메뉴 건너뛰기




Volumn 40, Issue 1, 2013, Pages 147-158

Sequence analysis and gene expression of putative oil palm chitinase and chitinase-like proteins in response to colonization of Ganoderma boninense and Trichoderma harzianum

Author keywords

Basal stem rot; Chitinases; Ganoderma; Gene expression; Oil palm; Trichoderma

Indexed keywords

CHITINASE; PROTEIN EGCHIT1-1; PROTEIN EGCHIT3-1; PROTEIN EGCHIT5-1; UNCLASSIFIED DRUG;

EID: 84871281993     PISSN: 03014851     EISSN: 15734978     Source Type: Journal    
DOI: 10.1007/s11033-012-2043-8     Document Type: Article
Times cited : (42)

References (50)
  • 1
    • 0141645390 scopus 로고    scopus 로고
    • Plant chitinases-regulation and function
    • 12949620 1:CAS:528:DC%2BD3sXoslyqsbs%3D
    • Kasprzewska A (2003) Plant chitinases-regulation and function. Cell Mol Biol Lett 8:809-824
    • (2003) Cell Mol Biol Lett , vol.8 , pp. 809-824
    • Kasprzewska, A.1
  • 2
    • 0002886806 scopus 로고
    • Chitinase in bean leaves: Induction by ethylene, purification, properties and possible function
    • 10.1007/BF00394536 1:CAS:528:DyaL3sXht1WrtLc%3D
    • Boller T, Gehri A, Mauch F, Vögeli U (1983) Chitinase in bean leaves: induction by ethylene, purification, properties and possible function. Planta 157:22-31
    • (1983) Planta , vol.157 , pp. 22-31
    • Boller, T.1    Gehri, A.2    Mauch, F.3    Vögeli, U.4
  • 3
    • 0027225980 scopus 로고
    • New families in the classification of glycosyl hydrolases based on amino-acid-sequence similarities
    • 8352747 1:CAS:528:DyaK3sXmt1Sgu70%3D
    • Henrissat B, Bairoch A (1993) New families in the classification of glycosyl hydrolases based on amino-acid-sequence similarities. Biochem J 293:781-788
    • (1993) Biochem J , vol.293 , pp. 781-788
    • Henrissat, B.1    Bairoch, A.2
  • 4
    • 0030904072 scopus 로고    scopus 로고
    • Heterologous expression and characterization of wild-type and mutant forms of a 26kDa endochitinase from barley (Hordeum vulgare L.)
    • 9148754 1:CAS:528:DyaK2sXit1Ogurc%3D
    • Andersen MD, Jensen A, Robertus JD, Skriver K (1997) Heterologous expression and characterization of wild-type and mutant forms of a 26kDa endochitinase from barley (Hordeum vulgare L.). Biochem J 322:815-822
    • (1997) Biochem J , vol.322 , pp. 815-822
    • Andersen, M.D.1    Jensen, A.2    Robertus, J.D.3    Skriver, K.4
  • 5
    • 34547842599 scopus 로고    scopus 로고
    • Chitinase family GH18: Evolutionary insights from the genomic history of a diverse protein family
    • 17594485 10.1186/1471-2148-7-96
    • Funkhouser JD, Aronson NN Jr (2007) Chitinase family GH18: evolutionary insights from the genomic history of a diverse protein family. BMC Evol Biol 7:96
    • (2007) BMC Evol Biol , vol.7 , pp. 96
    • Funkhouser, J.D.1    Aronson Jr., N.N.2
  • 6
    • 85056330647 scopus 로고    scopus 로고
    • Chapter 4. Plant chitinases (PR-3, PR-4, PR-8, PR-11)
    • S.K. Datta S. Muthukrishnan (eds) CRC Press LLC Boca Raton
    • Neuhaus JM (1999) Chapter 4. Plant chitinases (PR-3, PR-4, PR-8, PR-11). In: Datta SK, Muthukrishnan S (eds) Pathogenesis-related proteins in plants. CRC Press LLC, Boca Raton, pp 77-105
    • (1999) Pathogenesis-related Proteins in Plants , pp. 77-105
    • Neuhaus, J.M.1
  • 8
    • 0025840612 scopus 로고
    • A short C-terminal sequence is necessary and sufficient for the targeting of chitinases to the plant vacuole
    • 1946457 10.1073/pnas.88.22.10362 1:CAS:528:DyaK38Xjs1eg
    • Neuhaus JM, Sticher L, Meins F Jr, Boller T (1991) A short C-terminal sequence is necessary and sufficient for the targeting of chitinases to the plant vacuole. Proc Natl Acad Sci USA 88:10362-10366
    • (1991) Proc Natl Acad Sci USA , vol.88 , pp. 10362-10366
    • Neuhaus, J.M.1    Sticher, L.2    Meins Jr., F.3    Boller, T.4
  • 9
    • 1942480195 scopus 로고    scopus 로고
    • Arabidopsis chitinases: A genomic survey
    • C.R. Somerville E.M. Meyerowitz (eds) American Society of Plant Biologists Rockville
    • Passarinho PA, de Vries AC (2002) Arabidopsis chitinases: a genomic survey. In: Somerville CR, Meyerowitz EM (eds) The Arabidopsis book. American Society of Plant Biologists, Rockville, pp 1-25
    • (2002) The Arabidopsis Book , pp. 1-25
    • Passarinho, P.A.1    De Vries, A.C.2
  • 10
    • 0028113585 scopus 로고
    • Molecular characterization of a novel tobacco pathogenesis-related (PR) protein: A new plant chitinase/lysozyme
    • 7816033 10.1007/BF00283273 1:CAS:528:DyaK2MXjvFGlsbg%3D
    • Heitz T, Segond S, Kauffmann S, Geoffroy P, Prasad V, Brunner F, Fritig B, Legrand M (1994) Molecular characterization of a novel tobacco pathogenesis-related (PR) protein: a new plant chitinase/lysozyme. Mol Gen Genet 245:246-254
    • (1994) Mol Gen Genet , vol.245 , pp. 246-254
    • Heitz, T.1    Segond, S.2    Kauffmann, S.3    Geoffroy, P.4    Prasad, V.5    Brunner, F.6    Fritig, B.7    Legrand, M.8
  • 12
    • 0001480645 scopus 로고
    • Biological function of pathogenesis-related proteins: Four tobacco pathogenesis-related proteins are chitinases
    • 16578819 10.1073/pnas.84.19.6750 1:CAS:528:DyaL1cXhvVagsA%3D%3D
    • Legrand M, Kauffmann S, Geoffroy P, Fritig B (1987) Biological function of pathogenesis-related proteins: four tobacco pathogenesis-related proteins are chitinases. Proc Natl Acad Sci USA 84:6750-6754
    • (1987) Proc Natl Acad Sci USA , vol.84 , pp. 6750-6754
    • Legrand, M.1    Kauffmann, S.2    Geoffroy, P.3    Fritig, B.4
  • 13
    • 0000234469 scopus 로고
    • Several "pathogenesis-related" proteins in potato are 1,3-β -glucanases and chitinases
    • 16578829 10.1073/pnas.85.3.782 1:CAS:528:DyaL1cXhsVOgs7w%3D
    • Kombrink E, Schroder M, Hahlbrock K (1988) Several "pathogenesis- related" proteins in potato are 1,3-β -glucanases and chitinases. Proc Natl Acad Sci USA 85:782-786
    • (1988) Proc Natl Acad Sci USA , vol.85 , pp. 782-786
    • Kombrink, E.1    Schroder, M.2    Hahlbrock, K.3
  • 14
    • 3242813940 scopus 로고    scopus 로고
    • Temporal and spatial profiles of chitinase expression by norway spruce in response to bark colonization by Heterobasidion annosum
    • 15240268 10.1128/AEM.70.7.3948-3953.2004 1:CAS:528:DC%2BD2cXmtFWntr0%3D
    • Hietala AM, Kvaalen H, Schmidt A, Johnk N, Solheim H, Fossdal CG (2004) Temporal and spatial profiles of chitinase expression by norway spruce in response to bark colonization by Heterobasidion annosum. Appl Environ Microbiol 70:3948-3953
    • (2004) Appl Environ Microbiol , vol.70 , pp. 3948-3953
    • Hietala, A.M.1    Kvaalen, H.2    Schmidt, A.3    Johnk, N.4    Solheim, H.5    Fossdal, C.G.6
  • 15
    • 14844329050 scopus 로고    scopus 로고
    • A class IV chitinase is up-regulated by fungal infection and abiotic stresses and associated with slow-canker-growth resistance to Cronartium ribicola in western white pine (Pinus monticola)
    • 18943122 10.1094/PHYTO-95-0284 1:CAS:528:DC%2BD2MXis1Wktb4%3D
    • Liu JJ, Ekramoddoullah AKM, Zamani A (2005) A class IV chitinase is up-regulated by fungal infection and abiotic stresses and associated with slow-canker-growth resistance to Cronartium ribicola in western white pine (Pinus monticola). Phytopathology 95:284-291
    • (2005) Phytopathology , vol.95 , pp. 284-291
    • Liu, J.J.1    Ekramoddoullah, A.K.M.2    Zamani, A.3
  • 16
    • 33644921245 scopus 로고    scopus 로고
    • Changes in host chitinase isoforms in relation to wounding and colonization by Heterobasidion annosum: Early and strong defense response in 33-year-old resistant Norway spruce clone
    • 16356913 10.1093/treephys/26.2.169 1:CAS:528:DC%2BD28XhslWqsrk%3D
    • Fossdal CG, Hietala AM, Kvaalen H, Solheim H (2006) Changes in host chitinase isoforms in relation to wounding and colonization by Heterobasidion annosum: early and strong defense response in 33-year-old resistant Norway spruce clone. Tree Physiol 26:169-177
    • (2006) Tree Physiol , vol.26 , pp. 169-177
    • Fossdal, C.G.1    Hietala, A.M.2    Kvaalen, H.3    Solheim, H.4
  • 18
    • 0001008022 scopus 로고
    • Functional implications of the subcellular localization of ethylene-induced chitinase and β-1,3-glucanase in bean leaves
    • 12359894 1:CAS:528:DyaK3cXjtlCktA%3D%3D
    • Mauch F, Staehelin LA (1989) Functional implications of the subcellular localization of ethylene-induced chitinase and β-1,3-glucanase in bean leaves. Plant Cell 1:447-457
    • (1989) Plant Cell , vol.1 , pp. 447-457
    • Mauch, F.1    Staehelin, L.A.2
  • 21
    • 34748873304 scopus 로고    scopus 로고
    • The cell wall: A carbohydrate armour for the fungal cell
    • 17854405 10.1111/j.1365-2958.2007.05872.x
    • Latgé JP (2007) The cell wall: a carbohydrate armour for the fungal cell. Mol Microbiol 66:279-290
    • (2007) Mol Microbiol , vol.66 , pp. 279-290
    • Latgé, J.P.1
  • 22
  • 23
    • 0022537615 scopus 로고
    • Ethylene-regulated gene expression: Molecular cloning of the genes encoding an endochitinase from Phaseolus vulgaris
    • 2428042 10.1073/pnas.83.18.6820 1:CAS:528:DyaL28XmtF2qtbg%3D
    • Broglie KE, Gaynor JJ, Broglie RM (1986) Ethylene-regulated gene expression: molecular cloning of the genes encoding an endochitinase from Phaseolus vulgaris. Proc Natl Acad Sci USA 83:6820-6824
    • (1986) Proc Natl Acad Sci USA , vol.83 , pp. 6820-6824
    • Broglie, K.E.1    Gaynor, J.J.2    Broglie, R.M.3
  • 24
    • 17744365510 scopus 로고    scopus 로고
    • Status of Ganoderma in oil palm
    • J. Flood D. Bridge M. Holderness (eds) CABI Publishing Wallingford 10.1079/9780851993881.0049
    • Ariffin D, Idris AS, Singh G (2000) Status of Ganoderma in oil palm. In: Flood J, Bridge PD, Holderness M (eds) Ganoderma diseases of perennial crops. CABI Publishing, Wallingford, pp 49-68
    • (2000) Ganoderma Diseases of Perennial Crops , pp. 49-68
    • Ariffin, D.1    Idris, A.S.2    Singh, G.3
  • 25
    • 34548017866 scopus 로고    scopus 로고
    • Ganoderma disease of oil palm-a white rot perspective necessary for integrated control
    • 10.1016/j.cropro.2006.11.009
    • Paterson RRM (2007) Ganoderma disease of oil palm-a white rot perspective necessary for integrated control. Crop Prot 26:1369-1376
    • (2007) Crop Prot , vol.26 , pp. 1369-1376
    • Paterson, R.R.M.1
  • 26
    • 56049104698 scopus 로고    scopus 로고
    • Disease suppression in Ganoderma-infected oil palm seedlings treated with Trichoderma harzianum
    • Nur Ain Izzati MZ, Faridah A (2008) Disease suppression in Ganoderma-infected oil palm seedlings treated with Trichoderma harzianum. Plant Prot Sci 44:101-107
    • (2008) Plant Prot Sci , vol.44 , pp. 101-107
    • Nur Ain Izzati, M.Z.1    Faridah, A.2
  • 27
    • 73949125555 scopus 로고    scopus 로고
    • In vitro studies on the potential Trichoderma harzianum for antagonistic properties against Ganoderma boninense
    • Shafiquzzaman S, Umi KY, Kausar H, Sarwar J (2009) In vitro studies on the potential Trichoderma harzianum for antagonistic properties against Ganoderma boninense. J Food Agric Environ 7:970-976
    • (2009) J Food Agric Environ , vol.7 , pp. 970-976
    • Shafiquzzaman, S.1    Umi, K.Y.2    Kausar, H.3    Sarwar, J.4
  • 29
    • 84866181953 scopus 로고    scopus 로고
    • Chitinase and β-1,3- glucanase activities against Ganoderma sp. in oil palm
    • J.S. Tahardi T.W. Darmono S.D. Siswanto R. Nataatmadja (eds) Bogor Indonesia
    • Siswanto SD, Darmono TW (1998) Chitinase and β-1,3- glucanase activities against Ganoderma sp. in oil palm. In: Tahardi JS, Darmono TW, Siswanto SD, Nataatmadja R (eds) Proceedings of the BTIG Workshop on oil palm improvement through biotechnology. Bogor, Indonesia, pp 104-114
    • (1998) Proceedings of the BTIG Workshop on Oil Palm Improvement Through Biotechnology , pp. 104-114
    • Siswanto, S.D.1    Darmono, T.W.2
  • 30
    • 0035028330 scopus 로고    scopus 로고
    • N-acetylglucosamine and glucosamine-containing arabinogalactan proteins control somatic embryogenesis
    • 11299367 10.1104/pp.125.4.1880
    • van Hengel AJ, Tadesse Z, Immerzeel P, Schols H, van Kammen A, de Vries SC (2001) N-acetylglucosamine and glucosamine-containing arabinogalactan proteins control somatic embryogenesis. Plant Physiol 125:1880-1890
    • (2001) Plant Physiol , vol.125 , pp. 1880-1890
    • Van Hengel, A.J.1    Tadesse, Z.2    Immerzeel, P.3    Schols, H.4    Van Kammen, A.5    De Vries, S.C.6
  • 31
    • 0036007921 scopus 로고    scopus 로고
    • Mutation of a chitinase-like gene causes ectopic deposition of lignin, aberrant cell shapes, and overproduction of ethylene
    • 11826306 10.1105/tpc.010278 1:CAS:528:DC%2BD38Xht1Srtrw%3D
    • Zhong RQ, Kays SJ, Schroeder BP, Ye ZH (2002) Mutation of a chitinase-like gene causes ectopic deposition of lignin, aberrant cell shapes, and overproduction of ethylene. Plant Cell 14:165-179
    • (2002) Plant Cell , vol.14 , pp. 165-179
    • Zhong, R.Q.1    Kays, S.J.2    Schroeder, B.P.3    Ye, Z.H.4
  • 32
    • 80455164604 scopus 로고    scopus 로고
    • Cloning of transcripts encoding chitinases from Elaeis guineensis Jacq. and their expression profiles in response to fungal infections
    • 10.1016/j.pmpp.2011.06.006 1:CAS:528:DC%2BC3MXhtlyksbbL
    • Naher L, Ho CL, Tan SG, Umi KY, Faridah A (2011) Cloning of transcripts encoding chitinases from Elaeis guineensis Jacq. and their expression profiles in response to fungal infections. Physiol Mol Plant P 76:96-103
    • (2011) Physiol Mol Plant P , vol.76 , pp. 96-103
    • Naher, L.1    Ho, C.L.2    Tan, S.G.3    Umi, K.Y.4    Faridah, A.5
  • 34
    • 20944447661 scopus 로고    scopus 로고
    • Isolation of RNA of high quality and yield from Ginkgo biloba leaves
    • 15977069 10.1007/s10529-005-3629-1
    • Wang T, Zhang NH, Du LF (2005) Isolation of RNA of high quality and yield from Ginkgo biloba leaves. Biotechnol Lett 27:629-633
    • (2005) Biotechnol Lett , vol.27 , pp. 629-633
    • Wang, T.1    Zhang, N.H.2    Du, L.F.3
  • 35
  • 36
    • 0027968068 scopus 로고
    • CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • 7984417 10.1093/nar/22.22.4673 1:CAS:528:DyaK2MXitlSgu74%3D
    • Thompson JD, Higgins DG, Gibson TJ (1994) CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic Acids Res 22:4673-4680
    • (1994) Nucleic Acids Res , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 37
    • 0002051540 scopus 로고    scopus 로고
    • Bioedit: A user-friendly biological sequence alignment editor and analysis program for Windows 95/98/NT
    • 1:CAS:528:DC%2BD3cXhtVyjs7Y%3D
    • Hall TA (1999) Bioedit: a user-friendly biological sequence alignment editor and analysis program for Windows 95/98/NT. Nucleic Acids Symp Ser 41:95-98
    • (1999) Nucleic Acids Symp ser , vol.41 , pp. 95-98
    • Hall, T.A.1
  • 38
    • 34547781750 scopus 로고    scopus 로고
    • Molecular evolutionary genetics analysis (MEGA) software version 4.0
    • 17488738 10.1093/molbev/msm092 1:CAS:528:DC%2BD2sXpsVGrsL8%3D
    • Tamura K, Dudley J, Nei M, Kumar S (2007) Molecular evolutionary genetics analysis (MEGA) software version 4.0. Mol Biol Evol 24:1596-1599
    • (2007) Mol Biol Evol , vol.24 , pp. 1596-1599
    • Tamura, K.1    Dudley, J.2    Nei, M.3    Kumar, S.4
  • 39
    • 80052301538 scopus 로고    scopus 로고
    • Efficacy of single and mixed treatments of Trichoderma harzianum as biocontrol agents of Ganoderma basal stem rot in oil palm
    • Shamala S, Faridah A, Zainal AMA, Umi KY (2008) Efficacy of single and mixed treatments of Trichoderma harzianum as biocontrol agents of Ganoderma basal stem rot in oil palm. J Oil Palm Res 20:470-483
    • (2008) J Oil Palm Res , vol.20 , pp. 470-483
    • Shamala, S.1    Faridah, A.2    Zainal, A.M.A.3    Umi, K.Y.4
  • 40
    • 0037129827 scopus 로고    scopus 로고
    • Accurate normalization of real-time quantitative RT-PCR data by geometric averaging of multiple internal control genes
    • 10.1186/gb-2002-3-7-research0034
    • Vandesompele J, De Preter K, Pattyn F, Poppe B, Van Roy N, De Paepe A, Speleman F (2002) Accurate normalization of real-time quantitative RT-PCR data by geometric averaging of multiple internal control genes. Genome Biol 3:1-12
    • (2002) Genome Biol , vol.3 , pp. 1-12
    • Vandesompele, J.1    De Preter, K.2    Pattyn, F.3    Poppe, B.4    Van Roy, N.5    De Paepe, A.6    Speleman, F.7
  • 41
    • 58949098440 scopus 로고    scopus 로고
    • Cloning and characterization of an antifungal class III chitinase from suspension-cultured bamboo (Bambusa oldhamii) cells
    • 18998701 10.1021/jf8017589 1:CAS:528:DC%2BD1cXhtlGrsrzJ
    • Kuo CJ, Liao YC, Yang JH, Huang LC, Chang CT, Sung HY (2008) Cloning and characterization of an antifungal class III chitinase from suspension-cultured bamboo (Bambusa oldhamii) cells. J Agric Food Chem 56:11507-11514
    • (2008) J Agric Food Chem , vol.56 , pp. 11507-11514
    • Kuo, C.J.1    Liao, Y.C.2    Yang, J.H.3    Huang, L.C.4    Chang, C.T.5    Sung, H.Y.6
  • 42
    • 79959507253 scopus 로고    scopus 로고
    • A class v chitinase from Arabidopsis thaliana: Gene responses, enzymatic properties, and crystallographic analysis
    • 21390509 10.1007/s00425-011-1390-3 1:CAS:528:DC%2BC3MXotVelt74%3D
    • Ohnuma T, Numata T, Osawa T, Mizuhara M, Lampela O, Juffer AH, Skriver K, Fukamizo T (2011) A class V chitinase from Arabidopsis thaliana: gene responses, enzymatic properties, and crystallographic analysis. Planta 234:123-137
    • (2011) Planta , vol.234 , pp. 123-137
    • Ohnuma, T.1    Numata, T.2    Osawa, T.3    Mizuhara, M.4    Lampela, O.5    Juffer, A.H.6    Skriver, K.7    Fukamizo, T.8
  • 44
    • 34250648099 scopus 로고    scopus 로고
    • A novel family of lectins evolutionarily related to class v chitinases: An example of neofunctionalization in legumes
    • 17098856 10.1104/pp.106.087981
    • van Damme EJM, Culerrier R, Barre A, Alvarez R, Rougé P, Peumans WJ (2007) A novel family of lectins evolutionarily related to class V chitinases: an example of neofunctionalization in legumes. Plant Physiol 144:662-672
    • (2007) Plant Physiol , vol.144 , pp. 662-672
    • Van Damme, E.J.M.1    Culerrier, R.2    Barre, A.3    Alvarez, R.4    Rougé, P.5    Peumans, W.J.6
  • 45
    • 77956188382 scopus 로고    scopus 로고
    • Cloning, heterologous expression, and functional characterization of a chitinase gene, Lbchi32, from Limonium bicolor
    • 20512617 10.1007/s10528-010-9348-x 1:CAS:528:DC%2BC3cXos1Giurk%3D
    • Liu ZH, Yang CP, Qi XT, Xiu LL, Wang YC (2010) Cloning, heterologous expression, and functional characterization of a chitinase gene, Lbchi32, from Limonium bicolor. Biochem Genet 48:669-679
    • (2010) Biochem Genet , vol.48 , pp. 669-679
    • Liu, Z.H.1    Yang, C.P.2    Qi, X.T.3    Xiu, L.L.4    Wang, Y.C.5
  • 46
    • 0001413068 scopus 로고
    • Developmental and pathogen-induced activation of the Arabidopsis acidic chitinase promoter
    • 12324582 1:CAS:528:DyaK38Xjslam
    • Samac DA, Shah DM (1991) Developmental and pathogen-induced activation of the Arabidopsis acidic chitinase promoter. Plant Cell 3:1063-1072
    • (1991) Plant Cell , vol.3 , pp. 1063-1072
    • Samac, D.A.1    Shah, D.M.2
  • 47
    • 0028039707 scopus 로고
    • Regulation of cucumber class III chitinase gene expression
    • 8167370 10.1094/MPMI-7-0048 1:CAS:528:DyaK2cXmt1entrg%3D
    • Lawton KA, Beck J, Potter S, Ward E, Ryals J (1994) Regulation of cucumber class III chitinase gene expression. Mol Plant Microbe Interact 7:48-57
    • (1994) Mol Plant Microbe Interact , vol.7 , pp. 48-57
    • Lawton, K.A.1    Beck, J.2    Potter, S.3    Ward, E.4    Ryals, J.5
  • 48
    • 0027634201 scopus 로고
    • Spatial and temporal accumulation of defence gene transcripts in bean (Phaseolus vulgaris) leaves in relation to bacteria-induced hypersensitive cell death
    • 8400375 10.1094/MPMI-6-453 1:CAS:528:DyaK2cXitFaktL8%3D
    • Meier BM, Shaw N, Ślusarenko AJ (1993) Spatial and temporal accumulation of defence gene transcripts in bean (Phaseolus vulgaris) leaves in relation to bacteria-induced hypersensitive cell death. Mol Plant Microbe Interact 6:453-466
    • (1993) Mol Plant Microbe Interact , vol.6 , pp. 453-466
    • Meier, B.M.1    Shaw, N.2    Ślusarenko, A.J.3
  • 49
    • 1842591134 scopus 로고    scopus 로고
    • Trichoderma species-opportunistic, avirulent plant symbionts
    • 15035008 10.1038/nrmicro797 1:CAS:528:DC%2BD2cXht1Krsbo%3D
    • Harman GE, Howell CR, Viterbo A, Chet I, Lorito M (2004) Trichoderma species-opportunistic, avirulent plant symbionts. Nat Rev Microbiol 2:43-56
    • (2004) Nat Rev Microbiol , vol.2 , pp. 43-56
    • Harman, G.E.1    Howell, C.R.2    Viterbo, A.3    Chet, I.4    Lorito, M.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.