-and two-electron redox chemistry of 1-carba-1-deazariboflavin. Biochemistry 16: 3586-3594.
    • (1977) Biochemistry , vol.16 , pp. 3586-3594
    • Spencer, R.1    Fisher, J.2    Walsh, C.3
  • 26
    • 77954288774 scopus 로고    scopus 로고
    • Dali server: conservation mapping in 3D
    • Holm L, Rosenström P, (2010) Dali server: conservation mapping in 3D. Nucl. Acids Res. 38: W545-W549.
    • (2010) Nucl. Acids Res , vol.38
    • Holm, L.1    Rosenström, P.2
  • 27
    • 33846013952 scopus 로고    scopus 로고
    • Crystal structure of protoporphyrinogen oxidase from Myxococcus xanthus and its complex with the inhibitor acifluorfen
    • Corradi HR, Corrigall AV, Boix E, Mohan CG, Sturrock ED, et al. (2006) Crystal structure of protoporphyrinogen oxidase from Myxococcus xanthus and its complex with the inhibitor acifluorfen. J. Biol. Chem. 281: 38625-38633.
    • (2006) J. Biol. Chem , vol.281 , pp. 38625-38633
    • Corradi, H.R.1    Corrigall, A.V.2    Boix, E.3    Mohan, C.G.4    Sturrock, E.D.5
  • 28
    • 2442563409 scopus 로고    scopus 로고
    • Crystal structure of protoporphyrinogen IX oxidase: a key enzyme in haem and chlorophyll biosynthesis
    • Koch M, Breithaupt C, Kiefersauer R, Freigang J, Huber R, et al. (2004) Crystal structure of protoporphyrinogen IX oxidase: a key enzyme in haem and chlorophyll biosynthesis. EMBO J. 23: 1720-1728.
    • (2004) EMBO J , vol.23 , pp. 1720-1728
    • Koch, M.1    Breithaupt, C.2    Kiefersauer, R.3    Freigang, J.4    Huber, R.5
  • 29
    • 77950518147 scopus 로고    scopus 로고
    • Structural insight into unique properties of protoporphyrinogen oxidase from Bacillus subtilis
    • Qin X, Sun L, Wen X, Yang X, Tan Y, et al. (2010) Structural insight into unique properties of protoporphyrinogen oxidase from Bacillus subtilis. J. Struct. Biol. 170: 76-82.
    • (2010) J. Struct. Biol , vol.170 , pp. 76-82
    • Qin, X.1    Sun, L.2    Wen, X.3    Yang, X.4    Tan, Y.5
  • 30
    • 33847013408 scopus 로고    scopus 로고
    • The structure of a bacterial L-amino acid oxidase from Rhodococcus opacus gives new evidence for the hydride mechanism for dehydrogenation
    • Faust A, Niefind K, Hummel W, Schomburg D, (2007) The structure of a bacterial L-amino acid oxidase from Rhodococcus opacus gives new evidence for the hydride mechanism for dehydrogenation. J. Mol. Biol. 367: 234-248.
    • (2007) J. Mol. Biol , vol.367 , pp. 234-248
    • Faust, A.1    Niefind, K.2    Hummel, W.3    Schomburg, D.4
  • 31
    • 0028103275 scopus 로고
    • Acta Crystallogr
    • Collaborative computational project number 4 D 50, 760-763
    • Collaborative computational project number 4 (1994) Acta Crystallogr. D 50, 760-763.
    • (1994)
  • 32
    • 0026705643 scopus 로고
    • Expression in Escherichia coli, purification, and reactivation of the recombinant Erwinia uredovora phytoene desaturase
    • Fraser PD, Misawa N, Linden H, Yamano S, Kobayashi K, et al. (1992) Expression in Escherichia coli, purification, and reactivation of the recombinant Erwinia uredovora phytoene desaturase. J. Biol. Chem. 267: 19891-19895.
    • (1992) J. Biol. Chem , vol.267 , pp. 19891-19895
    • Fraser, P.D.1    Misawa, N.2    Linden, H.3    Yamano, S.4    Kobayashi, K.5
  • 33
    • 0032577574 scopus 로고    scopus 로고
    • Identification of an FAD superfamily containing protoporphyrinogen oxidases, monoamine oxidases, and phytoene desaturase. Expression and characterization of phytoene desaturase of Myxococcus xanthus
    • Dailey TA, Dailey HA, (1998) Identification of an FAD superfamily containing protoporphyrinogen oxidases, monoamine oxidases, and phytoene desaturase. Expression and characterization of phytoene desaturase of Myxococcus xanthus. J. Biol. Chem. 273: 13658-13662.
    • (1998) J. Biol. Chem , vol.273 , pp. 13658-13662
    • Dailey, T.A.1    Dailey, H.A.2
  • 34
    • 0030138514 scopus 로고    scopus 로고
    • A novel, soluble form of phytoene desaturase from Narcissus pseudonarcissus chromoplasts is Hsp70-complexed and competent for flavinylation, membrane association and enzymatic activation
    • Al-Babili S, Lintig J von, Haubruck H, Beyer P, (1996) A novel, soluble form of phytoene desaturase from Narcissus pseudonarcissus chromoplasts is Hsp70-complexed and competent for flavinylation, membrane association and enzymatic activation. Plant J. 9: 601-612.
    • (1996) Plant J , vol.9 , pp. 601-612
    • Al-Babili, S.1    von Lintig, J.2    Haubruck, H.3    Beyer, P.4
  • 35
    • 0030849191 scopus 로고    scopus 로고
    • Chloroplast import of four carotenoid biosynthetic enzymes in vitro reveals differential fates prior to membrane binding and oligomeric assembly
    • Bonk M, Hoffmann B, von Lintig J, Schledz M, Al-Babili S, et al. (1997) Chloroplast import of four carotenoid biosynthetic enzymes in vitro reveals differential fates prior to membrane binding and oligomeric assembly. Eur. J. Biochem. 247: 942-950.
    • (1997) Eur. J. Biochem , vol.247 , pp. 942-950
    • Bonk, M.1    Hoffmann, B.2    von Lintig, J.3    Schledz, M.4    Al-Babili, S.5
  • 36
    • 0030194514 scopus 로고    scopus 로고
    • Purification and characterization of chaperonin 60 and heat-shock protein 70 from chromoplasts of Narcissus pseudonarcissus
    • Bonk M, Tadros M, Vandekerckhove J, Al-Babili S, Beyer P, (1996) Purification and characterization of chaperonin 60 and heat-shock protein 70 from chromoplasts of Narcissus pseudonarcissus. Plant Physiol. 111: 931-939.
    • (1996) Plant Physiol , vol.111 , pp. 931-939
    • Bonk, M.1    Tadros, M.2    Vandekerckhove, J.3    Al-Babili, S.4    Beyer, P.5
  • 37
    • 0346035943 scopus 로고    scopus 로고
    • Chemiosmotic ATP synthesis in photosynthetically inactive chromoplasts from Narcissus pseudonarcissus L. linked to a redox pathway potentially also involved in carotene desaturation
    • Morstadt L, Gräber P, Pascalis LDe, Kleinig H, Speth V, et al. (2002) Chemiosmotic ATP synthesis in photosynthetically inactive chromoplasts from Narcissus pseudonarcissus L. linked to a redox pathway potentially also involved in carotene desaturation. Planta 215: 134-140.
    • (2002) Planta , vol.215 , pp. 134-140
    • Morstadt, L.1    Gräber, P.2    de Pascalis, L.3    Kleinig, H.4    Speth, V.5
  • 38
    • 78649769205 scopus 로고    scopus 로고
    • Structural and kinetics properties of a mutated phytoene desaturase from Rubrivivax gelatinosus with modified product specificity
    • Stickforth P, Sandmann G, (2011) Structural and kinetics properties of a mutated phytoene desaturase from Rubrivivax gelatinosus with modified product specificity. Arch. Biochem. Biophys. 505: 118-122.
    • (2011) Arch. Biochem. Biophys , vol.505 , pp. 118-122
    • Stickforth, P.1    Sandmann, G.2
  • 39
  • 40
    • 69949178284 scopus 로고    scopus 로고
    • A structural basis for the pH-dependent xanthophyll cycle in Arabidopsis thaliana
    • Arnoux P, Morosinotto T, Saga G, Bassi R, Pignol D, (2009) A structural basis for the pH-dependent xanthophyll cycle in Arabidopsis thaliana. Plant Cell 21: 2036-2044.
    • (2009) Plant Cell , vol.21 , pp. 2036-2044
    • Arnoux, P.1    Morosinotto, T.2    Saga, G.3    Bassi, R.4    Pignol, D.5
  • 41
    • 77954888720 scopus 로고    scopus 로고
    • Mutation analysis of violaxanthin de-epoxidase identifies substrate-binding sites and residues involved in catalysis
    • Saga G, Giorgetti A, Fufezan C, Giacometti GM, Bassi R, Morosinotto T, (2010) Mutation analysis of violaxanthin de-epoxidase identifies substrate-binding sites and residues involved in catalysis. J. Biol. Chem. 285: 23763-23770.
    • (2010) J. Biol. Chem , vol.285 , pp. 23763-23770
    • Saga, G.1    Giorgetti, A.2    Fufezan, C.3    Giacometti, G.M.4    Bassi, R.5    Morosinotto, T.6
  • 42
    • 0842330598 scopus 로고    scopus 로고
    • Acyl-CoA dehydrogenases. A mechanistic overview
    • Ghisla S, Thorpe C, (2004) Acyl-CoA dehydrogenases. A mechanistic overview. Eur. J. Biochem. 271: 494-508.
    • (2004) Eur. J. Biochem , vol.271 , pp. 494-508
    • Ghisla, S.1    Thorpe, C.2
  • 43
    • 0842265784 scopus 로고    scopus 로고
    • Acyl-CoA dehydrogenases and acyl-CoA oxidases. Structural basis for mechanistic similarities and differences
    • Kim JJP, Miura R, (2004) Acyl-CoA dehydrogenases and acyl-CoA oxidases. Structural basis for mechanistic similarities and differences. Eur. J. Biochem. 271: 483-493.
    • (2004) Eur. J. Biochem , vol.271 , pp. 483-493
    • Kim, J.J.P.1    Miura, R.2
  • 44
    • 0035881923 scopus 로고    scopus 로고
    • Thioester Enolate Stabilization in the Acyl-CoA Dehydrogenases?: The effect of 5-deaza-flavin substitution
    • Rudik I, Thorpe C, (2001) Thioester Enolate Stabilization in the Acyl-CoA Dehydrogenases?: The effect of 5-deaza-flavin substitution. Arch. Biochem. Biophys. 392: 341-348.
    • (2001) Arch. Biochem. Biophys , vol.392 , pp. 341-348
    • Rudik, I.1    Thorpe, C.2
  • 45
    • 34248559599 scopus 로고    scopus 로고
    • Gene splicing and mutagenesis by PCR-driven overlap extension
    • Heckman KL, Pease LR, (2007) Gene splicing and mutagenesis by PCR-driven overlap extension. Nat. Protoc. 2: 924-932.
    • (2007) Nat. Protoc , vol.2 , pp. 924-932
    • Heckman, K.L.1    Pease, L.R.2
  • 46
    • 33847290484 scopus 로고    scopus 로고
    • Production of selenomethionyl proteins in prokaryotic and eukaryotic expression systems
    • Doublié S, (2007) Production of selenomethionyl proteins in prokaryotic and eukaryotic expression systems. Meth. Mol. Bio. 363: 91-108.
    • (2007) Meth. Mol. Bio , vol.363 , pp. 91-108
    • Doublié, S.1
  • 47
    • 0019082041 scopus 로고
    • Unilamellar liposomes made with the French Pressure Cell: a simple preparative and semiquantitative technique
    • Hamilton R L, Goerke J, Guo LS, Williams MC, Havel RJ, (1980) Unilamellar liposomes made with the French Pressure Cell: a simple preparative and semiquantitative technique. J. Lipid Res. 21: 981-992.
    • (1980) J. Lipid Res , vol.21 , pp. 981-992
    • Hamilton R, L.1    Goerke, J.2    Guo, L.S.3    Williams, M.C.4    Havel, R.J.5
  • 48
    • 84987505467 scopus 로고
    • Synthesis, isolation and NMR-spectroscopic characterization of fourteen (Z)-isomers of lycopene and some acetylenic didehydro- and tetradehydrolycopenes
    • Hengartner U, Bernhard K, Meyer K, Englert G, Glinz E, (1992) Synthesis, isolation and NMR-spectroscopic characterization of fourteen (Z)-isomers of lycopene and some acetylenic didehydro- and tetradehydrolycopenes. Helv. Chim. Acta 75: 1848-1865.
    • (1992) Helv. Chim. Acta , vol.75 , pp. 1848-1865
    • Hengartner, U.1    Bernhard, K.2    Meyer, K.3    Englert, G.4    Glinz, E.5
  • 49
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski Z, Minor W, (1997) Processing of X-ray diffraction data collected in oscillation mode. Meth. Enzymol. 276: 307-326.
    • (1997) Meth. Enzymol , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 50
    • 0242460576 scopus 로고    scopus 로고
    • Generation, representation and flow of phase information in structure determination: recent developments in and around SHARP 2.0
    • Bricogne G, Vonrhein C, Flensburg C, Schiltz M, Paciorek W, (2003) Generation, representation and flow of phase information in structure determination: recent developments in and around SHARP 2.0. Acta Crystallogr. D 59: 2023-2030.
    • (2003) Acta Crystallogr. D , vol.59 , pp. 2023-2030
    • Bricogne, G.1    Vonrhein, C.2    Flensburg, C.3    Schiltz, M.4    Paciorek, W.5
  • 51
    • 0030038464 scopus 로고    scopus 로고
    • Methods used in the structure determination of bovine mitochondrial F1 ATPase
    • Abrahams JP, Leslie AG, (1996) Methods used in the structure determination of bovine mitochondrial F1 ATPase. Acta Crystallogr. D 52: 30-42.
    • (1996) Acta Crystallogr D , vol.52 , pp. 30-42
    • Abrahams, J.P.1    Leslie, A.G.2
  • 52
    • 33748337934 scopus 로고    scopus 로고
    • The Buccaneer software for automated model building. 1. Tracing protein chains
    • Cowtan K, (2006) The Buccaneer software for automated model building. 1. Tracing protein chains. Acta Crystallogr. D 62: 1002-1011.
    • (2006) Acta Crystallogr D , vol.62 , pp. 1002-1011
    • Cowtan, K.1
  • 54
    • 0030924992 scopus 로고    scopus 로고
    • Refinement of macromolecular structures by the maximum-likelihood method
    • Murshudov GN, Vagin AA, Dodson EJ, (1997) Refinement of macromolecular structures by the maximum-likelihood method. Acta Crystallogr. D 53: 240-255.
    • (1997) Acta Crystallogr D , vol.53 , pp. 240-255
    • Murshudov, G.N.1    Vagin, A.A.2    Dodson, E.J.3
  • 56
    • 76449098262 scopus 로고    scopus 로고
    • PHENIX: a comprehensive Python-based system for macromolecular structure solution
    • Adams PD, Afonine PV, Bunkóczi G, Chen VB, Davis IW, et al. (2010) PHENIX: a comprehensive Python-based system for macromolecular structure solution. Acta Crystallogr. D 66: 213-221.
    • (2010) Acta Crystallogr D , vol.66 , pp. 213-221
    • Adams, P.D.1    Afonine, P.V.2    Bunkóczi, G.3    Chen, V.B.4    Davis, I.W.5
  • 57
    • 74549178560 scopus 로고    scopus 로고
    • MolProbity?: all-atom structure validation for macromolecular crystallography research papers
    • Chen VB, Arendall WB, Headd JJ, Keedy DA, Immormino RM, et al. (2010) MolProbity?: all-atom structure validation for macromolecular crystallography research papers. Acta Crystallogr. D 66: 12-21.
    • (2010) Acta Crystallogr. D , vol.66 , pp. 12-21
    • Chen, V.B.1    Arendall, W.B.2    Headd, J.J.3    Keedy, D.A.4    Immormino, R.M.5
  • 58
  • 59
    • 11644261806 scopus 로고    scopus 로고
    • Automated docking using a Lamarckian genetic algorithm and an empirical binding free energy function
    • Morris GM, Goodsell DS, Halliday RS, Huey R, Hart WE, et al. (1998) Automated docking using a Lamarckian genetic algorithm and an empirical binding free energy function. J. Comput. Chem. 19: 1639-1662.
    • (1998) J. Comput. Chem , vol.19 , pp. 1639-1662
    • Morris, G.M.1    Goodsell, D.S.2    Halliday, R.S.3    Huey, R.4    Hart, W.E.5
  • 60
    • 0033625531 scopus 로고    scopus 로고
    • TEXshade: shading and labeling multiple sequence alignments using LATEX2ε
    • Beitz E, (2000) TEXshade: shading and labeling multiple sequence alignments using LATEX2ε. Bioinformatics 16: 135-139.
    • (2000) Bioinformatics , vol.16 , pp. 135-139
    • Beitz, E.1


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