메뉴 건너뛰기




Volumn 15, Issue 1, 2014, Pages

Correction to Comparative analysis of fungal genomes reveals different plant cell wall degrading capacity in fungi [BMC Genomics 14(2013) 274]

Author keywords

Carbohydrate esterase; CAZymes; Cutinase; Fungi; Glycoside hydrolase; Lignocellulase; Pectinase; Polysaccharide lyase

Indexed keywords

CARBOHYDRATE ESTERASE; CELLULOSE; ESTERASE; GLYCOSIDASE; GLYCOSYLTRANSFERASE; POLYGALACTURONASE; POLYSACCHARIDE LYASE; PROTEOME; UNCLASSIFIED DRUG;

EID: 84892409004     PISSN: None     EISSN: 14712164     Source Type: Journal    
DOI: 10.1186/1471-2164-15-6     Document Type: Erratum
Times cited : (133)

References (56)
  • 1
    • 84876739031 scopus 로고    scopus 로고
    • Comparative analysis of fungal genomes reveals different plant cell wall degrading capacity in fungi
    • 10.1186/1471-2164-14-274, 3652786, 23617724
    • Zhao Z, Liu H, Wang C, Xu JR. Comparative analysis of fungal genomes reveals different plant cell wall degrading capacity in fungi. BMC Genomics 2013, 14(1):274. 10.1186/1471-2164-14-274, 3652786, 23617724.
    • (2013) BMC Genomics , vol.14 , Issue.1 , pp. 274
    • Zhao, Z.1    Liu, H.2    Wang, C.3    Xu, J.R.4
  • 2
    • 58149200943 scopus 로고    scopus 로고
    • The Carbohydrate-Active EnZymes database (CAZy): an expert resource for Glycogenomics
    • Database issue, 2686590, 18838391
    • Cantarel BL, Coutinho PM, Rancurel C, Bernard T, Lombard V, Henrissat B. The Carbohydrate-Active EnZymes database (CAZy): an expert resource for Glycogenomics. Nucleic Acids Res 2009, 37(Database issue):D233-D238. 2686590, 18838391.
    • (2009) Nucleic Acids Res , vol.37
    • Cantarel, B.L.1    Coutinho, P.M.2    Rancurel, C.3    Bernard, T.4    Lombard, V.5    Henrissat, B.6
  • 3
    • 77957156894 scopus 로고    scopus 로고
    • The CAZyome of Phytophthora spp: a comprehensive analysis of the gene complement coding for carbohydrate-active enzymes in species of the genus Phytophthora
    • 10.1186/1471-2164-11-525, 2997016, 20920201
    • Ospina-Giraldo MD, Griffith JG, Laird EW, Mingora C. The CAZyome of Phytophthora spp: a comprehensive analysis of the gene complement coding for carbohydrate-active enzymes in species of the genus Phytophthora. BMC Genomics 2010, 11:525. 10.1186/1471-2164-11-525, 2997016, 20920201.
    • (2010) BMC Genomics , vol.11 , pp. 525
    • Ospina-Giraldo, M.D.1    Griffith, J.G.2    Laird, E.W.3    Mingora, C.4
  • 4
    • 80053340547 scopus 로고    scopus 로고
    • Curation of characterized glycoside hydrolases of fungal origin
    • doi: 10.1093/database/bar020
    • Murphy C, Powlowski J, Wu M, Butler G, Tsang A. Curation of characterized glycoside hydrolases of fungal origin. Database (Oxford) 2011, doi: 10.1093/database/bar020.
    • (2011) Database (Oxford)
    • Murphy, C.1    Powlowski, J.2    Wu, M.3    Butler, G.4    Tsang, A.5
  • 5
    • 84856460892 scopus 로고    scopus 로고
    • Post-genomic analyses of fungal lignocellulosic biomass degradation reveal the unexpected potential of the plant pathogen Ustilago maydis
    • 10.1186/1471-2164-13-57, 3298532, 22300648
    • Couturier M, Navarro D, Olive C, Chevret D, Haon M, Favel A, Lesage-Meessen L, Henrissat B, Coutinho PM, Berrin JG. Post-genomic analyses of fungal lignocellulosic biomass degradation reveal the unexpected potential of the plant pathogen Ustilago maydis. BMC Genomics 2012, 13:57. 10.1186/1471-2164-13-57, 3298532, 22300648.
    • (2012) BMC Genomics , vol.13 , pp. 57
    • Couturier, M.1    Navarro, D.2    Olive, C.3    Chevret, D.4    Haon, M.5    Favel, A.6    Lesage-Meessen, L.7    Henrissat, B.8    Coutinho, P.M.9    Berrin, J.G.10
  • 6
    • 79951554626 scopus 로고    scopus 로고
    • Arsenal of plant cell wall degrading enzymes reflects host preference among plant pathogenic fungi
    • 10.1186/1754-6834-4-4, 3051899, 21324176
    • King BC, Waxman KD, Nenni NV, Walker LP, Bergstrom GC, Gibson DM. Arsenal of plant cell wall degrading enzymes reflects host preference among plant pathogenic fungi. Biotechnol Biofuels 2011, 4:4. 10.1186/1754-6834-4-4, 3051899, 21324176.
    • (2011) Biotechnol Biofuels , vol.4 , pp. 4
    • King, B.C.1    Waxman, K.D.2    Nenni, N.V.3    Walker, L.P.4    Bergstrom, G.C.5    Gibson, D.M.6
  • 7
    • 77950948619 scopus 로고    scopus 로고
    • The intra- and extracellular proteome of Aspergillus niger growing on defined medium with xylose or maltose as carbon substrate
    • 10.1186/1475-2859-9-23, 2874515, 20406453
    • Lu X, Sun J, Nimtz M, Wissing J, Zeng A-P, Rinas U. The intra- and extracellular proteome of Aspergillus niger growing on defined medium with xylose or maltose as carbon substrate. Microb Cell Fact 2010, 9(1):23. 10.1186/1475-2859-9-23, 2874515, 20406453.
    • (2010) Microb Cell Fact , vol.9 , Issue.1 , pp. 23
    • Lu, X.1    Sun, J.2    Nimtz, M.3    Wissing, J.4    Zeng, A.-P.5    Rinas, U.6
  • 8
    • 44149100746 scopus 로고    scopus 로고
    • Aspergillus niger genome-wide analysis reveals a large number of novel alpha-glucan acting enzymes with unexpected expression profiles
    • 10.1007/s00438-008-0332-7, 2413074, 18320228
    • Yuan X-L, Kaaij RM, van den Hondel CA, Punt PJ, Maarel MJEC, Dijkhuizen L, Ram AFJ. Aspergillus niger genome-wide analysis reveals a large number of novel alpha-glucan acting enzymes with unexpected expression profiles. Mol Genet Genomics 2008, 279(6):545-561. 10.1007/s00438-008-0332-7, 2413074, 18320228.
    • (2008) Mol Genet Genomics , vol.279 , Issue.6 , pp. 545-561
    • Yuan, X.-L.1    Kaaij, R.M.2    van den Hondel, C.A.3    Punt, P.J.4    Maarel, M.J.E.C.5    Dijkhuizen, L.6    Ram, A.F.J.7
  • 9
    • 34748923122 scopus 로고    scopus 로고
    • Comparative proteomics of extracellular proteins in vitro and in planta from the pathogenic fungus Fusarium graminearum
    • 10.1002/pmic.200700184, 17676664
    • Paper JM, Scott-Craig JS, Adhikari ND, Cuomo CA, Walton JD. Comparative proteomics of extracellular proteins in vitro and in planta from the pathogenic fungus Fusarium graminearum. Proteomics 2007, 7(17):3171-3183. 10.1002/pmic.200700184, 17676664.
    • (2007) Proteomics , vol.7 , Issue.17 , pp. 3171-3183
    • Paper, J.M.1    Scott-Craig, J.S.2    Adhikari, N.D.3    Cuomo, C.A.4    Walton, J.D.5
  • 10
    • 41449085026 scopus 로고    scopus 로고
    • Comparative secretome analysis suggests low plant cell wall degrading capacity in Frankia symbionts
    • 10.1186/1471-2164-9-47, 2266912, 18226217
    • Mastronunzio JE, Tisa LS, Normand P, Benson DR. Comparative secretome analysis suggests low plant cell wall degrading capacity in Frankia symbionts. BMC Genomics 2008, 9(1):47. 10.1186/1471-2164-9-47, 2266912, 18226217.
    • (2008) BMC Genomics , vol.9 , Issue.1 , pp. 47
    • Mastronunzio, J.E.1    Tisa, L.S.2    Normand, P.3    Benson, D.R.4
  • 11
    • 84859512402 scopus 로고    scopus 로고
    • The predicted secretome of the plant pathogenic fungus Fusarium graminearum: a refined comparative analysis
    • 10.1371/journal.pone.0033731, 3320895, 22493673
    • Brown NA, Antoniw J, Hammond-Kosack KE. The predicted secretome of the plant pathogenic fungus Fusarium graminearum: a refined comparative analysis. PLoS One 2012, 7(4):e33731. 10.1371/journal.pone.0033731, 3320895, 22493673.
    • (2012) PLoS One , vol.7 , Issue.4
    • Brown, N.A.1    Antoniw, J.2    Hammond-Kosack, K.E.3
  • 12
    • 78651390306 scopus 로고    scopus 로고
    • Carbohydrate-active enzymes from the zygomycete fungus Rhizopus oryzae: a highly specialized approach to carbohydrate degradation depicted at genome level
    • 10.1186/1471-2164-12-38, 3032700, 21241472
    • Battaglia E, Benoit I, van den Brink J, Wiebenga A, Coutinho PM, Henrissat B, de Vries RP. Carbohydrate-active enzymes from the zygomycete fungus Rhizopus oryzae: a highly specialized approach to carbohydrate degradation depicted at genome level. BMC Genomics 2011, 12:38. 10.1186/1471-2164-12-38, 3032700, 21241472.
    • (2011) BMC Genomics , vol.12 , pp. 38
    • Battaglia, E.1    Benoit, I.2    Van Den Brink, J.3    Wiebenga, A.4    Coutinho, P.M.5    Henrissat, B.6    de Vries, R.P.7
  • 13
    • 76049107428 scopus 로고    scopus 로고
    • Systems analysis of plant cell wall degradation by the model filamentous fungus Neurospora crassa
    • 10.1073/pnas.0906810106, 2794032, 20018766
    • Tian C, Beeson WT, Iavarone AT, Sun J, Marletta MA, Cate JHD, Glass NL. Systems analysis of plant cell wall degradation by the model filamentous fungus Neurospora crassa. Proc Natl Acad Sci 2009, 106(52):22157-22162. 10.1073/pnas.0906810106, 2794032, 20018766.
    • (2009) Proc Natl Acad Sci , vol.106 , Issue.52 , pp. 22157-22162
    • Tian, C.1    Beeson, W.T.2    Iavarone, A.T.3    Sun, J.4    Marletta, M.A.5    Cate, J.H.D.6    Glass, N.L.7
  • 14
    • 79952178786 scopus 로고    scopus 로고
    • Fungal biodegradation and enzymatic modification of lignin
    • 3180040, 21968746
    • Dashtban M, Schraft H, Syed TA, Qin W. Fungal biodegradation and enzymatic modification of lignin. Int J Biochem Mol Biol 2010, 1(1):36-50. 3180040, 21968746.
    • (2010) Int J Biochem Mol Biol , vol.1 , Issue.1 , pp. 36-50
    • Dashtban, M.1    Schraft, H.2    Syed, T.A.3    Qin, W.4
  • 16
    • 33846275331 scopus 로고    scopus 로고
    • Correlative analysis of Mycosphaerella graminicola pathogenicity and cell wall-degrading enzymes produced in vitro: the importance of xylanase and polygalacturonase
    • Douaiher MN, Nowak E, Durand R, Halama P, Reignault P. Correlative analysis of Mycosphaerella graminicola pathogenicity and cell wall-degrading enzymes produced in vitro: the importance of xylanase and polygalacturonase. Plant Pathol 2007, 56(1):79-86.
    • (2007) Plant Pathol , vol.56 , Issue.1 , pp. 79-86
    • Douaiher, M.N.1    Nowak, E.2    Durand, R.3    Halama, P.4    Reignault, P.5
  • 17
    • 38949133173 scopus 로고    scopus 로고
    • Transgenic Expression of a Fungal endo-Polygalacturonase Increases Plant Resistance to Pathogens and Reduces Auxin Sensitivity
    • 10.1104/pp.107.109686, 2245817, 18065558
    • Ferrari S, Galletti R, Pontiggia D, Manfredini C, Lionetti V, Bellincampi D, Cervone F, De Lorenzo G. Transgenic Expression of a Fungal endo-Polygalacturonase Increases Plant Resistance to Pathogens and Reduces Auxin Sensitivity. Plant Physiol 2007, 146(2):669-681. 10.1104/pp.107.109686, 2245817, 18065558.
    • (2007) Plant Physiol , vol.146 , Issue.2 , pp. 669-681
    • Ferrari, S.1    Galletti, R.2    Pontiggia, D.3    Manfredini, C.4    Lionetti, V.5    Bellincampi, D.6    Cervone, F.7    De Lorenzo, G.8
  • 18
    • 67650445157 scopus 로고    scopus 로고
    • Contribution of cell wall degrading enzymes to pathogenesis of Fusarium graminearum: a review
    • 10.1002/jobm.200800231, 19025875
    • Kikot GE, Hours RA, Alconada TM. Contribution of cell wall degrading enzymes to pathogenesis of Fusarium graminearum: a review. J Basic Microbiol 2009, 49(3):231-241. 10.1002/jobm.200800231, 19025875.
    • (2009) J Basic Microbiol , vol.49 , Issue.3 , pp. 231-241
    • Kikot, G.E.1    Hours, R.A.2    Alconada, T.M.3
  • 19
    • 80053581493 scopus 로고    scopus 로고
    • The fate of gene duplicates in the genomes of fungal pathogens
    • 10.4161/cib.1.2.7144, 2686021, 19513258
    • Skamnioti P, Furlong RF, Gurrl SJ. The fate of gene duplicates in the genomes of fungal pathogens. Commun Integr Biol 2008, 1(2):196-198. 10.4161/cib.1.2.7144, 2686021, 19513258.
    • (2008) Commun Integr Biol , vol.1 , Issue.2 , pp. 196-198
    • Skamnioti, P.1    Furlong, R.F.2    Gurrl, S.J.3
  • 20
    • 43849088205 scopus 로고    scopus 로고
    • Unique aspects of the grass cell wall
    • 10.1016/j.pbi.2008.03.002, 18434239
    • Vogel J. Unique aspects of the grass cell wall. Curr Opin Plant Biol 2008, 11(3):301-307. 10.1016/j.pbi.2008.03.002, 18434239.
    • (2008) Curr Opin Plant Biol , vol.11 , Issue.3 , pp. 301-307
    • Vogel, J.1
  • 21
    • 70450225258 scopus 로고    scopus 로고
    • Plant cell walls: Protecting the barrier from degradation by microbial enzymes
    • 10.1016/j.semcdb.2009.05.008, 19497379
    • Lagaert S, Belien T, Volckaert G. Plant cell walls: Protecting the barrier from degradation by microbial enzymes. Semin Cell Dev Biol 2009, 20(9):1064-1073. 10.1016/j.semcdb.2009.05.008, 19497379.
    • (2009) Semin Cell Dev Biol , vol.20 , Issue.9 , pp. 1064-1073
    • Lagaert, S.1    Belien, T.2    Volckaert, G.3
  • 22
    • 84864442502 scopus 로고    scopus 로고
    • DbCAN: a web resource for automated carbohydrate-active enzyme annotation
    • Web Server issue, 3394287, 22645317
    • Yin Y, Mao X, Yang J, Chen X, Mao F, Xu Y. dbCAN: a web resource for automated carbohydrate-active enzyme annotation. Nucleic Acids Res 2012, 40(Web Server issue):W445-W451. 3394287, 22645317.
    • (2012) Nucleic Acids Res , vol.40
    • Yin, Y.1    Mao, X.2    Yang, J.3    Chen, X.4    Mao, F.5    Xu, Y.6
  • 23
    • 77958127184 scopus 로고    scopus 로고
    • Annotation and comparative analysis of the glycoside hydrolase genes in Brachypodium distachyon
    • 10.1186/1471-2164-11-600, 3091745, 20973991
    • Tyler L, Bragg JN, Wu J, Yang X, Tuskan GA, Vogel JP. Annotation and comparative analysis of the glycoside hydrolase genes in Brachypodium distachyon. BMC Genomics 2010, 11:600. 10.1186/1471-2164-11-600, 3091745, 20973991.
    • (2010) BMC Genomics , vol.11 , pp. 600
    • Tyler, L.1    Bragg, J.N.2    Wu, J.3    Yang, X.4    Tuskan, G.A.5    Vogel, J.P.6
  • 24
    • 33645213849 scopus 로고    scopus 로고
    • Breakdown of oligosaccharides by the process of elimination
    • 10.1016/j.cbpa.2006.02.005, 16495121
    • Yip VL, Withers SG. Breakdown of oligosaccharides by the process of elimination. Curr Opin Chem Biol 2006, 10(2):147-155. 10.1016/j.cbpa.2006.02.005, 16495121.
    • (2006) Curr Opin Chem Biol , vol.10 , Issue.2 , pp. 147-155
    • Yip, V.L.1    Withers, S.G.2
  • 25
    • 84867731209 scopus 로고    scopus 로고
    • Microbial carbohydrate esterases deacetylating plant polysaccharides
    • 10.1016/j.biotechadv.2012.04.010, 22580218
    • Biely P. Microbial carbohydrate esterases deacetylating plant polysaccharides. Biotechnol Adv 2012, 30(6):1575-1588. 10.1016/j.biotechadv.2012.04.010, 22580218.
    • (2012) Biotechnol Adv , vol.30 , Issue.6 , pp. 1575-1588
    • Biely, P.1
  • 26
    • 4744368323 scopus 로고    scopus 로고
    • Carbohydrate-binding modules: fine-tuning polysaccharide recognition
    • 1133952, 15214846
    • Boraston AB, Bolam DN, Gilbert HJ, Davies GJ. Carbohydrate-binding modules: fine-tuning polysaccharide recognition. Biochem J 2004, 382(Pt 3):769-781. 1133952, 15214846.
    • (2004) Biochem J , vol.382 , Issue.PART 3 , pp. 769-781
    • Boraston, A.B.1    Bolam, D.N.2    Gilbert, H.J.3    Davies, G.J.4
  • 28
    • 0028850988 scopus 로고
    • Pectin-degrading enzymes and plant-parasite interactions
    • Alghisi P, Favaron F. Pectin-degrading enzymes and plant-parasite interactions. Eur J Plant Pathol 1995, 101:365-375.
    • (1995) Eur J Plant Pathol , vol.101 , pp. 365-375
    • Alghisi, P.1    Favaron, F.2
  • 30
    • 84856072252 scopus 로고    scopus 로고
    • Cellulases dig deep: in situ observation of the mesoscopic structural dynamics of enzymatic cellulose degradation
    • 3268433, 22128148
    • Bubner P, Dohr J, Plank H, Mayrhofer C, Nidetzky B. Cellulases dig deep: in situ observation of the mesoscopic structural dynamics of enzymatic cellulose degradation. J Biol Chem 2011, 287(4):2759-2765. 3268433, 22128148.
    • (2011) J Biol Chem , vol.287 , Issue.4 , pp. 2759-2765
    • Bubner, P.1    Dohr, J.2    Plank, H.3    Mayrhofer, C.4    Nidetzky, B.5
  • 31
    • 23744496272 scopus 로고    scopus 로고
    • Transcriptional regulation of plant cell wall degradation by filamentous fungi
    • 10.1016/j.femsre.2004.11.006, 16102600
    • Aro N, Pakula T, Penttila M. Transcriptional regulation of plant cell wall degradation by filamentous fungi. FEMS Microbiol Rev 2005, 29(4):719-739. 10.1016/j.femsre.2004.11.006, 16102600.
    • (2005) FEMS Microbiol Rev , vol.29 , Issue.4 , pp. 719-739
    • Aro, N.1    Pakula, T.2    Penttila, M.3
  • 32
    • 84867788061 scopus 로고    scopus 로고
    • Cellulases from thermophilic fungi: recent insights and biotechnological potential
    • 3226318, 22145076
    • Li DC, Li AN, Papageorgiou AC. Cellulases from thermophilic fungi: recent insights and biotechnological potential. Enzyme Res 2011, 2011:308730. 3226318, 22145076.
    • (2011) Enzyme Res , vol.2011 , pp. 308730
    • Li, D.C.1    Li, A.N.2    Papageorgiou, A.C.3
  • 33
    • 19944427947 scopus 로고    scopus 로고
    • Biochemical characterization and identification of the catalytic residues of a family 43 beta-D-xylosidase from Geobacillus stearothermophilus T-6
    • 10.1021/bi048059w, 15628881
    • Shallom D, Leon M, Bravman T, Ben-David A, Zaide G, Belakhov V, Shoham G, Schomburg D, Baasov T, Shoham Y. Biochemical characterization and identification of the catalytic residues of a family 43 beta-D-xylosidase from Geobacillus stearothermophilus T-6. Biochemistry 2005, 44(1):387-397. 10.1021/bi048059w, 15628881.
    • (2005) Biochemistry , vol.44 , Issue.1 , pp. 387-397
    • Shallom, D.1    Leon, M.2    Bravman, T.3    Ben-David, A.4    Zaide, G.5    Belakhov, V.6    Shoham, G.7    Schomburg, D.8    Baasov, T.9    Shoham, Y.10
  • 34
    • 84857193370 scopus 로고    scopus 로고
    • Genome analyses highlight the different biological roles of cellulases
    • 10.1038/nrmicro2729, 22266780
    • Medie FM, Davies GJ, Drancourt M, Henrissat B. Genome analyses highlight the different biological roles of cellulases. Nat Rev Microbiol 2012, 10(3):227-234. 10.1038/nrmicro2729, 22266780.
    • (2012) Nat Rev Microbiol , vol.10 , Issue.3 , pp. 227-234
    • Medie, F.M.1    Davies, G.J.2    Drancourt, M.3    Henrissat, B.4
  • 35
    • 0034333059 scopus 로고    scopus 로고
    • Comparative modeling of the three-dimensional structures of family 3 glycoside hydrolases
    • 10.1002/1097-0134(20001101)41:2<257::AID-PROT100>3.0.CO;2-C, 10966578
    • Harvey AJ, Hrmova M, De Gori R, Varghese JN, Fincher GB. Comparative modeling of the three-dimensional structures of family 3 glycoside hydrolases. Proteins 2000, 41(2):257-269. 10.1002/1097-0134(20001101)41:2<257::AID-PROT100>3.0.CO;2-C, 10966578.
    • (2000) Proteins , vol.41 , Issue.2 , pp. 257-269
    • Harvey, A.J.1    Hrmova, M.2    De Gori, R.3    Varghese, J.N.4    Fincher, G.B.5
  • 36
    • 84866500048 scopus 로고    scopus 로고
    • Evolution, substrate specificity and subfamily classification of glycoside hydrolase family 5 (GH5)
    • 10.1186/1471-2148-12-186, 3526467, 22992189
    • Aspeborg H, Coutinho PM, Wang Y, Brumer H, Henrissat B. Evolution, substrate specificity and subfamily classification of glycoside hydrolase family 5 (GH5). BMC Evol Biol 2012, 12:186. 10.1186/1471-2148-12-186, 3526467, 22992189.
    • (2012) BMC Evol Biol , vol.12 , pp. 186
    • Aspeborg, H.1    Coutinho, P.M.2    Wang, Y.3    Brumer, H.4    Henrissat, B.5
  • 37
    • 2942565674 scopus 로고    scopus 로고
    • Insights into the molecular determinants of substrate specificity in glycoside hydrolase family 5 revealed by the crystal structure and kinetics of Cellvibrio mixtus mannosidase 5A
    • 10.1074/jbc.M401647200, 15014076
    • Dias FM, Vincent F, Pell G, Prates JA, Centeno MS, Tailford LE, Ferreira LM, Fontes CM, Davies GJ, Gilbert HJ. Insights into the molecular determinants of substrate specificity in glycoside hydrolase family 5 revealed by the crystal structure and kinetics of Cellvibrio mixtus mannosidase 5A. J Biol Chem 2004, 279(24):25517-25526. 10.1074/jbc.M401647200, 15014076.
    • (2004) J Biol Chem , vol.279 , Issue.24 , pp. 25517-25526
    • Dias, F.M.1    Vincent, F.2    Pell, G.3    Prates, J.A.4    Centeno, M.S.5    Tailford, L.E.6    Ferreira, L.M.7    Fontes, C.M.8    Davies, G.J.9    Gilbert, H.J.10
  • 38
    • 80052614037 scopus 로고    scopus 로고
    • Fungal enzyme sets for plant polysaccharide degradation
    • 10.1007/s00253-011-3473-2, 3160556, 21785931
    • van den Brink J, de Vries RP. Fungal enzyme sets for plant polysaccharide degradation. Appl Microbiol Biotechnol 2011, 91(6):1477-1492. 10.1007/s00253-011-3473-2, 3160556, 21785931.
    • (2011) Appl Microbiol Biotechnol , vol.91 , Issue.6 , pp. 1477-1492
    • Van Den Brink, J.1    De Vries, R.P.2
  • 39
    • 0034725651 scopus 로고    scopus 로고
    • Substrate specificity in glycoside hydrolase family 10. Structural and kinetic analysis of the Streptomyces lividans xylanase 10A
    • 10.1074/jbc.275.30.23020, 10930426
    • Ducros V, Charnock SJ, Derewenda U, Derewenda ZS, Dauter Z, Dupont C, Shareck F, Morosoli R, Kluepfel D, Davies GJ. Substrate specificity in glycoside hydrolase family 10. Structural and kinetic analysis of the Streptomyces lividans xylanase 10A. J Biol Chem 2000, 275(30):23020-23026. 10.1074/jbc.275.30.23020, 10930426.
    • (2000) J Biol Chem , vol.275 , Issue.30 , pp. 23020-23026
    • Ducros, V.1    Charnock, S.J.2    Derewenda, U.3    Derewenda, Z.S.4    Dauter, Z.5    Dupont, C.6    Shareck, F.7    Morosoli, R.8    Kluepfel, D.9    Davies, G.J.10
  • 40
    • 47249161669 scopus 로고    scopus 로고
    • The structure of the complex between a branched pentasaccharide and Thermobacillus xylanilyticus GH-51 arabinofuranosidase reveals xylan-binding determinants and induced fit
    • 10.1021/bi800424e, 18563919
    • Paes G, Skov LK, O'Donohue MJ, Remond C, Kastrup JS, Gajhede M, Mirza O. The structure of the complex between a branched pentasaccharide and Thermobacillus xylanilyticus GH-51 arabinofuranosidase reveals xylan-binding determinants and induced fit. Biochemistry 2008, 47(28):7441-7451. 10.1021/bi800424e, 18563919.
    • (2008) Biochemistry , vol.47 , Issue.28 , pp. 7441-7451
    • Paes, G.1    Skov, L.K.2    O'Donohue, M.J.3    Remond, C.4    Kastrup, J.S.5    Gajhede, M.6    Mirza, O.7
  • 41
    • 65649118570 scopus 로고    scopus 로고
    • Crystal structure of glycoside hydrolase family 55 β-1,3-glucanase from the basidiomycete Phanerochaete chrysosporium
    • 10.1074/jbc.M808122200, 2665064, 19193645
    • Ishida T, Fushinobu S, Kawai R, Kitaoka M, Igarashi K, Samejima M. Crystal structure of glycoside hydrolase family 55 β-1,3-glucanase from the basidiomycete Phanerochaete chrysosporium. J Biol Chem 2009, 284(15):10100-10109. 10.1074/jbc.M808122200, 2665064, 19193645.
    • (2009) J Biol Chem , vol.284 , Issue.15 , pp. 10100-10109
    • Ishida, T.1    Fushinobu, S.2    Kawai, R.3    Kitaoka, M.4    Igarashi, K.5    Samejima, M.6
  • 42
    • 35348871356 scopus 로고    scopus 로고
    • Magnaporthe grisea cutinase2 mediates appressorium differentiation and host penetration and is required for full virulence
    • Skamnioti P, Gurr SJ. Magnaporthe grisea cutinase2 mediates appressorium differentiation and host penetration and is required for full virulence. The Plant Cell Online 2007, 19(8):2674-2689.
    • (2007) The Plant Cell Online , vol.19 , Issue.8 , pp. 2674-2689
    • Skamnioti, P.1    Gurr, S.J.2
  • 43
    • 42549129802 scopus 로고    scopus 로고
    • Cutinase and hydrophobin interplay: A herald for pathogenesis?
    • 10.4161/psb.3.4.5181, 2634192, 19704644
    • Skamnioti P, Gurr SJ. Cutinase and hydrophobin interplay: A herald for pathogenesis?. Plant Signal Behav 2008, 3(4):248-250. 10.4161/psb.3.4.5181, 2634192, 19704644.
    • (2008) Plant Signal Behav , vol.3 , Issue.4 , pp. 248-250
    • Skamnioti, P.1    Gurr, S.J.2
  • 46
    • 78649748702 scopus 로고    scopus 로고
    • Pyrenophora teres: profile of an increasingly damaging barley pathogen
    • 10.1111/j.1364-3703.2010.00649.x, 21118345
    • Liu Z, Ellwood SR, Oliver RP, Friesen TL. Pyrenophora teres: profile of an increasingly damaging barley pathogen. Mol Plant Pathol 2011, 12(1):1-19. 10.1111/j.1364-3703.2010.00649.x, 21118345.
    • (2011) Mol Plant Pathol , vol.12 , Issue.1 , pp. 1-19
    • Liu, Z.1    Ellwood, S.R.2    Oliver, R.P.3    Friesen, T.L.4
  • 47
    • 36248986710 scopus 로고    scopus 로고
    • Malassezia globosa and restricta: Breakthrough Understanding of the Etiology and Treatment of Dandruff and Seborrheic Dermatitis through Whole-Genome Analysis
    • 10.1038/sj.jidsymp.5650049, 18004291
    • Dawson TL. Malassezia globosa and restricta: Breakthrough Understanding of the Etiology and Treatment of Dandruff and Seborrheic Dermatitis through Whole-Genome Analysis. J Investig Dermatol Symp Proc 2007, 12(2):15-19. 10.1038/sj.jidsymp.5650049, 18004291.
    • (2007) J Investig Dermatol Symp Proc , vol.12 , Issue.2 , pp. 15-19
    • Dawson, T.L.1
  • 48
    • 49249096419 scopus 로고    scopus 로고
    • Growth characteristics and enzyme activity in Batrachochytrium dendrobatidis isolates
    • 10.1007/s11046-008-9135-y, 18568420
    • Symonds EP, Trott DJ, Bird PS, Mills P. Growth characteristics and enzyme activity in Batrachochytrium dendrobatidis isolates. Mycopathologia 2008, 166(3):143-147. 10.1007/s11046-008-9135-y, 18568420.
    • (2008) Mycopathologia , vol.166 , Issue.3 , pp. 143-147
    • Symonds, E.P.1    Trott, D.J.2    Bird, P.S.3    Mills, P.4
  • 50
    • 0032189651 scopus 로고    scopus 로고
    • A plasma membrane-bound putative endo-1,4-beta-D-glucanase is required for normal wall assembly and cell elongation in Arabidopsis
    • 10.1093/emboj/17.19.5563, 1170885, 9755157
    • Nicol F, His I, Jauneau A, Vernhettes S, Canut H, Hofte H. A plasma membrane-bound putative endo-1,4-beta-D-glucanase is required for normal wall assembly and cell elongation in Arabidopsis. EMBO J 1998, 17(19):5563-5576. 10.1093/emboj/17.19.5563, 1170885, 9755157.
    • (1998) EMBO J , vol.17 , Issue.19 , pp. 5563-5576
    • Nicol, F.1    His, I.2    Jauneau, A.3    Vernhettes, S.4    Canut, H.5    Hofte, H.6
  • 51
    • 77951190275 scopus 로고    scopus 로고
    • Mayday-integrative analytics for expression data
    • 10.1186/1471-2105-11-121, 2848234, 20214778
    • Battke F, Symons S, Nieselt K. Mayday-integrative analytics for expression data. BMC Bioinformatics 2010, 11:121. 10.1186/1471-2105-11-121, 2848234, 20214778.
    • (2010) BMC Bioinformatics , vol.11 , pp. 121
    • Battke, F.1    Symons, S.2    Nieselt, K.3
  • 53
    • 77952988108 scopus 로고    scopus 로고
    • A new generation of homology search tools based on probabilistic inference
    • Eddy SR. A new generation of homology search tools based on probabilistic inference. Genome Inform 2009, 23(1):205-211.
    • (2009) Genome Inform , vol.23 , Issue.1 , pp. 205-211
    • Eddy, S.R.1
  • 54
    • 79959959356 scopus 로고    scopus 로고
    • T-Coffee: a web server for the multiple sequence alignment of protein and RNA sequences using structural information and homology extension
    • Web Server issue, 3125728, 21558174
    • Di Tommaso P, Moretti S, Xenarios I, Orobitg M, Montanyola A, Chang JM, Taly JF, Notredame C. T-Coffee: a web server for the multiple sequence alignment of protein and RNA sequences using structural information and homology extension. Nucleic Acids Res 2011, 39(Web Server issue):W13-W17. 3125728, 21558174.
    • (2011) Nucleic Acids Res , vol.39
    • Di Tommaso, P.1    Moretti, S.2    Xenarios, I.3    Orobitg, M.4    Montanyola, A.5    Chang, J.M.6    Taly, J.F.7    Notredame, C.8
  • 55
    • 18744382506 scopus 로고    scopus 로고
    • ProtTest: selection of best-fit models of protein evolution
    • 10.1093/bioinformatics/bti263, 15647292
    • Abascal F, Zardoya R, Posada D. ProtTest: selection of best-fit models of protein evolution. Bioinformatics 2005, 21(9):2104-2105. 10.1093/bioinformatics/bti263, 15647292.
    • (2005) Bioinformatics , vol.21 , Issue.9 , pp. 2104-2105
    • Abascal, F.1    Zardoya, R.2    Posada, D.3
  • 56
    • 81755178934 scopus 로고    scopus 로고
    • Oxidoreductive cellulose depolymerization by the enzymes cellobiose dehydrogenase and glycoside hydrolase 61
    • 10.1128/AEM.05815-11, 3187118, 21821740
    • Langston JA, Shaghasi T, Abbate E, Xu F, Vlasenko E, Sweeney MD. Oxidoreductive cellulose depolymerization by the enzymes cellobiose dehydrogenase and glycoside hydrolase 61. Appl Environ Microbiol 2011, 77(19):7007-7015. 10.1128/AEM.05815-11, 3187118, 21821740.
    • (2011) Appl Environ Microbiol , vol.77 , Issue.19 , pp. 7007-7015
    • Langston, J.A.1    Shaghasi, T.2    Abbate, E.3    Xu, F.4    Vlasenko, E.5    Sweeney, M.D.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.