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Volumn 30, Issue 5, 2012, Pages 1119-1139

Production of recombinant proteins by filamentous fungi

Author keywords

Aspergillus; Filamentous; Fungi; Genome; Heterologous; Pathogenesis; Penicillium; Protease; Recombinant protein; Trichoderma

Indexed keywords

FILAMENTOUS; HETEROLOGOUS; PATHOGENESIS; PENICILLIUM; PROTEASE; TRICHODERMA;

EID: 84864942946     PISSN: 07349750     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.biotechadv.2011.09.012     Document Type: Article
Times cited : (195)

References (288)
  • 2
    • 77955684963 scopus 로고    scopus 로고
    • Changes in nitrogen assimilation, metabolism and growth in transgenic rice plants expressing a fungal NADP(H)-dependent glutamate dehydrogenase (gdhA)
    • Abiko T., Wakayama M., Kawakami A., Obara M., Kisaka H., Miwa T., et al. Changes in nitrogen assimilation, metabolism and growth in transgenic rice plants expressing a fungal NADP(H)-dependent glutamate dehydrogenase (gdhA). Planta 2010, 232:299-311.
    • (2010) Planta , vol.232 , pp. 299-311
    • Abiko, T.1    Wakayama, M.2    Kawakami, A.3    Obara, M.4    Kisaka, H.5    Miwa, T.6
  • 3
    • 77955445449 scopus 로고    scopus 로고
    • Quantitative iTRAQ secretome analysis of Aspergillus niger reveals nivel hydrolytic enzymes
    • Adav S.S., Li A.A., Manavalan A., Punt P., Sze S.K. Quantitative iTRAQ secretome analysis of Aspergillus niger reveals nivel hydrolytic enzymes. J Proteome Res 2010, 9:3932-3940.
    • (2010) J Proteome Res , vol.9 , pp. 3932-3940
    • Adav, S.S.1    Li, A.A.2    Manavalan, A.3    Punt, P.4    Sze, S.K.5
  • 4
    • 30044434276 scopus 로고    scopus 로고
    • Culture-based strategies for minimization of protease activity in filtrates from Aspergillus niger
    • Ahamed A., Singh A., Ward O.P. Culture-based strategies for minimization of protease activity in filtrates from Aspergillus niger. World J Microbiol Biotechnol 2005, 21:1577-1583.
    • (2005) World J Microbiol Biotechnol , vol.21 , pp. 1577-1583
    • Ahamed, A.1    Singh, A.2    Ward, O.P.3
  • 5
    • 0027179130 scopus 로고
    • δ-(L -α-Aminoadipyl)-L-cysteinyl-d-valine synthetase, the multienzyme integrating the four primary reactions in β-lactam biosynthesis, as a model peptide synthetase
    • Aharonowitz Y., Bergmeyer J., Cantoral J.M., Cohen G., Demain A.L., Fink U., et al. δ-(L -α-Aminoadipyl)-L-cysteinyl-d-valine synthetase, the multienzyme integrating the four primary reactions in β-lactam biosynthesis, as a model peptide synthetase. Biotechnology 1993, 11:807-810.
    • (1993) Biotechnology , vol.11 , pp. 807-810
    • Aharonowitz, Y.1    Bergmeyer, J.2    Cantoral, J.M.3    Cohen, G.4    Demain, A.L.5    Fink, U.6
  • 6
    • 12244299847 scopus 로고    scopus 로고
    • Subtractive cloning of cDNA from Aspergillus oryzae differentially regulated between solid-state and liquid (submerged) culture
    • Akao T., Gomi K., Goto K., Okazaki N., Akita O. Subtractive cloning of cDNA from Aspergillus oryzae differentially regulated between solid-state and liquid (submerged) culture. Curr Genet 2002, 41:275-281.
    • (2002) Curr Genet , vol.41 , pp. 275-281
    • Akao, T.1    Gomi, K.2    Goto, K.3    Okazaki, N.4    Akita, O.5
  • 7
    • 84872621565 scopus 로고    scopus 로고
    • Regulatable growth of filamentous fungi. United States Patent Application No. 20030045697. 2003.
    • Akin AR, Bodie, EA, Burrow, S, Dunn-Coleman N, Turner G, Ward M. Regulatable growth of filamentous fungi. United States Patent Application No. 20030045697. 2003.
    • Akin, A.R.1    Bodie, E.A.2    Burrow, S.3    Dunn-Coleman, N.4    Turner, G.5    Ward, M.6
  • 9
    • 4644268556 scopus 로고    scopus 로고
    • From genomics to post-genomics in Aspergillus
    • Archer D.B., Dyer P.S. From genomics to post-genomics in Aspergillus. Curr Opin Microbiol 2004, 7:499-504.
    • (2004) Curr Opin Microbiol , vol.7 , pp. 499-504
    • Archer, D.B.1    Dyer, P.S.2
  • 10
    • 11944257160 scopus 로고
    • Hen egg white lysozyme expressed and secreted from A. niger is correctly processed and folded
    • Archer D.B., Jeens D.J., MacKenzie D.A., Brightwell G., Lambert N., Lorne G., et al. Hen egg white lysozyme expressed and secreted from A. niger is correctly processed and folded. Biotechnology 1990, 8:741-745.
    • (1990) Biotechnology , vol.8 , pp. 741-745
    • Archer, D.B.1    Jeens, D.J.2    MacKenzie, D.A.3    Brightwell, G.4    Lambert, N.5    Lorne, G.6
  • 11
    • 23744496272 scopus 로고    scopus 로고
    • Transcriptional regulation of plant cell wall degradation by filamentous fungi
    • Aro N., Pakula T., Penttila M. Transcriptional regulation of plant cell wall degradation by filamentous fungi. FEMS Microbiol Rev 2005, 29:719-739.
    • (2005) FEMS Microbiol Rev , vol.29 , pp. 719-739
    • Aro, N.1    Pakula, T.2    Penttila, M.3
  • 12
    • 34548069725 scopus 로고    scopus 로고
    • Terrequinone A biosynthesis through l-tryptophan oxidation, dimerization and bisprenylation
    • Balibar C.J., Howard-Jones A.R., Walsh C.T. Terrequinone A biosynthesis through l-tryptophan oxidation, dimerization and bisprenylation. Nat Chem Biol 2007, 3:584-592.
    • (2007) Nat Chem Biol , vol.3 , pp. 584-592
    • Balibar, C.J.1    Howard-Jones, A.R.2    Walsh, C.T.3
  • 13
    • 0028082188 scopus 로고
    • PDR5, a novel yeast multidrug conferring transporter controlled by a transcription regulator PDR1
    • Balzi E., Wang S., Leterme S., Van Dyck L., Goffeau A. PDR5, a novel yeast multidrug conferring transporter controlled by a transcription regulator PDR1. J Biol Chem 1994, 269:2206-2214.
    • (1994) J Biol Chem , vol.269 , pp. 2206-2214
    • Balzi, E.1    Wang, S.2    Leterme, S.3    Van Dyck, L.4    Goffeau, A.5
  • 14
    • 84872604974 scopus 로고    scopus 로고
    • Promoters of the genes glutamate dehydrogenase beta-N-acetylhexosaminidase and γ-actin and their use in filamentous fungi expression, secretion and antisense systems. United States Patent 6,300,095. 2001.
    • Barredo Fuente JL, Rodriguez Saiz M, Collados De La Vieja AJ, Moreno Valle MA, Salto Maldonado F, Diez Garcia B. Promoters of the genes glutamate dehydrogenase beta-N-acetylhexosaminidase and γ-actin and their use in filamentous fungi expression, secretion and antisense systems. United States Patent 6,300,095. 2001.
    • Barredo Fuente, J.L.1    Rodriguez Saiz, M.2    Collados De La Vieja, A.J.3    Moreno Valle, M.A.4    Salto Maldonado, F.5    Diez Garcia, B.6
  • 16
    • 0029161160 scopus 로고
    • Expression of a functional fungal polyketide synthase in the bacterium Streptomyces coelicolor A3(2)
    • Bedford D.J., Schweizer E., Hopwood D.A., Khosla C. Expression of a functional fungal polyketide synthase in the bacterium Streptomyces coelicolor A3(2). J Bacteriol 1995, 177:4544-4548.
    • (1995) J Bacteriol , vol.177 , pp. 4544-4548
    • Bedford, D.J.1    Schweizer, E.2    Hopwood, D.A.3    Khosla, C.4
  • 17
    • 84872597923 scopus 로고    scopus 로고
    • Agrobacterium mediated transformation of moulds, in particular those belonging to the genus Aspergillus. United States Patent 6255115. 2001.
    • Beijersbergen AGM, Bundock P, Gouka RJ, de Groot MJA, Hooykaas PJJ. Agrobacterium mediated transformation of moulds, in particular those belonging to the genus Aspergillus. United States Patent 6255115. 2001.
    • Beijersbergen, A.G.M.1    Bundock, P.2    Gouka, R.J.3    De Groot, M.J.A.4    Hooykaas, P.J.J.5
  • 18
    • 84872602163 scopus 로고    scopus 로고
    • The molds of Katrina. Update (NY Acad Sci) 2006; Jan/Feb: 6-9.
    • Bennett JW. The molds of Katrina. Update (NY Acad Sci) 2006; Jan/Feb: 6-9.
    • Bennett, J.W.1
  • 20
    • 84872603401 scopus 로고    scopus 로고
    • Heterologous polypeptides expressed in filamentous fungi, processes for making same, and vectors for making same. United States Patent 6,379,928. 2002.
    • Berka RM, Cullen D, Gray GL, Gregory Lawrence H, Hayenga KJ, Lawlis VB. Heterologous polypeptides expressed in filamentous fungi, processes for making same, and vectors for making same. United States Patent 6,379,928. 2002.
    • Berka, R.M.1    Cullen, D.2    Gray, G.L.3    Gregory Lawrence, H.4    Hayenga, K.J.5    Lawlis, V.B.6
  • 21
    • 84872602256 scopus 로고    scopus 로고
    • Heterologous polypeptides expressed in filamentous fungi, processes for making same, vectors for making same. United States Patent Application 20030224482. 2003.
    • Berka RM, Cullen D, Gray GL, Hayenga KJ, and Lawlis VB. Heterologous polypeptides expressed in filamentous fungi, processes for making same, vectors for making same. United States Patent Application 20030224482. 2003.
    • Berka, R.M.1    Cullen, D.2    Gray, G.L.3    Hayenga, K.J.4    Lawlis, V.B.5
  • 22
    • 84864917407 scopus 로고    scopus 로고
    • Peroxisome carnithine acetyl transferase is required for elaboration of penetration hyphae during plant infection by Magnaporthe grisea
    • Bhambra G.K., Wang Z.-Y., Soanes D.M., Wakley G.E., Talbot N.J. Peroxisome carnithine acetyl transferase is required for elaboration of penetration hyphae during plant infection by Magnaporthe grisea. Mol Microbiol 2006, 72:6345-6354.
    • (2006) Mol Microbiol , vol.72 , pp. 6345-6354
    • Bhambra, G.K.1    Wang, Z.-Y.2    Soanes, D.M.3    Wakley, G.E.4    Talbot, N.J.5
  • 23
    • 84872618907 scopus 로고    scopus 로고
    • Process for production of protein products in Aspergillus. United States Patent 5,536,661. 1996.
    • Boel E, Christensen T, Woldike H. Process for production of protein products in Aspergillus. United States Patent 5,536,661. 1996.
    • Boel, E.1    Christensen, T.2    Woldike, H.3
  • 24
    • 0033959611 scopus 로고    scopus 로고
    • Expression of endochitinase from Trichoderma harzianum in transgenic apple increases resistance to apple scab and reduces vigor
    • Bolar J.P., Norelli J.L., Wong K.W., Hayes C.K., Harman G.E., Aldwinckle H.S. Expression of endochitinase from Trichoderma harzianum in transgenic apple increases resistance to apple scab and reduces vigor. Phytopathology 2000, 90:72-77.
    • (2000) Phytopathology , vol.90 , pp. 72-77
    • Bolar, J.P.1    Norelli, J.L.2    Wong, K.W.3    Hayes, C.K.4    Harman, G.E.5    Aldwinckle, H.S.6
  • 25
    • 65649123807 scopus 로고    scopus 로고
    • Innate immunity in plants: an arms race between pattern recognition receptors in plants and effectors in microbial pathogens
    • Boller T., He S.Y. Innate immunity in plants: an arms race between pattern recognition receptors in plants and effectors in microbial pathogens. Science 2009, 324:742-744.
    • (2009) Science , vol.324 , pp. 742-744
    • Boller, T.1    He, S.Y.2
  • 26
    • 77957907451 scopus 로고    scopus 로고
    • An inventory of the Aspergillus niger secretome by combining in silico predictions with shotgun proteomics data
    • Braaksma M., Martens-Uzonova E.M., Punt P.J., Schaap P.J. An inventory of the Aspergillus niger secretome by combining in silico predictions with shotgun proteomics data. BMC Genome 2010, 11:584-595.
    • (2010) BMC Genome , vol.11 , pp. 584-595
    • Braaksma, M.1    Martens-Uzonova, E.M.2    Punt, P.J.3    Schaap, P.J.4
  • 27
    • 84881064245 scopus 로고    scopus 로고
    • Aspergillus as a cell factory for protein production: controlling protease activity in fungal production
    • CRC Press, Boca Raton, G.H. Goldman, S.A. Osmani (Eds.)
    • Braaksma M., Punt P.J. Aspergillus as a cell factory for protein production: controlling protease activity in fungal production. The Aspergilli: genomics, medical aspects, biotechnology and research methods 2008, 441-455. CRC Press, Boca Raton. G.H. Goldman, S.A. Osmani (Eds.).
    • (2008) The Aspergilli: genomics, medical aspects, biotechnology and research methods , pp. 441-455
    • Braaksma, M.1    Punt, P.J.2
  • 28
    • 0026000815 scopus 로고
    • Use of highly purified alpha 1-antitrypsin standard to establish ranges for the common normal and deficient alpha 1-antitrypsin phenotypes
    • Brantly M.L., Wittes J.T., Vogelmeier C.F., Hubbard R.C., Fells G.A., Crystal R.G. Use of highly purified alpha 1-antitrypsin standard to establish ranges for the common normal and deficient alpha 1-antitrypsin phenotypes. Chest 1991, 100:703-708.
    • (1991) Chest , vol.100 , pp. 703-708
    • Brantly, M.L.1    Wittes, J.T.2    Vogelmeier, C.F.3    Hubbard, R.C.4    Fells, G.A.5    Crystal, R.G.6
  • 29
    • 0025897602 scopus 로고
    • Chromosome-specific recombinant DNA libraries from the fungus Aspergillus nidulans
    • Brody H., Griffith J., Cuticchia A.J., Arnold J., Timberlake W.E. Chromosome-specific recombinant DNA libraries from the fungus Aspergillus nidulans. Nucleic Acids Res 1991, 19:3105-3109.
    • (1991) Nucleic Acids Res , vol.19 , pp. 3105-3109
    • Brody, H.1    Griffith, J.2    Cuticchia, A.J.3    Arnold, J.4    Timberlake, W.E.5
  • 30
    • 0027508505 scopus 로고
    • Secretion of heterologous proteins by Aspergillus niger: Production of active human interleukin-6 in a protease deficient mutant by KEX2-like processing of a glucoamylase-hIL6 fusion protein
    • Broekhuijsen M.P., Mattern I.E., Contreras R., Kinghorn J.R., van den Hondel C.A.M.J.J. Secretion of heterologous proteins by Aspergillus niger: Production of active human interleukin-6 in a protease deficient mutant by KEX2-like processing of a glucoamylase-hIL6 fusion protein. J Biotechnol 1993, 31:135-145.
    • (1993) J Biotechnol , vol.31 , pp. 135-145
    • Broekhuijsen, M.P.1    Mattern, I.E.2    Contreras, R.3    Kinghorn, J.R.4    Van Den Hondel, C.A.M.J.J.5
  • 31
    • 0001646214 scopus 로고    scopus 로고
    • Applications of Trichoderma reesei enzymes in the pulp and paper industry
    • Taylor and Francis, London, G.E. Harman, C.P. Kubicek (Eds.)
    • Buchert T., Oksanen T., Pere J., Siika-Aho M., Suurnakki A., Viikari L. Applications of Trichoderma reesei enzymes in the pulp and paper industry. Trichoderma and Gliocladium 1998, 2:343-363. Taylor and Francis, London. G.E. Harman, C.P. Kubicek (Eds.).
    • (1998) Trichoderma and Gliocladium , vol.2 , pp. 343-363
    • Buchert, T.1    Oksanen, T.2    Pere, J.3    Siika-Aho, M.4    Suurnakki, A.5    Viikari, L.6
  • 32
    • 84872613573 scopus 로고    scopus 로고
    • Aspergillus niger vacuolar aspartyl protease. United States Patent 5674728. 1997.
    • Buxton FJ, Gabor V, Jacob NL. Aspergillus niger vacuolar aspartyl protease. United States Patent 5674728. 1997.
    • Buxton, F.J.1    Gabor, V.2    Jacob, N.L.3
  • 34
    • 76649083237 scopus 로고    scopus 로고
    • Evaluation of properties of several cheese-ripening fungi for potential biotechnological applications
    • Chavez R., Roa A., Navarrete K., Trebotich J., Espinosa Y., Vaca I. Evaluation of properties of several cheese-ripening fungi for potential biotechnological applications. Mycoscience 2010, 51:84-87.
    • (2010) Mycoscience , vol.51 , pp. 84-87
    • Chavez, R.1    Roa, A.2    Navarrete, K.3    Trebotich, J.4    Espinosa, Y.5    Vaca, I.6
  • 35
    • 77950577400 scopus 로고    scopus 로고
    • Promotion of efficient saccharification of crystalline cellulose by Aspergillus fumigatus Swo1
    • Chen X.A., Ishida N., Todaka N., Nakamura R., Maruyama J.I., Takahashi H., et al. Promotion of efficient saccharification of crystalline cellulose by Aspergillus fumigatus Swo1. Appl Environ Microbiol 2010, 76:2556-2561.
    • (2010) Appl Environ Microbiol , vol.76 , pp. 2556-2561
    • Chen, X.A.1    Ishida, N.2    Todaka, N.3    Nakamura, R.4    Maruyama, J.I.5    Takahashi, H.6
  • 36
    • 0000188915 scopus 로고
    • Cytochemical aspects of chitin breakdown during the parasitic action of a Trichoderma sp. on Fusarium oxysporum f.sp. radicislycopersici
    • Cherif M., Benhamou N. Cytochemical aspects of chitin breakdown during the parasitic action of a Trichoderma sp. on Fusarium oxysporum f.sp. radicislycopersici. Phytopathology 1990, 80:1406-1414.
    • (1990) Phytopathology , vol.80 , pp. 1406-1414
    • Cherif, M.1    Benhamou, N.2
  • 37
    • 0042432086 scopus 로고    scopus 로고
    • Directed evolution of industrial enzymes: an update
    • Cherry J., Fidantsef A. Directed evolution of industrial enzymes: an update. Curr Opin Biotechnol 2003, 14:438-443.
    • (2003) Curr Opin Biotechnol , vol.14 , pp. 438-443
    • Cherry, J.1    Fidantsef, A.2
  • 39
    • 84872616497 scopus 로고    scopus 로고
    • Christensen T, Lehmbeck J. Fungus wherein the areA, pepC and/or pepE genes have been inactivated. United States Patent 6013452. 2000.
    • Christensen T, Lehmbeck J. Fungus wherein the areA, pepC and/or pepE genes have been inactivated. United States Patent 6013452. 2000.
  • 42
    • 0031170751 scopus 로고    scopus 로고
    • The validity of the Aspergillus nidulans linkage map
    • Clutterbuck A.J. The validity of the Aspergillus nidulans linkage map. Fungal Genet Biol 1997, 21:267-277.
    • (1997) Fungal Genet Biol , vol.21 , pp. 267-277
    • Clutterbuck, A.J.1
  • 43
    • 0035805435 scopus 로고    scopus 로고
    • Genetic engineering of the Trichoderma reesei endoglucanase I (Cel7B) for enhanced partitioning in aqueous two-phase systems containing thermoseparating ethylene oxide-propylene oxide copolymers
    • Collen A., Ward M., Tjerneld F., Stalbrand H. Genetic engineering of the Trichoderma reesei endoglucanase I (Cel7B) for enhanced partitioning in aqueous two-phase systems containing thermoseparating ethylene oxide-propylene oxide copolymers. J Biotechnol 2001, 87:179-191.
    • (2001) J Biotechnol , vol.87 , pp. 179-191
    • Collen, A.1    Ward, M.2    Tjerneld, F.3    Stalbrand, H.4
  • 44
    • 33745924142 scopus 로고    scopus 로고
    • A high-throughput gene knockout procedure for Neurospora reveals functions for multiple transcription factors
    • Colot H.V., Park G., Turner G.E., Ringelberg C., Crew C.M., Litvinkova L., et al. A high-throughput gene knockout procedure for Neurospora reveals functions for multiple transcription factors. Proc Natl Acad Sci USA 2006, 103:10352-10357.
    • (2006) Proc Natl Acad Sci USA , vol.103 , pp. 10352-10357
    • Colot, H.V.1    Park, G.2    Turner, G.E.3    Ringelberg, C.4    Crew, C.M.5    Litvinkova, L.6
  • 46
    • 0033931925 scopus 로고    scopus 로고
    • Studies on the production of fungal peroxidases in Aspergillus niger
    • Conesa A., van den Hondel C.A.M.J.J., Punt P.J. Studies on the production of fungal peroxidases in Aspergillus niger. Appl Environ Microbiol 2000, 66:3016-3023.
    • (2000) Appl Environ Microbiol , vol.66 , pp. 3016-3023
    • Conesa, A.1    Van Den Hondel, C.A.M.J.J.2    Punt, P.J.3
  • 47
    • 84872595806 scopus 로고    scopus 로고
    • Overproduction of fungal peroxidases in filamentous fungi (Thesis). University of Leiden; 2001.
    • Conesa A. Overproduction of fungal peroxidases in filamentous fungi (Thesis). University of Leiden; 2001.
    • Conesa, A.1
  • 48
    • 33750966150 scopus 로고    scopus 로고
    • Identification of a starter unit acyl-carrier protein transacylase domain in an iterative type I polyketide synthase
    • Crawford J.M., Dancy B.C.R., Hill E.A., Udwary D.W., Townsend C.A. Identification of a starter unit acyl-carrier protein transacylase domain in an iterative type I polyketide synthase. Proc Natl Acad Sci USA 2006, 103:16728-16733.
    • (2006) Proc Natl Acad Sci USA , vol.103 , pp. 16728-16733
    • Crawford, J.M.1    Dancy, B.C.R.2    Hill, E.A.3    Udwary, D.W.4    Townsend, C.A.5
  • 49
    • 0028835709 scopus 로고
    • Production of cephalosporin intermediates by feeding adipic acid to recombinant Penicillium chrysogenum strains expressing ring expansion activity
    • Crawford L., Stepan A.M., McAda P.C., Rambosek J.A., Conder M.J., Vinci V.A., et al. Production of cephalosporin intermediates by feeding adipic acid to recombinant Penicillium chrysogenum strains expressing ring expansion activity. Bio-Technology 1995, 13:58-62.
    • (1995) Bio-Technology , vol.13 , pp. 58-62
    • Crawford, L.1    Stepan, A.M.2    McAda, P.C.3    Rambosek, J.A.4    Conder, M.J.5    Vinci, V.A.6
  • 51
    • 0343924592 scopus 로고    scopus 로고
    • Recent advances on the molecular genetics of ligninolytic fungi
    • Cullen D. Recent advances on the molecular genetics of ligninolytic fungi. J Biotechnol 1997, 53:273-289.
    • (1997) J Biotechnol , vol.53 , pp. 273-289
    • Cullen, D.1
  • 52
    • 34548669353 scopus 로고    scopus 로고
    • The Fusarium graminearum genome reveals a link between localized polymorphism and pathogen specialization
    • Cuomo C.A., Guldener U., Xu J.-R., Trail F., Turgeon B.G., Di Pietro A., et al. The Fusarium graminearum genome reveals a link between localized polymorphism and pathogen specialization. Science 2007, 317:1400-1402.
    • (2007) Science , vol.317 , pp. 1400-1402
    • Cuomo, C.A.1    Guldener, U.2    Xu, J.-R.3    Trail, F.4    Turgeon, B.G.5    Di Pietro, A.6
  • 53
    • 33845670895 scopus 로고    scopus 로고
    • Advances in combating fungal diseases: vaccines on the threshold
    • Cutler J.E., Deepe G.S., Klein B.S. Advances in combating fungal diseases: vaccines on the threshold. Nat Rev Microbiol 2007, 5:13-28.
    • (2007) Nat Rev Microbiol , vol.5 , pp. 13-28
    • Cutler, J.E.1    Deepe, G.S.2    Klein, B.S.3
  • 54
    • 16544392267 scopus 로고    scopus 로고
    • Identification of genes associated with morphology in Aspergillus niger by using suppression subtractive hybridization
    • Dai Z., Mao X., Magnuson J.K., Lasure L.L. Identification of genes associated with morphology in Aspergillus niger by using suppression subtractive hybridization. Appl Environ Microbiol 2004, 70:2474-2485.
    • (2004) Appl Environ Microbiol , vol.70 , pp. 2474-2485
    • Dai, Z.1    Mao, X.2    Magnuson, J.K.3    Lasure, L.L.4
  • 55
    • 33745475386 scopus 로고    scopus 로고
    • Identification of bifunctional 12/3 fatty acid desaturases for improving the ratio of 3-6 fatty acids in microbes and plants
    • Damude H.G., Zhang H., Farrall L., Ripp K.G., Tomb J.-F., Hollerbach D., et al. Identification of bifunctional 12/3 fatty acid desaturases for improving the ratio of 3-6 fatty acids in microbes and plants. Proc Natl Acad Sci USA 2006, 103:9446-9451.
    • (2006) Proc Natl Acad Sci USA , vol.103 , pp. 9446-9451
    • Damude, H.G.1    Zhang, H.2    Farrall, L.3    Ripp, K.G.4    Tomb, J.-F.5    Hollerbach, D.6
  • 56
    • 77955558145 scopus 로고    scopus 로고
    • Engineering of glycosylation in yeast and other fungi: current state and perspectives
    • De Pourcq K., De Schutter K., Callewaert N. Engineering of glycosylation in yeast and other fungi: current state and perspectives. Appl Microbiol Biotechnol 2010, 87:1617-1631.
    • (2010) Appl Microbiol Biotechnol , vol.87 , pp. 1617-1631
    • De Pourcq, K.1    De Schutter, K.2    Callewaert, N.3
  • 57
    • 0037364791 scopus 로고    scopus 로고
    • Regulation of Aspergillus genes encoding plant cell wall polysaccharide-degrading enzymes; relevance for industrial production
    • de Vries R.P. Regulation of Aspergillus genes encoding plant cell wall polysaccharide-degrading enzymes; relevance for industrial production. Appl Microbiol Biotechnol 2003, 61:10-20.
    • (2003) Appl Microbiol Biotechnol , vol.61 , pp. 10-20
    • de Vries, R.P.1
  • 58
    • 61349178501 scopus 로고    scopus 로고
    • Production of recombinant proteins by microbes and higher organisms
    • Demain A.L., Vaishnav P. Production of recombinant proteins by microbes and higher organisms. Biotechnol Advances 2009, 27:297-306.
    • (2009) Biotechnol Advances , vol.27 , pp. 297-306
    • Demain, A.L.1    Vaishnav, P.2
  • 59
    • 61349131965 scopus 로고    scopus 로고
    • Biosolutions to the energy problem
    • Demain A.L. Biosolutions to the energy problem. J Indust Microbiol 2009, 36:319-332.
    • (2009) J Indust Microbiol , vol.36 , pp. 319-332
    • Demain, A.L.1
  • 60
    • 0033924468 scopus 로고    scopus 로고
    • PH regulation of gene expression
    • Denison S.H. pH regulation of gene expression. Fungal Genet Biol 2000, 29:61-71.
    • (2000) Fungal Genet Biol , vol.29 , pp. 61-71
    • Denison, S.H.1
  • 61
    • 0002119417 scopus 로고
    • Antagonistic properties of species-groups of Thrichoderma. 1. Production of non-volatile antibiotics
    • Dennis C., Webster J. Antagonistic properties of species-groups of Thrichoderma. 1. Production of non-volatile antibiotics. Trans Brit Mycol Soc 1971, 57:25-39.
    • (1971) Trans Brit Mycol Soc , vol.57 , pp. 25-39
    • Dennis, C.1    Webster, J.2
  • 62
    • 0002119417 scopus 로고
    • Antagonistic properties of species-groups of Thrichoderma. 2. Production of volatile antibiotics
    • Dennis C., Webster J. Antagonistic properties of species-groups of Thrichoderma. 2. Production of volatile antibiotics. Trans Brit Mycol Soc 1971, 57:41-48.
    • (1971) Trans Brit Mycol Soc , vol.57 , pp. 41-48
    • Dennis, C.1    Webster, J.2
  • 63
    • 0002119415 scopus 로고
    • Antagonistic properties of species-groups of Thrichoderma. 3. Hyphal interaction
    • Dennis C., Webster J. Antagonistic properties of species-groups of Thrichoderma. 3. Hyphal interaction. Trans Brit Mycol Soc 1971, 57:363-369.
    • (1971) Trans Brit Mycol Soc , vol.57 , pp. 363-369
    • Dennis, C.1    Webster, J.2
  • 65
    • 0041352961 scopus 로고    scopus 로고
    • Metabolic engineering of fatty acids for breeding of new oilseed crops: strategies, problems and first results
    • Drexler H., Spiekermann P., Meyer A., Domergue F., Zank T., Sperling P., et al. Metabolic engineering of fatty acids for breeding of new oilseed crops: strategies, problems and first results. J Plant Physiol 2003, 160:779-802.
    • (2003) J Plant Physiol , vol.160 , pp. 779-802
    • Drexler, H.1    Spiekermann, P.2    Meyer, A.3    Domergue, F.4    Zank, T.5    Sperling, P.6
  • 66
    • 77951546919 scopus 로고    scopus 로고
    • Morphology engineering of Aspergillus niger for improved enzyme production
    • Driouch H., Sommer B., Wittmann C. Morphology engineering of Aspergillus niger for improved enzyme production. Biotech Bioeng 2010, 105:1058-1068.
    • (2010) Biotech Bioeng , vol.105 , pp. 1058-1068
    • Driouch, H.1    Sommer, B.2    Wittmann, C.3
  • 68
    • 0032948875 scopus 로고    scopus 로고
    • The role of Trichoderma harzianum protease in the biocontrol of Botrytis cinerea
    • Elad Y., Kapat A. The role of Trichoderma harzianum protease in the biocontrol of Botrytis cinerea. Eur J Plant Pathol 1999, 105:177-189.
    • (1999) Eur J Plant Pathol , vol.105 , pp. 177-189
    • Elad, Y.1    Kapat, A.2
  • 69
    • 0002860518 scopus 로고
    • Strain improvement and preservation of beta-lactam producing microorganisms
    • Springer-Verlag, New York, A.L. Demain, N. Solomon (Eds.)
    • Elander R. Strain improvement and preservation of beta-lactam producing microorganisms. Antibiotics containing the β-lactam structure I 1983, 97-146. Springer-Verlag, New York. A.L. Demain, N. Solomon (Eds.).
    • (1983) Antibiotics containing the β-lactam structure I , pp. 97-146
    • Elander, R.1
  • 70
    • 78650200742 scopus 로고    scopus 로고
    • Surveys of non-ribosomal peptide and polyketide assembly lines in fungi and prospects for their analysis in vitro and in vivo
    • Evans B.S., Robinson S.J., Kelleher N.L. Surveys of non-ribosomal peptide and polyketide assembly lines in fungi and prospects for their analysis in vitro and in vivo. Fungal Genet Biol 2011, 48:49-61.
    • (2011) Fungal Genet Biol , vol.48 , pp. 49-61
    • Evans, B.S.1    Robinson, S.J.2    Kelleher, N.L.3
  • 72
    • 0345446982 scopus 로고    scopus 로고
    • Some factors affecting production of pectic enzymes by Aspergillus niger
    • Fawole O.B., Odunfa S.A. Some factors affecting production of pectic enzymes by Aspergillus niger. Int Biodeter Biodegr 2003, 52:223-227.
    • (2003) Int Biodeter Biodegr , vol.52 , pp. 223-227
    • Fawole, O.B.1    Odunfa, S.A.2
  • 73
    • 77954497649 scopus 로고    scopus 로고
    • Biodiesel-fuel: content, production, producers, contemporary biotechnology (review)
    • Feofilova E.P., Dergeeva Y.E., Inashechkin A.A. Biodiesel-fuel: content, production, producers, contemporary biotechnology (review). Appl Biochem Microbiol 2010, 46:369-378.
    • (2010) Appl Biochem Microbiol , vol.46 , pp. 369-378
    • Feofilova, E.P.1    Dergeeva, Y.E.2    Inashechkin, A.A.3
  • 74
    • 77955557873 scopus 로고    scopus 로고
    • Expression and export: recombinant protein production systems for Aspergillus
    • Fleissner A., Dersch P. Expression and export: recombinant protein production systems for Aspergillus. Appl Microbiol Biotechnol 2010, 87:1255-1270.
    • (2010) Appl Microbiol Biotechnol , vol.87 , pp. 1255-1270
    • Fleissner, A.1    Dersch, P.2
  • 76
    • 77952922758 scopus 로고    scopus 로고
    • Functional analysis of fungal polyketide biosynthesis genes
    • Fujii I. Functional analysis of fungal polyketide biosynthesis genes. J Antibiot 2010, 63:207-218.
    • (2010) J Antibiot , vol.63 , pp. 207-218
    • Fujii, I.1
  • 77
    • 1542723495 scopus 로고    scopus 로고
    • The molecular structure and catalytic mechanism of a novel carboxyl peptidase from Scytalidium lignicolum
    • Fujinaga M., Cherney M.M., Oyama H., Oda K., James M.N.G. The molecular structure and catalytic mechanism of a novel carboxyl peptidase from Scytalidium lignicolum. Proc Natl Acad Sci USA 2004, 101:3364-3369.
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 3364-3369
    • Fujinaga, M.1    Cherney, M.M.2    Oyama, H.3    Oda, K.4    James, M.N.G.5
  • 78
    • 34247116457 scopus 로고    scopus 로고
    • Quelling: post-translational gene silencing guided by small RNAs in Neurospora crassa
    • Fulci V., Macino G. Quelling: post-translational gene silencing guided by small RNAs in Neurospora crassa. Curr Opin Microbiol 2007, 10:199-203.
    • (2007) Curr Opin Microbiol , vol.10 , pp. 199-203
    • Fulci, V.1    Macino, G.2
  • 80
    • 28844461287 scopus 로고    scopus 로고
    • Sequencing of Aspergillus nidulans and comparative analysis with A. fumigatus and A. oryzae
    • Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S., et al. Sequencing of Aspergillus nidulans and comparative analysis with A. fumigatus and A. oryzae. Nature 2005, 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    Batzoglou, S.6
  • 81
    • 0001098948 scopus 로고    scopus 로고
    • Applications of Trichoderma enzymes in the textile industry
    • Taylor and Francis, London
    • Galanti Y.M., De Conti A., Monteverdi R. Applications of Trichoderma enzymes in the textile industry. Trichoderma and Gliocladium 1998, Vol 2:311-326. Taylor and Francis, London.
    • (1998) Trichoderma and Gliocladium , vol.2 , pp. 311-326
    • Galanti, Y.M.1    De Conti, A.2    Monteverdi, R.3
  • 82
    • 0027245389 scopus 로고
    • Molecular characterization of the proteinase-encoding gene, prb1, related to mycoparasitism by Trichoderma harzianum
    • Geremia R.A., Goldman G.H., Jacobs D., Ardrtes W., Vila S.B., Van Montagu M., et al. Molecular characterization of the proteinase-encoding gene, prb1, related to mycoparasitism by Trichoderma harzianum. Mol Microbiol 1993, 8:603-613.
    • (1993) Mol Microbiol , vol.8 , pp. 603-613
    • Geremia, R.A.1    Goldman, G.H.2    Jacobs, D.3    Ardrtes, W.4    Vila, S.B.5    Van Montagu, M.6
  • 83
    • 8344271025 scopus 로고    scopus 로고
    • Advances in the production of human therapeutic proteins yeasts and filamentous fungi
    • Gerngross T.U. Advances in the production of human therapeutic proteins yeasts and filamentous fungi. Nature Biotechnol 2004, 22:1409-1414.
    • (2004) Nature Biotechnol , vol.22 , pp. 1409-1414
    • Gerngross, T.U.1
  • 84
    • 77954266383 scopus 로고    scopus 로고
    • Genomics of protein folding in the endoplasmic reticulum, secretion stress and glycosylation in the aspergilli
    • Geysens S., Whyteside G., Archer D.B. Genomics of protein folding in the endoplasmic reticulum, secretion stress and glycosylation in the aspergilli. Fungal Genet Biol 2009, 46:S121-S140.
    • (2009) Fungal Genet Biol , vol.46
    • Geysens, S.1    Whyteside, G.2    Archer, D.B.3
  • 86
    • 78651060300 scopus 로고    scopus 로고
    • Proteomic analysis in non-denaturing condition of the secretome reveals the presence of multienzyme complexes in Penicillium purpurogenum
    • Gonzalez-Vogel A., Eyzaguirre J., Oleas G., Callegari E., Navarette M. Proteomic analysis in non-denaturing condition of the secretome reveals the presence of multienzyme complexes in Penicillium purpurogenum. Appl Microbiol Biotechnol 2011, 89:145-155.
    • (2011) Appl Microbiol Biotechnol , vol.89 , pp. 145-155
    • Gonzalez-Vogel, A.1    Eyzaguirre, J.2    Oleas, G.3    Callegari, E.4    Navarette, M.5
  • 87
    • 0033801513 scopus 로고    scopus 로고
    • A glucoamylase::GFP gene fusion to study protein secretion by individual hyphae of Aspergillus niger
    • Gordon C.L., Archer D.B., Jeenes D.J., Doonan J.H., Wells B., Trinci A.P.J., et al. A glucoamylase::GFP gene fusion to study protein secretion by individual hyphae of Aspergillus niger. J Microbiol Meth 2000, 42:39-48.
    • (2000) J Microbiol Meth , vol.42 , pp. 39-48
    • Gordon, C.L.1    Archer, D.B.2    Jeenes, D.J.3    Doonan, J.H.4    Wells, B.5    Trinci, A.P.J.6
  • 88
    • 34347327263 scopus 로고    scopus 로고
    • Protein O-glycosylation in fungi: diverse structures and multiple functions
    • Goto M. Protein O-glycosylation in fungi: diverse structures and multiple functions. Biosci Biotechnol Biochem 2007, 1415-1427.
    • (2007) Biosci Biotechnol Biochem , pp. 1415-1427
    • Goto, M.1
  • 89
    • 0031054007 scopus 로고    scopus 로고
    • Efficient production of secreted proteins by Aspergillus: progress, limitations and prospects
    • Gouka R.J., Punt P.J., van den Hondel C.A.M.J.J. Efficient production of secreted proteins by Aspergillus: progress, limitations and prospects. Appl Microbiol Biotechnol 1997, 47:1-11.
    • (1997) Appl Microbiol Biotechnol , vol.47 , pp. 1-11
    • Gouka, R.J.1    Punt, P.J.2    Van Den Hondel, C.A.M.J.J.3
  • 90
    • 0030942270 scopus 로고    scopus 로고
    • Glucoamylase gene fusions alleviate limitations for protein production in Aspergillus awamori at the transcriptional and (post) translational levels
    • Gouka R.J., Punt P.J., van den Hondel C.A.M.J.J. Glucoamylase gene fusions alleviate limitations for protein production in Aspergillus awamori at the transcriptional and (post) translational levels. Appl Environ Microbiol 1997, 63:488-497.
    • (1997) Appl Environ Microbiol , vol.63 , pp. 488-497
    • Gouka, R.J.1    Punt, P.J.2    Van Den Hondel, C.A.M.J.J.3
  • 92
    • 77955654728 scopus 로고    scopus 로고
    • Characterization of the family GH54 α-l-arabinofuranosidases in Penicillium funiculosum, including a novel protein bearing a cellulose-binding domain
    • Guais O., Tourrasse O., Dourdoigne M., Parrou J.L., Francois J.M. Characterization of the family GH54 α-l-arabinofuranosidases in Penicillium funiculosum, including a novel protein bearing a cellulose-binding domain. Applied Microbiol Biotechnol 2010, 87:1007-1021.
    • (2010) Applied Microbiol Biotechnol , vol.87 , pp. 1007-1021
    • Guais, O.1    Tourrasse, O.2    Dourdoigne, M.3    Parrou, J.L.4    Francois, J.M.5
  • 93
    • 55949099223 scopus 로고    scopus 로고
    • Proteomics analysis of "Rovabio Excel", a secreted protein cocktail from the filamentous fungus Penicillium funiculosum grown under industrial process fermentation
    • Guasi O., Borderies G., Pichereaux C., Maestracci M., Neugnot V., Rossignol M., et al. Proteomics analysis of "Rovabio Excel", a secreted protein cocktail from the filamentous fungus Penicillium funiculosum grown under industrial process fermentation. J Indust Microbiol Biotechnol 2008, 35:1659-1668.
    • (2008) J Indust Microbiol Biotechnol , vol.35 , pp. 1659-1668
    • Guasi, O.1    Borderies, G.2    Pichereaux, C.3    Maestracci, M.4    Neugnot, V.5    Rossignol, M.6
  • 94
    • 33646900283 scopus 로고    scopus 로고
    • An endophytic taxol-producing fungus BT2 isolated from Taxus chinensis var. mairei
    • Guo B.H., Wang Y.C., Zhou X.W., Hu K., Tan F., Miao Z.Q., Tang K.X. An endophytic taxol-producing fungus BT2 isolated from Taxus chinensis var. mairei. Afr J Biotechnol 2006, 5:875-877.
    • (2006) Afr J Biotechnol , vol.5 , pp. 875-877
    • Guo, B.H.1    Wang, Y.C.2    Zhou, X.W.3    Hu, K.4    Tan, F.5    Miao, Z.Q.6    Tang, K.X.7
  • 95
    • 0026030134 scopus 로고
    • Expression of the penDE gene of Penicillium chrysogenum encoding isopenicillin N acyltransferase in Cephalosporium acremonium: production of benzylpenicillin by the transformants
    • Gutierrez S., Diez B., Alvarez E., Barredo J.L., Martin J.F. Expression of the penDE gene of Penicillium chrysogenum encoding isopenicillin N acyltransferase in Cephalosporium acremonium: production of benzylpenicillin by the transformants. Mol Gen Genet 1991, 225:56-64.
    • (1991) Mol Gen Genet , vol.225 , pp. 56-64
    • Gutierrez, S.1    Diez, B.2    Alvarez, E.3    Barredo, J.L.4    Martin, J.F.5
  • 96
    • 0026490708 scopus 로고
    • Expression of foreign proteins in the genus Aspergillus
    • Gwynne D.I., Devchand M. Expression of foreign proteins in the genus Aspergillus. Biotechnology 1992, 23:203-214.
    • (1992) Biotechnology , vol.23 , pp. 203-214
    • Gwynne, D.I.1    Devchand, M.2
  • 97
    • 15544367902 scopus 로고    scopus 로고
    • RNA silencing in Aspergillus nidulans is independent of RNA-dependent RNA polymerases
    • Hammond T.M., Keller N.P. RNA silencing in Aspergillus nidulans is independent of RNA-dependent RNA polymerases. Genetics 2005, 169:607-617.
    • (2005) Genetics , vol.169 , pp. 607-617
    • Hammond, T.M.1    Keller, N.P.2
  • 99
    • 0024348312 scopus 로고
    • A novel fungal expression system: secretion of actice calf chymosin from the filamentous fungus Trichoderma reesei
    • Harkki A., Uusitalo J., Bailey M., Penttila M., Knowles J.K.C. A novel fungal expression system: secretion of actice calf chymosin from the filamentous fungus Trichoderma reesei. Nature Biotechnol 1989, 7:596-603.
    • (1989) Nature Biotechnol , vol.7 , pp. 596-603
    • Harkki, A.1    Uusitalo, J.2    Bailey, M.3    Penttila, M.4    Knowles, J.K.C.5
  • 101
    • 61349128396 scopus 로고    scopus 로고
    • Engineering of Penicillium chrysogenum for fermentative production of a novel carbamoylated cephem antibiotic precursor
    • Harris D.M., Westerlaken I., Schipper D., van der Krogt Z.A., Gombert A.K., Sutherland J., et al. Engineering of Penicillium chrysogenum for fermentative production of a novel carbamoylated cephem antibiotic precursor. Metab Eng 2009, 11:125-137.
    • (2009) Metab Eng , vol.11 , pp. 125-137
    • Harris, D.M.1    Westerlaken, I.2    Schipper, D.3    van der Krogt, Z.A.4    Gombert, A.K.5    Sutherland, J.6
  • 103
    • 0035712954 scopus 로고    scopus 로고
    • The magnitude of fungal diversity: the 1.5million species estimate revisited
    • Hawksworth D.L. The magnitude of fungal diversity: the 1.5million species estimate revisited. Mycol Res 2001, 105:1422-1432.
    • (2001) Mycol Res , vol.105 , pp. 1422-1432
    • Hawksworth, D.L.1
  • 104
    • 0036000059 scopus 로고    scopus 로고
    • High-level production of γ-linolenic acid in Brassica juncea using a δ6 desaturase from Pythium irregulare
    • Hong H., Datla N., Reed D.W., Covello P.S., MacKenzie S.L., Qiu X. High-level production of γ-linolenic acid in Brassica juncea using a δ6 desaturase from Pythium irregulare. Plant Physiol 2002, 354-362.
    • (2002) Plant Physiol , pp. 354-362
    • Hong, H.1    Datla, N.2    Reed, D.W.3    Covello, P.S.4    MacKenzie, S.L.5    Qiu, X.6
  • 105
    • 77952891807 scopus 로고    scopus 로고
    • Cloning and heterologous expression of a novel endoglucanase gene egVIII from Trichoderma viride in Saccharomyces cerevisiae
    • Huang X.-M., Yang Q., Liu Z.-H., Fan J.-X., Chen X.-L., Song J.-Z., et al. Cloning and heterologous expression of a novel endoglucanase gene egVIII from Trichoderma viride in Saccharomyces cerevisiae. Appl Biochem Biotechnol 2010, 162:103-115.
    • (2010) Appl Biochem Biotechnol , vol.162 , pp. 103-115
    • Huang, X.-M.1    Yang, Q.2    Liu, Z.-H.3    Fan, J.-X.4    Chen, X.-L.5    Song, J.-Z.6
  • 106
    • 0032587474 scopus 로고    scopus 로고
    • 6-desaturases from Mortierella alpina and recombinant production of γ-linolenic acid in Saccharomyces cerevisiae
    • 6-desaturases from Mortierella alpina and recombinant production of γ-linolenic acid in Saccharomyces cerevisiae. Lipids 1999, 34:649-659.
    • (1999) Lipids , vol.34 , pp. 649-659
    • Huang, Y.-S.1    Chaudhary, S.2    Thurmond, J.M.3    Bobik, E.G.4    Yuan, L.5    Chan, G.M.6
  • 107
    • 0141954482 scopus 로고    scopus 로고
    • Zygomycosis
    • Oxford University Press, New York, W.E. Dismukes, P.G. Pappas, J.D. Sobel (Eds.)
    • Ibrahim A.S., Edwards J.E.J., Filler S.G. Zygomycosis. Clinical mycology 2003, 241-251. Oxford University Press, New York. W.E. Dismukes, P.G. Pappas, J.D. Sobel (Eds.).
    • (2003) Clinical mycology , pp. 241-251
    • Ibrahim, A.S.1    Edwards, J.E.J.2    Filler, S.G.3
  • 108
    • 0033137074 scopus 로고    scopus 로고
    • Molecular and enzymatic properties of recombinant 1,2-α-mannosidase from Aspergillus saitoi overexpressed in Aspergillus oryzae cells
    • Ichishima E., Taya N., Ikeguichi M., Chiba Y., Nakamura M., Kawabata C., et al. Molecular and enzymatic properties of recombinant 1,2-α-mannosidase from Aspergillus saitoi overexpressed in Aspergillus oryzae cells. Biochem J 1999, 339:589-597.
    • (1999) Biochem J , vol.339 , pp. 589-597
    • Ichishima, E.1    Taya, N.2    Ikeguichi, M.3    Chiba, Y.4    Nakamura, M.5    Kawabata, C.6
  • 109
    • 76049085091 scopus 로고    scopus 로고
    • Cultivation characteristics and gene expression profiles of Aspergillus oryzae by membrane-surface liquid culture, shaking-flask culture and agar-plate culture
    • Imanaka H., Tanaka S., Feng B., Imamura K., Nakanishi K. Cultivation characteristics and gene expression profiles of Aspergillus oryzae by membrane-surface liquid culture, shaking-flask culture and agar-plate culture. J Biosci Bioeng 2010, 109:267-273.
    • (2010) J Biosci Bioeng , vol.109 , pp. 267-273
    • Imanaka, H.1    Tanaka, S.2    Feng, B.3    Imamura, K.4    Nakanishi, K.5
  • 110
    • 77953486651 scopus 로고    scopus 로고
    • Contribution of peroxisomes to secondary metabolism and pathogenicity in the fungal plant pathogen Alternaria alternata
    • Imazaka A., Tanaka A., Harimoto Y., Yamamoto M., Akimitsu K., Park P., et al. Contribution of peroxisomes to secondary metabolism and pathogenicity in the fungal plant pathogen Alternaria alternata. Eukaryot Cell 2010, 9:682-694.
    • (2010) Eukaryot Cell , vol.9 , pp. 682-694
    • Imazaka, A.1    Tanaka, A.2    Harimoto, Y.3    Yamamoto, M.4    Akimitsu, K.5    Park, P.6
  • 111
    • 0034789607 scopus 로고    scopus 로고
    • Establishment of a hyper-protein production system in submerged Aspergillus oryzae culture under tyrosinase-encoding gene (melO) promoter control
    • Ishida H., Matsumura K., Hata Y., Kawato A., Suginami K., Abe Y., et al. Establishment of a hyper-protein production system in submerged Aspergillus oryzae culture under tyrosinase-encoding gene (melO) promoter control. Appl Microbiol Biotechnol 2001, 57:131-137.
    • (2001) Appl Microbiol Biotechnol , vol.57 , pp. 131-137
    • Ishida, H.1    Matsumura, K.2    Hata, Y.3    Kawato, A.4    Suginami, K.5    Abe, Y.6
  • 112
    • 0036968875 scopus 로고    scopus 로고
    • Recent studies of protein secretion by filamentous fungi-review
    • Iwashita K. Recent studies of protein secretion by filamentous fungi-review. J Biosci Bioeng 2002, 94:530-535.
    • (2002) J Biosci Bioeng , vol.94 , pp. 530-535
    • Iwashita, K.1
  • 113
    • 63849246735 scopus 로고    scopus 로고
    • Effective lead saelection for improved porotein production in Aspergillus niger based on integrated genomics
    • Jacobs D.I., Olsthoorn M.M.A., Maillet I., Akeroyd M., Breestraat S., Donkers S., et al. Effective lead saelection for improved porotein production in Aspergillus niger based on integrated genomics. Fungal Genet Biol 2009, 46:S141-S152.
    • (2009) Fungal Genet Biol , vol.46
    • Jacobs, D.I.1    Olsthoorn, M.M.A.2    Maillet, I.3    Akeroyd, M.4    Breestraat, S.5    Donkers, S.6
  • 114
    • 77953172467 scopus 로고    scopus 로고
    • Proteome analysis of the penicillin producer Penicillium chrysogenum: characterization of protein changes during industrial strain improvement
    • Jami M.S., Barreiro C., Garcia Estradfa C., Martin J.F. Proteome analysis of the penicillin producer Penicillium chrysogenum: characterization of protein changes during industrial strain improvement. Mol Cell Proteomics 2010, 9:1182-1198.
    • (2010) Mol Cell Proteomics , vol.9 , pp. 1182-1198
    • Jami, M.S.1    Barreiro, C.2    Garcia Estradfa, C.3    Martin, J.F.4
  • 115
    • 0028500342 scopus 로고
    • Transcriptional and post translational events affect the production of secreted hen egg white lysozyme by A. niger
    • Jeenes D.J., MacKenzie D.A., Archer D.B. Transcriptional and post translational events affect the production of secreted hen egg white lysozyme by A. niger. Transgen Res 1994, 3:297-303.
    • (1994) Transgen Res , vol.3 , pp. 297-303
    • Jeenes, D.J.1    MacKenzie, D.A.2    Archer, D.B.3
  • 116
    • 0027411139 scopus 로고
    • A truncated glucoamylase gene fusion for heterologous protein secretion from A. niger
    • Jeenes D.J., Marczinke B., MacKenzie D.A., Archer D.B. A truncated glucoamylase gene fusion for heterologous protein secretion from A. niger. FEMS Microbiol Lett 1993, 107:267-271.
    • (1993) FEMS Microbiol Lett , vol.107 , pp. 267-271
    • Jeenes, D.J.1    Marczinke, B.2    MacKenzie, D.A.3    Archer, D.B.4
  • 117
    • 0030787806 scopus 로고    scopus 로고
    • Isolation and characterization of a novel stress inducible PDI family gene from A. niger
    • Jeenes D.J., Pfaller R., Archer D.B. Isolation and characterization of a novel stress inducible PDI family gene from A. niger. Gene 1997, 194:151-156.
    • (1997) Gene , vol.194 , pp. 151-156
    • Jeenes, D.J.1    Pfaller, R.2    Archer, D.B.3
  • 118
    • 84872614382 scopus 로고    scopus 로고
    • Thermophilic fungal expression system. United States Patent 5695985. 1997.
    • Jensen EB, Boominathan KC. Thermophilic fungal expression system. United States Patent 5695985. 1997.
    • Jensen, E.B.1    Boominathan, K.C.2
  • 119
    • 34548666443 scopus 로고    scopus 로고
    • Double disruption of the proteinase genes, tppA and pepE, increase the production level of human lysozyme by Aspergillus oryzae
    • Jin F.J., Watanabe T., Juvvadi P.R., Maruyama J.-I., Arioka M., Kitamoto K. Double disruption of the proteinase genes, tppA and pepE, increase the production level of human lysozyme by Aspergillus oryzae. Appl Gen Mol Biotechnol 2007, 76:1059-1068.
    • (2007) Appl Gen Mol Biotechnol , vol.76 , pp. 1059-1068
    • Jin, F.J.1    Watanabe, T.2    Juvvadi, P.R.3    Maruyama, J.-I.4    Arioka, M.5    Kitamoto, K.6
  • 120
    • 75949109975 scopus 로고    scopus 로고
    • Hydrophobin fusions for high-level transient protein expression and purification in Nicotiana benthamiana
    • Joensuu J.J., Conley A.J., Lienemann M., Brandle J.E., Linder M.B., Menassa R. Hydrophobin fusions for high-level transient protein expression and purification in Nicotiana benthamiana. Plant Physiol 2010, 152:622-633.
    • (2010) Plant Physiol , vol.152 , pp. 622-633
    • Joensuu, J.J.1    Conley, A.J.2    Lienemann, M.3    Brandle, J.E.4    Linder, M.B.5    Menassa, R.6
  • 122
    • 33745065087 scopus 로고    scopus 로고
    • Recombinant human alpha-1-proteinase inhibitor towards therapeutic use
    • Karnaukhova E., Ophir Y., Golding B. Recombinant human alpha-1-proteinase inhibitor towards therapeutic use. Amino Acids 2006, 30:317-332.
    • (2006) Amino Acids , vol.30 , pp. 317-332
    • Karnaukhova, E.1    Ophir, Y.2    Golding, B.3
  • 124
    • 33751418445 scopus 로고    scopus 로고
    • In vivo expression of UDP-N-acetylglucosamine: α-3-d-mannoside β-1,2-N-acetylglucosyl-transferase 1 (GnT-1) in Aspergillus oryzae and effects on the sugar chain of alpha-amylase
    • Kasajima T., Yamaguichi M., Hirai N., Ohmachi T., Yoshida T. In vivo expression of UDP-N-acetylglucosamine: α-3-d-mannoside β-1,2-N-acetylglucosyl-transferase 1 (GnT-1) in Aspergillus oryzae and effects on the sugar chain of alpha-amylase. Biosci Biotechnol Biochem 2006, 70:2662-2668.
    • (2006) Biosci Biotechnol Biochem , vol.70 , pp. 2662-2668
    • Kasajima, T.1    Yamaguichi, M.2    Hirai, N.3    Ohmachi, T.4    Yoshida, T.5
  • 125
    • 0031905709 scopus 로고    scopus 로고
    • Production of a polyketide natural product in nonpolyketide-producing prokaryotic and eukaryotic hosts
    • Kealey J.T., Liu L., Santi D.V., Betlach M.C., Barr P.J. Production of a polyketide natural product in nonpolyketide-producing prokaryotic and eukaryotic hosts. Proc Natl Acad Sci USA 1998, 95:499-505.
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 499-505
    • Kealey, J.T.1    Liu, L.2    Santi, D.V.3    Betlach, M.C.4    Barr, P.J.5
  • 126
    • 0033591447 scopus 로고    scopus 로고
    • Modulation of polyketide synthase activity by accessory proteins during lovastatin biosynthesis
    • Kennedy J., Auclair K., Kendrew S.G., Park C., Vederas J.C., Hutchinson C.R. Modulation of polyketide synthase activity by accessory proteins during lovastatin biosynthesis. Science 1999, 284:1368-1372.
    • (1999) Science , vol.284 , pp. 1368-1372
    • Kennedy, J.1    Auclair, K.2    Kendrew, S.G.3    Park, C.4    Vederas, J.C.5    Hutchinson, C.R.6
  • 127
    • 33947138087 scopus 로고    scopus 로고
    • Engineering primary metabolic pathways of industrial micro-organisms
    • Kern A., Tilley E., Hunter I.S., Legisa M., Glieder A. Engineering primary metabolic pathways of industrial micro-organisms. J Biotechnol 2007, 129:6-29.
    • (2007) J Biotechnol , vol.129 , pp. 6-29
    • Kern, A.1    Tilley, E.2    Hunter, I.S.3    Legisa, M.4    Glieder, A.5
  • 130
    • 0023478845 scopus 로고
    • Enzymatic "combustion": the microbial degradation of lignin
    • Kirk T.K., Farrel R.L. Enzymatic "combustion": the microbial degradation of lignin. Ann Rev Microbiol 1987, 41:465-505.
    • (1987) Ann Rev Microbiol , vol.41 , pp. 465-505
    • Kirk, T.K.1    Farrel, R.L.2
  • 131
    • 85006164721 scopus 로고
    • Electrophoretic karyotype and gene assignment to chromosomes of Aspergillus oryzae
    • Kitamoto K., Kimura K., Gomi K., Kumagai C. Electrophoretic karyotype and gene assignment to chromosomes of Aspergillus oryzae. Biosci Biotechnol Biochem 1994, 58:1467-1470.
    • (1994) Biosci Biotechnol Biochem , vol.58 , pp. 1467-1470
    • Kitamoto, K.1    Kimura, K.2    Gomi, K.3    Kumagai, C.4
  • 132
    • 0025024567 scopus 로고
    • Non-ribosomal biosynthesis of peptide antibiotics
    • Kleinkauf H., von Döhren H. Non-ribosomal biosynthesis of peptide antibiotics. Eur J Biochem 1990, 192:1-15.
    • (1990) Eur J Biochem , vol.192 , pp. 1-15
    • Kleinkauf, H.1    von Döhren, H.2
  • 133
    • 0032491316 scopus 로고    scopus 로고
    • Identification of δ5-desaturase from Mortierella alpina by heterologous expression in bakers' yeast and canola
    • Knutzon D.S., Thurmond J.M., Huang Y.-S., Chaudhary S., Bobik E.G., Chan G.M., et al. Identification of δ5-desaturase from Mortierella alpina by heterologous expression in bakers' yeast and canola. J Biol Chem 1998, 273:29360-29366.
    • (1998) J Biol Chem , vol.273 , pp. 29360-29366
    • Knutzon, D.S.1    Thurmond, J.M.2    Huang, Y.-S.3    Chaudhary, S.4    Bobik, E.G.5    Chan, G.M.6
  • 135
    • 42149108423 scopus 로고    scopus 로고
    • Bioconversion of lignocellulosic biomass: biochemical and molecular perspectives
    • Kumar R., Singh S., Singh O.V. Bioconversion of lignocellulosic biomass: biochemical and molecular perspectives. J Indust Microbiol Biotechnol 2008, 35:377-391.
    • (2008) J Indust Microbiol Biotechnol , vol.35 , pp. 377-391
    • Kumar, R.1    Singh, S.2    Singh, O.V.3
  • 137
    • 84872613992 scopus 로고    scopus 로고
    • Alkaline protease deficient filamentous fungi. United States Patent 6, 291,209. 2001.
    • Lehmbeck J. Alkaline protease deficient filamentous fungi. United States Patent 6, 291,209. 2001.
    • Lehmbeck, J.1
  • 138
    • 78149468198 scopus 로고    scopus 로고
    • Cloning and expression of a cellulose gene in the silkworm, Bombyx mori by improved Bac-to-Bac/BmNPV baculovirus expression system
    • Li X., Wang D., Zhou F., Yang H., Bhaskar R., Hu J., et al. Cloning and expression of a cellulose gene in the silkworm, Bombyx mori by improved Bac-to-Bac/BmNPV baculovirus expression system. Mol Biol Rep 2010, 8:3721-3728.
    • (2010) Mol Biol Rep , vol.8 , pp. 3721-3728
    • Li, X.1    Wang, D.2    Zhou, F.3    Yang, H.4    Bhaskar, R.5    Hu, J.6
  • 139
    • 33646722917 scopus 로고    scopus 로고
    • Recent research and prospect on taxol and its producing fungi
    • Lin F.C., Liu X.H., Wang H.K., Zhang C.L. Recent research and prospect on taxol and its producing fungi. Acta Microbiol Sin 2003, 43:534-538.
    • (2003) Acta Microbiol Sin , vol.43 , pp. 534-538
    • Lin, F.C.1    Liu, X.H.2    Wang, H.K.3    Zhang, C.L.4
  • 141
    • 0038357730 scopus 로고    scopus 로고
    • Improving heterologous gene expression in Aspergillus niger by introducing multiple copies of protein-binding sequence containing CCAAT to the promoter
    • Liu L., Liu J., Qiu R.X., Zhu X.G., Dong Z.Y., Tang G.M. Improving heterologous gene expression in Aspergillus niger by introducing multiple copies of protein-binding sequence containing CCAAT to the promoter. Lett Appl Microbiol 2003, 36:358-361.
    • (2003) Lett Appl Microbiol , vol.36 , pp. 358-361
    • Liu, L.1    Liu, J.2    Qiu, R.X.3    Zhu, X.G.4    Dong, Z.Y.5    Tang, G.M.6
  • 142
    • 0015086080 scopus 로고
    • Isolation and nature of intracellular peptides from a cephalosporin C producing Cephalosporium sp
    • Loder P.B., Abraham E.B. Isolation and nature of intracellular peptides from a cephalosporin C producing Cephalosporium sp. Biochem J 1971, 123:471-476.
    • (1971) Biochem J , vol.123 , pp. 471-476
    • Loder, P.B.1    Abraham, E.B.2
  • 144
    • 57249097123 scopus 로고    scopus 로고
    • Developing Aspergillus as a host for heterologous expression
    • Lubertozzi D., Keasling J.D. Developing Aspergillus as a host for heterologous expression. Biotechnol Adv 2009, 27:53-75.
    • (2009) Biotechnol Adv , vol.27 , pp. 53-75
    • Lubertozzi, D.1    Keasling, J.D.2
  • 145
    • 68249097196 scopus 로고    scopus 로고
    • Genomic analysis of the basal lineage fungus Rhizopus oryzae reveals a whole-genome duplication author(s): source
    • Article No: e1000549.
    • Ma L.J., Ibrahim A.S., Skory C., Grabherr M.G., Burger G., Butler M., et al. Genomic analysis of the basal lineage fungus Rhizopus oryzae reveals a whole-genome duplication author(s): source. PLoS Genet 2009, 5(7). Article No: e1000549.
    • (2009) PLoS Genet , vol.5 , Issue.7
    • Ma, L.J.1    Ibrahim, A.S.2    Skory, C.3    Grabherr, M.G.4    Burger, G.5    Butler, M.6
  • 146
    • 34848890676 scopus 로고    scopus 로고
    • Enzymatic synthesis of aromatic polyketides using PKS4 from Gibberella fujikuroi
    • Ma S.M., et al. Enzymatic synthesis of aromatic polyketides using PKS4 from Gibberella fujikuroi. J Am Chem Soc 2007, 129:10642-10643.
    • (2007) J Am Chem Soc , vol.129 , pp. 10642-10643
    • Ma, S.M.1
  • 147
    • 0037255672 scopus 로고    scopus 로고
    • Regulation of gene expression in industrial fungi: Trichoderma
    • Mach R.L., Zeilinger S. Regulation of gene expression in industrial fungi: Trichoderma. Appl Microbiol Biotechnol 2003, 60:515-522.
    • (2003) Appl Microbiol Biotechnol , vol.60 , pp. 515-522
    • Mach, R.L.1    Zeilinger, S.2
  • 148
    • 0036360821 scopus 로고    scopus 로고
    • Progress of Aspergillus oryzae genomics
    • Machida M. Progress of Aspergillus oryzae genomics. Adv Appl Microbiol 2002, 51:81-106.
    • (2002) Adv Appl Microbiol , vol.51 , pp. 81-106
    • Machida, M.1
  • 149
    • 29244442741 scopus 로고    scopus 로고
    • Genome sequencing and analysis of Aspergillus oryzae
    • Machida M., Asai K., Sano M., Tanaka T., Kumagai T., Terai G., et al. Genome sequencing and analysis of Aspergillus oryzae. Nature 2005, 438:1157-1161.
    • (2005) Nature , vol.438 , pp. 1157-1161
    • Machida, M.1    Asai, K.2    Sano, M.3    Tanaka, T.4    Kumagai, T.5    Terai, G.6
  • 150
    • 0033754270 scopus 로고    scopus 로고
    • Isolation and use of a homologous histone H4 promoter and a ribosomal DNA region in a transformation vector for the oil-producing fungus Mortierella alpina
    • MacKenzie D.A., Wongwathanarat P., Carter A.T., Archer D.B. Isolation and use of a homologous histone H4 promoter and a ribosomal DNA region in a transformation vector for the oil-producing fungus Mortierella alpina. Appl Environ Microbiol 2000, 66:4655-4661.
    • (2000) Appl Environ Microbiol , vol.66 , pp. 4655-4661
    • MacKenzie, D.A.1    Wongwathanarat, P.2    Carter, A.T.3    Archer, D.B.4
  • 151
    • 0345369597 scopus 로고    scopus 로고
    • Aberrant processing of wild-type and mutant bovine pancreatic trypsin inhibitor secreted by Aspergillus niger
    • MacKenzie D.A., Kraunsoe J.A.E., Chesshyre J.A., Lowe G., Komiyama T., Fuller R.S., et al. Aberrant processing of wild-type and mutant bovine pancreatic trypsin inhibitor secreted by Aspergillus niger. J Biotechnol 1998, 63:137-146.
    • (1998) J Biotechnol , vol.63 , pp. 137-146
    • MacKenzie, D.A.1    Kraunsoe, J.A.E.2    Chesshyre, J.A.3    Lowe, G.4    Komiyama, T.5    Fuller, R.S.6
  • 152
    • 3843067671 scopus 로고    scopus 로고
    • Transcriptional analysis of genes for energy catabolism and hydrolytic enzymes in the filamentous fungus Aspergillus oryzae using cDNA microarrays and expressed sequence tags
    • Maeda H., Sano M., Maruyama Y., Tanno T., Akao T., Totsuka Y., et al. Transcriptional analysis of genes for energy catabolism and hydrolytic enzymes in the filamentous fungus Aspergillus oryzae using cDNA microarrays and expressed sequence tags. Appl Microbiol Biotechnol 2004, 65:74-83.
    • (2004) Appl Microbiol Biotechnol , vol.65 , pp. 74-83
    • Maeda, H.1    Sano, M.2    Maruyama, Y.3    Tanno, T.4    Akao, T.5    Totsuka, Y.6
  • 153
    • 34547114237 scopus 로고    scopus 로고
    • Production in Trichoderma reesei of three xylanases from Chaetomium thermophilum: a recombinant thermoxylanase for biobleaching of kraft pulp
    • Mantyla A., Paloheimo M., Hakola S., Lindberg E., Leskinen S., Kallio J., et al. Production in Trichoderma reesei of three xylanases from Chaetomium thermophilum: a recombinant thermoxylanase for biobleaching of kraft pulp. Appl Microbiol Biotechnol 2007, 76:377-386.
    • (2007) Appl Microbiol Biotechnol , vol.76 , pp. 377-386
    • Mantyla, A.1    Paloheimo, M.2    Hakola, S.3    Lindberg, E.4    Leskinen, S.5    Kallio, J.6
  • 154
    • 22644444310 scopus 로고    scopus 로고
    • The arms race continues: battle strategies between plants and fungal pathogens
    • Maor R., Shirasu K. The arms race continues: battle strategies between plants and fungal pathogens. Curr Opin Microbiol 2005, 8:399-404.
    • (2005) Curr Opin Microbiol , vol.8 , pp. 399-404
    • Maor, R.1    Shirasu, K.2
  • 155
    • 0026696975 scopus 로고
    • Multidomain enzymes involved in peptide synthesis
    • Marahiel M.A. Multidomain enzymes involved in peptide synthesis. FEBS Lett 1992, 307:40-43.
    • (1992) FEBS Lett , vol.307 , pp. 40-43
    • Marahiel, M.A.1
  • 156
    • 0033005982 scopus 로고    scopus 로고
    • In vivo synthesis of complex N-glycans by expression of human N-acetylglucosamyltransferase 1 in the filamentous fungus Trichoderma reesei
    • Maras M., De Bruyn A., Vervecken W., Uusitalo J., Penttila M., Busson R., et al. In vivo synthesis of complex N-glycans by expression of human N-acetylglucosamyltransferase 1 in the filamentous fungus Trichoderma reesei. FEBS Lett 1999, 452:365-370.
    • (1999) FEBS Lett , vol.452 , pp. 365-370
    • Maras, M.1    De Bruyn, A.2    Vervecken, W.3    Uusitalo, J.4    Penttila, M.5    Busson, R.6
  • 157
    • 0030724163 scopus 로고    scopus 로고
    • In vitro conversion of the carbohydrate moiety of fungal glycoproteins to mammalian-type oligosaccharides-evidence for N-acetylglucosaminetransferase-1-accepting glycans from Trichoderma reesei
    • Maras M., Saelens X., Laroy W., Piens K., Claeyssens M., Fiers W., et al. In vitro conversion of the carbohydrate moiety of fungal glycoproteins to mammalian-type oligosaccharides-evidence for N-acetylglucosaminetransferase-1-accepting glycans from Trichoderma reesei. Eur J Biochem 1997, 249:701-707.
    • (1997) Eur J Biochem , vol.249 , pp. 701-707
    • Maras, M.1    Saelens, X.2    Laroy, W.3    Piens, K.4    Claeyssens, M.5    Fiers, W.6
  • 158
    • 0002596901 scopus 로고    scopus 로고
    • Filamentous fungi as production organisms for glycoproteins of bio-medical interest
    • Maras M., van Die I., Contreras R., van den Hondel C.A.M.J.J. Filamentous fungi as production organisms for glycoproteins of bio-medical interest. Glycoconj J 1999, 16:99-107.
    • (1999) Glycoconj J , vol.16 , pp. 99-107
    • Maras, M.1    van Die, I.2    Contreras, R.3    Van Den Hondel, C.A.M.J.J.4
  • 159
    • 0141991096 scopus 로고    scopus 로고
    • Cloning and expression of fungal phytases in genetically modified strains of Aspergillus awamori
    • Martin J.A., Murphy R.A., Power R.F.G. Cloning and expression of fungal phytases in genetically modified strains of Aspergillus awamori. J Ind Microbiol Biotechnol 2003, 30:568-576.
    • (2003) J Ind Microbiol Biotechnol , vol.30 , pp. 568-576
    • Martin, J.A.1    Murphy, R.A.2    Power, R.F.G.3
  • 160
    • 0026816531 scopus 로고
    • Clusters of genes for the biosynthesis of antibiotics-regulatory genes and overproduction of pharmaceuticals
    • Martin J.F. Clusters of genes for the biosynthesis of antibiotics-regulatory genes and overproduction of pharmaceuticals. J Ind Microbiol Biotechnol 1992, 9:73-90.
    • (1992) J Ind Microbiol Biotechnol , vol.9 , pp. 73-90
    • Martin, J.F.1
  • 161
    • 0024460765 scopus 로고
    • Organization and expression of genes involved in the biosynthesis of antibiotics and other secondary metabolites
    • Martín J.F., Liras P. Organization and expression of genes involved in the biosynthesis of antibiotics and other secondary metabolites. Annu Rev Microbiol 1989, 43:173-206.
    • (1989) Annu Rev Microbiol , vol.43 , pp. 173-206
    • Martín, J.F.1    Liras, P.2
  • 162
    • 43449098828 scopus 로고    scopus 로고
    • Genome sequencing and analysis of the biomass-degrading fungus Trichoderma reesei (syn. Hypocrea jecorina)
    • Martinez D., Berka R.M., Henrissat B., Saloheimo M., Arvas M., Baker S.E., et al. Genome sequencing and analysis of the biomass-degrading fungus Trichoderma reesei (syn. Hypocrea jecorina). Nature Biotechnol 2008, 26:553-560.
    • (2008) Nature Biotechnol , vol.26 , pp. 553-560
    • Martinez, D.1    Berka, R.M.2    Henrissat, B.3    Saloheimo, M.4    Arvas, M.5    Baker, S.E.6
  • 163
    • 2542601548 scopus 로고    scopus 로고
    • Genome sequence of the lignocellulose degrading fungus Phanerochaete chrysosporium strain RP78
    • Martinez D., Larrondo L.F., Putnam N., Gelpke M.D., Huang K., Chapman J., et al. Genome sequence of the lignocellulose degrading fungus Phanerochaete chrysosporium strain RP78. Nature Biotechnol 2004, 22:695-700.
    • (2004) Nature Biotechnol , vol.22 , pp. 695-700
    • Martinez, D.1    Larrondo, L.F.2    Putnam, N.3    Gelpke, M.D.4    Huang, K.5    Chapman, J.6
  • 164
    • 0034233071 scopus 로고    scopus 로고
    • Production and product quality assessment of human hepatitis B virus-preS2 antigen in submerged and solid state cultures of A. oryzae
    • Maruyama J., Ohnuma H., Yoshikawa A., Kadokura H., Nakajima H., Kitamoto K. Production and product quality assessment of human hepatitis B virus-preS2 antigen in submerged and solid state cultures of A. oryzae. J Biosci Bioeng 2000, 90:118-120.
    • (2000) J Biosci Bioeng , vol.90 , pp. 118-120
    • Maruyama, J.1    Ohnuma, H.2    Yoshikawa, A.3    Kadokura, H.4    Nakajima, H.5    Kitamoto, K.6
  • 166
    • 49849100967 scopus 로고    scopus 로고
    • Proteomic and metabolomic analyses of the white-rot fungus Phanerochaete chrysogenum exposed to exogenous benzoic acid
    • Matsuzaki F., Shimizu M., Wariishi H. Proteomic and metabolomic analyses of the white-rot fungus Phanerochaete chrysogenum exposed to exogenous benzoic acid. J Proteome Res 2008, 7:2342-2350.
    • (2008) J Proteome Res , vol.7 , pp. 2342-2350
    • Matsuzaki, F.1    Shimizu, M.2    Wariishi, H.3
  • 167
    • 34547109406 scopus 로고    scopus 로고
    • Primary structure, regioselectivity, and evolution of the membrane-bound fatty acid desaturases of Claviceps purpurea
    • Meesapyodsuk D., Reed D.W., Covello P.S., Qiu X. Primary structure, regioselectivity, and evolution of the membrane-bound fatty acid desaturases of Claviceps purpurea. J Biol Chem 2007, 282:20191-20199.
    • (2007) J Biol Chem , vol.282 , pp. 20191-20199
    • Meesapyodsuk, D.1    Reed, D.W.2    Covello, P.S.3    Qiu, X.4
  • 168
    • 1542741006 scopus 로고    scopus 로고
    • Molds in floor dust and building-related symptoms in adolescent school children
    • Meyer H.W. Molds in floor dust and building-related symptoms in adolescent school children. Indoor Air 2004, 14:65-72.
    • (2004) Indoor Air , vol.14 , pp. 65-72
    • Meyer, H.W.1
  • 169
    • 38349002470 scopus 로고    scopus 로고
    • Genetic engineering of filamentous fungi-progress, obstacles and future trends
    • Meyer V. Genetic engineering of filamentous fungi-progress, obstacles and future trends. Biotechnol Adv 2008, 26:177-185.
    • (2008) Biotechnol Adv , vol.26 , pp. 177-185
    • Meyer, V.1
  • 171
    • 0031795569 scopus 로고    scopus 로고
    • Improvement of promoter activity by the introduction of multiple copies of the conserved region III sequence, involved in the efficient expression of Aspergillus oryzae amylase-encoding genes
    • Minetoki T., Kumagai C., Gomi K., Kitamoto K., Takahashi K. Improvement of promoter activity by the introduction of multiple copies of the conserved region III sequence, involved in the efficient expression of Aspergillus oryzae amylase-encoding genes. Appl Microbiol Biotechnol 1998, 50:459-467.
    • (1998) Appl Microbiol Biotechnol , vol.50 , pp. 459-467
    • Minetoki, T.1    Kumagai, C.2    Gomi, K.3    Kitamoto, K.4    Takahashi, K.5
  • 172
    • 47849102650 scopus 로고    scopus 로고
    • Outwitting multidrug resistance to antifungals
    • Monk B.C., Goffeau A. Outwitting multidrug resistance to antifungals. Science 2008, 321:367-369.
    • (2008) Science , vol.321 , pp. 367-369
    • Monk, B.C.1    Goffeau, A.2
  • 174
    • 0036304602 scopus 로고    scopus 로고
    • Silencing of the Aspergillopepsin B (pepB) gene of Aspergillus awamori by antisense RNA expression or protease removal by gene disruption results in a large increase in thaumatin production
    • Moralejo F.J., Cardoza R.E., Gutierrez S., Lombrana M., Fierro F., Martin J.F. Silencing of the Aspergillopepsin B (pepB) gene of Aspergillus awamori by antisense RNA expression or protease removal by gene disruption results in a large increase in thaumatin production. Appl Environ Microbiol 2002, 68:3550-3559.
    • (2002) Appl Environ Microbiol , vol.68 , pp. 3550-3559
    • Moralejo, F.J.1    Cardoza, R.E.2    Gutierrez, S.3    Lombrana, M.4    Fierro, F.5    Martin, J.F.6
  • 175
    • 77952024582 scopus 로고    scopus 로고
    • Hidden function of catalytic domain in 6-methylsalicylic acid synthase for product release
    • Moriguchi T., Kezuka Y., Nonaka T., Ebizuka Y., Fujii I. Hidden function of catalytic domain in 6-methylsalicylic acid synthase for product release. J Biol Chem 2010, 285:15637-15643.
    • (2010) J Biol Chem , vol.285 , pp. 15637-15643
    • Moriguchi, T.1    Kezuka, Y.2    Nonaka, T.3    Ebizuka, Y.4    Fujii, I.5
  • 176
    • 33646487125 scopus 로고    scopus 로고
    • Application of hammerhead ribozymes in filamentous fungi
    • Muller D., Stahl U., Meyer V. Application of hammerhead ribozymes in filamentous fungi. J Microbiol Meth 2006, 65:585-595.
    • (2006) J Microbiol Meth , vol.65 , pp. 585-595
    • Muller, D.1    Stahl, U.2    Meyer, V.3
  • 179
    • 33646565945 scopus 로고    scopus 로고
    • Extracellular production of neoculin, a sweet-tasting heterodimeric protein with taste-modifying activity by Aspergillus oryzae
    • Nakajima K., Asakura T., Maruyama J., Morita Y., Oike H., Shimizu-Ibuka A., et al. Extracellular production of neoculin, a sweet-tasting heterodimeric protein with taste-modifying activity by Aspergillus oryzae. Appl Environ Microbiol 2006, 72:3716-3723.
    • (2006) Appl Environ Microbiol , vol.72 , pp. 3716-3723
    • Nakajima, K.1    Asakura, T.2    Maruyama, J.3    Morita, Y.4    Oike, H.5    Shimizu-Ibuka, A.6
  • 182
    • 0033950413 scopus 로고    scopus 로고
    • Characterization of a foldase, protein disulfide isomerase A in the protein secretory pathway of Aspergillus niger
    • Ngiam C., Jeenes D.A., Punt P.J., van den Hondel C.A.M.J.J., Archer D.A. Characterization of a foldase, protein disulfide isomerase A in the protein secretory pathway of Aspergillus niger. Appl Environ Microbiol 2000, 66:775-782.
    • (2000) Appl Environ Microbiol , vol.66 , pp. 775-782
    • Ngiam, C.1    Jeenes, D.A.2    Punt, P.J.3    Van Den Hondel, C.A.M.J.J.4    Archer, D.A.5
  • 183
    • 0023474863 scopus 로고
    • The biosynthesis of sulfur-containing β-lactam antibiotics
    • Nuesch J., Heim J., Treichler H.-J. The biosynthesis of sulfur-containing β-lactam antibiotics. Annu Rev Microbiol 1987, 41:51-75.
    • (1987) Annu Rev Microbiol , vol.41 , pp. 51-75
    • Nuesch, J.1    Heim, J.2    Treichler, H.-J.3
  • 185
    • 0034764850 scopus 로고    scopus 로고
    • Enhanced heterologous protein production in Aspergillus niger through pH control of extracellular protease activity
    • O'Donnell D., Wang L., Xu J., Ridgway D., Gu T., Moo-Young M. Enhanced heterologous protein production in Aspergillus niger through pH control of extracellular protease activity. Biochem Eng 2001, 8:187-193.
    • (2001) Biochem Eng , vol.8 , pp. 187-193
    • O'Donnell, D.1    Wang, L.2    Xu, J.3    Ridgway, D.4    Gu, T.5    Moo-Young, M.6
  • 186
    • 33646570211 scopus 로고    scopus 로고
    • Proteomic analysis of extracellular proteins of Aspergillus oryzae grown under submerged and solid-state culture conditions
    • Oda K., Kakizono D., Yamada O., Lefuji H., Akita O., Iwashita K. Proteomic analysis of extracellular proteins of Aspergillus oryzae grown under submerged and solid-state culture conditions. Appl Environ Microbiol 2006, 72:3448-3457.
    • (2006) Appl Environ Microbiol , vol.72 , pp. 3448-3457
    • Oda, K.1    Kakizono, D.2    Yamada, O.3    Lefuji, H.4    Akita, O.5    Iwashita, K.6
  • 187
    • 39049186224 scopus 로고    scopus 로고
    • A complete protein pattern of cellulose and hemicellulase genes in the filamentous fungus Trichoderma reesei
    • Ouyang J., Yan M., Kong D., Xu L. A complete protein pattern of cellulose and hemicellulase genes in the filamentous fungus Trichoderma reesei. Biotechnol J 2006, 1:1266-1274.
    • (2006) Biotechnol J , vol.1 , pp. 1266-1274
    • Ouyang, J.1    Yan, M.2    Kong, D.3    Xu, L.4
  • 188
    • 0036090485 scopus 로고    scopus 로고
    • Protease secretion in glucoamylase producer Aspergillus niger cultures: fungal morphology and inoculum effects
    • Papagianni M., Young M.M. Protease secretion in glucoamylase producer Aspergillus niger cultures: fungal morphology and inoculum effects. Proc Biochem 2002, l37:1271-1278.
    • (2002) Proc Biochem , vol.L37 , pp. 1271-1278
    • Papagianni, M.1    Young, M.M.2
  • 189
    • 0030018122 scopus 로고    scopus 로고
    • The hapC gene of Aspergillus nidulans is involved in the expression of CCAAT-containing promoters
    • Papagiannopoulos P., Andrianopoulos A., Sharp J.A., Davis M.A., Hynes M.J. The hapC gene of Aspergillus nidulans is involved in the expression of CCAAT-containing promoters. Mol Gen Genet 1996, 251:412-421.
    • (1996) Mol Gen Genet , vol.251 , pp. 412-421
    • Papagiannopoulos, P.1    Andrianopoulos, A.2    Sharp, J.A.3    Davis, M.A.4    Hynes, M.J.5
  • 190
    • 34748923122 scopus 로고    scopus 로고
    • Comparative proteomics of extracellular proteins in vitro and in planta from the pathogenic fungus Fusarium graminearum
    • Paper J.M., Scott-Craig J.S., Adhikari N.D., Cuomo C.A., Walton J.D. Comparative proteomics of extracellular proteins in vitro and in planta from the pathogenic fungus Fusarium graminearum. Proteomics 2007, 7:3171-3183.
    • (2007) Proteomics , vol.7 , pp. 3171-3183
    • Paper, J.M.1    Scott-Craig, J.S.2    Adhikari, N.D.3    Cuomo, C.A.4    Walton, J.D.5
  • 191
    • 18744369064 scopus 로고    scopus 로고
    • Suicidal genetically engineered microorganisms for bioremediation: need and perspectives
    • Paul D., Pandey G., Jain R.K. Suicidal genetically engineered microorganisms for bioremediation: need and perspectives. Bioessays 2005, 563-573.
    • (2005) Bioessays , pp. 563-573
    • Paul, D.1    Pandey, G.2    Jain, R.K.3
  • 192
    • 33846861493 scopus 로고    scopus 로고
    • Genome sequencing and analysis of the versatile cell factory Aspergillus niger CBS 513.88
    • Pel H.J., de Winde J.H., Archer D.B., Dyer P.S., Hofmann G., Schaap P.J., et al. Genome sequencing and analysis of the versatile cell factory Aspergillus niger CBS 513.88. Nature Biotechnol 2007, 25:221-231.
    • (2007) Nature 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    Schaap, P.J.6
  • 193
    • 0001442653 scopus 로고    scopus 로고
    • Heterologous protein production in Trichoderma
    • Taylor and Francis, London, G.E. Harman, C.P. Kubicek (Eds.)
    • Penttila M. Heterologous protein production in Trichoderma. Trichoderma and Gliocladium 1998, 365-382. Taylor and Francis, London. G.E. Harman, C.P. Kubicek (Eds.).
    • (1998) Trichoderma and Gliocladium , pp. 365-382
    • Penttila, M.1
  • 194
    • 77249143323 scopus 로고    scopus 로고
    • Heterologous expression of an Agaricus meleagris pyranose dehydrogenase-encoding gene in Aspergillus spp. and characterization of the recombinant enzyme
    • Pisanelli I., Kujawa M., Gschnitzer D., Spaduit O., Seiboth B., Peterbauer C. Heterologous expression of an Agaricus meleagris pyranose dehydrogenase-encoding gene in Aspergillus spp. and characterization of the recombinant enzyme. Appl Microbiol Biotechnol 2010, 86:599-606.
    • (2010) Appl Microbiol Biotechnol , vol.86 , pp. 599-606
    • Pisanelli, I.1    Kujawa, M.2    Gschnitzer, D.3    Spaduit, O.4    Seiboth, B.5    Peterbauer, C.6
  • 195
    • 70449505226 scopus 로고    scopus 로고
    • Heterologous production of the Piromyces equi cinnamoyl esterase in Trichoderma reesei for biotechnological applications
    • Poidevin L., Levasseur A., Paes G., Navarro D., Heiss-Blanquet S., Asther M., et al. Heterologous production of the Piromyces equi cinnamoyl esterase in Trichoderma reesei for biotechnological applications. Letts Appl Microbiol 2009, 49:673-678.
    • (2009) Letts Appl Microbiol , vol.49 , pp. 673-678
    • Poidevin, L.1    Levasseur, A.2    Paes, G.3    Navarro, D.4    Heiss-Blanquet, S.5    Asther, M.6
  • 197
    • 0031794850 scopus 로고    scopus 로고
    • Analysis of the role of the gene bipA, encoding the major endoplasmic reticulum chaperone protein in the secretion of homologous and heterologous proteins in black Aspergilli
    • Punt P.J., van Gemeren I.A., Drint-Kuijvenhoven A., Hessing J.G.M., van Muijlwijk-Harteveld G.M., Beijersbergen A., et al. Analysis of the role of the gene bipA, encoding the major endoplasmic reticulum chaperone protein in the secretion of homologous and heterologous proteins in black Aspergilli. Appl Microbiol Biotechnol 1998, 50:447-454.
    • (1998) Appl Microbiol Biotechnol , vol.50 , pp. 447-454
    • Punt, P.J.1    van Gemeren, I.A.2    Drint-Kuijvenhoven, A.3    Hessing, J.G.M.4    van Muijlwijk-Harteveld, G.M.5    Beijersbergen, A.6
  • 198
    • 56049127329 scopus 로고    scopus 로고
    • Characterization of the Aspergillus niger prtT, a unique regulator of extracellular protease encoding genes
    • Punt P.J., Schuren F.H.J., Lehmbeck J., Christens J., Hjort C., van den Hondel C. Characterization of the Aspergillus niger prtT, a unique regulator of extracellular protease encoding genes. Fungal Genet Biol 2008, 45:1591-1599.
    • (2008) Fungal Genet Biol , vol.45 , pp. 1591-1599
    • Punt, P.J.1    Schuren, F.H.J.2    Lehmbeck, J.3    Christens, J.4    Hjort, C.5    van den Hondel, C.6
  • 199
    • 77954696088 scopus 로고    scopus 로고
    • Integration of insecticidal Vip3Aa1 into Beauveria bassiana enhances fungal virulence to Spodoptera litura larvae by cuticle and per os infection
    • Qin Y., Ying S.H., Chen Y., Shen Z.C., Feng M.G. Integration of insecticidal Vip3Aa1 into Beauveria bassiana enhances fungal virulence to Spodoptera litura larvae by cuticle and per os infection. Appl Environ Microbiol 2010, 76:4611-4618.
    • (2010) Appl Environ Microbiol , vol.76 , pp. 4611-4618
    • Qin, Y.1    Ying, S.H.2    Chen, Y.3    Shen, Z.C.4    Feng, M.G.5
  • 200
    • 0343924362 scopus 로고    scopus 로고
    • Synthesis of biotechnologically relevant heterologous proteins in filamentous fungi
    • Radzio R., Kueck U. Synthesis of biotechnologically relevant heterologous proteins in filamentous fungi. Proc Biochem 1997, 32:529-537.
    • (1997) Proc Biochem , vol.32 , pp. 529-537
    • Radzio, R.1    Kueck, U.2
  • 201
    • 0010268840 scopus 로고
    • Lipids in fatty acids
    • Academic Press, London, A.H. Rose (Ed.)
    • Ratledge C. Lipids in fatty acids. Primary products of metabolism 1978, 263-296. Academic Press, London. A.H. Rose (Ed.).
    • (1978) Primary products of metabolism , pp. 263-296
    • Ratledge, C.1
  • 202
    • 0026476276 scopus 로고
    • Heterologous gene expression in A. niger: A glucoamylase-porcine pancreatic phospholipase A2 fusion protein is secreted and processed to yield mature enzyme
    • Roberts I.N., Jeenes D.J., Mackenzie D.A., Wilkinson A.P., Summer I.G., Archer D.B. Heterologous gene expression in A. niger: A glucoamylase-porcine pancreatic phospholipase A2 fusion protein is secreted and processed to yield mature enzyme. Gene 1992, 122:155-161.
    • (1992) Gene , vol.122 , pp. 155-161
    • Roberts, I.N.1    Jeenes, D.J.2    Mackenzie, D.A.3    Wilkinson, A.P.4    Summer, I.G.5    Archer, D.B.6
  • 203
    • 0034788786 scopus 로고    scopus 로고
    • Physiological characterisation of Penicillium chrysogenum strains expressing the expandase gene from Streptomyces clavuligerus during batch cultivations. Growth and adipoyl-7-aminodeacetoxycephalosporanic acid production
    • Robin J., Jakobsen M., Beyer M., Noorman H., Nielsen J. Physiological characterisation of Penicillium chrysogenum strains expressing the expandase gene from Streptomyces clavuligerus during batch cultivations. Growth and adipoyl-7-aminodeacetoxycephalosporanic acid production. Appl Microbiol Biotechnol 2001, 57:357-362.
    • (2001) Appl Microbiol Biotechnol , vol.57 , pp. 357-362
    • Robin, J.1    Jakobsen, M.2    Beyer, M.3    Noorman, H.4    Nielsen, J.5
  • 204
    • 0038449119 scopus 로고    scopus 로고
    • Continuous cultivations of a Penicillium chrysogenum strain expressing the expandase gene from Streptomyces clavuligerus: growth yields and morphological characterization
    • Robin J., Lettier G., McIntyre M., Noorman H., Nielsen J. Continuous cultivations of a Penicillium chrysogenum strain expressing the expandase gene from Streptomyces clavuligerus: growth yields and morphological characterization. Biotechnol Bioeng 2003, 83:361-368.
    • (2003) Biotechnol Bioeng , vol.83 , pp. 361-368
    • Robin, J.1    Lettier, G.2    McIntyre, M.3    Noorman, H.4    Nielsen, J.5
  • 205
    • 0037500097 scopus 로고    scopus 로고
    • Influence of the adipate and dissolved oxygen concentrations on the beta-lactam production during continuous cultivations of a Penicillium chrysogenum strain expressing the expandase gene from Streptomyces clavuligerus
    • Robin J., Bonneau S., Schipper D., Noorman H., Nielsen J. Influence of the adipate and dissolved oxygen concentrations on the beta-lactam production during continuous cultivations of a Penicillium chrysogenum strain expressing the expandase gene from Streptomyces clavuligerus. Metab Eng 2003, 5:42-48.
    • (2003) Metab Eng , vol.5 , pp. 42-48
    • Robin, J.1    Bonneau, S.2    Schipper, D.3    Noorman, H.4    Nielsen, J.5
  • 207
    • 84872599964 scopus 로고    scopus 로고
    • Methods and compositions for highly efficient transformation of filamentous fungi. United States Patent Application 20020070007. 2002.
    • Romaine PC, Chen X. Methods and compositions for highly efficient transformation of filamentous fungi. United States Patent Application 20020070007. 2002.
    • Romaine, P.C.1    Chen, X.2
  • 208
    • 0008245499 scopus 로고    scopus 로고
    • Production of organic acids by fungi
    • Ruijter G.J.G., Kubicek C.P., Visser J. Production of organic acids by fungi. Mycota 2002, 10:213-220.
    • (2002) Mycota , vol.10 , pp. 213-220
    • Ruijter, G.J.G.1    Kubicek, C.P.2    Visser, J.3
  • 209
    • 0030887664 scopus 로고    scopus 로고
    • Overexpression of phosphofructokinase and pyruvate kinase in citric acid producing Aspergillus niger
    • Ruijter G.J.G., Panneman H., Visser J. Overexpression of phosphofructokinase and pyruvate kinase in citric acid producing Aspergillus niger. Biochim Biophys Acta 1997, 1334:317-326.
    • (1997) Biochim Biophys Acta , vol.1334 , pp. 317-326
    • Ruijter, G.J.G.1    Panneman, H.2    Visser, J.3
  • 210
    • 77955850991 scopus 로고    scopus 로고
    • Enzyme systems for biodegradation of polychlorinated dibenzo-p-dioxins
    • Sakaki T., Munetsuna E. Enzyme systems for biodegradation of polychlorinated dibenzo-p-dioxins. Appl Microbiol Biotechnol 2010, 88:23-30.
    • (2010) Appl Microbiol Biotechnol , vol.88 , pp. 23-30
    • Sakaki, T.1    Munetsuna, E.2
  • 211
    • 0032589910 scopus 로고    scopus 로고
    • δ6-fatty acid desaturase from an arachidonic acid-producing Mortierella fungus-gene cloning and its heterologous expression in a fungus, Aspergillus
    • Sakuradani E., Kobayashi M., Shimizu S. δ6-fatty acid desaturase from an arachidonic acid-producing Mortierella fungus-gene cloning and its heterologous expression in a fungus, Aspergillus. Gene 1999, 238:445-453.
    • (1999) Gene , vol.238 , pp. 445-453
    • Sakuradani, E.1    Kobayashi, M.2    Shimizu, S.3
  • 212
    • 77249172624 scopus 로고    scopus 로고
    • Molecular genetic analysis of the orsellinic acid/F9775 gene cluster of Aspergillus nidulans
    • Sanchez J.F., Chiang Y.M., Szewczyk E., Davidson A.D., Ahuja M., Oakley C.E., et al. Molecular genetic analysis of the orsellinic acid/F9775 gene cluster of Aspergillus nidulans. Mol Biosyst 2009, 6:587-593.
    • (2009) Mol Biosyst , vol.6 , pp. 587-593
    • Sanchez, J.F.1    Chiang, Y.M.2    Szewczyk, E.3    Davidson, A.D.4    Ahuja, M.5    Oakley, C.E.6
  • 213
    • 79251612884 scopus 로고    scopus 로고
    • A comprehensive overview on genomically directed assembly of aromatic polyketides and macrolide lactones using fungal megasynthases
    • Saruwatari T., Praseuth A.P., Sato M., Torikai K., Noguchi H., Watanabe K. A comprehensive overview on genomically directed assembly of aromatic polyketides and macrolide lactones using fungal megasynthases. J Antibiotics 2011, 64:9-17.
    • (2011) J Antibiotics , vol.64 , pp. 9-17
    • Saruwatari, T.1    Praseuth, A.P.2    Sato, M.3    Torikai, K.4    Noguchi, H.5    Watanabe, K.6
  • 214
    • 0028100107 scopus 로고
    • Parallel formation and synergism of hydrolytic enzymes and peptaibol antibiotics, molecular mechanisms involved in the antagonistic action of Trichoderma harzianum against phytopathogenic fungi
    • Schirmböck M., Lorito M., Wang Y.L., Hayes C.K., Arisan-Atac I., Scala F., et al. Parallel formation and synergism of hydrolytic enzymes and peptaibol antibiotics, molecular mechanisms involved in the antagonistic action of Trichoderma harzianum against phytopathogenic fungi. Appl Environ Microbiol 1994, 60:4364-4370.
    • (1994) Appl Environ Microbiol , vol.60 , pp. 4364-4370
    • Schirmböck, M.1    Lorito, M.2    Wang, Y.L.3    Hayes, C.K.4    Arisan-Atac, I.5    Scala, F.6
  • 215
    • 0041886864 scopus 로고    scopus 로고
    • Regulation of Trichoderma cellulose formation: lessons in molecular biology from an industrial fungus. A review
    • Schmoll M., Kubicek C.P. Regulation of Trichoderma cellulose formation: lessons in molecular biology from an industrial fungus. A review. Acta Microbiol Immunol Hung 2003, 50:125-145.
    • (2003) Acta Microbiol Immunol Hung , vol.50 , pp. 125-145
    • Schmoll, M.1    Kubicek, C.P.2
  • 216
    • 77955852810 scopus 로고    scopus 로고
    • Recombinant production of an Aspergillus bidulans class 1 hydrophobin (DewA) in Hypocrea jecorina (Trichoderma reesei) is promoter dependent
    • Schmoll M., Seibel C., Kotlowski C., Vendt F.W.G., Liebmann B., Kubicek C. Recombinant production of an Aspergillus bidulans class 1 hydrophobin (DewA) in Hypocrea jecorina (Trichoderma reesei) is promoter dependent. Appl Microbiol Biotechnol 2010, 88:95-103.
    • (2010) Appl Microbiol Biotechnol , vol.88 , pp. 95-103
    • Schmoll, M.1    Seibel, C.2    Kotlowski, C.3    Vendt, F.W.G.4    Liebmann, B.5    Kubicek, C.6
  • 217
    • 0036180541 scopus 로고    scopus 로고
    • Molecular cloning of an extracellular aspartic proteinase from Rhizopus microsporus and evidence for its expression during infection
    • Schoen C., Reichard U., Monod M., Kratzin H.D., Ruchel R. Molecular cloning of an extracellular aspartic proteinase from Rhizopus microsporus and evidence for its expression during infection. Med Mycol 2002, 40:61-71.
    • (2002) Med Mycol , vol.40 , pp. 61-71
    • Schoen, C.1    Reichard, U.2    Monod, M.3    Kratzin, H.D.4    Ruchel, R.5
  • 218
  • 220
    • 33645302916 scopus 로고    scopus 로고
    • Current approaches to diagnosis and treatment of invasive aspergillosis
    • Segal B.H., Walsh T.J. Current approaches to diagnosis and treatment of invasive aspergillosis. Am J Respir Crit Care Med 2006, 173:707-717.
    • (2006) Am J Respir Crit Care Med , vol.173 , pp. 707-717
    • Segal, B.H.1    Walsh, T.J.2
  • 221
    • 35748970166 scopus 로고    scopus 로고
    • The d-xylose reductase of Hypocrea jecorina is the major aldose reductase in pentose and d-galactose catabolism and necessary for beta-galactosidase and cellulase induction by lactose
    • Seiboth B., Gamauf C., Pail M., Hartl L., Kubicek C.P. The d-xylose reductase of Hypocrea jecorina is the major aldose reductase in pentose and d-galactose catabolism and necessary for beta-galactosidase and cellulase induction by lactose. Mol Microbiol 2007, 66:890-900.
    • (2007) Mol Microbiol , vol.66 , pp. 890-900
    • Seiboth, B.1    Gamauf, C.2    Pail, M.3    Hartl, L.4    Kubicek, C.P.5
  • 222
    • 76349125108 scopus 로고    scopus 로고
    • Approaches for refining heterologous protein production in filamentous fungi
    • Sharma R., Katoch M., Srivastava P., Qazi G. Approaches for refining heterologous protein production in filamentous fungi. World J Microbiol Biotechnol 2009, 25:2083-2094.
    • (2009) World J Microbiol Biotechnol , vol.25 , pp. 2083-2094
    • Sharma, R.1    Katoch, M.2    Srivastava, P.3    Qazi, G.4
  • 223
    • 0037398774 scopus 로고    scopus 로고
    • Polyketide biosynthesis beyond the type I, II and III polyketide synthase paradigms
    • Shen B. Polyketide biosynthesis beyond the type I, II and III polyketide synthase paradigms. Curr Opin Chem Biol 2003, 7:285-295.
    • (2003) Curr Opin Chem Biol , vol.7 , pp. 285-295
    • Shen, B.1
  • 224
    • 0030624098 scopus 로고    scopus 로고
    • Screening of novel microbial enzymes for the production of biologically and chemically useful compounds
    • Shimizu S., Ogawa J., Kataoka M., Kobayashi M. Screening of novel microbial enzymes for the production of biologically and chemically useful compounds. Adv Biochem Eng Biotech 1997, 58:45-87.
    • (1997) Adv Biochem Eng Biotech , vol.58 , pp. 45-87
    • Shimizu, S.1    Ogawa, J.2    Kataoka, M.3    Kobayashi, M.4
  • 225
    • 70449520062 scopus 로고    scopus 로고
    • Heterologous production of non-ribosomal peptide LLD-ACV in Saccharomyces cerevisiae
    • Siewers V., Chen X., Huang L., Zhang J., Nielsen J. Heterologous production of non-ribosomal peptide LLD-ACV in Saccharomyces cerevisiae. Metab Eng 2009, 11:391-397.
    • (2009) Metab Eng , vol.11 , pp. 391-397
    • Siewers, V.1    Chen, X.2    Huang, L.3    Zhang, J.4    Nielsen, J.5
  • 226
    • 0347985840 scopus 로고    scopus 로고
    • Use of expressed sequence tag analysis and cDNA microarrays of the filamentous fungus Aspergillus nidulans
    • Sims A.H., Robson G.D., Hoyle D.C., Oliver S.G., Turner G., Prade R.A., et al. Use of expressed sequence tag analysis and cDNA microarrays of the filamentous fungus Aspergillus nidulans. Fungal Genet Biol 2004, 41:199-212.
    • (2004) Fungal Genet Biol , vol.41 , pp. 199-212
    • Sims, A.H.1    Robson, G.D.2    Hoyle, D.C.3    Oliver, S.G.4    Turner, G.5    Prade, R.A.6
  • 227
    • 0025004152 scopus 로고
    • The multifunctional peptide synthetase performing the first step of penicillin biosynthesis in Penicillium chrysogenum is a 421 073 dalton protein similar to Bacillus brevis peptide antibiotic synthetases
    • Smith D.J., Earl A.J., Turner G. The multifunctional peptide synthetase performing the first step of penicillin biosynthesis in Penicillium chrysogenum is a 421 073 dalton protein similar to Bacillus brevis peptide antibiotic synthetases. EMBO J 1990, 9:2743-2750.
    • (1990) EMBO J , vol.9 , pp. 2743-2750
    • Smith, D.J.1    Earl, A.J.2    Turner, G.3
  • 228
    • 0032533738 scopus 로고    scopus 로고
    • Determinants of the fidelity of processing glucoamylase-lysozyme fusions by Aspergillus niger
    • Spencer J.A., Jeenes D.J., MacKenzie D.A., Hyanie D.T., Archer D.B. Determinants of the fidelity of processing glucoamylase-lysozyme fusions by Aspergillus niger. Eur J Biochem 1998, 258:107-112.
    • (1998) Eur J Biochem , vol.258 , pp. 107-112
    • Spencer, J.A.1    Jeenes, D.J.2    MacKenzie, D.A.3    Hyanie, D.T.4    Archer, D.B.5
  • 229
    • 37849185905 scopus 로고    scopus 로고
    • Characterization of an extracellular subtilisin protease of Rhizopus microsporus and evidence for its expression during invasive rhinoorbital mycosis
    • Spreer A., Ruchel R., Reichard U. Characterization of an extracellular subtilisin protease of Rhizopus microsporus and evidence for its expression during invasive rhinoorbital mycosis. Med Mycol 2006, 44:723-731.
    • (2006) Med Mycol , vol.44 , pp. 723-731
    • Spreer, A.1    Ruchel, R.2    Reichard, U.3
  • 230
    • 84864912712 scopus 로고    scopus 로고
    • Trichoderma: systematics, molecular taxonomy and agricultural and industrial applications
    • Science Publishers, Enfield, R.C. Ray (Ed.)
    • Sriram S., Ray R.C. Trichoderma: systematics, molecular taxonomy and agricultural and industrial applications. Microbial Biotechnology in Agriculture and Aquaculture 2005, Vol 1:335-376. Science Publishers, Enfield. R.C. Ray (Ed.).
    • (2005) Microbial Biotechnology in Agriculture and Aquaculture , vol.1 , pp. 335-376
    • Sriram, S.1    Ray, R.C.2
  • 231
    • 0029987451 scopus 로고    scopus 로고
    • Construction of an improved mycoinsecticide overexpressing a toxic protease
    • St Leger R.J., Joshi L., Bidochka M.J., Roberts D.W. Construction of an improved mycoinsecticide overexpressing a toxic protease. Proc Natl Acad Sci USA 1996, 93:6349-6354.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 6349-6354
    • St Leger, R.J.1    Joshi, L.2    Bidochka, M.J.3    Roberts, D.W.4
  • 232
    • 0028837014 scopus 로고
    • Modular structure of genes encoding multifunctional peptide synthetases required for non-ribosomal peptide synthesis
    • Stachelhaus T., Marahiel M.A. Modular structure of genes encoding multifunctional peptide synthetases required for non-ribosomal peptide synthesis. FEMS Microbiol Lett 1995, 125:3-14.
    • (1995) FEMS Microbiol Lett , vol.125 , pp. 3-14
    • Stachelhaus, T.1    Marahiel, M.A.2
  • 234
    • 0018736190 scopus 로고
    • Induction of cellulolytic enzymes in Trichoderma reesei by sophorose
    • Sternberg D., Mandels G.R. Induction of cellulolytic enzymes in Trichoderma reesei by sophorose. J Bacteriol 1979, 139:761-769.
    • (1979) J Bacteriol , vol.139 , pp. 761-769
    • Sternberg, D.1    Mandels, G.R.2
  • 235
    • 0029961704 scopus 로고    scopus 로고
    • Efficient expression of a Phanerochaete chrysosporium manganese peroxidase gene in Aspergillus oryzae
    • Stewart P., Whitwam R.E., Kersten P.J., Cullen D., Tien M. Efficient expression of a Phanerochaete chrysosporium manganese peroxidase gene in Aspergillus oryzae. Appl Microbiol Biotechnol 1996, 62:860-864.
    • (1996) Appl Microbiol Biotechnol , vol.62 , pp. 860-864
    • Stewart, P.1    Whitwam, R.E.2    Kersten, P.J.3    Cullen, D.4    Tien, M.5
  • 236
    • 0032215489 scopus 로고    scopus 로고
    • Recombinant glucoamylase production by Aspergillus niger B1 in chemostat and pH-autostat cultures
    • Swift R.J., Wiebe M.G., Robson G.D., Trinci A.P.J. Recombinant glucoamylase production by Aspergillus niger B1 in chemostat and pH-autostat cultures. Fungal Genet Biol 1998, 25:100-109.
    • (1998) Fungal Genet Biol , vol.25 , pp. 100-109
    • Swift, R.J.1    Wiebe, M.G.2    Robson, G.D.3    Trinci, A.P.J.4
  • 238
    • 0018599365 scopus 로고
    • Application of microbial enzymes in food systems and in biotechnology
    • Tailor M.J., Richardson T. Application of microbial enzymes in food systems and in biotechnology. Adv Appl Microbiol 1979, 25:7-35.
    • (1979) Adv Appl Microbiol , vol.25 , pp. 7-35
    • Tailor, M.J.1    Richardson, T.2
  • 239
    • 84954951817 scopus 로고
    • A 155K acid carboxypeptidase O from Aspergillus oryzae
    • Takuchi M., Ichishima E. A 155K acid carboxypeptidase O from Aspergillus oryzae. Agric Biol Chem 1986, 50:633-638.
    • (1986) Agric Biol Chem , vol.50 , pp. 633-638
    • Takuchi, M.1    Ichishima, E.2
  • 242
    • 0034663740 scopus 로고    scopus 로고
    • Cloning and sequencing of the triacylglycerol lipase gene of Aspergillus oryzae and its expression in Escherichia coli
    • Toida J., Fukuzawa M., Kobayashi G., Ito K., Sekiguchi J. Cloning and sequencing of the triacylglycerol lipase gene of Aspergillus oryzae and its expression in Escherichia coli. FEMS Microbiol Lett 2000, 189:159-164.
    • (2000) FEMS Microbiol Lett , vol.189 , pp. 159-164
    • Toida, J.1    Fukuzawa, M.2    Kobayashi, G.3    Ito, K.4    Sekiguchi, J.5
  • 243
    • 0030569904 scopus 로고    scopus 로고
    • Optimization of nonlinear biotechnological processes with linear programming: application to citric acid production by Aspergillus niger
    • Torres N.V., Voit E.O., Gonzalez-Alcon C. Optimization of nonlinear biotechnological processes with linear programming: application to citric acid production by Aspergillus niger. Biotechnol Bioeng 1996, 49:247-258.
    • (1996) Biotechnol Bioeng , vol.49 , pp. 247-258
    • Torres, N.V.1    Voit, E.O.2    Gonzalez-Alcon, C.3
  • 244
    • 65149088593 scopus 로고
    • The role of hydrolytic enzymes produced by Trichoderma harzianum in biological control of plant diseases
    • P. Suominen, T. Reinikainen (Eds.) Proc 2nd Tricel Symposium on Trichoderma Cellulases and other Hydrolases
    • Tronsmo A., Klemsdal S.S., Hayes C.K., Lorito M., Harman G.E. The role of hydrolytic enzymes produced by Trichoderma harzianum in biological control of plant diseases. Found Biotechnol Indust Fermenation Res 1993, 8:159-168. P. Suominen, T. Reinikainen (Eds.).
    • (1993) Found Biotechnol Indust Fermenation Res , vol.8 , pp. 159-168
    • Tronsmo, A.1    Klemsdal, S.S.2    Hayes, C.K.3    Lorito, M.4    Harman, G.E.5
  • 245
    • 67650621098 scopus 로고    scopus 로고
    • Analytical and computational approaches to define the Aspergillus niger secretome
    • Tsang A., Butler G., Powlowski, Panisko E.A., Baker S.E. Analytical and computational approaches to define the Aspergillus niger secretome. Fungal Genet Biol 2009, 46(Suppl 1):S153-S160.
    • (2009) Fungal Genet Biol , vol.46 , Issue.SUPPL 1
    • Tsang, A.1    Butler, G.2    Powlowski3    Panisko, E.A.4    Baker, S.E.5
  • 246
    • 85007767228 scopus 로고
    • High level secretion of calf chymosin using a glucoamylase prochymosin fusion gene in Aspergillus oryzae
    • Tsuchiya K., Nagasjhiam T., Yamamoto Y., Gomi K., Kitamoto K., Umagai C. High level secretion of calf chymosin using a glucoamylase prochymosin fusion gene in Aspergillus oryzae. Biosci Biotechnol Biochem 1994, 58:895-899.
    • (1994) Biosci Biotechnol Biochem , vol.58 , pp. 895-899
    • Tsuchiya, K.1    Nagasjhiam, T.2    Yamamoto, Y.3    Gomi, K.4    Kitamoto, K.5    Umagai, C.6
  • 248
    • 0018668809 scopus 로고
    • Formation and release of cellulolytic enzymes during growth of Trichoderma reesei on cellobiose and glycerol
    • Vaheri M.P., Vaheri M.E.O., Kauppinen V.S. Formation and release of cellulolytic enzymes during growth of Trichoderma reesei on cellobiose and glycerol. Eur J Appl Microbiol Biotechnol 1979, 8:73-80.
    • (1979) Eur J Appl Microbiol Biotechnol , vol.8 , pp. 73-80
    • Vaheri, M.P.1    Vaheri, M.E.O.2    Kauppinen, V.S.3
  • 249
    • 0034343389 scopus 로고    scopus 로고
    • Innovations in cephalosporin and penicillin production: painting the antibiotics industry green
    • van de Sandt E.J.A.X., de Vroom E. Innovations in cephalosporin and penicillin production: painting the antibiotics industry green. Chim Oggi-Chem Today 2000, 18:72-75.
    • (2000) Chim Oggi-Chem Today , vol.18 , pp. 72-75
    • van de Sandt, E.J.A.X.1    de Vroom, E.2
  • 253
    • 0038159924 scopus 로고    scopus 로고
    • On the safety of a new generation of DSM Aspergillus niger enzyme production strains
    • Van Dijck P.W.M., Selten G.C.M., Hempenius R.A. On the safety of a new generation of DSM Aspergillus niger enzyme production strains. Regulat Toxicol Pharmacol 2003, 38:27-35.
    • (2003) Regulat Toxicol Pharmacol , vol.38 , pp. 27-35
    • Van Dijck, P.W.M.1    Selten, G.C.M.2    Hempenius, R.A.3
  • 255
    • 76549107629 scopus 로고    scopus 로고
    • An alternative to fish oils: metabolic engineering of oil-seed crops to produce omega-3 long chain polyunsaturated fatty acids
    • Venegas-Caleron M., Sayanova O., Napier J.A. An alternative to fish oils: metabolic engineering of oil-seed crops to produce omega-3 long chain polyunsaturated fatty acids. Prog Lipid Res 2010, 49:108-119.
    • (2010) Prog Lipid Res , vol.49 , pp. 108-119
    • Venegas-Caleron, M.1    Sayanova, O.2    Napier, J.A.3
  • 256
    • 34047238347 scopus 로고    scopus 로고
    • A dedicated vector for efficient library construction and high throughput screening in the hyphal fungus Chrysosporium lucknowense
    • Verdoes J.C., Punt P.J., Burlingame R., Bartels J., Van Dijk R., Slump E., et al. A dedicated vector for efficient library construction and high throughput screening in the hyphal fungus Chrysosporium lucknowense. Ind Biotechnol 2007, 3:48-57.
    • (2007) Ind Biotechnol , vol.3 , pp. 48-57
    • Verdoes, J.C.1    Punt, P.J.2    Burlingame, R.3    Bartels, J.4    Van Dijk, R.5    Slump, E.6
  • 257
    • 63849314526 scopus 로고    scopus 로고
    • A survey of nonribosomal peptide synthetase (NRPS) genes in Aspergillus nidulans
    • von Dohren H. A survey of nonribosomal peptide synthetase (NRPS) genes in Aspergillus nidulans. Fungal Genet Biol 2009, 46(Suppl 1):S45-S52.
    • (2009) Fungal Genet Biol , vol.46 , Issue.SUPPL 1
    • von Dohren, H.1
  • 258
    • 79952215337 scopus 로고    scopus 로고
    • Molecular cloning and expression analysis of a delta 6-fatty acid desaturase gene from Rhizopus stolonifer strain YF6 which can accumulate high levels of gamma-linolenic acid
    • Wan X., Zhang Y.B., Wang P., Jiang M. Molecular cloning and expression analysis of a delta 6-fatty acid desaturase gene from Rhizopus stolonifer strain YF6 which can accumulate high levels of gamma-linolenic acid. J Microbiol 2011, 49:151-154.
    • (2011) J Microbiol , vol.49 , pp. 151-154
    • Wan, X.1    Zhang, Y.B.2    Wang, P.3    Jiang, M.4
  • 259
    • 34250643216 scopus 로고    scopus 로고
    • Involvement of nitric oxide in cerebroside-induced defense responses and taxol production in Taxus yunnanensis suspension cells
    • Wang J.W., Zheng L.P., Tan R.X. Involvement of nitric oxide in cerebroside-induced defense responses and taxol production in Taxus yunnanensis suspension cells. Appl Microbiol Biotechnol 2007, 75:1183-1190.
    • (2007) Appl Microbiol Biotechnol , vol.75 , pp. 1183-1190
    • Wang, J.W.1    Zheng, L.P.2    Tan, R.X.3
  • 260
    • 0344530293 scopus 로고    scopus 로고
    • Effects of process parameters on heterologous protein production in Aspergillus niger fermentation
    • Wang L., Darin R., Tingyue G., Moo-Young M. Effects of process parameters on heterologous protein production in Aspergillus niger fermentation. J Chem Technol Biotechnol 2003, 78:1259-1266.
    • (2003) J Chem Technol Biotechnol , vol.78 , pp. 1259-1266
    • Wang, L.1    Darin, R.2    Tingyue, G.3    Moo-Young, M.4
  • 261
    • 20644462160 scopus 로고    scopus 로고
    • Bioprocessing strategies to improve heterologous protein production in filamentous fungal fermentations
    • Wang L., Ridgway D., Gu T., Moo-Young M. Bioprocessing strategies to improve heterologous protein production in filamentous fungal fermentations. Biotechnol Advances 2005, 23:115-129.
    • (2005) Biotechnol Advances , vol.23 , pp. 115-129
    • Wang, L.1    Ridgway, D.2    Gu, T.3    Moo-Young, M.4
  • 262
    • 77952839023 scopus 로고    scopus 로고
    • Research advances on taxol production by microbe fermentation
    • Wang S.W., Ma X., Ping W.X., Zhou D.P. Research advances on taxol production by microbe fermentation. Microbiology 2007, 34:561-565.
    • (2007) Microbiology , vol.34 , pp. 561-565
    • Wang, S.W.1    Ma, X.2    Ping, W.X.3    Zhou, D.P.4
  • 263
    • 34447618285 scopus 로고    scopus 로고
    • Transformation of taxol-producing endophytic fungi by restriction enzyme-mediated integration (REMI)
    • Wang Y.C., Guo B.H., Miao Z.Q., Tang K.X. Transformation of taxol-producing endophytic fungi by restriction enzyme-mediated integration (REMI). FEMS Microbiol Lett 2007, 273:253-259.
    • (2007) FEMS Microbiol Lett , vol.273 , pp. 253-259
    • Wang, Y.C.1    Guo, B.H.2    Miao, Z.Q.3    Tang, K.X.4
  • 264
    • 34247340584 scopus 로고    scopus 로고
    • Functional analysis of lipid metabolism in Magnaporthe grisea reveals a requirement for peroxisomal fatty acid β-oxidation during appressorium-mediated plant infection
    • Wang Z.-Y., Soanes D.M., Kershaw M.J., Talbot N.J. Functional analysis of lipid metabolism in Magnaporthe grisea reveals a requirement for peroxisomal fatty acid β-oxidation during appressorium-mediated plant infection. Mol Plant Microbe Interact 2007, 20:475-491.
    • (2007) Mol Plant Microbe Interact , vol.20 , pp. 475-491
    • Wang, Z.-Y.1    Soanes, D.M.2    Kershaw, M.J.3    Talbot, N.J.4
  • 265
    • 0015211527 scopus 로고
    • Plant antitumor agents. VI. The isolation and structure of taxol, a novel antileukemic and antitumor agent from Taxus brevifolia
    • Wani M.C., Taylor H.L., Wall M.E., Coggon P., McPhail A.T. Plant antitumor agents. VI. The isolation and structure of taxol, a novel antileukemic and antitumor agent from Taxus brevifolia. J Am Chem Soc 1971, 93:2325-2327.
    • (1971) J Am Chem Soc , vol.93 , pp. 2325-2327
    • Wani, M.C.1    Taylor, H.L.2    Wall, M.E.3    Coggon, P.4    McPhail, A.T.5
  • 266
    • 11944256451 scopus 로고
    • Improved production of chymosin in Aspergillus by expression as a glucoamylase-chymosin fusion
    • Ward M., Wilson L.J., Kodama K.H., Rey M.W., Berka R.M. Improved production of chymosin in Aspergillus by expression as a glucoamylase-chymosin fusion. Bio-Technology 1990, 8:435-440.
    • (1990) Bio-Technology , vol.8 , pp. 435-440
    • Ward, M.1    Wilson, L.J.2    Kodama, K.H.3    Rey, M.W.4    Berka, R.M.5
  • 269
    • 26844565513 scopus 로고    scopus 로고
    • Omega-3/6 fatty acids: alternative sources of production
    • Ward O.P., Singh A. Omega-3/6 fatty acids: alternative sources of production. Process Biochem 2005, 40:3627-3652.
    • (2005) Process Biochem , vol.40 , pp. 3627-3652
    • Ward, O.P.1    Singh, A.2
  • 270
    • 0004226069 scopus 로고
    • Open University Press, Milton Keynes
    • Ward O.P. Bioprocessing 1991, Open University Press, Milton Keynes.
    • (1991) Bioprocessing
    • Ward, O.P.1
  • 272
    • 85012844614 scopus 로고    scopus 로고
    • Proteases. Comprehensive Biotechnology 2nd ed. Moo-Young M, editor.
    • Ward OP. Proteases. Comprehensive Biotechnology 2nd ed. Moo-Young M, editor. Vol. 3. 2011. pp 571-582.
    • (2011) , vol.3 , pp. 571-582
    • Ward, O.P.1
  • 273
    • 0026448560 scopus 로고
    • An inducible expression system for the production of human lactoferrin in A. nidulans
    • Ward P.P., May G.S., Headon D.R., Conneely O.M. An inducible expression system for the production of human lactoferrin in A. nidulans. Gene 1992, 122:219-223.
    • (1992) Gene , vol.122 , pp. 219-223
    • Ward, P.P.1    May, G.S.2    Headon, D.R.3    Conneely, O.M.4
  • 274
    • 0029026622 scopus 로고
    • A system for production of commercial quantities of human lactoferrin: a broad spectrum natural antibiotic
    • Ward P.P., Peddington C.S., Cunnighham G.A., Zhou X., Wyatt R.D., Conneely O.M. A system for production of commercial quantities of human lactoferrin: a broad spectrum natural antibiotic. Biotechnology 1995, 13:498-503.
    • (1995) Biotechnology , vol.13 , pp. 498-503
    • Ward, P.P.1    Peddington, C.S.2    Cunnighham, G.A.3    Zhou, X.4    Wyatt, R.D.5    Conneely, O.M.6
  • 275
    • 0030155688 scopus 로고    scopus 로고
    • Demonstration of the catalytic roles and evidence for the physical association of type I fatty acid synthases and a polyketide synthase in the biosynthesis of aflatoxin B1
    • Watanabe C.M., Wilson D., Linz J.E., Townsend C.A. Demonstration of the catalytic roles and evidence for the physical association of type I fatty acid synthases and a polyketide synthase in the biosynthesis of aflatoxin B1. Chem Biol 1996, 3:463-469.
    • (1996) Chem Biol , vol.3 , pp. 463-469
    • Watanabe, C.M.1    Wilson, D.2    Linz, J.E.3    Townsend, C.A.4
  • 276
    • 0028284699 scopus 로고
    • The peptide synthetase catalyzing cyclosporin production in Tolypocladium niveum is encoded by a giant 45.8-kilobase open reading frame
    • Weber G., Schörgendorfer K., Schneider-Scherzer E., Leitner E. The peptide synthetase catalyzing cyclosporin production in Tolypocladium niveum is encoded by a giant 45.8-kilobase open reading frame. Curr Genet 1994, 26:120-125.
    • (1994) Curr Genet , vol.26 , pp. 120-125
    • Weber, G.1    Schörgendorfer, K.2    Schneider-Scherzer, E.3    Leitner, E.4
  • 278
    • 0034092485 scopus 로고    scopus 로고
    • Increased heterologous protein production in Aspergillus niger fermentation through extracellular proteases inhibition by pelleted growth
    • Xu J., Wang L., Ridgway D., Gu T., Moo-Young M. Increased heterologous protein production in Aspergillus niger fermentation through extracellular proteases inhibition by pelleted growth. Biotechnol Prog 2000, 16:222-227.
    • (2000) Biotechnol Prog , vol.16 , pp. 222-227
    • Xu, J.1    Wang, L.2    Ridgway, D.3    Gu, T.4    Moo-Young, M.5
  • 280
    • 77956586581 scopus 로고    scopus 로고
    • Enhanced production and secretion of heterologous proteins by the filamentous fungus Aspergillus oryzae via disruption of the vacuolar protein sorting receptor gene Aovps10
    • Yoon J., Aishan T., Maruyama J., Kitamoto K. Enhanced production and secretion of heterologous proteins by the filamentous fungus Aspergillus oryzae via disruption of the vacuolar protein sorting receptor gene Aovps10. Appl Environ Microbiol 2010, 76:5718-5727.
    • (2010) Appl Environ Microbiol , vol.76 , pp. 5718-5727
    • Yoon, J.1    Aishan, T.2    Maruyama, J.3    Kitamoto, K.4
  • 281
    • 79251569555 scopus 로고    scopus 로고
    • Disruption of ten protease genes in the filamentous fungus Aspergillus oryzae highly improves production of heterologous proteins
    • Yoon J., Maruyama J., Kitamoto K. Disruption of ten protease genes in the filamentous fungus Aspergillus oryzae highly improves production of heterologous proteins. Appl Microbiol Biotechnol 2011, 89:747-759.
    • (2011) Appl Microbiol Biotechnol , vol.89 , pp. 747-759
    • Yoon, J.1    Maruyama, J.2    Kitamoto, K.3
  • 283
    • 10444267229 scopus 로고    scopus 로고
    • A rapid method for promoter exchange in Aspergillus nidulans using recombinant PCR
    • Zarrin M., Leeder A.C., Turner G. A rapid method for promoter exchange in Aspergillus nidulans using recombinant PCR. Fungal Genet Biol 2005, 42:1-8.
    • (2005) Fungal Genet Biol , vol.42 , pp. 1-8
    • Zarrin, M.1    Leeder, A.C.2    Turner, G.3
  • 284
    • 33846225277 scopus 로고    scopus 로고
    • Identification of a novel bifunctional 12/15 fatty acid desaturase from a basidiomycete, Coprinus cinereus TD#822-2
    • Zhang S., Sakuradani E., Ito K., Shimizu S. Identification of a novel bifunctional 12/15 fatty acid desaturase from a basidiomycete, Coprinus cinereus TD#822-2. FEBS Lett 2007, 581:315-319.
    • (2007) FEBS Lett , vol.581 , pp. 315-319
    • Zhang, S.1    Sakuradani, E.2    Ito, K.3    Shimizu, S.4
  • 285
    • 58549085193 scopus 로고    scopus 로고
    • Engineered biosynthesis of bacterial aromatic polyketides in Escherichia coli
    • Zhang W., Li Y., Tang Y. Engineered biosynthesis of bacterial aromatic polyketides in Escherichia coli. Proc Natl Acad Sci USA 2008, 105:20683-20688.
    • (2008) Proc Natl Acad Sci USA , vol.105 , pp. 20683-20688
    • Zhang, W.1    Li, Y.2    Tang, Y.3
  • 286
    • 0031963541 scopus 로고    scopus 로고
    • Construction of a low-serine-typecarboxypeptidase-producing mutant of Aspergillus oryzae by the expression of antisense RNA and its use as a host for heterologous protein secretion
    • Zheng X.F., Kobayashi Y., Takeuchi A. Construction of a low-serine-typecarboxypeptidase-producing mutant of Aspergillus oryzae by the expression of antisense RNA and its use as a host for heterologous protein secretion. Appl Microbiol Biotechnol 1998, 49:39-44.
    • (1998) Appl Microbiol Biotechnol , vol.49 , pp. 39-44
    • Zheng, X.F.1    Kobayashi, Y.2    Takeuchi, A.3
  • 287
    • 77952837839 scopus 로고    scopus 로고
    • A review: recent advances and future prospects of taxol-producing endophytic fungi
    • Zhou X., Zhu H., Liu L., Lin J., Tang K. A review: recent advances and future prospects of taxol-producing endophytic fungi. Appl Microbiol Biotechnol 2010, 86:1707-1717.
    • (2010) Appl Microbiol Biotechnol , vol.86 , pp. 1707-1717
    • Zhou, X.1    Zhu, H.2    Liu, L.3    Lin, J.4    Tang, K.5
  • 288
    • 46349089230 scopus 로고    scopus 로고
    • Protoplast formation, regeneration and transformation from the taxol-producing fungus Ozonium sp
    • Zhou X.W., Wei Y.M., Zhu H.F., Wang Z.N., Lin J., Liu L., Tang K.X. Protoplast formation, regeneration and transformation from the taxol-producing fungus Ozonium sp. Afr J Biotechnol 2008, 7:2017-2024.
    • (2008) Afr J Biotechnol , vol.7 , pp. 2017-2024
    • Zhou, X.W.1    Wei, Y.M.2    Zhu, H.F.3    Wang, Z.N.4    Lin, J.5    Liu, L.6    Tang, K.X.7


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