메뉴 건너뛰기




Volumn 55, Issue 44, 2016, Pages 6175-6186

Crystal Structure of Os79 (Os04g0206600) from Oryza sativa: A UDP-glucosyltransferase Involved in the Detoxification of Deoxynivalenol

Author keywords

[No Author keywords available]

Indexed keywords

CATALYSIS; CROPS; DETOXIFICATION; ENZYME ACTIVITY; FUNGI; GLUCOSE; QUANTUM CHEMISTRY; SUBSTRATES; TOXICITY;

EID: 84994741721     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/acs.biochem.6b00709     Document Type: Article
Times cited : (53)

References (55)
  • 2
    • 84926196159 scopus 로고    scopus 로고
    • Biogeography of Fusarium graminearum species complex and chemotypes: A review
    • van der Lee, T., Zhang, H., van Diepeningen, A., and Waalwijk, C. (2015) Biogeography of Fusarium graminearum species complex and chemotypes: a review Food Addit. Contam., Part A 32, 453-460 10.1080/19440049.2014.984244
    • (2015) Food Addit. Contam., Part A , vol.32 , pp. 453-460
    • Van Der Lee, T.1    Zhang, H.2    Van Diepeningen, A.3    Waalwijk, C.4
  • 3
    • 0002617428 scopus 로고
    • Mechanism of inhibition of eukaryotic protein synthesis by trichothecene fungal toxins
    • Cundliffe, E., Cannon, M., and Davies, J. (1974) Mechanism of inhibition of eukaryotic protein synthesis by trichothecene fungal toxins Proc. Natl. Acad. Sci. U. S. A. 71, 30-34 10.1073/pnas.71.1.30
    • (1974) Proc. Natl. Acad. Sci. U. S. A. , vol.71 , pp. 30-34
    • Cundliffe, E.1    Cannon, M.2    Davies, J.3
  • 4
    • 77957802278 scopus 로고    scopus 로고
    • Deoxynivalenol: Mechanisms of action, human exposure, and toxicological relevance
    • Pestka, J. J. (2010) Deoxynivalenol: mechanisms of action, human exposure, and toxicological relevance Arch. Toxicol. 84, 663-679 10.1007/s00204-010-0579-8
    • (2010) Arch. Toxicol. , vol.84 , pp. 663-679
    • Pestka, J.J.1
  • 6
    • 79960795507 scopus 로고    scopus 로고
    • Trichothecenes: From simple to complex mycotoxins
    • McCormick, S. P., Stanley, A. M., Stover, N. A., and Alexander, N. J. (2011) Trichothecenes: from simple to complex mycotoxins Toxins 3, 802-814 10.3390/toxins3070802
    • (2011) Toxins , vol.3 , pp. 802-814
    • McCormick, S.P.1    Stanley, A.M.2    Stover, N.A.3    Alexander, N.J.4
  • 7
    • 33847717080 scopus 로고    scopus 로고
    • The trichothecenes and their biosynthesis
    • Grovey, J. F. (2007) The trichothecenes and their biosynthesis Fortschr. Chem. Org. Naturst. 88, 63-130 10.1007/978-3-211-49389-2-2
    • (2007) Fortschr. Chem. Org. Naturst. , vol.88 , pp. 63-130
    • Grovey, J.F.1
  • 8
    • 0024537199 scopus 로고
    • Structure-activity studies of trichothecenes: Cytotoxicity of analogues and reaction products derived from T-2 toxin and neosolaniol
    • Anderson, D. W., Black, R. M., Lee, C. G., Pottage, C., Rickard, R. L., Sandford, M. S., Webber, T. D., and Williams, N. E. (1989) Structure-activity studies of trichothecenes: cytotoxicity of analogues and reaction products derived from T-2 toxin and neosolaniol J. Med. Chem. 32, 555-562 10.1021/jm00123a008
    • (1989) J. Med. Chem. , vol.32 , pp. 555-562
    • Anderson, D.W.1    Black, R.M.2    Lee, C.G.3    Pottage, C.4    Rickard, R.L.5    Sandford, M.S.6    Webber, T.D.7    Williams, N.E.8
  • 9
    • 0037314817 scopus 로고    scopus 로고
    • Polymorphism of trichothecene biosynthesis genes in deoxynivalenol- and nivalenol-producing Fusarium graminearum isolates
    • Kim, H. S., Lee, T., Dawlatana, M., Yun, S. H., and Lee, Y. W. (2003) Polymorphism of trichothecene biosynthesis genes in deoxynivalenol- and nivalenol-producing Fusarium graminearum isolates Mycol. Res. 107, 190-197 10.1017/S0953756203007317
    • (2003) Mycol. Res. , vol.107 , pp. 190-197
    • Kim, H.S.1    Lee, T.2    Dawlatana, M.3    Yun, S.H.4    Lee, Y.W.5
  • 10
    • 4444249333 scopus 로고    scopus 로고
    • Workshop on trichothecenes with a focus on DON: Summary report
    • Larsen, J. C., Hunt, J., Perrin, I., and Ruckenbauer, P. (2004) Workshop on trichothecenes with a focus on DON: summary report Toxicol. Lett. 153, 1-22 10.1016/j.toxlet.2004.04.020
    • (2004) Toxicol. Lett. , vol.153 , pp. 1-22
    • Larsen, J.C.1    Hunt, J.2    Perrin, I.3    Ruckenbauer, P.4
  • 11
    • 0029328518 scopus 로고
    • Reduced virulence of Gibberella zeae caused by disruption of a trichothecene toxin biosynthetic gene
    • Proctor, R. H., Hohn, T. M., and McCormick, S. P. (1995) Reduced virulence of Gibberella zeae caused by disruption of a trichothecene toxin biosynthetic gene Mol. Plant-Microbe Interact. 8, 593-601 10.1094/MPMI-8-0593
    • (1995) Mol. Plant-Microbe Interact. , vol.8 , pp. 593-601
    • Proctor, R.H.1    Hohn, T.M.2    McCormick, S.P.3
  • 12
    • 28044447217 scopus 로고    scopus 로고
    • Infection patterns in barley and wheat spikes inoculated with wild-type and trichodiene synthase gene disrupted Fusarium graminearum
    • Jansen, C., von Wettstein, D., Schafer, W., Kogel, K. H., Felk, A., and Maier, F. J. (2005) Infection patterns in barley and wheat spikes inoculated with wild-type and trichodiene synthase gene disrupted Fusarium graminearum Proc. Natl. Acad. Sci. U. S. A. 102, 16892-16897 10.1073/pnas.0508467102
    • (2005) Proc. Natl. Acad. Sci. U. S. A. , vol.102 , pp. 16892-16897
    • Jansen, C.1    Von Wettstein, D.2    Schafer, W.3    Kogel, K.H.4    Felk, A.5    Maier, F.J.6
  • 14
    • 77953206450 scopus 로고    scopus 로고
    • Transcriptome analysis of the barley-deoxynivalenol interaction: Evidence for a role of glutathione in deoxynivalenol detoxification
    • Gardiner, S. A., Boddu, J., Berthiller, F., Hametner, C., Stupar, R. M., Adam, G., and Muehlbauer, G. J. (2010) Transcriptome analysis of the barley-deoxynivalenol interaction: evidence for a role of glutathione in deoxynivalenol detoxification Mol. Plant-Microbe Interact. 23, 962-976 10.1094/MPMI-23-7-0962
    • (2010) Mol. Plant-Microbe Interact. , vol.23 , pp. 962-976
    • Gardiner, S.A.1    Boddu, J.2    Berthiller, F.3    Hametner, C.4    Stupar, R.M.5    Adam, G.6    Muehlbauer, G.J.7
  • 17
    • 77950891848 scopus 로고    scopus 로고
    • Molecular cloning and characterization of an up-regulated UDP-glucosyltransferase gene induced by DON from Triticum aestivum L. Cv. Wangshuibai
    • Lulin, M., Yi, S., Aizhong, C., Zengjun, Q., Liping, X., Peidu, C., Dajun, L., and Xiu-e, W. (2010) Molecular cloning and characterization of an up-regulated UDP-glucosyltransferase gene induced by DON from Triticum aestivum L. cv. Wangshuibai Mol. Biol. Rep. 37, 785-795 10.1007/s11033-009-9606-3
    • (2010) Mol. Biol. Rep. , vol.37 , pp. 785-795
    • Lulin, M.1    Yi, S.2    Aizhong, C.3    Zengjun, Q.4    Liping, X.5    Peidu, C.6    Dajun, L.7    Xiu-E, W.8
  • 18
  • 19
    • 0035113472 scopus 로고    scopus 로고
    • Higher plant glycosyltransferases
    • Ross, J., Li, Y., Lim, E., and Bowles, D. J. (2001) Higher plant glycosyltransferases Genome biology 2, reviews3004.1 10.1186/gb-2001-2-2-reviews3004
    • (2001) Genome Biology , vol.2
    • Ross, J.1    Li, Y.2    Lim, E.3    Bowles, D.J.4
  • 20
    • 15544364507 scopus 로고    scopus 로고
    • Genomics-based selection and functional characterization of triterpene glycosyltransferases from the model legume Medicago truncatula
    • Achnine, L., Huhman, D. V., Farag, M. A., Sumner, L. W., Blount, J. W., and Dixon, R. A. (2005) Genomics-based selection and functional characterization of triterpene glycosyltransferases from the model legume Medicago truncatula Plant J. 41, 875-887 10.1111/j.1365-313X.2005.02344.x
    • (2005) Plant J. , vol.41 , pp. 875-887
    • Achnine, L.1    Huhman, D.V.2    Farag, M.A.3    Sumner, L.W.4    Blount, J.W.5    Dixon, R.A.6
  • 21
    • 84859165041 scopus 로고    scopus 로고
    • A genome-wide phylogenetic reconstruction of family 1 UDP-glycosyltransferases revealed the expansion of the family during the adaptation of plants to life on land
    • Caputi, L., Malnoy, M., Goremykin, V., Nikiforova, S., and Martens, S. (2012) A genome-wide phylogenetic reconstruction of family 1 UDP-glycosyltransferases revealed the expansion of the family during the adaptation of plants to life on land Plant J. 69, 1030-1042 10.1111/j.1365-313X.2011.04853.x
    • (2012) Plant J. , vol.69 , pp. 1030-1042
    • Caputi, L.1    Malnoy, M.2    Goremykin, V.3    Nikiforova, S.4    Martens, S.5
  • 23
    • 84938152152 scopus 로고    scopus 로고
    • Biochemical Characterization of a Recombinant UDP-glucosyltransferase from Rice and Enzymatic Production of Deoxynivalenol-3-O-beta-D-glucoside
    • Michlmayr, H., Malachova, A., Varga, E., Kleinova, J., Lemmens, M., Newmister, S., Rayment, I., Berthiller, F., and Adam, G. (2015) Biochemical Characterization of a Recombinant UDP-glucosyltransferase from Rice and Enzymatic Production of Deoxynivalenol-3-O-beta-D-glucoside Toxins 7, 2685-2700 10.3390/toxins7072685
    • (2015) Toxins , vol.7 , pp. 2685-2700
    • Michlmayr, H.1    Malachova, A.2    Varga, E.3    Kleinova, J.4    Lemmens, M.5    Newmister, S.6    Rayment, I.7    Berthiller, F.8    Adam, G.9
  • 24
    • 41549104836 scopus 로고    scopus 로고
    • Construction and use of new cloning vectors for the rapid isolation of recombinant proteins from Escherichia coli
    • Rocco, C. J., Dennison, K. L., Klenchin, V. A., Rayment, I., and Escalante-Semerena, J. C. (2008) Construction and use of new cloning vectors for the rapid isolation of recombinant proteins from Escherichia coli Plasmid 59, 231-237 10.1016/j.plasmid.2008.01.001
    • (2008) Plasmid , vol.59 , pp. 231-237
    • Rocco, C.J.1    Dennison, K.L.2    Klenchin, V.A.3    Rayment, I.4    Escalante-Semerena, J.C.5
  • 25
    • 0034099072 scopus 로고    scopus 로고
    • Restriction site-free insertion of PCR products directionally into vectors
    • 498500
    • Chen, G. J., Qiu, N., Karrer, C., Caspers, P., and Page, M. G. (2000) Restriction site-free insertion of PCR products directionally into vectors BioTechniques 28 (498-500) 504-495
    • (2000) BioTechniques , vol.28 , pp. 495-504
    • Chen, G.J.1    Qiu, N.2    Karrer, C.3    Caspers, P.4    Page, M.G.5
  • 26
    • 33645021327 scopus 로고    scopus 로고
    • RF cloning: A restriction-free method for inserting target genes into plasmids
    • van den Ent, F. and Lowe, J. (2006) RF cloning: a restriction-free method for inserting target genes into plasmids J. Biochem. Biophys. Methods 67, 67-74 10.1016/j.jbbm.2005.12.008
    • (2006) J. Biochem. Biophys. Methods , vol.67 , pp. 67-74
    • Van Den Ent, F.1    Lowe, J.2
  • 27
    • 0027439390 scopus 로고
    • Atomic structures of the human immunophilin FKBP-12 complexes with FK506 and rapamycin
    • Van Duyne, G. D., Standaert, R. F., Karplus, P. A., Schreiber, S. L., and Clardy, J. (1993) Atomic structures of the human immunophilin FKBP-12 complexes with FK506 and rapamycin J. Mol. Biol. 229, 105-124 10.1006/jmbi.1993.1012
    • (1993) J. Mol. Biol. , vol.229 , pp. 105-124
    • Van Duyne, G.D.1    Standaert, R.F.2    Karplus, P.A.3    Schreiber, S.L.4    Clardy, J.5
  • 28
    • 34250348569 scopus 로고    scopus 로고
    • A combined approach to improving large-scale production of tobacco etch virus protease
    • Blommel, P. G. and Fox, B. G. (2007) A combined approach to improving large-scale production of tobacco etch virus protease Protein Expression Purif. 55, 53-68 10.1016/j.pep.2007.04.013
    • (2007) Protein Expression Purif. , vol.55 , pp. 53-68
    • Blommel, P.G.1    Fox, B.G.2
  • 29
    • 0034612999 scopus 로고    scopus 로고
    • Enzymatic synthesis of UDP-(3-deoxy-3-fluoro)-D-galactose and UDP-(2-deoxy-2-fluoro)-D-galactose and substrate activity with UDP-galactopyranose mutase
    • Barlow, J. N. and Blanchard, J. S. (2000) Enzymatic synthesis of UDP-(3-deoxy-3-fluoro)-D-galactose and UDP-(2-deoxy-2-fluoro)-D-galactose and substrate activity with UDP-galactopyranose mutase Carbohydr. Res. 328, 473-480 10.1016/S0008-6215(00)00135-X
    • (2000) Carbohydr. Res. , vol.328 , pp. 473-480
    • Barlow, J.N.1    Blanchard, J.S.2
  • 30
    • 0031105795 scopus 로고    scopus 로고
    • A chemoenzymatic synthesis of UDP-(2-deoxy-2-fluoro)-galactose and evaluation of its interaction with galactosyltransferase
    • Hayashi, T., Murray, B. W., Wang, R., and Wong, C. H. (1997) A chemoenzymatic synthesis of UDP-(2-deoxy-2-fluoro)-galactose and evaluation of its interaction with galactosyltransferase Bioorg. Med. Chem. 5, 497-500 10.1016/S0968-0896(96)00263-5
    • (1997) Bioorg. Med. Chem. , vol.5 , pp. 497-500
    • Hayashi, T.1    Murray, B.W.2    Wang, R.3    Wong, C.H.4
  • 31
    • 33745933955 scopus 로고    scopus 로고
    • HKL-3000: The integration of data reduction and structure solution - From diffraction images to an initial model in minutes
    • Minor, W., Cymborowski, M., Otwinowski, Z., and Chruszcz, M. (2006) HKL-3000: the integration of data reduction and structure solution - from diffraction images to an initial model in minutes Acta Crystallogr., Sect. D: Biol. Crystallogr. 62, 859-866 10.1107/S0907444906019949
    • (2006) Acta Crystallogr., Sect. D: Biol. Crystallogr. , vol.62 , pp. 859-866
    • Minor, W.1    Cymborowski, M.2    Otwinowski, Z.3    Chruszcz, M.4
  • 33
    • 0002634621 scopus 로고
    • (Wolf, W. Evans, P. R. and Leslie, A. G. W. Eds.), Science and Engineering Research Council, Daresbury Laboratroy, Warrington, U.K
    • Otwinowski, Z. (1991) Proceedings of the CCP4 Study Weekend. Isomorphous Replacement and Anomalous Scattering (Wolf, W., Evans, P. R., and Leslie, A. G. W., Eds.) pp 80-86, Science and Engineering Research Council, Daresbury Laboratroy, Warrington, U.K.
    • (1991) Proceedings of the CCP4 Study Weekend. Isomorphous Replacement and Anomalous Scattering , pp. 80-86
    • Otwinowski, Z.1
  • 34
    • 0032872798 scopus 로고    scopus 로고
    • Density modification for macromolecular phase improvement
    • Cowtan, K. D. and Zhang, K. Y. (1999) Density modification for macromolecular phase improvement Prog. Biophys. Mol. Biol. 72, 245-270 10.1016/S0079-6107(99)00008-5
    • (1999) Prog. Biophys. Mol. Biol. , vol.72 , pp. 245-270
    • Cowtan, K.D.1    Zhang, K.Y.2
  • 35
    • 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., Sect. D: Biol. Crystallogr. 62, 1002-1011 10.1107/S0907444906022116
    • (2006) Acta Crystallogr., Sect. D: Biol. Crystallogr. , vol.62 , pp. 1002-1011
    • Cowtan, K.1
  • 36
  • 40
    • 0037417869 scopus 로고    scopus 로고
    • Crystal structure of the MurG:UDP-GlcNAc complex reveals common structural principles of a superfamily of glycosyltransferases
    • Hu, Y., Chen, L., Ha, S., Gross, B., Falcone, B., Walker, D., Mokhtarzadeh, M., and Walker, S. (2003) Crystal structure of the MurG:UDP-GlcNAc complex reveals common structural principles of a superfamily of glycosyltransferases Proc. Natl. Acad. Sci. U. S. A. 100, 845-849 10.1073/pnas.0235749100
    • (2003) Proc. Natl. Acad. Sci. U. S. A. , vol.100 , pp. 845-849
    • Hu, Y.1    Chen, L.2    Ha, S.3    Gross, B.4    Falcone, B.5    Walker, D.6    Mokhtarzadeh, M.7    Walker, S.8
  • 41
    • 33645281589 scopus 로고    scopus 로고
    • Crystal structures of a multifunctional triterpene/flavonoid glycosyltransferase from Medicago truncatula
    • Shao, H., He, X., Achnine, L., Blount, J. W., Dixon, R. A., and Wang, X. (2005) Crystal structures of a multifunctional triterpene/flavonoid glycosyltransferase from Medicago truncatula Plant Cell 17, 3141-3154 10.1105/tpc.105.035055
    • (2005) Plant Cell , vol.17 , pp. 3141-3154
    • Shao, H.1    He, X.2    Achnine, L.3    Blount, J.W.4    Dixon, R.A.5    Wang, X.6
  • 43
    • 34250172749 scopus 로고    scopus 로고
    • Crystal structure of Medicago truncatula UGT85H2 - Insights into the structural basis of a multifunctional (iso)flavonoid glycosyltransferase
    • Li, L., Modolo, L. V., Escamilla-Trevino, L. L., Achnine, L., Dixon, R. A., and Wang, X. (2007) Crystal structure of Medicago truncatula UGT85H2 - insights into the structural basis of a multifunctional (iso)flavonoid glycosyltransferase J. Mol. Biol. 370, 951-963 10.1016/j.jmb.2007.05.036
    • (2007) J. Mol. Biol. , vol.370 , pp. 951-963
    • Li, L.1    Modolo, L.V.2    Escamilla-Trevino, L.L.3    Achnine, L.4    Dixon, R.A.5    Wang, X.6
  • 45
    • 84885574194 scopus 로고    scopus 로고
    • Crystal structure of UDP-glucose:anthocyanidin 3-O-glucosyltransferase from Clitoria ternatea
    • Hiromoto, T., Honjo, E., Tamada, T., Noda, N., Kazuma, K., Suzuki, M., and Kuroki, R. (2013) Crystal structure of UDP-glucose:anthocyanidin 3-O-glucosyltransferase from Clitoria ternatea J. Synchrotron Radiat. 20, 894-898 10.1107/S0909049513020712
    • (2013) J. Synchrotron Radiat. , vol.20 , pp. 894-898
    • Hiromoto, T.1    Honjo, E.2    Tamada, T.3    Noda, N.4    Kazuma, K.5    Suzuki, M.6    Kuroki, R.7
  • 46
    • 70149104455 scopus 로고    scopus 로고
    • Crystal structures of glycosyltransferase UGT78G1 reveal the molecular basis for glycosylation and deglycosylation of (iso)flavonoids
    • Modolo, L. V., Li, L., Pan, H., Blount, J. W., Dixon, R. A., and Wang, X. (2009) Crystal structures of glycosyltransferase UGT78G1 reveal the molecular basis for glycosylation and deglycosylation of (iso)flavonoids J. Mol. Biol. 392, 1292-1302 10.1016/j.jmb.2009.08.017
    • (2009) J. Mol. Biol. , vol.392 , pp. 1292-1302
    • Modolo, L.V.1    Li, L.2    Pan, H.3    Blount, J.W.4    Dixon, R.A.5    Wang, X.6
  • 47
    • 84946713618 scopus 로고    scopus 로고
    • Structural basis for acceptor-substrate recognition of UDP-glucose: Anthocyanidin 3-O-glucosyltransferase from Clitoria ternatea
    • Hiromoto, T., Honjo, E., Noda, N., Tamada, T., Kazuma, K., Suzuki, M., Blaber, M., and Kuroki, R. (2015) Structural basis for acceptor-substrate recognition of UDP-glucose: anthocyanidin 3-O-glucosyltransferase from Clitoria ternatea Protein Sci. 24, 395-407 10.1002/pro.2630
    • (2015) Protein Sci. , vol.24 , pp. 395-407
    • Hiromoto, T.1    Honjo, E.2    Noda, N.3    Tamada, T.4    Kazuma, K.5    Suzuki, M.6    Blaber, M.7    Kuroki, R.8
  • 48
    • 0028312482 scopus 로고
    • Multiple secondary plant product UDP-glucose glucosyltransferase genes expressed in cassava (Manihot esculenta Crantz) cotyledons
    • Hughes, J. and Hughes, M. A. (1994) Multiple secondary plant product UDP-glucose glucosyltransferase genes expressed in cassava (Manihot esculenta Crantz) cotyledons DNA Sequence 5, 41-49 10.3109/10425179409039703
    • (1994) DNA Sequence , vol.5 , pp. 41-49
    • Hughes, J.1    Hughes, M.A.2
  • 49
    • 0037309606 scopus 로고    scopus 로고
    • On the origin of family 1 plant glycosyltransferases
    • Paquette, S., Møller, B. L., and Bak, S. (2003) On the origin of family 1 plant glycosyltransferases Phytochemistry 62, 399-413 10.1016/S0031-9422(02)00558-7
    • (2003) Phytochemistry , vol.62 , pp. 399-413
    • Paquette, S.1    Møller, B.L.2    Bak, S.3
  • 50
    • 49449087287 scopus 로고    scopus 로고
    • Glycosyltransferases: Structures, functions, and mechanisms
    • Lairson, L. L., Henrissat, B., Davies, G. J., and Withers, S. G. (2008) Glycosyltransferases: structures, functions, and mechanisms Annu. Rev. Biochem. 77, 521-555 10.1146/annurev.biochem.76.061005.092322
    • (2008) Annu. Rev. Biochem. , vol.77 , pp. 521-555
    • Lairson, L.L.1    Henrissat, B.2    Davies, G.J.3    Withers, S.G.4
  • 51
    • 33749516464 scopus 로고    scopus 로고
    • Tri4 encodes a multifunctional oxygenase required for trichothecene biosynthesis
    • McCormick, S. P., Alexander, N. J., and Proctor, R. H. (2006) Tri4 encodes a multifunctional oxygenase required for trichothecene biosynthesis Can. J. Microbiol. 52, 636-642 10.1139/w06-011
    • (2006) Can. J. Microbiol. , vol.52 , pp. 636-642
    • McCormick, S.P.1    Alexander, N.J.2    Proctor, R.H.3
  • 52
    • 84938124638 scopus 로고    scopus 로고
    • Transgenic Wheat Expressing a Barley UDP-Glucosyltransferase Detoxifies Deoxynivalenol and Provides High Levels of Resistance to Fusarium graminearum
    • Li, X., Shin, S., Heinen, S., Dill-Macky, R., Berthiller, F., Nersesian, N., Clemente, T., McCormick, S., and Muehlbauer, G. J. (2015) Transgenic Wheat Expressing a Barley UDP-Glucosyltransferase Detoxifies Deoxynivalenol and Provides High Levels of Resistance to Fusarium graminearum Mol. Plant-Microbe Interact. 28, 1237-1246 10.1094/MPMI-03-15-0062-R
    • (2015) Mol. Plant-Microbe Interact. , vol.28 , pp. 1237-1246
    • Li, X.1    Shin, S.2    Heinen, S.3    Dill-Macky, R.4    Berthiller, F.5    Nersesian, N.6    Clemente, T.7    McCormick, S.8    Muehlbauer, G.J.9
  • 54
    • 0027764344 scopus 로고
    • Protein sequence alignments: A strategy for the hierarchical analysis of residue conservation
    • Livingstone, C. D. and Barton, G. J. (1993) Protein sequence alignments: a strategy for the hierarchical analysis of residue conservation Bioinformatics 9, 745-756 10.1093/bioinformatics/9.6.745
    • (1993) Bioinformatics , vol.9 , pp. 745-756
    • Livingstone, C.D.1    Barton, G.J.2
  • 55
    • 65449188232 scopus 로고    scopus 로고
    • Jalview Version 2 - A multiple sequence alignment editor and analysis workbench
    • Waterhouse, A. M., Procter, J. B., Martin, D. M., Clamp, M., and Barton, G. J. (2009) Jalview Version 2 - a multiple sequence alignment editor and analysis workbench Bioinformatics 25, 1189-1191 10.1093/bioinformatics/btp033
    • (2009) Bioinformatics , vol.25 , pp. 1189-1191
    • Waterhouse, A.M.1    Procter, J.B.2    Martin, D.M.3    Clamp, M.4    Barton, G.J.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.