메뉴 건너뛰기




Volumn 2, Issue , 2009, Pages

Metabolic engineering strategies for the improvement of cellulase production by Hypocrea jecorina

Author keywords

[No Author keywords available]

Indexed keywords

CELLULASE PRODUCTION; CHEMICAL INTERMEDIATES; COMPLETE GENOMES; HEMICELLULASES; HYPOCREA; INDUSTRIAL SOURCES; PLANT BIOMASS; TRICHODERMA REESEI;

EID: 70349772781     PISSN: 17546834     EISSN: None     Source Type: Journal    
DOI: 10.1186/1754-6834-2-19     Document Type: Review
Times cited : (315)

References (112)
  • 2
    • 0001646214 scopus 로고    scopus 로고
    • Applications of Trichoderma reesei enzymes in the pulp and paper industry
    • London: Taylor & Francis Harman GE, Kubicek CP
    • Applications of Trichoderma reesei enzymes in the pulp and paper industry. J Buchert, J Oksanen, J Pere, M Siika-Aho, A Suurnäkki, L Viikari, Trichoderma and Gliocladium London: Taylor & Francis, Harman GE, Kubicek CP, 1998 2 343 364
    • (1998) Trichoderma and Gliocladium , vol.2 , pp. 343-364
    • Buchert, J.1    Oksanen, J.2    Pere, J.3    Siika-Aho, M.4    Suurnäkki, A.5    Viikari, L.6
  • 3
    • 0001098948 scopus 로고    scopus 로고
    • Applications of Trichoderma reesei enzymes in the food and feed industries
    • London: Taylor & Francis Harman GE, Kubicek CP
    • Applications of Trichoderma reesei enzymes in the food and feed industries. YM Galante, A De Conti, R Monteverdi, Trichoderma and Gliocladium London: Taylor & Francis, Harman GE, Kubicek CP, 1998 2 338 342
    • (1998) Trichoderma and Gliocladium , vol.2 , pp. 338-342
    • Galante, Y.M.1    De Conti, A.2    Monteverdi, R.3
  • 4
    • 0001098948 scopus 로고    scopus 로고
    • Applications of Trichoderma reesei enzymes in the textile industry
    • London: Taylor & Francis Harman GE, Kubicek CP
    • Applications of Trichoderma reesei enzymes in the textile industry. YM Galante, A De Conti, R Monteverdi, Trichoderma and Gliocladium London: Taylor & Francis, Harman GE, Kubicek CP, 1998 2 311 326
    • (1998) Trichoderma and Gliocladium , vol.2 , pp. 311-326
    • Galante, Y.M.1    De Conti, A.2    Monteverdi, R.3
  • 5
    • 0001973467 scopus 로고    scopus 로고
    • Carbohydrate-active enzymes: An integrated database approach
    • Cambridge: Royal Society of Chemistry Svensson B
    • Carbohydrate-active enzymes: An integrated database approach. PM Coutinho, B Henrissat, Recent Advances in Carbohydrate Bioengineering Cambridge: Royal Society of Chemistry, Svensson B, 1999 3 14
    • (1999) Recent Advances in Carbohydrate Bioengineering , pp. 3-14
    • Coutinho, P.M.1    Henrissat, B.2
  • 6
    • 42149108423 scopus 로고    scopus 로고
    • Bioconversion of lignocellulosic biomass: Biochemical and molecular perspectives
    • 18338189 10.1007/s10295-008-0327-8
    • Bioconversion of lignocellulosic biomass: biochemical and molecular perspectives. R Kumar, S Singh, OV Singh, J Ind Microbiol Biotechnol 2008 35 377 391 18338189 10.1007/s10295-008-0327-8
    • (2008) J Ind Microbiol Biotechnol , vol.35 , pp. 377-391
    • Kumar, R.1    Singh, S.2    Singh, O.V.3
  • 7
    • 34249949390 scopus 로고    scopus 로고
    • The potential of cellulases and cellulosomes for cellulosic waste management
    • DOI 10.1016/j.copbio.2007.04.004, PII S0958166907000535, Energy biotechnology / Environmental biotechnology
    • The potential of cellulases and cellulosomes for cellulosic waste management. EA Bayer, R Lamed, ME Himmel, Curr Opin Biotechnol 2007 18 237 245 17462879 10.1016/j.copbio.2007.04.004 (Pubitemid 46880283)
    • (2007) Current Opinion in Biotechnology , vol.18 , Issue.3 , pp. 237-245
    • Bayer, E.A.1    Lamed, R.2    Himmel, M.E.3
  • 8
    • 33746121105 scopus 로고    scopus 로고
    • Outlook for cellulase improvement: Screening and selection strategies
    • DOI 10.1016/j.biotechadv.2006.03.003, PII S0734975006000413
    • Outlook for cellulase improvement: screening and selection strategies. YH Percival Zhang, ME Himmel, JR Mielenz, Biotechnol Adv 2006 24 452 481 16690241 10.1016/j.biotechadv.2006.03.003 (Pubitemid 44082013)
    • (2006) Biotechnology Advances , vol.24 , Issue.5 , pp. 452-481
    • Percival Zhang, Y.-H.1    Himmel, M.E.2    Mielenz, J.R.3
  • 14
    • 0025818705 scopus 로고
    • Cellobiohydrolase II is the main conidial bound cellulase in Trichoderma reesei and other Trichoderma strains
    • 1953300 10.1007/BF00245356
    • Cellobiohydrolase II is the main conidial bound cellulase in Trichoderma reesei and other Trichoderma strains. R Messner, EM Kubicek-Pranz, A Gsur, CP Kubicek, Arch Microbiol 1991 155 601 606 1953300 10.1007/BF00245356
    • (1991) Arch Microbiol , vol.155 , pp. 601-606
    • Messner, R.1    Kubicek-Pranz, E.M.2    Gsur, A.3    Kubicek, C.P.4
  • 15
    • 0025816748 scopus 로고
    • Transformation of Trichoderma reesei with the cellobiohydrolase II gene as a means for obtaining strains with increased cellulase production and specific activity
    • 10.1016/0168-1656(91)90037-V
    • Transformation of Trichoderma reesei with the cellobiohydrolase II gene as a means for obtaining strains with increased cellulase production and specific activity. EM Kubicek-Pranz, F Gruber, CP Kubicek, J Biotechnol 1991 20 83 94 10.1016/0168-1656(91)90037-V
    • (1991) J Biotechnol , vol.20 , pp. 83-94
    • Kubicek-Pranz, E.M.1    Gruber, F.2    Kubicek, C.P.3
  • 16
    • 0026750715 scopus 로고    scopus 로고
    • Disruption of the Trichoderma reesei cbh2 gene coding for cellobiohydrolase II leads to a delay in the triggering of cellulase formation by cellulose
    • Disruption of the Trichoderma reesei cbh2 gene coding for cellobiohydrolase II leads to a delay in the triggering of cellulase formation by cellulose. B Seiboth, R Messner, F Gruber, CP Kubicek, J Gen Microbiol 138 1259 1264
    • J Gen Microbiol , vol.138 , pp. 1259-1264
    • Seiboth, B.1    Messner, R.2    Gruber, F.3    Kubicek, C.P.4
  • 18
    • 0000992883 scopus 로고
    • Sophorose as an inducer of cellulase in Trichoderma viride
    • 14469205
    • Sophorose as an inducer of cellulase in Trichoderma viride. M Mandels, FW Parrish, ET Reese, J Bacteriol 1962 83 400 408 14469205
    • (1962) J Bacteriol , vol.83 , pp. 400-408
    • Mandels, M.1    Parrish, F.W.2    Reese, E.T.3
  • 19
    • 0001051337 scopus 로고
    • The cellulase system of Trichoderma: Relationship betweeen purified extracellular enzymes from induced or cellulose-grown cells
    • The cellulase system of Trichoderma: relationship betweeen purified extracellular enzymes from induced or cellulose-grown cells. M Gritzali, RDJ Brown, Adv Chem Ser 1979 181 237 260
    • (1979) Adv Chem ser , vol.181 , pp. 237-260
    • Gritzali, M.1    Brown, R.D.J.2
  • 20
    • 0001903549 scopus 로고
    • Transglycosylation products of cellulase system of Trichoderma reesei
    • 10.1007/BF01395789
    • Transglycosylation products of cellulase system of Trichoderma reesei. M Vaheri, M Leisola, V Kauppinen, Biotechnol Lett 1979 1 696 699 10.1007/BF01395789
    • (1979) Biotechnol Lett , vol.1 , pp. 696-699
    • Vaheri, M.1    Leisola, M.2    Kauppinen, V.3
  • 21
    • 0018736190 scopus 로고
    • Induction of cellulolytic enzymes in Trichoderma reesei by sophorose
    • Induction of cellulolytic enzymes in Trichoderma reesei by sophorose. D Sternberg, GR Mandels, J Bacteriol 1979 139 761 769 39061 (Pubitemid 10234086)
    • (1979) Journal of Bacteriology , vol.139 , Issue.3 , pp. 761-769
    • Sternberg, D.1    Mandels, G.R.2
  • 22
    • 0019205532 scopus 로고
    • Regulation of the cellulolytic system in Trichoderma reesei by sophorose: Induction of cellulase and repression of β-glucosidase
    • Regulation of the cellulolytic system in Trichoderma reesei by sophorose: induction of cellulase and repression of beta-glucosidase. D Sternberg, GR Mandels, J Bacteriol 1980 144 1197 1199 6777367 (Pubitemid 11172235)
    • (1980) Journal of Bacteriology , vol.144 , Issue.3 , pp. 1197-1199
    • Sternberg, D.1    Mandels, G.R.2
  • 23
    • 0027214236 scopus 로고
    • Triggering of cellulase biosynthesis by cellulose in Trichoderma reesei. Involvement of a constitutive, sophorose-inducible, glucose-inhibited β- diglucoside permease
    • Triggering of cellulase biosynthesis in Trichoderma reesei: involvement of a constitutive, sophorose-inducible, glucose-inhibited β-diglucoside permease. CP Kubicek, R Messner, F Gruber, M Mandels, EM Kubicek-Pranz, J Biol Chem 1993 268 19364 19368 8366083 (Pubitemid 23270712)
    • (1993) Journal of Biological Chemistry , vol.268 , Issue.26 , pp. 19364-19368
    • Kubicek, C.P.1    Messner, R.2    Gruber, F.3    Mandels, M.4    Kubicek-Pranz, E.M.5
  • 24
    • 0017406649 scopus 로고
    • Sophorose metabolism and cellulase induction in Trichoderma
    • Sophorose metabolism and cellulase induction in Trichoderma. JR Loewenberg, CM Chapman, Arch Microbiol 1977 113 61 64 560832 10.1007/BF00428581 (Pubitemid 8097083)
    • (1977) Archives of Microbiology , vol.113 , Issue.1-2 , pp. 61-64
    • Loewenberg, J.R.1    Chapman, C.M.2
  • 25
    • 0026539878 scopus 로고
    • The bgl1 gene encoding extracellular β-glucosidase from Trichoderma reesei is required for rapid induction of the cellulase complex
    • 1453960 10.1111/j.1365-2958.1992.tb01777.x
    • The bgl1 gene encoding extracellular β-glucosidase from Trichoderma reesei is required for rapid induction of the cellulase complex. T Fowler, RD Brown Jr, Mol Microbiol 1992 6 3225 3235 1453960 10.1111/j.1365-2958.1992. tb01777.x
    • (1992) Mol Microbiol , vol.6 , pp. 3225-3235
    • Fowler, T.1    Brown Jr., R.D.2
  • 26
    • 0025483048 scopus 로고
    • Evidence for a single, specific β-glucosidase in cell walls from Trichoderma reesei QM9414
    • DOI 10.1016/0141-0229(90)90008-E
    • Evidence for a single, specific β-glucosidase in cell walls from Trichoderma reesei QM 9414. R Messner, CP Kubicek, Enzyme Microb Technol 1990 12 685 690 10.1016/0141-0229(90)90008-E (Pubitemid 20313135)
    • (1990) Enzyme and Microbial Technology , vol.12 , Issue.9 , pp. 685-690
    • Messner, R.1    Kubicek, C.P.2
  • 27
    • 0022619781 scopus 로고
    • A constitutive, plasma-membrane bound β-glucosidase in Trichoderma reesei
    • DOI 10.1016/0378-1097(86)90372-1
    • A constitutive, plasma-membrane bound β-glucosidase in Trichoderma reesei. C Umile, CP Kubicek, FEMS Microbiol Lett 1986 34 291 295 (Pubitemid 16116541)
    • (1986) FEMS Microbiology Letters , vol.34 , Issue.3 , pp. 291-295
    • Umile, C.1    Kubicek, C.P.2
  • 28
    • 0018980548 scopus 로고
    • Partial purification and characterization of a new intracellular beta-glucosidase of Trichoderma reesei
    • 6772150
    • Partial purification and characterization of a new intracellular beta-glucosidase of Trichoderma reesei. M Inglin, BA Feinberg, JR Loewenberg, Biochem J 1980 185 515 519 6772150
    • (1980) Biochem J , vol.185 , pp. 515-519
    • Inglin, M.1    Feinberg, B.A.2    Loewenberg, J.R.3
  • 29
    • 0036729340 scopus 로고    scopus 로고
    • Enzymatic properties and intracellular localization of the novel Trichoderma reesei β-glucosidase BGLII (Cel1A)
    • DOI 10.1128/AEM.68.9.4546-4553.2002
    • Enzymatic properties and intracellular localization of the novel Trichoderma reesei beta-glucosidase BGLII (CEL1A). M Saloheimo, J Kuja-Panula, E Ylösmäki, M Ward, M Penttilä Appl Environ Microbiol 2002 68 4546 4553 12200312 10.1128/AEM.68.9.4546-4553.2002 (Pubitemid 34988140)
    • (2002) Applied and Environmental Microbiology , vol.68 , Issue.9 , pp. 4546-4553
    • Saloheimo, M.1    Kuja-Panula, J.2    Ylosmaki, E.3    Ward, M.4    Penttila, M.5
  • 30
    • 0029045457 scopus 로고
    • The bgl1 gene of Trichoderma reesei QM 9414 encodes an extracellular, cellulose-inducible β-glucosidase involved in cellulase induction by sophorose
    • 7476163 10.1111/j.1365-2958.1995.tb02430.x
    • The bgl1 gene of Trichoderma reesei QM 9414 encodes an extracellular, cellulose-inducible β-glucosidase involved in cellulase induction by sophorose. RL Mach, B Seiboth, A Myasnikov, R Gonzalez, J Strauss, AM Harkki, CP Kubicek, Mol Microbiol 1995 16 687 697 7476163 10.1111/j.1365-2958.1995. tb02430.x
    • (1995) Mol Microbiol , vol.16 , pp. 687-697
    • Mach, R.L.1    Seiboth, B.2    Myasnikov, A.3    Gonzalez, R.4    Strauss, J.5    Harkki, A.M.6    Kubicek, C.P.7
  • 31
    • 33845671822 scopus 로고    scopus 로고
    • Xyr1 (Xylanase Regulator 1) regulates both the hydrolytic enzyme system and D-xylose metabolism in Hypocrea jecorina
    • DOI 10.1128/EC.00211-06
    • Xyr1 (xylanase regulator 1) regulates both the hydrolytic enzyme system and D -xylose metabolism in Hypocrea jecorina. AR Stricker, K Grosstessner-Hain, E Würleitner, RL Mach, Eukaryot Cell 2006 5 2128 2137 17056741 10.1128/EC.00211-06 (Pubitemid 44956824)
    • (2006) Eukaryotic Cell , vol.5 , Issue.12 , pp. 2128-2137
    • Stricker, A.R.1    Grosstessner-Hain, K.2    Wurleitner, E.3    Mach, R.L.4
  • 32
    • 38649100624 scopus 로고    scopus 로고
    • Regulation of transcription of cellulases- and hemicellulases-encoding genes in Aspergillus niger and Hypocrea jecorina (Trichoderma reesei)
    • 18197406 10.1007/s00253-007-1322-0
    • Regulation of transcription of cellulases- and hemicellulases-encoding genes in Aspergillus niger and Hypocrea jecorina (Trichoderma reesei). AR Stricker, RL Mach, LH de Graaff, Appl Microbiol Biotechnol 2008 78 211 220 18197406 10.1007/s00253-007-1322-0
    • (2008) Appl Microbiol Biotechnol , vol.78 , pp. 211-220
    • Stricker, A.R.1    Mach, R.L.2    De Graaff, L.H.3
  • 33
    • 55049124006 scopus 로고    scopus 로고
    • Transcriptional regulation of xyr1, encoding the main regulator of the xylanolytic and cellulolytic enzyme system in Hypocrea jecorina
    • 18791032 10.1128/AEM.01143-08
    • Transcriptional regulation of xyr1, encoding the main regulator of the xylanolytic and cellulolytic enzyme system in Hypocrea jecorina. AR Mach-Aigner, ME Pucher, MG Steiger, GE Bauer, SJ Preis, RL Mach, Appl Environ Microbiol 2008 74 6554 6562 18791032 10.1128/AEM.01143-08
    • (2008) Appl Environ Microbiol , vol.74 , pp. 6554-6562
    • Mach-Aigner, A.R.1    Pucher, M.E.2    Steiger, M.G.3    Bauer, G.E.4    Preis, S.J.5    Mach, R.L.6
  • 34
    • 0035968258 scopus 로고    scopus 로고
    • ACEII, a novel transcriptional activator involved in regulation of cellulase and xylanase genes of Trichoderma reesei
    • 11304525 10.1074/jbc.M003624200
    • ACEII, a novel transcriptional activator involved in regulation of cellulase and xylanase genes of Trichoderma reesei. N Aro, A Saloheimo, M Ilmén, M Penttilä J Biol Chem 2001 276 24309 24314 11304525 10.1074/jbc.M003624200
    • (2001) J Biol Chem , vol.276 , pp. 24309-24314
    • Aro, N.1    Saloheimo, A.2    Ilmén, M.3    Penttilä, M.4
  • 35
    • 39749127156 scopus 로고    scopus 로고
    • Role of Ace2 (Activator of Cellulases 2) within the xyn2 transcriptosome of Hypocrea jecorina
    • DOI 10.1016/j.fgb.2007.08.005, PII S108718450700151X
    • Role of Ace2 (Activator of Cellulases 2) within the xyn2 transcriptosome of Hypocrea jecorina. AR Stricker, P Trefflinger, N Aro, M Penttilä RL Mach, Fungal Genet Biol 2008 45 436 445 17920314 10.1016/j.fgb.2007.08.005 (Pubitemid 351296468)
    • (2008) Fungal Genetics and Biology , vol.45 , Issue.4 , pp. 436-445
    • Stricker, A.R.1    Trefflinger, P.2    Aro, N.3    Penttila, M.4    Mach, R.L.5
  • 36
    • 0032545260 scopus 로고    scopus 로고
    • Two adjacent protein binding motifs in the cbh2 (Cellobiohydrolase II- encoding) promoter of the fungus Hypocrea jecorina (Trichoderma reesei) cooperate in the induction by cellulose
    • DOI 10.1074/jbc.273.51.34463
    • Two adjacent protein binding motifs in the cbh2 (cellobiohydrolase II-encoding) promoter of the fungus Hypocrea jecorina (Trichoderma reesei) cooperate in the induction by cellulose. S Zeilinger, RL Mach, CP Kubicek, J Biol Chem 1998 273 34463 24471 9852114 10.1074/jbc.273.51.34463 (Pubitemid 29008926)
    • (1998) Journal of Biological Chemistry , vol.273 , Issue.51 , pp. 34463-34471
    • Zeilinger, S.1    Mach, R.L.2    Kubicek, C.P.3
  • 37
    • 0034887339 scopus 로고    scopus 로고
    • The Hypocrea jecorina HAP 2/3/5 protein complex binds to the inverted CCAAT-box (ATTGG) within the cbh2 (cellobiohydrolase II-gene) activating element
    • DOI 10.1007/s004380100518
    • The Hypocrea jecorina HAP 2/3/5 protein complex binds to the inverted CCAAT-box (ATTGG) within the cbh2 (cellobiohydrolase II-gene) activating element. S Zeilinger, A Ebner, T Marosits, R Mach, CP Kubicek, Mol Genet Genomics 2001 266 56 63 11589578 10.1007/s004380100518 (Pubitemid 32778663)
    • (2001) Molecular Genetics and Genomics , vol.266 , Issue.1 , pp. 56-63
    • Zeilinger, S.1    Ebner, A.2    Marosits, T.3    Mach, R.4    Kubicek, C.P.5
  • 38
    • 0032030308 scopus 로고    scopus 로고
    • A survey of 178 NF-Y binding CCAAT boxes
    • DOI 10.1093/nar/26.5.1135
    • A survey of 178 NF-Y binding CCAAT boxes. R Mantovani, Nucleic Acids Res 1998 26 1135 1143 9469818 10.1093/nar/26.5.1135 (Pubitemid 28291681)
    • (1998) Nucleic Acids Research , vol.26 , Issue.5 , pp. 1135-1143
    • Mantovani, R.1
  • 39
    • 0030743394 scopus 로고    scopus 로고
    • CCAAT-binding factor NF-Y and RFX are required for in vivo assembly of a nucleoprotein complex that spans 250 base pairs: The invariant chain promoter as a model
    • CCAAT-binding factor NF-Y and RFX are required for in vivo assembly of a nucleoprotein complex that spans 250 base pairs: the invariant chain promoter as a model. MW Linhoff, KL Wright, JP Ting, Mol Cell Biol 1997 17 4589 4596 9234716 (Pubitemid 27318135)
    • (1997) Molecular and Cellular Biology , vol.17 , Issue.8 , pp. 4589-4596
    • Linhoff, M.W.1    Wright, K.L.2    Ting, J.P.-Y.3
  • 40
    • 0032476596 scopus 로고    scopus 로고
    • Xenopus NF-Y pre-sets chromatin to potentiate p300 and acetylation-responsive transcription from the Xenopus hsp70 promoter in vivo
    • DOI 10.1093/emboj/17.21.6300
    • Xenopus NF-Y pre-sets chromatin to potentiate p300 and acetylation-responsive transcription from the Xenopus hsp70 promoter in vivo. Q Li, M Herrler, N Landsberger, N Kaludov, VV Ogryzko, Y Nakatani, AP Wolffe, EMBO J 1998 17 6300 6315 9799238 10.1093/emboj/17.21.6300 (Pubitemid 28497802)
    • (1998) EMBO Journal , vol.17 , Issue.21 , pp. 6300-6315
    • Li, Q.1    Herrler, M.2    Landsberger, N.3    Kaludov, N.4    Ogryzko, V.V.5    Nakatani, Y.6    Wolffe, A.P.7
  • 41
    • 0032506542 scopus 로고    scopus 로고
    • Regulation of activity of the transcription factor GATA-1 by acetylation
    • DOI 10.1038/25166
    • Regulation of activity of the transcription factor GATA-1 by acetylation. J Boyes, P Byfield, Y Nakatani, V Ogryzko, Nature 1998 396 594 598 9859997 10.1038/25166 (Pubitemid 28563723)
    • (1998) Nature , vol.396 , Issue.6711 , pp. 594-598
    • Boyes, J.1    Byfield, P.2    Nakatani, Y.3    Ogryzko, V.4
  • 42
    • 0142075910 scopus 로고    scopus 로고
    • Nucleosome transactions on the Hypocrea jecorina (Trichoderma reesei) cellulase promoter cbh2 associated with cellulase induction
    • DOI 10.1007/s00438-003-0895-2
    • Nucleosome transactions on the Hypocrea jecorina (Trichoderma reesei) cellulase promoter cbh2 associated with cellulase induction. S Zeilinger, M Schmoll, M Pail, RL Mach, CP Kubicek, Mol Genet Genomics 2003 270 46 55 12905071 10.1007/s00438-003-0895-2 (Pubitemid 37267103)
    • (2003) Molecular Genetics and Genomics , vol.270 , Issue.1 , pp. 46-55
    • Zeilinger, S.1    Schmoll, M.2    Pail, M.3    Mach, R.L.4    Kubicek, C.P.5
  • 43
    • 0034102428 scopus 로고    scopus 로고
    • 2 transcription factor involved in regulation of activity of the cellulase promoter cbh1 of Trichoderma reesei
    • DOI 10.1074/jbc.275.8.5817
    • Isolation of the ace1 gene encoding a Cys(2)-His(2) transcription factor involved in regulation of activity of the cellulase promoter cbh1 of Trichoderma reesei. A Saloheimo, N Aro, M Ilmén, M Penttilä J Biol Chem 2000 275 5817 5825 10681571 10.1074/jbc.275.8.5817 (Pubitemid 30115227)
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.8 , pp. 5817-5825
    • Saloheimo, A.1    Aro, N.2    Ilmen, M.3    Penttila, M.4
  • 44
    • 0037226849 scopus 로고    scopus 로고
    • ACEI of Trichoderma reesei is a repressor of cellulase and xylanase expression
    • DOI 10.1128/AEM.69.1.56-65.2003
    • ACEI of Trichoderma reesei is a repressor of cellulase and xylanase expression. N Aro, M Ilmén, A Saloheimo, M Penttilä Appl Environ Microbiol 2003 69 56 65 12513977 10.1128/AEM.69.1.56-65.2003 (Pubitemid 36077457)
    • (2003) Applied and Environmental Microbiology , vol.69 , Issue.1 , pp. 56-65
    • Aro, N.1    Ilmen, M.2    Saloheimo, A.3    Penttila, M.4
  • 45
    • 56549109281 scopus 로고    scopus 로고
    • The Aspergillus nidulans stress response transcription factor StzA is ascomycete-specific and shows species-specific polymorphisms in the C-terminal region
    • 18678248 10.1016/j.mycres.2008.06.028
    • The Aspergillus nidulans stress response transcription factor StzA is ascomycete-specific and shows species-specific polymorphisms in the C-terminal region. IJ Chilton, CE Delaney, J Barham-Morris, DA Fincham, P Hooley, MP Whitehead, Mycol Res 2008 112 1435 1446 18678248 10.1016/j.mycres.2008.06.028
    • (2008) Mycol Res , vol.112 , pp. 1435-1446
    • Chilton, I.J.1    Delaney, C.E.2    Barham-Morris, J.3    Fincham, D.A.4    Hooley, P.5    Whitehead, M.P.6
  • 46
    • 56349084184 scopus 로고    scopus 로고
    • Sulphur metabolism and cellulase gene expression are connected processes in the filamentous fungus Hypocrea jecorina (anamorph Trichoderma reesei)
    • 18842142 10.1186/1471-2180-8-174
    • Sulphur metabolism and cellulase gene expression are connected processes in the filamentous fungus Hypocrea jecorina (anamorph Trichoderma reesei). G Gremel, M Dorrer, M Schmoll, BMC Microbiol 2008 8 174 18842142 10.1186/1471-2180-8-174
    • (2008) BMC Microbiol , vol.8 , pp. 174
    • Gremel, G.1    Dorrer, M.2    Schmoll, M.3
  • 47
    • 0030480099 scopus 로고    scopus 로고
    • Functional analysis of the cellobiohydrolase I promoter of the filamentous fungus Trichoderma reesei
    • DOI 10.1007/s004380050326
    • Functional analysis of the cellobiohydrolase I promoter of the filamentous fungus Trichoderma reesei. M Ilmén, ML Onnela, S Klemsdal, S Keränen, M Penttilä Mol Gen Genet 1996 253 303 314 9003317 (Pubitemid 27023188)
    • (1996) Molecular and General Genetics , vol.253 , Issue.3 , pp. 303-314
    • Ilmen, M.1    Onnela, M.-L.2    Klemsdal, S.3    Keranen, S.4    Penttila, M.5
  • 48
    • 0017408123 scopus 로고
    • Mutants of Saccharomyces cerevisiae resistant to carbon catabolite repression
    • Mutants of Saccharomyces cerevisiae resistant to carbon catabolite repression. FK Zimmermann, I Scheel, Mol Gen Genet 1977 154 75 82 197390 10.1007/BF00265579 (Pubitemid 8114659)
    • (1977) Molecular and General Genetics , vol.154 , Issue.1 , pp. 75-82
    • Zimmermann, F.K.1    Scheel, I.2
  • 49
    • 0018558501 scopus 로고
    • Increasing yields of extracellular enzymes
    • 397739 full-text
    • Increasing yields of extracellular enzymes. DE Eveleigh, BS Montenecourt, Adv Appl Microbiol 1979 25 57 74 397739 full-text
    • (1979) Adv Appl Microbiol , vol.25 , pp. 57-74
    • Eveleigh, D.E.1    Montenecourt, B.S.2
  • 50
    • 0021136405 scopus 로고
    • Characterization of the secreted cellulases of Trichoderma reesei wild type and mutants during controlled fermentations
    • Characterization of the secreted cellulases of Trichoderma reesei wild type mutants during controlled fermentations. G Sheir-Neiss, BS Montenecourt, Appl Microbiol Biotechnol 1984 20 46 53 10.1007/BF00254645 (Pubitemid 14070563)
    • (1984) Applied Microbiology and Biotechnology , vol.20 , Issue.1 , pp. 46-53
    • Sheir-Neiss, G.1    Montenecourt, B.S.2
  • 51
    • 0024035173 scopus 로고
    • Genetic improvement of Trichoderma reesei for large scale cellulase production
    • 10.1016/0141-0229(88)90012-9
    • Genetic improvement of Trichoderma reesei for large scale cellulase production. H Durand, H Clanet, G Tiraby, Enzyme Microb Technol 1988 10 341 346 10.1016/0141-0229(88)90012-9
    • (1988) Enzyme Microb Technol , vol.10 , pp. 341-346
    • Durand, H.1    Clanet, H.2    Tiraby, G.3
  • 52
    • 0030036051 scopus 로고    scopus 로고
    • The glucose repressor gene cre1 of Trichoderma: Isolation and expression of a full-length and a truncated mutant form
    • 8709949
    • The glucose repressor gene cre1 of Trichoderma: isolation and expression of a full-length and a truncated mutant form. M Ilmén, C Thrane, M Penttilä Mol Gen Genet 1996 251 451 460 8709949
    • (1996) Mol Gen Genet , vol.251 , pp. 451-460
    • Ilmén, M.1    Thrane, C.2    Penttilä, M.3
  • 53
    • 0025944347 scopus 로고
    • Analysis of the creA gene, a regulator of carbon catabolite repression in Aspergillus nidulans
    • Analysis of the creA gene, a regulator of carbon catabolite repression in Aspergillus nidulans. CE Dowzer, JM Kelly, Mol Cell Biol 1991 11 5701 5709 1922072 (Pubitemid 21895337)
    • (1991) Molecular and Cellular Biology , vol.11 , Issue.11 , pp. 5701-5709
    • Dowzer, C.E.A.1    Kelly, J.M.2
  • 54
    • 48249114001 scopus 로고    scopus 로고
    • The Hypocrea jecorina (Trichoderma reesei) hypercellulolytic mutant RUT C30 lacks a 85 kb (29 gene-encoding) region of the wild-type genome
    • 18620557 10.1186/1471-2164-9-327
    • The Hypocrea jecorina (Trichoderma reesei) hypercellulolytic mutant RUT C30 lacks a 85 kb (29 gene-encoding) region of the wild-type genome. V Seidl, C Gamauf, IS Druzhinina, L Hartl, B Seiboth, CP Kubicek, BMC Genomics 2008 9 327 18620557 10.1186/1471-2164-9-327
    • (2008) BMC Genomics , vol.9 , pp. 327
    • Seidl, V.1    Gamauf, C.2    Druzhinina, I.S.3    Hartl, L.4    Seiboth, B.5    Kubicek, C.P.6
  • 55
    • 0027481684 scopus 로고
    • Specific binding sites in the alcR and alcA promoters of the ethanol regulon for the CREA repressor mediating carbon catabolite repression in Aspergillus nidulans
    • Specific binding sites in the alcR and alcA promoters of the ethanol regulon for the CREA repressor mediating carbon catabolite repression in Aspergillus nidulans. P Kulmburg, M Mathieu, C Dowzer, J Kelly, B Felenbok, Mol Microbiol 1993 7 847 857 8483416 10.1111/j.1365-2958.1993.tb01175.x (Pubitemid 23101397)
    • (1993) Molecular Microbiology , vol.7 , Issue.6 , pp. 847-857
    • Kulmburg, P.1    Mathieu, M.2    Dowzer, C.3    Kelly, J.4    Felenbok, B.5
  • 56
    • 0029832663 scopus 로고    scopus 로고
    • Carbon catabolite repression of xylanase I (xyn1) gene expression in Trichoderma reesei
    • Carbon catabolite repression of xyn1 (xylanase I-encoding) gene expression in Trichoderma reesei. RL Mach, J Strauss, S Zeilinger, M Schindler, CP Kubicek, Mol Microbiol 1996 21 1273 1281 8898395 10.1046/j.1365-2958.1996. 00094.x (Pubitemid 26313253)
    • (1996) Molecular Microbiology , vol.21 , Issue.6 , pp. 1273-1281
    • Mach, R.L.1    Strauss, J.2    Zeilinger, S.3    Schindler, M.4    Kubicek, C.P.5
  • 57
    • 0037177862 scopus 로고    scopus 로고
    • Phosphorylation positively regulates DNA binding of the carbon catabolite repressor Cre1 of Hypocrea jecorina (Trichoderma reesei)
    • DOI 10.1074/jbc.M200744200
    • Phosphorylation positively regulates DNA binding of the carbon catabolite repressor Cre1 of Hypocrea jecorina (Trichoderma reesei). A Cziferszky, RL Mach, CP Kubicek, J Biol Chem 2002 277 14688 14694 11850429 10.1074/jbc. M200744200 (Pubitemid 34952538)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.17 , pp. 14688-14694
    • Cziferszky, A.1    Mach, R.L.2    Kubicek, C.P.3
  • 58
    • 0037334895 scopus 로고    scopus 로고
    • One-thousand-and-one substrates of protein kinase CK2?
    • DOI 10.1096/fj.02-0473rev
    • One-thousand-and-one substrates of protein kinase CK2? F Meggio, LA Pinna, FASEB J 2003 17 349 368 12631575 10.1096/fj.02-0473rev (Pubitemid 36292951)
    • (2003) FASEB Journal , vol.17 , Issue.3 , pp. 349-368
    • Meggio, F.1    Pinna, L.A.2
  • 59
    • 0033118209 scopus 로고    scopus 로고
    • Glucose repression in yeast
    • DOI 10.1016/S1369-5274(99)80035-6
    • Glucose repression in yeast. M Carlson, Curr Opin Microbiol 1999 2 202 207 10322167 10.1016/S1369-5274(99)80035-6 (Pubitemid 29176946)
    • (1999) Current Opinion in Microbiology , vol.2 , Issue.2 , pp. 202-207
    • Carlson, M.1
  • 60
    • 0141850961 scopus 로고    scopus 로고
    • The Snf1 kinase of the filamentous fungus Hypocrea jecorina phosphorylates regulation-relevant serine residues in the yeast carbon catabolite repressor Mig1 but not in the filamentous fungal counterpart Cre1
    • DOI 10.1016/S1087-1845(03)00082-3
    • The Snf1 kinase of the filamentous fungus Hypocrea jecorina phosphorylates regulation-relevant serine residues in the yeast carbon catabolite repressor Mig1 but not in the filamentous fungal counterpart Cre1. A Czifersky, B Seiboth, CP Kubicek, Fungal Genet Biol 2003 40 166 175 14516769 10.1016/S1087-1845(03)00082-3 (Pubitemid 37152537)
    • (2003) Fungal Genetics and Biology , vol.40 , Issue.2 , pp. 166-175
    • Cziferszky, A.1    Seiboth, B.2    Kubicek, C.P.3
  • 61
    • 0033799307 scopus 로고    scopus 로고
    • The Aspergillus nidulans creC gene involved in carbon catabolite repression encodes a WD40 repeat protein
    • 10852476 10.1007/s004380051202
    • The Aspergillus nidulans creC gene involved in carbon catabolite repression encodes a WD40 repeat protein. RB Todd, RA Lockington, JM Kelly, Mol Gen Genet 2000 263 561 570 10852476 10.1007/s004380051202
    • (2000) Mol Gen Genet , vol.263 , pp. 561-570
    • Todd, R.B.1    Lockington, R.A.2    Kelly, J.M.3
  • 62
    • 0034942079 scopus 로고    scopus 로고
    • Carbon catabolite repression in Aspergillus nidulans involves deubiquitination
    • DOI 10.1046/j.1365-2958.2001.02474.x
    • Carbon catabolite repression in Aspergillus nidulans involves deubiquitination. RA Lockington, JM Kelly, Mol Microbiol 2001 40 1311 1321 11442830 10.1046/j.1365-2958.2001.02474.x (Pubitemid 32640211)
    • (2001) Molecular Microbiology , vol.40 , Issue.6 , pp. 1311-1321
    • Lockington, R.A.1    Kelly, J.M.2
  • 63
    • 0036223215 scopus 로고    scopus 로고
    • The WD40-repeat protein CreC interacts with and stabilizes the deubiquitinating enzyme CreB in vivo in Aspergillus nidulans
    • DOI 10.1046/j.1365-2958.2002.02811.x
    • The WD40-repeat protein CreC interacts with and stabilizes the deubiquitinating enzyme CreB in vivo in Aspergillus nidulans. RA Lockington, JM Kelly, Mol Microbiol 2002 43 1173 1182 11918805 10.1046/j.1365-2958.2002.02811.x (Pubitemid 34304535)
    • (2002) Molecular Microbiology , vol.43 , Issue.5 , pp. 1173-1182
    • Lockington, R.A.1    Kelly, J.M.2
  • 64
    • 70349768173 scopus 로고    scopus 로고
    • Identification and characterization of the Trichoderma reesei homologue of Aspergillus nidualns creB
    • Identification and characterization of the Trichoderma reesei homologue of Aspergillus nidualns creB. J Denton, JM Kelly, Fungal Genet Newsl 54 Suppl 98
    • Fungal Genet Newsl , vol.54 , Issue.SUPPL. , pp. 98
    • Denton, J.1    Kelly, J.M.2
  • 65
    • 3843055866 scopus 로고    scopus 로고
    • A role for creD, a carbon catabolite repression gene from Aspergillus nidulans, in ubiquitination
    • DOI 10.1111/j.1365-2958.2004.04172.x
    • A role for creD, a carbon catabolite repression gene from Aspergillus nidulans, in ubiquitination. NA Boase, JM Kelly, Mol Microbiol 2004 53 929 940 15255903 10.1111/j.1365-2958.2004.04172.x (Pubitemid 39036970)
    • (2004) Molecular Microbiology , vol.53 , Issue.3 , pp. 929-940
    • Boase, N.A.1    Kelly, J.M.2
  • 66
    • 55449109162 scopus 로고    scopus 로고
    • Finding the right partner: Science or ART?
    • 19013267 10.1016/j.cell.2008.10.032
    • Finding the right partner: science or ART? S Polo, PP Di Fiore, Cell 2008 135 590 592 19013267 10.1016/j.cell.2008.10.032
    • (2008) Cell , vol.135 , pp. 590-592
    • Polo, S.1    Di Fiore, P.P.2
  • 67
    • 0035979738 scopus 로고    scopus 로고
    • Regulation of transcriptional activation domain function by ubiquitin
    • DOI 10.1126/science.1062079
    • Regulation of transcriptional activation domain function by ubiquitin. SE Salghetti, AA Caudy, JG Chenoweth, JW Tansey, Science 2001 293 1651 1653 11463878 10.1126/science.1062079 (Pubitemid 32807843)
    • (2001) Science , vol.293 , Issue.5535 , pp. 1651-1653
    • Salghetti, S.E.1    Caudy, A.A.2    Chenoweth, J.G.3    Tansey, W.P.4
  • 68
    • 0036281361 scopus 로고    scopus 로고
    • Glucose-sensing and -signalling mechanisms in yeast
    • DOI 10.1016/S1567-1356(02)00046-6, PII S1567135602000466
    • Glucose-sensing and -signalling mechanisms in yeast. F Rolland, J Winderickx, JM Thevelein, FEMS Yeast Res 2002 2 183 201 12702307 (Pubitemid 34628612)
    • (2002) FEMS Yeast Research , vol.2 , Issue.2 , pp. 183-201
    • Rolland, F.1    Winderickx, J.2    Thevelein, J.M.3
  • 69
    • 0026512705 scopus 로고
    • Glucose repression in the yeast Saccharomyces cerevisiae
    • 1310793 10.1111/j.1365-2958.1992.tb00832.x
    • Glucose repression in the yeast Saccharomyces cerevisiae. RJ Trumbly, Mol Microbiol 1992 6 15 21 1310793 10.1111/j.1365-2958.1992.tb00832.x
    • (1992) Mol Microbiol , vol.6 , pp. 15-21
    • Trumbly, R.J.1
  • 70
    • 33645130011 scopus 로고    scopus 로고
    • Glucose signaling in Saccharomyces cerevisiae
    • 16524925 10.1128/MMBR.70.1.253-282.2006
    • Glucose signaling in Saccharomyces cerevisiae. GM Santangelo, Microbiol Mol Biol Rev 2006 70 253 282 16524925 10.1128/MMBR.70.1.253-282.2006
    • (2006) Microbiol Mol Biol Rev , vol.70 , pp. 253-282
    • Santangelo, G.M.1
  • 71
    • 0038146953 scopus 로고    scopus 로고
    • Onset of carbon catabolite repression in Aspergillus nidulans: Parallel involvement of hexokinase and glucokinase in sugar signaling
    • DOI 10.1074/jbc.M209443200
    • Onset of carbon catabolite repression in Aspergillus nidulans. Parallel involvement of hexokinase and glucokinase in sugar signalling. M Flipphi, PJ van de Vondervoort, GJ Ruijter, J Visser, HN Arst Jr, B Felenbok, J Biol Chem 2003 278 11849 11857 12519784 10.1074/jbc.M209443200 (Pubitemid 36800155)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.14 , pp. 11849-11857
    • Flipphi, M.1    Van De Vondervoort, P.J.I.2    Ruijter, G.J.G.3    Visser, J.4    Arst Jr., H.N.5    Felenbok, B.6
  • 72
    • 0021054305 scopus 로고
    • Development of a culture medium for large-scale production of cellulolytic enzymes by Trichoderma reesei
    • 18548634 10.1002/bit.260251216
    • Development of a culture medium for large-scale production of cellulolytic enzymes by Trichoderma reesei. M Warzywoda, V Ferre, J Pourquie, Biotechnol Bioeng 1983 25 3005 3011 18548634 10.1002/bit.260251216
    • (1983) Biotechnol Bioeng , vol.25 , pp. 3005-3011
    • Warzywoda, M.1    Ferre, V.2    Pourquie, J.3
  • 73
    • 33947205049 scopus 로고    scopus 로고
    • Characterization of the bga1-encoded glycoside hydrolase family 35 β-galactosidase of Hypocrea jecorina with galacto-β-D-galactanase activity
    • DOI 10.1111/j.1742-4658.2007.05714.x
    • Characterization of the bga1- encoded glycosyl hydrolase family 35 β-galactosidase of Hypocrea jecorina with galacto-galactanase activity. C Gamauf, M Marchetti, J Kallio, J Vehmaanperä G Allmaier, CP Kubicek, B Seiboth, FEBS J 2007 274 1691 1700 17381511 10.1111/j.1742-4658.2007.05714.x (Pubitemid 46426904)
    • (2007) FEBS Journal , vol.274 , Issue.7 , pp. 1691-1700
    • Gamauf, C.1    Marchetti, M.2    Kallio, J.3    Puranen, T.4    Vehmaanpera, J.5    Allmaier, G.6    Kubicek, C.P.7    Seiboth, B.8
  • 74
    • 34250621803 scopus 로고    scopus 로고
    • Lactose metabolism in filamentous fungi: How to deal with an unknown substrate
    • DOI 10.1016/j.fbr.2007.02.006, PII S1749461307000127
    • Lactose metabolism in filamentous fungi: how to deal with an unknown substrate. B Seiboth, BS Pakdaman, L Hartl, CP Kubicek, Fungal Biol Rev 2007 21 42 48 10.1016/j.fbr.2007.02.006 (Pubitemid 46946871)
    • (2007) Fungal Biology Reviews , vol.21 , Issue.1 , pp. 42-48
    • Seiboth, B.1    Pakdaman, B.S.2    Hartl, L.3    Kubicek, C.P.4
  • 75
    • 0037212970 scopus 로고    scopus 로고
    • Regulation of formation of the intracellular β-galactosidase activity of Aspergillus nidulans
    • 12471499 10.1007/s00203-002-0491-6
    • Regulation of formation of the intracellular β-galactosidase activity of Aspergillus nidulans. E Fekete, L Karaffa, E Sandor, B Seiboth, S Biro, A Szentirmai, CP Kubicek, Arch Microbiol 2002 179 7 14 12471499 10.1007/s00203-002-0491-6
    • (2002) Arch Microbiol , vol.179 , pp. 7-14
    • Fekete, E.1    Karaffa, L.2    Sandor, E.3    Seiboth, B.4    Biro, S.5    Szentirmai, A.6    Kubicek, C.P.7
  • 77
    • 1442300801 scopus 로고    scopus 로고
    • The galactokinase of Hypocrea jecorina is essential for cellulose induction by lactose but dispensable for growth on D-galactose
    • DOI 10.1046/j.1365-2958.2003.03901.x
    • The galactokinase of Hypocrea jecorina is essential for cellulase induction by lactose but dispensable for growth on D -galactose. B Seiboth, L Hartl, M Pail, E Fekete, L Karaffa, CP Kubicek, Mol Microbiol 2004 51 1015 1025 14763977 10.1046/j.1365-2958.2003.03901.x (Pubitemid 38270796)
    • (2004) Molecular Microbiology , vol.51 , Issue.4 , pp. 1015-1025
    • Seiboth, B.1    Hartl, L.2    Pail, M.3    Fekete, E.4    Karaffa, L.5    Kubicek, C.P.6
  • 78
    • 33646804514 scopus 로고    scopus 로고
    • D -galactose induces cellulase gene expression in Hypocrea jecorina at low growth rates
    • 16622067 10.1099/mic.0.28719-0
    • D -galactose induces cellulase gene expression in Hypocrea jecorina at low growth rates. L Karaffa, E Fekete, C Gamauf, A Szentirmai, CP Kubicek, B Seiboth, Microbiology 2006 152 1507 1514 16622067 10.1099/mic.0.28719-0
    • (2006) Microbiology , vol.152 , pp. 1507-1514
    • Karaffa, L.1    Fekete, E.2    Gamauf, C.3    Szentirmai, A.4    Kubicek, C.P.5    Seiboth, B.6
  • 79
    • 0242498430 scopus 로고    scopus 로고
    • Structure and Function of Enzymes of the Leloir Pathway for Galactose Metabolism
    • DOI 10.1074/jbc.R300025200
    • Structure and function of enzymes of the Leloir pathway for galactose metabolism. HM Holden, I Rayment, JB Thoden, J Biol Chem 2003 278 43885 43888 12923184 10.1074/jbc.R300025200 (Pubitemid 37377125)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.45 , pp. 43885-43888
    • Holden, H.M.1    Rayment, I.2    Thoden, J.B.3
  • 80
    • 9744253830 scopus 로고    scopus 로고
    • Galactokinase: Structure, function and role in type II galactosemia
    • DOI 10.1007/s00018-004-4160-6
    • Galactokinase: structure, function and role in type II galactosemia. HM Holden, JB Thoden, DJ Timson, RJ Reece, Cell Mol Life Sci 2004 61 2471 2484 15526155 10.1007/s00018-004-4160-6 (Pubitemid 39586512)
    • (2004) Cellular and Molecular Life Sciences , vol.61 , Issue.19-20 , pp. 2471-2484
    • Holden, H.M.1    Thoden, J.B.2    Timson, D.J.3    Reece, R.J.4
  • 81
    • 0027948942 scopus 로고
    • Dependence of lactose metabolism upon mutarotase encoded in the gal operon in Escherichia coli
    • DOI 10.1006/jmbi.1994.1728
    • Dependence of lactose metabolism upon mutarotase encoded in the gal operon in Escherichia coli. GG Bouffard, KE Rudd, SL Adhya, J Mol Biol 1994 244 269 278 7966338 10.1006/jmbi.1994.1728 (Pubitemid 24369227)
    • (1994) Journal of Molecular Biology , vol.244 , Issue.3 , pp. 269-278
    • Bouffard, G.G.1    Rudd, K.E.2    Adhya, S.L.3
  • 83
    • 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 β-galactosidase and cellulase induction by lactose
    • DOI 10.1111/j.1365-2958.2007.05953.x
    • The major D -xylose reductase of Hypocrea jecorina is necessary for efficient pentose and lactose catabolism and for cellulase induction by lactose. B Seiboth, C Gamauf, M Pail, L Hartl, CP Kubicek, Mol Microbiol 2007 66 890 900 17924946 10.1111/j.1365-2958.2007.05953.x (Pubitemid 350050415)
    • (2007) Molecular Microbiology , vol.66 , Issue.4 , pp. 890-900
    • Seiboth, B.1    Gamauf, C.2    Pail, M.3    Hartl, L.4    Kubicek, C.P.5
  • 84
    • 0142153888 scopus 로고    scopus 로고
    • D-xylose metabolism in Hypocrea jecorina: Loss of the xylitol dehydrogenase step can be partially compensated for by lad1-encoded L-arabinitol-4-dehydrogenase
    • DOI 10.1128/EC.2.5.867-875.2003
    • D -Xylose metabolism in Hypocrea jecorina: Loss of the xylitol dehydrogenase step can be partially compensated for by lad1-encoded L -arabinitol-4-dehydrogenase. B Seiboth, L Hartl, M Pail, CP Kubicek, Eukaryot Cell 2003 2 867 875 14555469 10.1128/EC.2.5.867-875.2003 (Pubitemid 37298700)
    • (2003) Eukaryotic Cell , vol.2 , Issue.5 , pp. 867-875
    • Seiboth, B.1    Hartl, L.2    Pail, M.3    Kubicek, C.P.4
  • 85
    • 2542494082 scopus 로고    scopus 로고
    • The metabolic role and evolution of L-arabinitol 4-dehydrogenase of Hypocrea jecorina
    • DOI 10.1111/j.1432-1033.2004.04088.x
    • The metabolic role and evolution of L -arabinitol 4-dehydrogenase of Hypocrea jecorina. M Pail, T Peterbauer, B Seiboth, C Hametner, I Druzhinina, CP Kubicek, Eur J Biochem 2004 271 1864 1872 15128296 10.1111/j.1432-1033.2004. 04088.x (Pubitemid 38678538)
    • (2004) European Journal of Biochemistry , vol.271 , Issue.10 , pp. 1864-1872
    • Pail, M.1    Peterbauer, T.2    Seiboth, B.3    Hametner, C.4    Druzhinina, I.5    Kubicek, C.P.6
  • 86
    • 0037150086 scopus 로고    scopus 로고
    • The missing link in the fungal L-arabinose catabolic pathway, identification of the L-xylulose reductase gene
    • DOI 10.1021/bi025529i
    • The missing link in the fungal L -arabinose catabolic pathway, identification of the L -xylulose reductase gene. P Richard, M Putkonen, R Väänänen, J Londesborough, M Penttilä Biochemistry 2002 41 6432 6437 12009906 10.1021/bi025529i (Pubitemid 34526009)
    • (2002) Biochemistry , vol.41 , Issue.20 , pp. 6432-6437
    • Richard, P.1    Putkonen, M.2    Vaananen, R.3    Londesborough, J.4    Penttila, M.5
  • 88
    • 33847203685 scopus 로고    scopus 로고
    • Induction of extracellular β-galactosidase (Bga1) formation by D -galactose in Hypocrea jecorina is mediated by galactitol
    • 17259622 10.1099/mic.0.2006/001602-0
    • Induction of extracellular β-galactosidase (Bga1) formation by D -galactose in Hypocrea jecorina is mediated by galactitol. E Fekete, L Karaffa, CP Kubicek, A Szentirmai, B Seiboth, Microbiology 2007 153 507 512 17259622 10.1099/mic.0.2006/001602-0
    • (2007) Microbiology , vol.153 , pp. 507-512
    • Fekete, E.1    Karaffa, L.2    Kubicek, C.P.3    Szentirmai, A.4    Seiboth, B.5
  • 89
    • 0035187264 scopus 로고    scopus 로고
    • L-Sorbose induces cellulase gene transcription in the cellulolytic fungus Trichoderma reesei
    • DOI 10.1007/s002940000165
    • L -Sorbose induces cellulase gene transcription in the cellulolytic fungus Trichoderma reesei. M Nogawa, M Goto, H Okada, Y Morikawa, Curr Genet 2001 38 329 334 11270575 10.1007/s002940000165 (Pubitemid 32058725)
    • (2001) Current Genetics , vol.38 , Issue.6 , pp. 329-334
    • Nogawa, M.1    Goto, M.2    Okada, H.3    Morikawa, Y.4
  • 90
    • 34547101006 scopus 로고    scopus 로고
    • Induction of the gal pathway and cellulase genes involves no transcriptional inducer function of the galactokinase in Hypocrea jecorina
    • DOI 10.1074/jbc.M700955200
    • Induction of the Leloir pathway in the fungus Hypocrea jecorina involves no transcriptional inducer function of the galactokinase. L Hartl, CP Kubicek, B Seiboth, J Biol Chem 2007 282 18654 18659 17452322 10.1074/jbc.M700955200 (Pubitemid 47100201)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.25 , pp. 18654-18659
    • Hartl, L.1    Kubicek, C.P.2    Seiboth, B.3
  • 91
    • 0036203256 scopus 로고    scopus 로고
    • Lactose metabolism and cellulase production in Hypocrea jecorina: The gal7 gene, encoding galactose-1-phosphate uridylyltransferase, is essential for growth on galactose but not for cellulase induction
    • DOI 10.1007/s00438-002-0654-9
    • Lactose metabolism and cellulase production in Hypocrea jecorina: the gal7 gene, encoding galactose-1-phosphate uridylyltransferase, is essential for growth on galactose but not for cellulase induction. B Seiboth, G Hofmann, CP Kubicek, Mol Genet Genomics 2002 267 124 132 11919723 10.1007/s00438-002-0654-9 (Pubitemid 34251591)
    • (2002) Molecular Genetics and Genomics , vol.267 , Issue.1 , pp. 124-132
    • Seiboth, B.1    Hofmann, G.2    Kubicek, C.3
  • 92
    • 34547690997 scopus 로고    scopus 로고
    • Xyr1 receives the lactose induction signal and regulates lactose metabolism in Hypocrea jecorina
    • DOI 10.1016/j.febslet.2007.07.025, PII S0014579307007739
    • Xyr1 receives the lactose induction signal and regulates lactose metabolism in Hypocrea jecorina. AR Stricker, MG Steiger, RL Mach, FEBS Lett 2007 581 3915 3920 17662982 10.1016/j.febslet.2007.07.025 (Pubitemid 47212095)
    • (2007) FEBS Letters , vol.581 , Issue.21 , pp. 3915-3920
    • Stricker, A.R.1    Steiger, M.G.2    Mach, R.L.3
  • 93
    • 41049088736 scopus 로고    scopus 로고
    • Interlocked feedback loops of the circadian clock of Neurospora crassa
    • DOI 10.1111/j.1365-2958.2008.06148.x
    • Interlocked feedback loops of the circadian clock of Neurospora crassa. M Brunner, K Kaldi, Mol Microbiol 2008 68 255 262 18312266 10.1111/j.1365-2958. 2008.06148.x (Pubitemid 351422954)
    • (2008) Molecular Microbiology , vol.68 , Issue.2 , pp. 255-262
    • Brunner, M.1    Kaldi, K.2
  • 94
    • 0036041204 scopus 로고    scopus 로고
    • Overexpression of White Collar-1 (WC-1) activates circadian clock-associated genes, but is not sufficient to induce most light-regulated gene expression in Neurospora crassa
    • DOI 10.1046/j.1365-2958.2002.03074.x
    • Overexpression of white collar-1 (WC-1) activates circadian clock-associated genes, but is not sufficient to induce most light-regulated gene expression in Neurospora crassa. ZA Lewis, A Correa, C Schwerdtfeger, KL Link, X Xie, RH Gomer, T Thomas, DJ Ebbole, D Bell-Pedersen, Mol Microbiol 2002 45 917 931 12180913 10.1046/j.1365-2958.2002.03074.x (Pubitemid 35007437)
    • (2002) Molecular Microbiology , vol.45 , Issue.4 , pp. 917-931
    • Lewis, Z.A.1    Correa, A.2    Schwerdtfeger, C.3    Link, K.L.4    Xie, X.5    Gomer, R.H.6    Thomas, T.7    Ebbole, D.J.8    Bell-Pedersen, D.9
  • 95
    • 33750728042 scopus 로고    scopus 로고
    • The rhythms of life: Circadian output pathways in Neurospora
    • DOI 10.1177/0748730406294396
    • The rhythms of life: circadian output pathways in Neurospora. MW Vitalini, RM de Paula, WD Park, D Bell-Pedersen, J Biol Rhythms 2006 21 432 444 17107934 10.1177/0748730406294396 (Pubitemid 44706825)
    • (2006) Journal of Biological Rhythms , vol.21 , Issue.6 , pp. 432-444
    • Vitalini, M.W.1    De Paula, R.M.2    Park, W.D.3    Bell-Pedersen, D.4
  • 96
    • 4544359281 scopus 로고    scopus 로고
    • The Neurospora circadian system
    • DOI 10.1177/0748730404269116
    • The Neurospora circadian system. JC Dunlap, JJ Loros, J Biol Rhythms 2004 19 414 424 15534321 10.1177/0748730404269116 (Pubitemid 39238209)
    • (2004) Journal of Biological Rhythms , vol.19 , Issue.5 , pp. 414-424
    • Dunlap, J.C.1    Loros, J.J.2
  • 97
    • 33751251331 scopus 로고    scopus 로고
    • How fungi keep time: Circadian system in Neurospora and other fungi
    • DOI 10.1016/j.mib.2006.10.008, PII S1369527406001627, Growth and Development
    • How fungi keep time: circadian system in Neurospora and other fungi. JC Dunlap, JJ Loros, Curr Opin Microbiol 2006 9 579 587 17064954 10.1016/j.mib.2006.10.008 (Pubitemid 44791992)
    • (2006) Current Opinion in Microbiology , vol.9 , Issue.6 , pp. 579-587
    • Dunlap, J.C.1    Loros, J.J.2
  • 98
    • 17844395528 scopus 로고    scopus 로고
    • Light controls growth and development via a conserved pathway in the fungal kingdom
    • DOI 10.1371/journal.pbio.0030095, e95
    • Light controls growth and development via a conserved pathway in the fungal kingdom. A Idnurm, J Heitman, PLoS Biol 2005 3 95 15760278 10.1371/journal.pbio.0030095 (Pubitemid 40721155)
    • (2005) PLoS Biology , vol.3 , Issue.4 , pp. 0615-0626
    • Idnurm, A.1    Heitman, J.2
  • 99
    • 3843103524 scopus 로고    scopus 로고
    • Cloning of genes expressed early during cellulase induction in Hypocrea jecorina by a rapid subtraction hybridization approach
    • DOI 10.1016/j.fgb.2004.06.002, PII S1087184504000921
    • Cloning of genes expressed early during cellulase induction in Hypocrea jecorina by a rapid subtraction hybridization approach. M Schmoll, S Zeilinger, RL Mach, CP Kubicek, Fungal Genet Biol 2004 41 877 213 15288024 10.1016/j.fgb.2004.06.002 (Pubitemid 39043801)
    • (2004) Fungal Genetics and Biology , vol.41 , Issue.9 , pp. 877-887
    • Schmoll, M.1    Zeilinger, S.2    Mach, R.L.3    Kubicek, C.P.4
  • 100
    • 29144497204 scopus 로고    scopus 로고
    • Envoy, a PAS/LOV domain protein of Hypocrea jecorina (anamorph Trichoderma reesei), modulates cellulase gene transcription in response to light
    • DOI 10.1128/EC.4.12.1998-2007.2005
    • ENVOY, a PAS/LOV domain protein of Hypocrea jecorina (Trichoderma reesei), modulates cellulase gene transcription in response to light. M Schmoll, L Franchi, CP Kubicek, Eukaryot Cell 2005 4 1998 2007 16339718 10.1128/EC.4.12.1998-2007.2005 (Pubitemid 41798306)
    • (2005) Eukaryotic Cell , vol.4 , Issue.12 , pp. 1998-2007
    • Schmoll, M.1    Franchi, L.2    Kubicek, C.P.3
  • 101
    • 38949140136 scopus 로고    scopus 로고
    • Impact of light on Hypocrea jecorina and the multiple cellular roles of ENVOY in this process
    • DOI 10.1186/1471-2164-8-449
    • Impact of light on Hypocrea jecorina and the multiple cellular roles of ENVOY in this process. A Schuster, CP Kubicek, MA Friedl, IS Druzhinina, M Schmoll, BMC Genomics 2007 8 449 18053205 10.1186/1471-2164-8-449 (Pubitemid 351228658)
    • (2007) BMC Genomics , vol.8 , pp. 449
    • Schuster, A.1    Kubicek, C.P.2    Friedl, M.A.3    Druzhinina, I.S.4    Schmoll, M.5
  • 102
    • 35848966373 scopus 로고    scopus 로고
    • Heterotrimeric G protein signaling in filamentous fungi
    • DOI 10.1146/annurev.micro.61.080706.093432
    • Heterotrimeric G protein signaling in filamentous fungi. L Li, SJ Wright, S Krystofova, G Park, KA Borkovich, Annu Rev Microbiol 2007 61 423 452 17506673 10.1146/annurev.micro.61.080706.093432 (Pubitemid 350058216)
    • (2007) Annual Review of Microbiology , vol.61 , pp. 423-452
    • Li, L.1    Wright, S.J.2    Krystofova, S.3    Park, G.4    Borkovich, K.A.5
  • 103
    • 33646730081 scopus 로고    scopus 로고
    • G-protein and cAMP-mediated signaling in aspergilli: A genomic perspective
    • DOI 10.1016/j.fgb.2006.02.001, PII S108718450600034X
    • G-protein and cAMP-mediated signaling in aspergilli: a genomic perspective. A Lafon, KH Han, JA Seo, JH Yu, C d'Enfert, Fungal Genet Biol 2006 43 490 502 16546420 10.1016/j.fgb.2006.02.001 (Pubitemid 43744480)
    • (2006) Fungal Genetics and Biology , vol.43 , Issue.7 , pp. 490-502
    • Lafon, A.1    Han, K.-H.2    Seo, J.-A.3    Yu, J.-H.4    Enfert, C.5
  • 104
    • 26444568777 scopus 로고    scopus 로고
    • The heterotrimeric G-protein GanB(α)-SfaD(β)-GpgA(γ) is a carbon source sensor involved in early cAMP-dependent germination in Aspergillus nidulans
    • DOI 10.1534/genetics.105.040584
    • The heterotrimeric G-protein GanB(alpha)-SfaD(beta)-GpgA(gamma) is a carbon source sensor involved in early cAMP-dependent germination in Aspergillus nidulans. A Lafon, JA Seo, KH Han, JH Yu, C d'Enfert, Genetics 2005 171 71 80 15944355 10.1534/genetics.105.040584 (Pubitemid 41437540)
    • (2005) Genetics , vol.171 , Issue.1 , pp. 71-80
    • Lafon, A.1    Seo, J.-A.2    Han, K.-H.3    Yu, J.-H.4    D'Enfert, C.5
  • 105
    • 23944450594 scopus 로고    scopus 로고
    • The G protein α subunit Tga1 of Trichoderma atroviride is involved in chitinase formation and differential production of antifungal metabolites
    • DOI 10.1016/j.fgb.2005.04.009, PII S1087184505000721
    • The G protein alpha subunit Tga1 of Trichoderma atroviride is involved in chitinase formation and differential production of antifungal metabolites. B Reithner, K Brunner, R Schuhmacher, I Peissl, V Seidl, R Krska, S Zeilinger, Fungal Genet Biol 2005 42 749 760 15964222 10.1016/j.fgb.2005.04.009 (Pubitemid 41188173)
    • (2005) Fungal Genetics and Biology , vol.42 , Issue.9 , pp. 749-760
    • Reithner, B.1    Brunner, K.2    Schuhmacher, R.3    Peissl, I.4    Seidl, V.5    Krska, R.6    Zeilinger, S.7
  • 106
    • 0036689944 scopus 로고    scopus 로고
    • Trichoderma atroviride G-protein α-subunit gene tga1 is involved in mycoparasitic coiling and conidiation
    • DOI 10.1128/EC.1.4.594-605.2002
    • Trichoderma atroviride G-protein alpha-subunit gene tga1 is involved in mycoparasitic coiling and conidiation. V Rocha-Ramirez, C Omero, I Chet, BA Horwitz, A Herrera-Estrella, Eukaryot Cell 2002 1 594 605 12456007 10.1128/EC.1.4.594-605.2002 (Pubitemid 36562385)
    • (2002) Eukaryotic Cell , vol.1 , Issue.4 , pp. 594-605
    • Rocha-Ramirez, V.1    Omero, C.2    Chet, I.3    Horwitz, B.A.4    Herrera-Estrella, A.5
  • 107
    • 0032589654 scopus 로고    scopus 로고
    • Mutational activation of a Gα(i) causes uncontrolled proliferation of aerial hyphae and increased sensitivity to heat and oxidative stress in Neurospora crassa
    • Mutational activation of a G-alpha-i causes uncontrolled proliferation of aerial hyphae and increased sensitivity to heat and oxidative stress in Neurospora crassa. Q Yang, KA Borkovich, Genetics 1999 151 107 117 9872952 (Pubitemid 29031880)
    • (1999) Genetics , vol.151 , Issue.1 , pp. 107-117
    • Yang, Q.1    Borkovich, K.A.2
  • 108
    • 0036617573 scopus 로고    scopus 로고
    • A G-protein β subunit required for sexual and vegetative development and maintenance of normal Gα protein levels in Neurospora crassa
    • DOI 10.1128/EC.1.3.378-390.2002
    • A G-protein beta subunit required for sexual and vegetative development and maintenance of normal G alpha protein levels in Neurospora crassa. Q Yang, SI Poole, KA Borkovich, Eukaryot Cell 2002 1 378 390 12455986 10.1128/EC.1.3.378-390.2002 (Pubitemid 36557747)
    • (2002) Eukaryotic Cell , vol.1 , Issue.3 , pp. 378-390
    • Yang, Q.1    Poole, S.I.2    Borkovich, K.A.3
  • 109
    • 53749103106 scopus 로고    scopus 로고
    • The information highways of a biotechnological workhorse - Signal transduction in Hypocrea jecorina
    • 18803869 10.1186/1471-2164-9-430
    • The information highways of a biotechnological workhorse-signal transduction in Hypocrea jecorina. M Schmoll, BMC Genomics 2008 9 430 18803869 10.1186/1471-2164-9-430
    • (2008) BMC Genomics , vol.9 , pp. 430
    • Schmoll, M.1
  • 110
    • 0027280825 scopus 로고
    • Metabolic regulation of endoglucanase synthesis in Trichoderma reesei: Participation of cyclic AMP and glucose-6-phosphate
    • Metabolic regulation of endoglucanase synthesis in Trichoderma reesei: participation of cyclic AMP and glucose-6-phosphate. S Sestak, V Farkas, Can J Microbiol 1993 39 342 347 7682891 (Pubitemid 23130409)
    • (1993) Canadian Journal of Microbiology , vol.39 , Issue.3 , pp. 342-347
    • Sestak, S.1    Farkas, V.2
  • 111
    • 0029558133 scopus 로고
    • Induction of a Cryphonectria parasitica cellobiohydrolase I gene is suppressed by hypovirus infection and regulated by a GTP-binding-protein- linked signaling pathway involved in fungal pathogenesis
    • DOI 10.1073/pnas.92.25.11529
    • Induction of a Cryphonectria parasitica cellobiohydrolase I gene is suppressed by hypovirus infection and regulated by a GTP-binding-protein-linked signaling pathway involved in fungal pathogenesis. P Wang, DL Nuss, Proc Natl Acad Sci USA 1995 92 11529 11533 8524797 10.1073/pnas.92.25.11529 (Pubitemid 26014147)
    • (1995) Proceedings of the National Academy of Sciences of the United States of America , vol.92 , Issue.25 , pp. 11529-11533
    • Wang, P.1    Nuss, D.L.2
  • 112
    • 61949360863 scopus 로고    scopus 로고
    • The G-alpha protein GNA3 of Hypocrea jecorina (anamorph Trichoderma reesei) regulates cellulase gene expression in the presence of light
    • 19136572 10.1128/EC.00256-08
    • The G-alpha protein GNA3 of Hypocrea jecorina (anamorph Trichoderma reesei) regulates cellulase gene expression in the presence of light. M Schmoll, A Schuster, RdN Silva, CP Kubicek, Eukaryot Cell 2009 8 410 20 19136572 10.1128/EC.00256-08
    • (2009) Eukaryot Cell , vol.8 , pp. 410-420
    • Schmoll, M.1    Schuster, A.2    Silva, R.3    Kubicek, C.P.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.