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Volumn 8, Issue 2, 2013, Pages

Genomic and Secretomic Analyses Reveal Unique Features of the Lignocellulolytic Enzyme System of Penicillium decumbens

Author keywords

[No Author keywords available]

Indexed keywords

CARBOHYDRATE BINDING PROTEIN; CELLULASE; CELLULOSE 1,4 BETA CELLOBIOSIDASE; CYTOCHROME P450; FUNGAL ENZYME; GLYCOSIDASE; HEMICELLULASE; LIGNOCELLULOSE; OXIDOREDUCTASE; UNCLASSIFIED DRUG;

EID: 84873261620     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0055185     Document Type: Article
Times cited : (169)

References (98)
  • 1
    • 33744801074 scopus 로고    scopus 로고
    • The billion-ton biofuels vision
    • Somerville C, (2006) The billion-ton biofuels vision. Science 312: 1277.
    • (2006) Science , vol.312 , pp. 1277
    • Somerville, C.1
  • 3
    • 77952257725 scopus 로고    scopus 로고
    • Microbial enzyme systems for biomass conversion: emerging paradigms
    • Himmel ME, Xu Q, Luo Y, Ding SY, Lamed R, et al. (2010) Microbial enzyme systems for biomass conversion: emerging paradigms. Biofuels 1: 323-341.
    • (2010) Biofuels , vol.1 , pp. 323-341
    • Himmel, M.E.1    Xu, Q.2    Luo, Y.3    Ding, S.Y.4    Lamed, R.5
  • 5
    • 70349772781 scopus 로고    scopus 로고
    • Metabolic engineering strategies for the improvement of cellulase production by Hypocrea jecorina
    • Kubicek CP, Mikus M, Schuster A, Schmoll M, Seiboth B, (2009) Metabolic engineering strategies for the improvement of cellulase production by Hypocrea jecorina. Biotechnol Biofuels 2: 19.
    • (2009) Biotechnol Biofuels , vol.2 , pp. 19
    • Kubicek, C.P.1    Mikus, M.2    Schuster, A.3    Schmoll, M.4    Seiboth, B.5
  • 6
    • 34249809704 scopus 로고    scopus 로고
    • Optimization of enzyme complexes for lignocellulose hydrolysis
    • Berlin A, Maximenko V, Gilkes N, Saddler J, (2007) Optimization of enzyme complexes for lignocellulose hydrolysis. Biotechnol Bioeng 97: 287-296.
    • (2007) Biotechnol Bioeng , vol.97 , pp. 287-296
    • Berlin, A.1    Maximenko, V.2    Gilkes, N.3    Saddler, J.4
  • 7
    • 34548754522 scopus 로고    scopus 로고
    • Progress and challenges in enzyme development for biomass utilization
    • Merino ST, Cherry J, (2007) Progress and challenges in enzyme development for biomass utilization. Adv Biochem Eng Biotechnol 108: 95-120.
    • (2007) Adv Biochem Eng Biotechnol , vol.108 , pp. 95-120
    • Merino, S.T.1    Cherry, J.2
  • 8
    • 84864183238 scopus 로고    scopus 로고
    • Cellulases from Penicillium species for producing fuels from biomass
    • Gusakov AV, Sinitsyn AP, (2012) Cellulases from Penicillium species for producing fuels from biomass. Biofuels 3: 463-477.
    • (2012) Biofuels , vol.3 , pp. 463-477
    • Gusakov, A.V.1    Sinitsyn, A.P.2
  • 9
    • 77949873105 scopus 로고    scopus 로고
    • Status and prospect of lignocellulosic bioethanol production in China
    • Fang X, Shen Y, Zhao J, Bao X, Qu Y, (2010) Status and prospect of lignocellulosic bioethanol production in China. Bioresour Technol 101: 4814-4819.
    • (2010) Bioresour Technol , vol.101 , pp. 4814-4819
    • Fang, X.1    Shen, Y.2    Zhao, J.3    Bao, X.4    Qu, Y.5
  • 10
    • 0342828195 scopus 로고
    • Screening of catabolite repression-resistant mutants of cellulase producing Penicillium spp
    • Qu Y, Gao P, Wang Z, (1984) Screening of catabolite repression-resistant mutants of cellulase producing Penicillium spp. Acta Mycol Sinica 3: 238-243.
    • (1984) Acta Mycol Sinica , vol.3 , pp. 238-243
    • Qu, Y.1    Gao, P.2    Wang, Z.3
  • 11
    • 0026128544 scopus 로고
    • Cellulase production from spent sulfite liquor and paper-mill waste fiber
    • Qu Y, Zhao X, Gao P, Wang Z, (1991) Cellulase production from spent sulfite liquor and paper-mill waste fiber. Appl Biochem Biotechnol 28-29: 363-368.
    • (1991) Appl Biochem Biotechnol , vol.28-29 , pp. 363-368
    • Qu, Y.1    Zhao, X.2    Gao, P.3    Wang, Z.4
  • 12
    • 41849141240 scopus 로고    scopus 로고
    • Simultaneous saccharification and fermentation of acid-pretreated corncobs with a recombinant Saccharomyces cerevisiae expressing beta-glucosidase
    • Shen Y, Zhang Y, Ma T, Bao X, Du F, et al. (2008) Simultaneous saccharification and fermentation of acid-pretreated corncobs with a recombinant Saccharomyces cerevisiae expressing beta-glucosidase. Bioresour Technol 99: 5099-5103.
    • (2008) Bioresour Technol , vol.99 , pp. 5099-5103
    • Shen, Y.1    Zhang, Y.2    Ma, T.3    Bao, X.4    Du, F.5
  • 13
    • 34547828736 scopus 로고    scopus 로고
    • Biological hydrogen production from steam-exploded straw by simultaneous saccharification and fermentation
    • Li D, Chen H, (2007) Biological hydrogen production from steam-exploded straw by simultaneous saccharification and fermentation. Int J Hydrogen Energy 32: 1742-1748.
    • (2007) Int J Hydrogen Energy , vol.32 , pp. 1742-1748
    • Li, D.1    Chen, H.2
  • 14
    • 77949874241 scopus 로고    scopus 로고
    • High concentration ethanol production from corncob residues by fed-batch strategy
    • Liu K, Lin X, Yue J, Li X, Fang X, et al. (2010) High concentration ethanol production from corncob residues by fed-batch strategy. Bioresour Technol 101: 4952-4958.
    • (2010) Bioresour Technol , vol.101 , pp. 4952-4958
    • Liu, K.1    Lin, X.2    Yue, J.3    Li, X.4    Fang, X.5
  • 15
    • 39049193476 scopus 로고    scopus 로고
    • Studies on cellulosic ethanol production for sustainable supply of liquid fuel in China
    • Qu Y, Zhu M, Liu K, Bao X, Lin J, (2006) Studies on cellulosic ethanol production for sustainable supply of liquid fuel in China. Biotechnol J 1: 1235-1240.
    • (2006) Biotechnol J , vol.1 , pp. 1235-1240
    • Qu, Y.1    Zhu, M.2    Liu, K.3    Bao, X.4    Lin, J.5
  • 16
    • 33746787334 scopus 로고    scopus 로고
    • Application of enzymes in producing bleached pulp from wheat straw
    • Zhao J, Li X, Qu Y, (2006) Application of enzymes in producing bleached pulp from wheat straw. Bioresour Technol 97: 1470-1476.
    • (2006) Bioresour Technol , vol.97 , pp. 1470-1476
    • Zhao, J.1    Li, X.2    Qu, Y.3
  • 17
    • 78149409173 scopus 로고    scopus 로고
    • Enzyme-assisted extraction of flavonoids from Ginkgo biloba leaves: improvement effect of flavonol transglycosylation catalyzed by Penicillium decumbens cellulase
    • Chen S, Xing XH, Huang JJ, Xu MS, (2011) Enzyme-assisted extraction of flavonoids from Ginkgo biloba leaves: improvement effect of flavonol transglycosylation catalyzed by Penicillium decumbens cellulase. Enzyme Microb Technol 48: 100-105.
    • (2011) Enzyme Microb Technol , vol.48 , pp. 100-105
    • Chen, S.1    Xing, X.H.2    Huang, J.J.3    Xu, M.S.4
  • 18
    • 84860859607 scopus 로고    scopus 로고
    • N-glycoform diversity of cellobiohydrolase I from Penicillium decumbens and the synergism of a nonhydrolytic glycoform in cellulose degradation
    • Gao L, Gao F, Wang L, Geng C, Chi L, et al. (2012) N-glycoform diversity of cellobiohydrolase I from Penicillium decumbens and the synergism of a nonhydrolytic glycoform in cellulose degradation. J Biol Chem 287: 15906-15915.
    • (2012) J Biol Chem , vol.287 , pp. 15906-15915
    • Gao, L.1    Gao, F.2    Wang, L.3    Geng, C.4    Chi, L.5
  • 19
    • 79960846488 scopus 로고    scopus 로고
    • Purification and characterization of a novel cellobiohydrolase (PdCel6A) from Penicillium decumbens JU-A10 for bioethanol production
    • Gao L, Wang F, Gao F, Wang L, Zhao J, et al. (2011) Purification and characterization of a novel cellobiohydrolase (PdCel6A) from Penicillium decumbens JU-A10 for bioethanol production. Bioresour Technol 102: 8339-8342.
    • (2011) Bioresour Technol , vol.102 , pp. 8339-8342
    • Gao, L.1    Wang, F.2    Gao, F.3    Wang, L.4    Zhao, J.5
  • 20
    • 36248949932 scopus 로고
    • Studies on cellulase system from Penicillium decumbens
    • Qu Y, Gao P, Wang Z, (1988) Studies on cellulase system from Penicillium decumbens. Acta Microbiol Sin 28: 121-130.
    • (1988) Acta Microbiol Sin , vol.28 , pp. 121-130
    • Qu, Y.1    Gao, P.2    Wang, Z.3
  • 21
    • 77954708183 scopus 로고    scopus 로고
    • Characterization of the endoglucanase and glucomannanase activities of a glycoside hydrolase family 45 protein from Penicillium decumbens 114-2
    • Liu G, Wei X, Qin Y, Qu Y, (2010) Characterization of the endoglucanase and glucomannanase activities of a glycoside hydrolase family 45 protein from Penicillium decumbens 114-2. J Gen Appl Microbiol 56: 223-229.
    • (2010) J Gen Appl Microbiol , vol.56 , pp. 223-229
    • Liu, G.1    Wei, X.2    Qin, Y.3    Qu, Y.4
  • 22
    • 77649227915 scopus 로고    scopus 로고
    • Molecular cloning and characterization of two major endoglucanases from Penicillium decumbens
    • Wei X, Qin Y, Qu Y, (2010) Molecular cloning and characterization of two major endoglucanases from Penicillium decumbens. J Microbiol Biotechnol 20: 265-270.
    • (2010) J Microbiol Biotechnol , vol.20 , pp. 265-270
    • Wei, X.1    Qin, Y.2    Qu, Y.3
  • 23
    • 80051801763 scopus 로고    scopus 로고
    • Improvement of cellulase activity in Trichoderma reesei by heterologous expression of a beta-glucosidase gene from Penicillium decumbens
    • Ma L, Zhang J, Zou G, Wang C, Zhou Z, (2011) Improvement of cellulase activity in Trichoderma reesei by heterologous expression of a beta-glucosidase gene from Penicillium decumbens. Enzyme Microb Technol 49: 366-371.
    • (2011) Enzyme Microb Technol , vol.49 , pp. 366-371
    • Ma, L.1    Zhang, J.2    Zou, G.3    Wang, C.4    Zhou, Z.5
  • 24
    • 28844461287 scopus 로고    scopus 로고
    • Sequencing of Aspergillus nidulans and comparative analysis with A. fumigatus and A. oryzae
    • Galagan JE, Calvo SE, Cuomo C, Ma LJ, Wortman JR, et al. (2005) Sequencing of Aspergillus nidulans and comparative analysis with A. fumigatus and A. oryzae. Nature 438: 1105-1115.
    • (2005) Nature , vol.438 , pp. 1105-1115
    • Galagan, J.E.1    Calvo, S.E.2    Cuomo, C.3    Ma, L.J.4    Wortman, J.R.5
  • 25
    • 79957958102 scopus 로고    scopus 로고
    • Comparative genomics of citric-acid-producing Aspergillus niger ATCC 1015 versus enzyme-producing CBS 513.88
    • Andersen MR, Salazar MP, Schaap PJ, van de Vondervoort PJ, Culley D, et al. (2011) Comparative genomics of citric-acid-producing Aspergillus niger ATCC 1015 versus enzyme-producing CBS 513.88. Genome Res 21: 885-897.
    • (2011) Genome Res , vol.21 , pp. 885-897
    • Andersen, M.R.1    Salazar, M.P.2    Schaap, P.J.3    van de Vondervoort, P.J.4    Culley, D.5
  • 26
    • 0027135227 scopus 로고
    • Resolution of four large chromosomes in penicillin-producing filamentous fungi: the penicillin gene cluster is located on chromosome II (9.6 Mb) in Penicillium notatum and chromosome I (10.4 Mb) in Penicillium chrysogenum
    • Fierro F, Gutierrez S, Diez B, Martin JF, (1993) Resolution of four large chromosomes in penicillin-producing filamentous fungi: the penicillin gene cluster is located on chromosome II (9.6 Mb) in Penicillium notatum and chromosome I (10.4 Mb) in Penicillium chrysogenum. Mol Gen Genet 241: 573-578.
    • (1993) Mol Gen Genet , vol.241 , pp. 573-578
    • Fierro, F.1    Gutierrez, S.2    Diez, B.3    Martin, J.F.4
  • 28
    • 53649092922 scopus 로고    scopus 로고
    • Genome sequencing and analysis of the filamentous fungus Penicillium chrysogenum
    • van den Berg MA, Albang R, Albermann K, Badger JH, Daran JM, et al. (2008) Genome sequencing and analysis of the filamentous fungus Penicillium chrysogenum. Nat Biotechnol 26: 1161-1168.
    • (2008) Nat Biotechnol , vol.26 , pp. 1161-1168
    • van den Berg, M.A.1    Albang, R.2    Albermann, K.3    Badger, J.H.4    Daran, J.M.5
  • 30
    • 58249085751 scopus 로고    scopus 로고
    • Lignocellulosic residues: biodegradation and bioconversion by fungi
    • Sánchez C, (2009) Lignocellulosic residues: biodegradation and bioconversion by fungi. Biotechnol Adv 27: 185-194.
    • (2009) Biotechnol Adv , vol.27 , pp. 185-194
    • Sánchez, C.1
  • 32
    • 84055197660 scopus 로고    scopus 로고
    • Cellobiose dehydrogenase and a copper-dependent polysaccharide monooxygenase potentiate cellulose degradation by Neurospora crassa
    • Phillips CM, Beeson WT, Cate JH, Marletta MA, (2011) Cellobiose dehydrogenase and a copper-dependent polysaccharide monooxygenase potentiate cellulose degradation by Neurospora crassa. ACS Chem Biol 6: 1399-1406.
    • (2011) ACS Chem Biol , vol.6 , pp. 1399-1406
    • Phillips, C.M.1    Beeson, W.T.2    Cate, J.H.3    Marletta, M.A.4
  • 33
    • 77950341230 scopus 로고    scopus 로고
    • Isolation and characterization of a beta-glucosidase from Penicillium decumbens and improving hydrolysis of corncob residue by using it as cellulase supplementation
    • Chen M, Qin Y, Liu Z, Liu K, Wang F, et al. (2010) Isolation and characterization of a beta-glucosidase from Penicillium decumbens and improving hydrolysis of corncob residue by using it as cellulase supplementation. Enzyme Microb Technol 46: 444-449.
    • (2010) Enzyme Microb Technol , vol.46 , pp. 444-449
    • Chen, M.1    Qin, Y.2    Liu, Z.3    Liu, K.4    Wang, F.5
  • 34
    • 43449098828 scopus 로고    scopus 로고
    • Genome sequencing and analysis of the biomass-degrading fungus Trichoderma reesei (syn. Hypocrea jecorina)
    • Martinez D, Berka RM, Henrissat B, Saloheimo M, Arvas M, et al. (2008) Genome sequencing and analysis of the biomass-degrading fungus Trichoderma reesei (syn. Hypocrea jecorina). Nat Biotechnol 26: 553-560.
    • (2008) Nat Biotechnol , vol.26 , pp. 553-560
    • Martinez, D.1    Berka, R.M.2    Henrissat, B.3    Saloheimo, M.4    Arvas, M.5
  • 35
    • 33745194828 scopus 로고    scopus 로고
    • Enzymatic saccharification of wheat straw for bioethanol production by a combined cellulase xylanase and feruloyl esterase treatment
    • Tabka MG, Herpoel-Gimbert I, Monod F, Asther M, Sigoillot JC, (2006) Enzymatic saccharification of wheat straw for bioethanol production by a combined cellulase xylanase and feruloyl esterase treatment. Enzyme Microb Technol 39: 897-902.
    • (2006) Enzyme Microb Technol , vol.39 , pp. 897-902
    • Tabka, M.G.1    Herpoel-Gimbert, I.2    Monod, F.3    Asther, M.4    Sigoillot, J.C.5
  • 36
    • 34547134972 scopus 로고    scopus 로고
    • Characterization and three-dimensional structures of two distinct bacterial xyloglucanases from families GH5 and GH12
    • Gloster TM, Ibatullin FM, Macauley K, Eklof JM, Roberts S, et al. (2007) Characterization and three-dimensional structures of two distinct bacterial xyloglucanases from families GH5 and GH12. J Biol Chem 282: 19177-19189.
    • (2007) J Biol Chem , vol.282 , pp. 19177-19189
    • Gloster, T.M.1    Ibatullin, F.M.2    Macauley, K.3    Eklof, J.M.4    Roberts, S.5
  • 37
    • 80054733932 scopus 로고    scopus 로고
    • Comparative genomic analysis of the thermophilic biomass-degrading fungi Myceliophthora thermophila and Thielavia terrestris
    • Berka RM, Grigoriev IV, Otillar R, Salamov A, Grimwood J, et al. (2011) Comparative genomic analysis of the thermophilic biomass-degrading fungi Myceliophthora thermophila and Thielavia terrestris. Nat Biotechnol 29: 922-927.
    • (2011) Nat Biotechnol , vol.29 , pp. 922-927
    • Berka, R.M.1    Grigoriev, I.V.2    Otillar, R.3    Salamov, A.4    Grimwood, J.5
  • 38
    • 0026952339 scopus 로고
    • Synergism between Clostridium Thermocellum cellulases cloned in Escherichia coli
    • Tcika K, Zverlov VV, Velikodvorskaya GA, (1992) Synergism between Clostridium Thermocellum cellulases cloned in Escherichia coli. Appl Biochem Biotechnol 37: 201-207.
    • (1992) Appl Biochem Biotechnol , vol.37 , pp. 201-207
    • Tcika, K.1    Zverlov, V.V.2    Velikodvorskaya, G.A.3
  • 39
    • 84892291444 scopus 로고    scopus 로고
    • Xylanases: molecular properties and applications
    • In: Polaina J, MacCabe AP, editors, Dordrecht, The Netherlands: Springer
    • Javier PFI, Oscar G, Sanz-Aparicio J, Diaz P (2007) Xylanases: molecular properties and applications. In: Polaina J, MacCabe AP, editors. Industrial Enzymes. Dordrecht, The Netherlands: Springer. 65-82.
    • (2007) Industrial Enzymes , pp. 65-82
    • Javier, P.F.I.1    Oscar, G.2    Sanz-Aparicio, J.3    Diaz, P.4
  • 40
    • 0029824486 scopus 로고    scopus 로고
    • Evidence that linker sequences and cellulose-binding domains enhance the activity of hemicellulases against complex substrates
    • Black GW, Rixon JE, Clarke JH, Hazlewood GP, Theodorou MK, et al. (1996) Evidence that linker sequences and cellulose-binding domains enhance the activity of hemicellulases against complex substrates. Biochem J 319: 515-520.
    • (1996) Biochem J , vol.319 , pp. 515-520
    • Black, G.W.1    Rixon, J.E.2    Clarke, J.H.3    Hazlewood, G.P.4    Theodorou, M.K.5
  • 41
    • 80051781820 scopus 로고    scopus 로고
    • Development of a mature fungal technology and production platform for industrial enzymes based on a Myceliophthora thermophila isolate, previously known as Chrysosporium lucknowense C1
    • Visser H, Joosten V, Punt PJ, Gusakov AV, Olson PT, et al. (2011) Development of a mature fungal technology and production platform for industrial enzymes based on a Myceliophthora thermophila isolate, previously known as Chrysosporium lucknowense C1. Ind Biotechnol 7: 214-223.
    • (2011) Ind Biotechnol , vol.7 , pp. 214-223
    • Visser, H.1    Joosten, V.2    Punt, P.J.3    Gusakov, A.V.4    Olson, P.T.5
  • 42
    • 0036046037 scopus 로고    scopus 로고
    • Swollenin, a Trichoderma reesei protein with sequence similarity to the plant expansins, exhibits disruption activity on cellulosic materials
    • Saloheimo M, Paloheimo M, Hakola S, Pere J, Swanson B, et al. (2002) Swollenin, a Trichoderma reesei protein with sequence similarity to the plant expansins, exhibits disruption activity on cellulosic materials. Eur J Biochem 269: 4202-4211.
    • (2002) Eur J Biochem , vol.269 , pp. 4202-4211
    • Saloheimo, M.1    Paloheimo, M.2    Hakola, S.3    Pere, J.4    Swanson, B.5
  • 43
    • 61649097078 scopus 로고    scopus 로고
    • Telomere organization in the ligninolytic basidiomycete Pleurotus ostreatus
    • Pérez G, Pangilinan J, Pisabarro AG, Ramírez L, (2009) Telomere organization in the ligninolytic basidiomycete Pleurotus ostreatus. Appl Environ Microbiol 75: 1427-1436.
    • (2009) Appl Environ Microbiol , vol.75 , pp. 1427-1436
    • Pérez, G.1    Pangilinan, J.2    Pisabarro, A.G.3    Ramírez, L.4
  • 44
    • 42749096854 scopus 로고    scopus 로고
    • The composition of basal and induced cellulase systems in Penicillium decumbens under induction or repression conditions
    • Sun X, Liu Z, Zheng K, Song X, Qu Y, (2008) The composition of basal and induced cellulase systems in Penicillium decumbens under induction or repression conditions. Enzyme Microb Technol 42: 560-567.
    • (2008) Enzyme Microb Technol , vol.42 , pp. 560-567
    • Sun, X.1    Liu, Z.2    Zheng, K.3    Song, X.4    Qu, Y.5
  • 45
    • 80955158564 scopus 로고    scopus 로고
    • Transcription analysis of lignocellulolytic enzymes of Penicillium decumbens 114-2 and its catabolite-repression-resistant mutant
    • Wei X, Zheng K, Chen M, Liu G, Li J, et al. (2011) Transcription analysis of lignocellulolytic enzymes of Penicillium decumbens 114-2 and its catabolite-repression-resistant mutant. C R Biol 334: 806-811.
    • (2011) C R Biol , vol.334 , pp. 806-811
    • Wei, X.1    Zheng, K.2    Chen, M.3    Liu, G.4    Li, J.5
  • 46
    • 0033609898 scopus 로고    scopus 로고
    • Purification, characterization, and amino acid sequence of cerato-platanin, a new phytotoxic protein from Ceratocystis fimbriata f. sp. platani
    • Pazzagli L, Cappugi G, Manao G, Camici G, Santini A, et al. (1999) Purification, characterization, and amino acid sequence of cerato-platanin, a new phytotoxic protein from Ceratocystis fimbriata f. sp. platani. J Biol Chem 274: 24959-24964.
    • (1999) J Biol Chem , vol.274 , pp. 24959-24964
    • Pazzagli, L.1    Cappugi, G.2    Manao, G.3    Camici, G.4    Santini, A.5
  • 47
    • 60649098811 scopus 로고    scopus 로고
    • Comparative secretome analyses of two Trichoderma reesei RUT-C30 and CL847 hypersecretory strains
    • Herpoel-Gimbert I, Margeot A, Dolla A, Jan G, Molle D, et al. (2008) Comparative secretome analyses of two Trichoderma reesei RUT-C30 and CL847 hypersecretory strains. Biotechnol Biofuels 1: 18.
    • (2008) Biotechnol Biofuels , vol.1 , pp. 18
    • Herpoel-Gimbert, I.1    Margeot, A.2    Dolla, A.3    Jan, G.4    Molle, D.5
  • 48
    • 79251613225 scopus 로고    scopus 로고
    • Podospora anserina hemicellulases potentiate the Trichoderma reesei secretome for saccharification of lignocellulosic biomass
    • Couturier M, Haon M, Coutinho PM, Henrissat B, Lesage-Meessen L, et al. (2011) Podospora anserina hemicellulases potentiate the Trichoderma reesei secretome for saccharification of lignocellulosic biomass. Appl Environ Microbiol 77: 237-246.
    • (2011) Appl Environ Microbiol , vol.77 , pp. 237-246
    • Couturier, M.1    Haon, M.2    Coutinho, P.M.3    Henrissat, B.4    Lesage-Meessen, L.5
  • 49
    • 23744496272 scopus 로고    scopus 로고
    • Transcriptional regulation of plant cell wall degradation by filamentous fungi
    • Aro N, Pakula T, Penttila M, (2005) Transcriptional regulation of plant cell wall degradation by filamentous fungi. FEMS Microbiol Rev 29: 719-739.
    • (2005) FEMS Microbiol Rev , vol.29 , pp. 719-739
    • Aro, N.1    Pakula, T.2    Penttila, M.3
  • 50
    • 77955665245 scopus 로고    scopus 로고
    • Development of a highly efficient gene targeting system allowing rapid genetic manipulations in Penicillium decumbens
    • Li ZH, Du CM, Zhong YH, Wang TH, (2010) Development of a highly efficient gene targeting system allowing rapid genetic manipulations in Penicillium decumbens. Appl Microbiol Biotechnol 87: 1065-1076.
    • (2010) Appl Microbiol Biotechnol , vol.87 , pp. 1065-1076
    • Li, Z.H.1    Du, C.M.2    Zhong, Y.H.3    Wang, T.H.4
  • 51
    • 72849145046 scopus 로고    scopus 로고
    • Genome shuffling improves production of cellulase by Penicillium decumbens JU-A10
    • Cheng Y, Song X, Qin Y, Qu Y, (2009) Genome shuffling improves production of cellulase by Penicillium decumbens JU-A10. J Appl Microbiol 107: 1837-1846.
    • (2009) J Appl Microbiol , vol.107 , pp. 1837-1846
    • Cheng, Y.1    Song, X.2    Qin, Y.3    Qu, Y.4
  • 52
    • 24044455869 scopus 로고    scopus 로고
    • Genome sequencing in microfabricated high-density picolitre reactors
    • Margulies M, Egholm M, Altman WE, Attiya S, Bader JS, et al. (2005) Genome sequencing in microfabricated high-density picolitre reactors. Nature 437: 376-380.
    • (2005) Nature , vol.437 , pp. 376-380
    • Margulies, M.1    Egholm, M.2    Altman, W.E.3    Attiya, S.4    Bader, J.S.5
  • 54
    • 42949139823 scopus 로고    scopus 로고
    • A scaffold analysis tool using mate-pair information in genome sequencing
    • Kim PG, Cho HG, Park K, (2008) A scaffold analysis tool using mate-pair information in genome sequencing. J Biomed Biotechnol 2008: 675741.
    • (2008) J Biomed Biotechnol , vol.2008 , pp. 675741
    • Kim, P.G.1    Cho, H.G.2    Park, K.3
  • 56
    • 3042631307 scopus 로고    scopus 로고
    • Genome sequence assembly using trace signals and additional sequence information
    • Available
    • Chevreux B, Wetter T, Suhai S. (1999) Genome sequence assembly using trace signals and additional sequence information. German Conference on Bioinformatics. Available: http://www.bioinfo.de/isb/gcb99/talks/chevreux/main.html. Accessed 15 September 2011.
    • (1999) German Conference on Bioinformatics
    • Chevreux, B.1    Wetter, T.2    Suhai, S.3
  • 58
    • 40049091292 scopus 로고    scopus 로고
    • Using native and syntenically mapped cDNA alignments to improve de novo gene finding
    • Stanke M, Diekhans M, Baertsch R, Haussler D, (2008) Using native and syntenically mapped cDNA alignments to improve de novo gene finding. Bioinformatics 24: 637-644.
    • (2008) Bioinformatics , vol.24 , pp. 637-644
    • Stanke, M.1    Diekhans, M.2    Baertsch, R.3    Haussler, D.4
  • 59
    • 57149099395 scopus 로고    scopus 로고
    • Gene prediction in novel fungal genomes using an ab initio algorithm with unsupervised training
    • Ter-Hovhannisyan V, Lomsadze A, Chernoff YO, Borodovsky M, (2008) Gene prediction in novel fungal genomes using an ab initio algorithm with unsupervised training. Genome Res 18: 1979-1990.
    • (2008) Genome Res , vol.18 , pp. 1979-1990
    • Ter-Hovhannisyan, V.1    Lomsadze, A.2    Chernoff, Y.O.3    Borodovsky, M.4
  • 60
    • 77951238625 scopus 로고    scopus 로고
    • Using geneid to identify genes
    • In: Baxevanis AD, Davison DB, Page RDM, Petsko GA, Stein LD, Stormo GD, editors, New York: John Wiley & Sons. Chapter 4: Unit 4.3
    • Blanco E, Parra G, Guigó R (2007) Using geneid to identify genes. In: Baxevanis AD, Davison DB, Page RDM, Petsko GA, Stein LD, Stormo GD, editors. Current Protocols in Bioinformatics. New York: John Wiley & Sons. Chapter 4: Unit 4.3.
    • (2007) Current Protocols in Bioinformatics
    • Blanco, E.1    Parra, G.2    Guigó, R.3
  • 61
    • 0034065724 scopus 로고    scopus 로고
    • Ab initio gene finding in Drosophila genomic DNA
    • Salamov AA, Solovyev VV, (2000) Ab initio gene finding in Drosophila genomic DNA. Genome Res 10: 516-522.
    • (2000) Genome Res , vol.10 , pp. 516-522
    • Salamov, A.A.1    Solovyev, V.V.2
  • 63
    • 75849153303 scopus 로고    scopus 로고
    • The Universal Protein Resource (UniProt) in 2010
    • Consortium U, (2010) The Universal Protein Resource (UniProt) in 2010. Nucleic Acids Res 38: D142-148.
    • (2010) Nucleic Acids Res , vol.38
    • Consortium, U.1
  • 64
    • 75549090213 scopus 로고    scopus 로고
    • KEGG for representation and analysis of molecular networks involving diseases and drugs
    • Kanehisa M, Goto S, Furumichi M, Tanabe M, Hirakawa M, (2010) KEGG for representation and analysis of molecular networks involving diseases and drugs. Nucleic Acids Res 38: D355-360.
    • (2010) Nucleic Acids Res , vol.38
    • Kanehisa, M.1    Goto, S.2    Furumichi, M.3    Tanabe, M.4    Hirakawa, M.5
  • 65
    • 0037250152 scopus 로고    scopus 로고
    • STRING: a database of predicted functional associations between proteins
    • von Mering C, Huynen M, Jaeggi D, Schmidt S, Bork P, et al. (2003) STRING: a database of predicted functional associations between proteins. Nucleic Acids Res 31: 258-261.
    • (2003) Nucleic Acids Res , vol.31 , pp. 258-261
    • von Mering, C.1    Huynen, M.2    Jaeggi, D.3    Schmidt, S.4    Bork, P.5
  • 67
    • 0035798406 scopus 로고    scopus 로고
    • Assignment of homology to genome sequences using a library of hidden Markov models that represent all proteins of known structure
    • Gough J, Karplus K, Hughey R, Chothia C, (2001) Assignment of homology to genome sequences using a library of hidden Markov models that represent all proteins of known structure. J Mol Biol 313: 903-919.
    • (2001) J Mol Biol , vol.313 , pp. 903-919
    • Gough, J.1    Karplus, K.2    Hughey, R.3    Chothia, C.4
  • 68
    • 58149194624 scopus 로고    scopus 로고
    • SMART 6: recent updates and new developments
    • Letunic I, Doerks T, Bork P, (2009) SMART 6: recent updates and new developments. Nucleic Acids Res 37: D229-232.
    • (2009) Nucleic Acids Res , vol.37
    • Letunic, I.1    Doerks, T.2    Bork, P.3
  • 70
    • 0031743421 scopus 로고    scopus 로고
    • Profile hidden Markov models
    • Eddy SR, (1998) Profile hidden Markov models. Bioinformatics 14: 755-763.
    • (1998) Bioinformatics , vol.14 , pp. 755-763
    • Eddy, S.R.1
  • 72
    • 43949138227 scopus 로고    scopus 로고
    • Blast2GO: A comprehensive suite for functional analysis in plant genomics
    • Conesa A, Gotz S, (2008) Blast2GO: A comprehensive suite for functional analysis in plant genomics. Int J Plant Genomics 2008: 619832.
    • (2008) Int J Plant Genomics , vol.2008 , pp. 619832
    • Conesa, A.1    Gotz, S.2
  • 73
    • 84858602406 scopus 로고    scopus 로고
    • InterPro in 2011: new developments in the family and domain prediction database
    • Hunter S, Jones P, Mitchell A, Apweiler R, Attwood TK, et al. (2012) InterPro in 2011: new developments in the family and domain prediction database. Nucleic Acids Res 40: D306-312.
    • (2012) Nucleic Acids Res , vol.40
    • Hunter, S.1    Jones, P.2    Mitchell, A.3    Apweiler, R.4    Attwood, T.K.5
  • 74
    • 0038011429 scopus 로고    scopus 로고
    • Phosphoregulators: protein kinases and protein phosphatases of mouse
    • Forrest AR, Ravasi T, Taylor D, Huber T, Hume DA, et al. (2003) Phosphoregulators: protein kinases and protein phosphatases of mouse. Genome Res 13: 1443-1454.
    • (2003) Genome Res , vol.13 , pp. 1443-1454
    • Forrest, A.R.1    Ravasi, T.2    Taylor, D.3    Huber, T.4    Hume, D.A.5
  • 75
    • 41349093546 scopus 로고    scopus 로고
    • FTFD: an informatics pipeline supporting phylogenomic analysis of fungal transcription factors
    • Park J, Jang S, Kim S, Kong S, Choi J, et al. (2008) FTFD: an informatics pipeline supporting phylogenomic analysis of fungal transcription factors. Bioinformatics 24: 1024-1025.
    • (2008) Bioinformatics , vol.24 , pp. 1024-1025
    • Park, J.1    Jang, S.2    Kim, S.3    Kong, S.4    Choi, J.5
  • 79
    • 33846861493 scopus 로고    scopus 로고
    • Genome sequencing and analysis of the versatile cell factory Aspergillus niger CBS 513.88
    • Pel HJ, de Winde JH, Archer DB, Dyer PS, Hofmann G, et al. (2007) Genome sequencing and analysis of the versatile cell factory Aspergillus niger CBS 513.88. Nat Biotechnol 25: 221-231.
    • (2007) Nat Biotechnol , vol.25 , pp. 221-231
    • Pel, H.J.1    de Winde, J.H.2    Archer, D.B.3    Dyer, P.S.4    Hofmann, G.5
  • 80
    • 0141519279 scopus 로고    scopus 로고
    • OrthoMCL: identification of ortholog groups for eukaryotic genomes
    • Li L, Stoeckert CJ Jr, Roos DS, (2003) OrthoMCL: identification of ortholog groups for eukaryotic genomes. Genome Res 13: 2178-2189.
    • (2003) Genome Res , vol.13 , pp. 2178-2189
    • Li, L.1    Stoeckert Jr., C.J.2    Roos, D.S.3
  • 82
    • 34547489084 scopus 로고    scopus 로고
    • Improvement of phylogenies after removing divergent and ambiguously aligned blocks from protein sequence alignments
    • Talavera G, Castresana J, (2007) Improvement of phylogenies after removing divergent and ambiguously aligned blocks from protein sequence alignments. Syst Biol 56: 564-577.
    • (2007) Syst Biol , vol.56 , pp. 564-577
    • Talavera, G.1    Castresana, J.2
  • 83
    • 0036205377 scopus 로고    scopus 로고
    • TREE-PUZZLE: maximum likelihood phylogenetic analysis using quartets and parallel computing
    • Schmidt HA, Strimmer K, Vingron M, von Haeseler A, (2002) TREE-PUZZLE: maximum likelihood phylogenetic analysis using quartets and parallel computing. Bioinformatics 18: 502-504.
    • (2002) Bioinformatics , vol.18 , pp. 502-504
    • Schmidt, H.A.1    Strimmer, K.2    Vingron, M.3    von Haeseler, A.4
  • 84
    • 0036134748 scopus 로고    scopus 로고
    • Estimating amino acid substitution models: a comparison of Dayhoff's estimator, the resolvent approach and a maximum likelihood method
    • Muller T, Spang R, Vingron M, (2002) Estimating amino acid substitution models: a comparison of Dayhoff's estimator, the resolvent approach and a maximum likelihood method. Mol Biol Evol 19: 8-13.
    • (2002) Mol Biol Evol , vol.19 , pp. 8-13
    • Muller, T.1    Spang, R.2    Vingron, M.3
  • 85
    • 79957613599 scopus 로고    scopus 로고
    • MEGA5: molecular evolutionary genetics analysis using maximum likelihood, evolutionary distance, and maximum parsimony methods
    • Tamura K, Peterson D, Peterson N, Stecher G, Nei M, et al. (2011) MEGA5: molecular evolutionary genetics analysis using maximum likelihood, evolutionary distance, and maximum parsimony methods. Mol Biol Evol 28: 2731-2739.
    • (2011) Mol Biol Evol , vol.28 , pp. 2731-2739
    • Tamura, K.1    Peterson, D.2    Peterson, N.3    Stecher, G.4    Nei, M.5
  • 86
    • 49349118093 scopus 로고    scopus 로고
    • The effects of wheat bran composition on the production of biomass-hydrolyzing enzymes by Penicillium decumbens
    • Sun X, Liu Z, Qu Y, Li X, (2008) The effects of wheat bran composition on the production of biomass-hydrolyzing enzymes by Penicillium decumbens. Appl Biochem Biotechnol 146: 119-128.
    • (2008) Appl Biochem Biotechnol , vol.146 , pp. 119-128
    • Sun, X.1    Liu, Z.2    Qu, Y.3    Li, X.4
  • 87
    • 0031962771 scopus 로고    scopus 로고
    • Isolation and analysis of xlnR, encoding a transcriptional activator co-ordinating xylanolytic expression in Aspergillus niger
    • van Peij NN, Visser J, de Graaff LH, (1998) Isolation and analysis of xlnR, encoding a transcriptional activator co-ordinating xylanolytic expression in Aspergillus niger. Mol Microbiol 27: 131-142.
    • (1998) Mol Microbiol , vol.27 , pp. 131-142
    • van Peij, N.N.1    Visser, J.2    de Graaff, L.H.3
  • 88
    • 0035968258 scopus 로고    scopus 로고
    • ACEII, a novel transcriptional activator involved in regulation of cellulase and xylanase genes of Trichoderma reesei
    • Aro N, Saloheimo A, Ilmen M, Penttila M, (2001) ACEII, a novel transcriptional activator involved in regulation of cellulase and xylanase genes of Trichoderma reesei. J Biol Chem 276: 24309-24314.
    • (2001) J Biol Chem , vol.276 , pp. 24309-24314
    • Aro, N.1    Saloheimo, A.2    Ilmen, M.3    Penttila, M.4
  • 89
    • 84860805742 scopus 로고    scopus 로고
    • Conserved and essential transcription factors for cellulase gene expression in ascomycete fungi
    • Coradetti ST, Craig JP, Xiong Y, Shock T, Tian C, et al. (2012) Conserved and essential transcription factors for cellulase gene expression in ascomycete fungi. Proc Natl Acad Sci U S A 109: 7397-7402.
    • (2012) Proc Natl Acad Sci U S A , vol.109 , pp. 7397-7402
    • Coradetti, S.T.1    Craig, J.P.2    Xiong, Y.3    Shock, T.4    Tian, C.5
  • 90
    • 84874116514 scopus 로고    scopus 로고
    • A novel transcriptional regulator, ClbR, controls the cellobiose- and cellulose-responsive induction of cellulase and xylanase genes regulated by two distinct signaling pathways in Aspergillus aculeatus
    • DOI: 10.1007/s00253-012-4305-8
    • Kunitake E, Tani S, Sumitani JI, Kawaguchi T (2012) A novel transcriptional regulator, ClbR, controls the cellobiose- and cellulose-responsive induction of cellulase and xylanase genes regulated by two distinct signaling pathways in Aspergillus aculeatus. Appl Microbiol Biotechnol DOI: 10.1007/s00253-012-4305-8.
    • (2012) Appl Microbiol Biotechnol
    • Kunitake, E.1    Tani, S.2    Sumitani, J.I.3    Kawaguchi, T.4
  • 91
    • 0036431922 scopus 로고    scopus 로고
    • Regulation by carbon and nitrogen sources of a family of cellulases in Aspergillus nidulans
    • Lockington RA, Rodbourn L, Barnett S, Carter CJ, Kelly JM, (2002) Regulation by carbon and nitrogen sources of a family of cellulases in Aspergillus nidulans. Fungal Genet Biol 37: 190-196.
    • (2002) Fungal Genet Biol , vol.37 , pp. 190-196
    • Lockington, R.A.1    Rodbourn, L.2    Barnett, S.3    Carter, C.J.4    Kelly, J.M.5
  • 92
    • 0030036051 scopus 로고    scopus 로고
    • The glucose repressor gene cre1 of Trichoderma: isolation and expression of a full-length and a truncated mutant form
    • Ilmen M, Thrane C, Penttila M, (1996) The glucose repressor gene cre1 of Trichoderma: isolation and expression of a full-length and a truncated mutant form. Mol Gen Genet 251: 451-460.
    • (1996) Mol Gen Genet , vol.251 , pp. 451-460
    • Ilmen, M.1    Thrane, C.2    Penttila, M.3
  • 93
    • 0034102428 scopus 로고    scopus 로고
    • Isolation of the ace1 gene encoding a Cys(2)-His(2) transcription factor involved in regulation of activity of the cellulase promoter cbh1 of Trichoderma reesei
    • Saloheimo A, Aro N, Ilmen M, Penttila M, (2000) Isolation of the ace1 gene encoding a Cys(2)-His(2) transcription factor involved in regulation of activity of the cellulase promoter cbh1 of Trichoderma reesei. J Biol Chem 275: 5817-5825.
    • (2000) J Biol Chem , vol.275 , pp. 5817-5825
    • Saloheimo, A.1    Aro, N.2    Ilmen, M.3    Penttila, M.4
  • 94
    • 0031935479 scopus 로고    scopus 로고
    • Opposite patterns of expression of two Aspergillus nidulans xylanase genes with respect to ambient pH
    • MacCabe AP, Orejas M, Perez-Gonzalez JA, Ramon D, (1998) Opposite patterns of expression of two Aspergillus nidulans xylanase genes with respect to ambient pH. J Bacteriol 180: 1331-1333.
    • (1998) J Bacteriol , vol.180 , pp. 1331-1333
    • MacCabe, A.P.1    Orejas, M.2    Perez-Gonzalez, J.A.3    Ramon, D.4
  • 95
    • 0034887339 scopus 로고    scopus 로고
    • The Hypocrea jecorina HAP 2/3/5 protein complex binds to the inverted CCAAT-box (ATTGG) within the cbh2 (cellobiohydrolase II-gene) activating element
    • Zeilinger S, Ebner A, Marosits T, Mach R, Kubicek CP, (2001) The Hypocrea jecorina HAP 2/3/5 protein complex binds to the inverted CCAAT-box (ATTGG) within the cbh2 (cellobiohydrolase II-gene) activating element. Mol Genet Genomics 266: 56-63.
    • (2001) Mol Genet Genomics , vol.266 , pp. 56-63
    • Zeilinger, S.1    Ebner, A.2    Marosits, T.3    Mach, R.4    Kubicek, C.P.5
  • 97
    • 78349299471 scopus 로고    scopus 로고
    • From an electrophoretic mobility shift assay to isolated transcription factors: a fast genomic-proteomic approach
    • Mach-Aigner AR, Grosstessner-Hain K, Pocas-Fonseca MJ, Mechtler K, Mach RL, (2010) From an electrophoretic mobility shift assay to isolated transcription factors: a fast genomic-proteomic approach. BMC Genomics 11: 644.
    • (2010) BMC Genomics , vol.11 , pp. 644
    • Mach-Aigner, A.R.1    Grosstessner-Hain, K.2    Pocas-Fonseca, M.J.3    Mechtler, K.4    Mach, R.L.5
  • 98
    • 84860367312 scopus 로고    scopus 로고
    • A new Zn(II)(2)Cys(6)-type transcription factor BglR regulates beta-glucosidase expression in Trichoderma reesei
    • Nitta M, Furukawa T, Shida Y, Mori K, Kuhara S, et al. (2012) A new Zn(II)(2)Cys(6)-type transcription factor BglR regulates beta-glucosidase expression in Trichoderma reesei. Fungal Genet Biol 49: 388-397.
    • (2012) Fungal Genet Biol , vol.49 , pp. 388-397
    • Nitta, M.1    Furukawa, T.2    Shida, Y.3    Mori, K.4    Kuhara, S.5


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