메뉴 건너뛰기




Volumn 17, Issue 4, 1997, Pages 273-306

The molecular biology of secreted enzyme production by fungi

Author keywords

Aspergillus; Enzyme; Fungus; Glycosylation; Heterologous gene expression; Protein secretion; Trichoderma

Indexed keywords

ENZYME; FUNGAL PROTEIN;

EID: 0031307441     PISSN: 07388551     EISSN: None     Source Type: Journal    
DOI: 10.3109/07388559709146616     Document Type: Article
Times cited : (180)

References (206)
  • 1
    • 0003292833 scopus 로고
    • Fungal exoenzymes
    • Gow, N. A. R. and Gadd, G. M. (Eds.), Chapman and Hall, London
    • Archer, D. B. and Wood, D. A. 1995. Fungal exoenzymes. In: Gow, N. A. R. and Gadd, G. M. (Eds.), The Growing Fungus. Chapman and Hall, London, pp. 137-162.
    • (1995) The Growing Fungus , pp. 137-162
    • Archer, D.B.1    Wood, D.A.2
  • 2
    • 0026683946 scopus 로고
    • Proteolytic degradation of heterologous proteins expressed in Aspergillus niger
    • Archer, D. B., MacKenzie, D. A., Jeenes, D. J., and Roberts, I. N. 1992. Proteolytic degradation of heterologous proteins expressed in Aspergillus niger. Biotechnol. Lett. 14: 357-362.
    • (1992) Biotechnol. Lett. , vol.14 , pp. 357-362
    • Archer, D.B.1    MacKenzie, D.A.2    Jeenes, D.J.3    Roberts, I.N.4
  • 3
    • 0028086427 scopus 로고
    • Strategies for improving heterologous protein production from filamentous fungi
    • Archer, D. B., Jeenes, D. J., and MacKenzie, D. A. 1994. Strategies for improving heterologous protein production from filamentous fungi. Anton. van Leeuw. 65: 245-250.
    • (1994) Anton. Van Leeuw. , vol.65 , pp. 245-250
    • Archer, D.B.1    Jeenes, D.J.2    MacKenzie, D.A.3
  • 4
    • 0029983040 scopus 로고    scopus 로고
    • Translational initiation competence, leaky scanning and translational reinitiation in areA mRNA of Aspergillus nidulans
    • Arst, H. N. and Sheerins, A. 1996. Translational initiation competence, leaky scanning and translational reinitiation in areA mRNA of Aspergillus nidulans. Mol. Microbiol. 19: 1019-1024.
    • (1996) Mol. Microbiol. , vol.19 , pp. 1019-1024
    • Arst, H.N.1    Sheerins, A.2
  • 5
    • 0028587873 scopus 로고
    • Two new genes involved in signalling ambient pH in Aspergillus nidulans
    • Arst, H. N., Bignell, E., and Tilburn, J. 1994. Two new genes involved in signalling ambient pH in Aspergillus nidulans. Mol. Gen. Genet. 245: 787-790.
    • (1994) Mol. Gen. Genet. , vol.245 , pp. 787-790
    • Arst, H.N.1    Bignell, E.2    Tilburn, J.3
  • 6
    • 0026660034 scopus 로고
    • Efficient secretion of human lysozyme fused to the Sh ble phleomycin resistance protein by the fungus Tolypocladium geodes
    • Baron, M., Tiraby, G., Calmels, T., Parriche, M., and Durand, H. 1992. Efficient secretion of human lysozyme fused to the Sh ble phleomycin resistance protein by the fungus Tolypocladium geodes. J. Biotechnol. 24: 253-266.
    • (1992) J. Biotechnol. , vol.24 , pp. 253-266
    • Baron, M.1    Tiraby, G.2    Calmels, T.3    Parriche, M.4    Durand, H.5
  • 7
    • 0030667443 scopus 로고    scopus 로고
    • Trichoderma reesei sequences that bind to the nuclear matrix enhance transformation frequency
    • Belshaw, N. J., Hakola, S., Nevalainen, H., Penttilä, M., Suominen, P., and Archer, D. B. 1997. Trichoderma reesei sequences that bind to the nuclear matrix enhance transformation frequency. Mol. Gen. Genet. 256: 18-27.
    • (1997) Mol. Gen. Genet. , vol.256 , pp. 18-27
    • Belshaw, N.J.1    Hakola, S.2    Nevalainen, H.3    Penttilä, M.4    Suominen, P.5    Archer, D.B.6
  • 8
  • 9
    • 0025784815 scopus 로고
    • The development of Aspergillus niger var. awamori as a host for the expression and secretion of heterologous gene products
    • Berka, R. M., Kodama, K. H., Rey, M. W., Wilson, L. J., and Ward, M. 1991. The development of Aspergillus niger var. awamori as a host for the expression and secretion of heterologous gene products. Biochem. Soc. Trans. 19: 681-685.
    • (1991) Biochem. Soc. Trans. , vol.19 , pp. 681-685
    • Berka, R.M.1    Kodama, K.H.2    Rey, M.W.3    Wilson, L.J.4    Ward, M.5
  • 10
    • 0030468326 scopus 로고    scopus 로고
    • Structure, differentiation, and multiplication of Golgi apparatus in fungal hyphae
    • Bracker, C. E., Morre, D. J., and Grove, S. N. 1996. Structure, differentiation, and multiplication of Golgi apparatus in fungal hyphae. Protoplasma 194: 250-274.
    • (1996) Protoplasma , vol.194 , pp. 250-274
    • Bracker, C.E.1    Morre, D.J.2    Grove, S.N.3
  • 11
    • 0029097268 scopus 로고
    • Effects of leader sequences upon the heterologous expression of restrictocin in Aspergillus nidulans and Aspergillus niger
    • Brandhorst, T. and Kenealy, W. R. 1995. Effects of leader sequences upon the heterologous expression of restrictocin in Aspergillus nidulans and Aspergillus niger. Can. J. Microbiol. 41: 601-611.
    • (1995) Can. J. Microbiol. , vol.41 , pp. 601-611
    • Brandhorst, T.1    Kenealy, W.R.2
  • 13
    • 0027442912 scopus 로고
    • Hypersensitive sites in the 5′ promoter region of nit-3, a highly regulated structural gene of Neurospora crassa
    • Brito, N., Gonzalez, C., and Marzluf, G. A. 1993. Hypersensitive sites in the 5′ promoter region of nit-3, a highly regulated structural gene of Neurospora crassa. J. Bacteriol. 175: 6755-6759.
    • (1993) J. Bacteriol. , vol.175 , pp. 6755-6759
    • Brito, N.1    Gonzalez, C.2    Marzluf, G.A.3
  • 14
    • 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., and van den Hondel, C. A. M. J. J. 1993. 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. 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
  • 15
    • 26044469644 scopus 로고
    • The control of gene expression in filamentous fungi
    • Broda, P., Oliver, S. G. and Sims, P. F. G. (Eds.), Cambridge University Press
    • Caddick, M. X. and Turner, A. S. 1993. The control of gene expression in filamentous fungi. In: Broda, P., Oliver, S. G. and Sims, P. F. G. (Eds.), The Eukaryotic Genome, Organisation and Regulation, pp. 241-273, Cambridge University Press.
    • (1993) The Eukaryotic Genome, Organisation and Regulation , pp. 241-273
    • Caddick, M.X.1    Turner, A.S.2
  • 16
    • 0025977561 scopus 로고
    • Proteolytic events in the processing of secreted proteins in fungi
    • Calmels, T. P. G., Martin, F., Durand, H., and Tiraby, G. 1991. Proteolytic events in the processing of secreted proteins in fungi. J. Biotechnol. 17: 51-66.
    • (1991) J. Biotechnol. , vol.17 , pp. 51-66
    • Calmels, T.P.G.1    Martin, F.2    Durand, H.3    Tiraby, G.4
  • 17
    • 0026744443 scopus 로고
    • Chromosomal and genetic analysis of the electrophoretic karyotype of Trichoderma reesei: Mapping of the cellulase and xylanase genes
    • Carter, G., Allison, D., Rey, M. W., and Dunn-Coleman, N. S. 1992. Chromosomal and genetic analysis of the electrophoretic karyotype of Trichoderma reesei: mapping of the cellulase and xylanase genes. Mol. Microbiol. 6: 2167-2174.
    • (1992) Mol. Microbiol. , vol.6 , pp. 2167-2174
    • Carter, G.1    Allison, D.2    Rey, M.W.3    Dunn-Coleman, N.S.4
  • 18
    • 0028912305 scopus 로고
    • A C-terminal domain, which prevents secretion of the neuroendocrine protein 7B2 in Saccharomyces cerevisiae, inhibits Kex2 yet is processed by the Yap3 protease
    • Chaudhuri, B. and Stephan, C. 1995. A C-terminal domain, which prevents secretion of the neuroendocrine protein 7B2 in Saccharomyces cerevisiae, inhibits Kex2 yet is processed by the Yap3 protease. FEBS Lett. 364: 91-97.
    • (1995) FEBS Lett. , vol.364 , pp. 91-97
    • Chaudhuri, B.1    Stephan, C.2
  • 19
    • 0030570988 scopus 로고    scopus 로고
    • Purification and partial characterization of the high and low molecular weight form (S and F form) of invertase secreted by Aspergillus nidulans
    • Chen, J. S., Saxton, J., Hemming, F. W., and Peberdy, J. F. 1996. Purification and partial characterization of the high and low molecular weight form (S and F form) of invertase secreted by Aspergillus nidulans. Biochim. Biophys. Acta Protein Struct. Mol. Enzymol. 1296: 207-218.
    • (1996) Biochim. Biophys. Acta Protein Struct. Mol. Enzymol. , vol.1296 , pp. 207-218
    • Chen, J.S.1    Saxton, J.2    Hemming, F.W.3    Peberdy, J.F.4
  • 20
    • 0026591529 scopus 로고
    • Secretory pathway function in Saccharomyces cerevisiae
    • Cleves, A. E. and Bankaitis, V. A. 1991. Secretory pathway function in Saccharomyces cerevisiae. Adv. Microb. Physiol. 33: 73-144.
    • (1991) Adv. Microb. Physiol. , vol.33 , pp. 73-144
    • Cleves, A.E.1    Bankaitis, V.A.2
  • 21
    • 14744271483 scopus 로고
    • Efficient KEX2-like processing of a glucoamylase-interleukin-6 fusion protein by Aspergillus nidulans and secretion of mature interleukin-6
    • Contreras, R., Carrez, D., Kinghom, J. R., van den Hondel, C. A. M. J. J., and Fiers, W. 1991. Efficient KEX2-like processing of a glucoamylase-interleukin-6 fusion protein by Aspergillus nidulans and secretion of mature interleukin-6. Bio/ Technology 9: 378-381.
    • (1991) Bio/ Technology , vol.9 , pp. 378-381
    • Contreras, R.1    Carrez, D.2    Kinghom, J.R.3    Van Den Hondel, C.A.M.J.J.4    Fiers, W.5
  • 22
    • 0028264386 scopus 로고
    • The global transcriptional regulators, SSN6 and TUP1, play distinct roles in the establishment of a repressive chromatin structure
    • Cooper, J. P., Roth, S. Y., and Simpson, R. T. 1994. The global transcriptional regulators, SSN6 and TUP1, play distinct roles in the establishment of a repressive chromatin structure. Genes Dev. 8: 1400-1410.
    • (1994) Genes Dev. , vol.8 , pp. 1400-1410
    • Cooper, J.P.1    Roth, S.Y.2    Simpson, R.T.3
  • 23
    • 0030016595 scopus 로고    scopus 로고
    • Structure and functions of the 20S and 26S proteasomes
    • Coux, O., Tanaka, K., and Goldberg, A. L. 1996. Structure and functions of the 20S and 26S proteasomes. Annu. Rev. Biochem. 65: 801-847.
    • (1996) Annu. Rev. Biochem. , vol.65 , pp. 801-847
    • Coux, O.1    Tanaka, K.2    Goldberg, A.L.3
  • 24
    • 0028140060 scopus 로고
    • Two different, adjacent and divergent zinc finger binding sites are necessary for CREA-mediated carbon catabolite repression in the proline gene cluster of Aspergillus nidulans
    • Cubero, B. and Scazzocchio, C. 1994. Two different, adjacent and divergent zinc finger binding sites are necessary for CREA-mediated carbon catabolite repression in the proline gene cluster of Aspergillus nidulans. EMBO J. 13: 407-415.
    • (1994) EMBO J. , vol.13 , pp. 407-415
    • Cubero, B.1    Scazzocchio, C.2
  • 25
    • 0002986624 scopus 로고
    • Fungal enzymes for lignocellulose degradation
    • Kinghorn, J. R. and Turner, G., (Eds.), Blackie, London
    • Cullen, D. and Kersten, P. 1992. Fungal enzymes for lignocellulose degradation. In: Applied Molecular Genetics of Filamentous Fungi, Kinghorn, J. R. and Turner, G., (Eds.), pp. 100-131, Blackie, London.
    • (1992) Applied Molecular Genetics of Filamentous Fungi , pp. 100-131
    • Cullen, D.1    Kersten, P.2
  • 27
    • 0030442540 scopus 로고    scopus 로고
    • Endopolygalacturonase from Fusarium oxysporum f.sp. lycopsersici - Purification, characterisation and production during infection of tomato plants
    • Dipietro, A. and Roncero, M. I. G. 1996. Endopolygalacturonase from Fusarium oxysporum f.sp. lycopsersici - purification, characterisation and production during infection of tomato plants. Phytopathology 86: 1324-1330.
    • (1996) Phytopathology , vol.86 , pp. 1324-1330
    • Dipietro, A.1    Roncero, M.I.G.2
  • 28
    • 0023708177 scopus 로고
    • Reduction of endogenous GRP78 levels improves secretion of a heterologous protein in CHO cells
    • Dorner, A. J., Krane, M. G., and Kaufman, R. J. 1988. Reduction of endogenous GRP78 levels improves secretion of a heterologous protein in CHO cells. Mol. Cell. Biol. 8: 4063-4070.
    • (1988) Mol. Cell. Biol. , vol.8 , pp. 4063-4070
    • Dorner, A.J.1    Krane, M.G.2    Kaufman, R.J.3
  • 29
    • 0026511824 scopus 로고
    • Over-expression of GRP78 mitigates stress induction of glucose regulated proteins and blocks secretion of selective proteins in Chinese hamster ovary cells
    • Dorner, A. J., Wasley, L. C., and Kaufman, R. J. 1992. Over-expression of GRP78 mitigates stress induction of glucose regulated proteins and blocks secretion of selective proteins in Chinese hamster ovary cells. EMBO J. 11: 1563-1571.
    • (1992) EMBO J. , vol.11 , pp. 1563-1571
    • Dorner, A.J.1    Wasley, L.C.2    Kaufman, R.J.3
  • 30
    • 0024678261 scopus 로고
    • Cloning of the creA gene from Aspergillus nidulans: A gene involved in carbon catabolite repression
    • Dowzer, C. E. A. and Kelly, J. M. 1989. Cloning of the creA gene from Aspergillus nidulans: a gene involved in carbon catabolite repression. Curr. Genet. 15: 457-459.
    • (1989) Curr. Genet. , vol.15 , pp. 457-459
    • Dowzer, C.E.A.1    Kelly, J.M.2
  • 31
    • 0025944347 scopus 로고
    • Analysis of the creA gene, a regulator of carbon catabolite repression in Aspergillus nidulans
    • Dowzer, C. E. A. and Kelly, J. M. 1991. Analysis of the creA gene, a regulator of carbon catabolite repression in Aspergillus nidulans. Mol. Cell Biol. 11: 5701-5709.
    • (1991) Mol. Cell Biol. , vol.11 , pp. 5701-5709
    • Dowzer, C.E.A.1    Kelly, J.M.2
  • 32
    • 0027179822 scopus 로고
    • The Aspergillus niger carbon catabolite represser encoding gene, creA
    • Drysdale, M. R., Kolze, S. E., and Kelly, J. M. 1993. The Aspergillus niger carbon catabolite represser encoding gene, creA. Gene 130: 241-245.
    • (1993) Gene , vol.130 , pp. 241-245
    • Drysdale, M.R.1    Kolze, S.E.2    Kelly, J.M.3
  • 35
    • 0028323131 scopus 로고
    • In vitro binding of the two-finger repressor CreA to several consensus and non-consensus sites at the ipnA upstream region is context dependent
    • Espeso, E. A. and Peñalva, M. A. 1994. In vitro binding of the two-finger repressor CreA to several consensus and non-consensus sites at the ipnA upstream region is context dependent. FEBS Lett. 342: 43-48.
    • (1994) FEBS Lett. , vol.342 , pp. 43-48
    • Espeso, E.A.1    Peñalva, M.A.2
  • 36
    • 0029053448 scopus 로고
    • The role of N-glycans in the secretory pathway
    • Fiedler, K. and Simons, K. 1995. The role of N-glycans in the secretory pathway. Cell 81: 309-312.
    • (1995) Cell , vol.81 , pp. 309-312
    • Fiedler, K.1    Simons, K.2
  • 37
    • 0028151030 scopus 로고
    • Arabinase gene expression in Aspergillus niger: Indications for coordinated regulation
    • Flipphi, M. J. A., Visser, J., van der Veen, P., and de Graaff, L. H. 1994. Arabinase gene expression in Aspergillus niger: indications for coordinated regulation. J. Gen. Microbiol. 140: 2673-2682.
    • (1994) J. Gen. Microbiol. , vol.140 , pp. 2673-2682
    • Flipphi, M.J.A.1    Visser, J.2    Van Der Veen, P.3    De Graaff, L.H.4
  • 38
    • 0025601688 scopus 로고
    • Regulation of the glaA gene of Aspergillus niger
    • Fowler, T., Berka, R. M., and Ward, M. 1990. Regulation of the glaA gene of Aspergillus niger. Curr. Genet. 18: 537-545.
    • (1990) Curr. Genet. , vol.18 , pp. 537-545
    • Fowler, T.1    Berka, R.M.2    Ward, M.3
  • 40
    • 0027959156 scopus 로고
    • Protein disulfide isomerase: Building bridges in protein folding
    • Freedman, R. B., Hirst, T. R., and Tuite, M. F. 1994. Protein disulfide isomerase: building bridges in protein folding. Trends Biochem. Sci. 19: 331-336.
    • (1994) Trends Biochem. Sci. , vol.19 , pp. 331-336
    • Freedman, R.B.1    Hirst, T.R.2    Tuite, M.F.3
  • 42
    • 0002598441 scopus 로고
    • A glimpse at chromosomal order
    • Gasser, S. M. and Laemmli, U. K. 1987. A glimpse at chromosomal order. Trends Genet. 3: 16-22.
    • (1987) Trends Genet. , vol.3 , pp. 16-22
    • Gasser, S.M.1    Laemmli, U.K.2
  • 43
    • 0026584271 scopus 로고
    • Protein folding in the cell
    • Gething, M.-J. and Sambrook, J. 1992. Protein folding in the cell. Nature 355: 33-45.
    • (1992) Nature , vol.355 , pp. 33-45
    • Gething, M.-J.1    Sambrook, J.2
  • 44
    • 0024963567 scopus 로고
    • Signal sequences
    • Gierasch, L. M. 1989. Signal sequences. Biochemistry 28: 923-930.
    • (1989) Biochemistry , vol.28 , pp. 923-930
    • Gierasch, L.M.1
  • 45
    • 0027938897 scopus 로고
    • Protein chaperones and protein folding
    • Gilbert, H. F. 1994. Protein chaperones and protein folding. Curr. Opin. Biotechnol. 5: 534-539.
    • (1994) Curr. Opin. Biotechnol. , vol.5 , pp. 534-539
    • Gilbert, H.F.1
  • 47
    • 0030981454 scopus 로고    scopus 로고
    • The integration of nitrogen and carbon catabolite repression in Aspergillus nidulans requires the GATA factor AreA and an additional positive-acting element, ADA
    • Gonzalez, R., Gavrias, V., Gomez, D., Scazzocchio, C., and Cubero, B. 1997. The integration of nitrogen and carbon catabolite repression in Aspergillus nidulans requires the GATA factor AreA and an additional positive-acting element, ADA. EMBO J. 16: 2937-2944.
    • (1997) EMBO J. , vol.16 , pp. 2937-2944
    • Gonzalez, R.1    Gavrias, V.2    Gomez, D.3    Scazzocchio, C.4    Cubero, B.5
  • 48
    • 0029028453 scopus 로고
    • A novel strategy for the isolation of defined pyrG mutants and the development of a site-specific integration system for Aspergillus awamori
    • Gouka, R. J., Hessing, J. G. M., Stam, H., Musters, W., and van den Hondel, C. A. M. J. J. 1995. A novel strategy for the isolation of defined pyrG mutants and the development of a site-specific integration system for Aspergillus awamori. Curr. Genet. 27: 536-540.
    • (1995) Curr. Genet. , vol.27 , pp. 536-540
    • Gouka, R.J.1    Hessing, J.G.M.2    Stam, H.3    Musters, W.4    Van Den Hondel, C.A.M.J.J.5
  • 50
    • 0029952011 scopus 로고    scopus 로고
    • Analysis of heterologous protein production in defined recombinant Aspergillus awamori strains
    • Gouka, R. J., Punt, P. J., Hessing, J. G. M., and van den Hondel, C. A. M. J. J. 1996b. Analysis of heterologous protein production in defined recombinant Aspergillus awamori strains. Appl. Environ. Microbiol. 62: 1951-1957.
    • (1996) Appl. Environ. Microbiol. , vol.62 , pp. 1951-1957
    • Gouka, R.J.1    Punt, P.J.2    Hessing, J.G.M.3    Van Den Hondel, C.A.M.J.J.4
  • 52
    • 0031054007 scopus 로고    scopus 로고
    • Efficient production of secreted proteins by Aspergillus: Progress, limitations and prospects
    • Gouka, R. J., Punt, P. J., and van den Hondel, C. A. M. J. J. 1997a. Efficient production of secreted proteins by Aspergillus: progress, limitations and prospects. Appl. Microbiol. Biotechnol. 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
  • 53
    • 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., and van den Hondel, C. A. M. J. J. 1997b. Glucoamylase gene fusions alleviate limitations for protein production in Aspergillus awamori at the transcriptional and (post) translational levels. Appl. Environ. Microbiol. 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
  • 55
    • 0028329930 scopus 로고
    • Sorting and processing of secretory proteins
    • Halban, P. A. and Irminger, J. C. 1994. Sorting and processing of secretory proteins. Biochem. J. 299: 1-18.
    • (1994) Biochem. J. , vol.299 , pp. 1-18
    • Halban, P.A.1    Irminger, J.C.2
  • 56
    • 0029094253 scopus 로고
    • Quality control in the secretory pathway
    • Hammond, C. and Helenius, A. 1995. Quality control in the secretory pathway. Curr. Opin. Cell Biol. 7: 523-529.
    • (1995) Curr. Opin. Cell Biol. , vol.7 , pp. 523-529
    • Hammond, C.1    Helenius, A.2
  • 59
    • 0026688912 scopus 로고
    • Functional elements of the promoter region of the Aspergillus oryzae glaA gene encoding glucoamylase
    • Hata, Y., Kitamoto, K., Gomi, K., Kumagai, C. and Tamura, G. 1992. Functional elements of the promoter region of the Aspergillus oryzae glaA gene encoding glucoamylase. Curr. Genet. 22: 85-91.
    • (1992) Curr. Genet. , vol.22 , pp. 85-91
    • Hata, Y.1    Kitamoto, K.2    Gomi, K.3    Kumagai, C.4    Tamura, G.5
  • 60
    • 0025888946 scopus 로고
    • Nucleotide sequence and expression of the glucoamylase-encoding gene (glaA) from Aspergillus oryzae
    • Hata, Y., Tsuchiya, K., Kitamoto, K., Gomi, K., Kumagai, C., Tamura, G., and Hara, S. 1991. Nucleotide sequence and expression of the glucoamylase-encoding gene (glaA) from Aspergillus oryzae. Gene 108: 145-150.
    • (1991) Gene , vol.108 , pp. 145-150
    • Hata, Y.1    Tsuchiya, K.2    Kitamoto, K.3    Gomi, K.4    Kumagai, C.5    Tamura, G.6    Hara, S.7
  • 61
    • 0026620094 scopus 로고
    • The Ncypt1 gene from Neurospora crassa is located on chromosome 2; molecular cloning and structural analysis
    • Heintz, K., Palme, K., Diefenthal, T. and Russo, V. E. A. 1992. The Ncypt1 gene from Neurospora crassa is located on chromosome 2; molecular cloning and structural analysis. Mol. Gen. Genet. 235: 413-421.
    • (1992) Mol. Gen. Genet. , vol.235 , pp. 413-421
    • Heintz, K.1    Palme, K.2    Diefenthal, T.3    Russo, V.E.A.4
  • 62
    • 0029927285 scopus 로고    scopus 로고
    • The chicken lysozyme gene 5′ MAR and the Drosophila histone SAR are electroelutable from encapsulated and digested nuclei
    • Hempel, K. and Strätling, W. H. 1996. The chicken lysozyme gene 5′ MAR and the Drosophila histone SAR are electroelutable from encapsulated and digested nuclei. J. Cell Sci. 109: 1459-1469.
    • (1996) J. Cell Sci. , vol.109 , pp. 1459-1469
    • Hempel, K.1    Strätling, W.H.2
  • 63
    • 0030581647 scopus 로고    scopus 로고
    • Two regulatory regions controlling basal and cellulose-induced expression of the gene encoding cellobiohydrolase I of Trichoderma reesei are adjacent to its TATA box
    • Henrique-Silva, F., El-Gogary, S., Carle-Urioste, J. C., Matheucci, E., Crivellaro, O., and El-Dorry, H. 1996. Two regulatory regions controlling basal and cellulose-induced expression of the gene encoding cellobiohydrolase I of Trichoderma reesei are adjacent to its TATA box. Biochem. Biophys. Res. Commun. 228: 229-237.
    • (1996) Biochem. Biophys. Res. Commun. , vol.228 , pp. 229-237
    • Henrique-Silva, F.1    El-Gogary, S.2    Carle-Urioste, J.C.3    Matheucci, E.4    Crivellaro, O.5    El-Dorry, H.6
  • 64
    • 0000312026 scopus 로고
    • Two lipases from Candida antarctica - Cloning and expression in Aspergillus oryzae
    • Heogh, I., Patkar, S., Halkier, T., and Hansen, M. T. 1995. Two lipases from Candida antarctica - cloning and expression in Aspergillus oryzae. Can. J. Bot. 73 Suppl. 1E-H: S869-S875.
    • (1995) Can. J. Bot. , vol.73 , Issue.SUPPL. 1E-H
    • Heogh, I.1    Patkar, S.2    Halkier, T.3    Hansen, M.T.4
  • 65
    • 0030759130 scopus 로고    scopus 로고
    • Characterization of the bip gene of Aspergillus awamori with an HDEL retention signal homologous to the mammalian BiP involved in polypeptide secretion
    • Hijarrubia, M. J., Casqueiro, J., Gutiérrez, S., Fernandez, F. J., and Martin, J. F. 1997. Characterization of the bip gene of Aspergillus awamori with an HDEL retention signal homologous to the mammalian BiP involved in polypeptide secretion. Curr. Genet. 32: 139-146.
    • (1997) Curr. Genet. , vol.32 , pp. 139-146
    • Hijarrubia, M.J.1    Casqueiro, J.2    Gutiérrez, S.3    Fernandez, F.J.4    Martin, J.F.5
  • 66
    • 0026787869 scopus 로고
    • Stress-induced proteolysis in yeast
    • Hilt, W. and Wolf, D. H. 1992. Stress-induced proteolysis in yeast. Mol. Microbiol. 6: 2437-2442.
    • (1992) Mol. Microbiol. , vol.6 , pp. 2437-2442
    • Hilt, W.1    Wolf, D.H.2
  • 68
    • 14744281995 scopus 로고
    • A glucose-derepressed promoter for expression of heterologous products in the filamentous fungus Aspergillus nidulans
    • Hintz, W. E. and Lagosky, P. A. 1993. A glucose-derepressed promoter for expression of heterologous products in the filamentous fungus Aspergillus nidulans. Bio/Technology 11: 815-818.
    • (1993) Bio/Technology , vol.11 , pp. 815-818
    • Hintz, W.E.1    Lagosky, P.A.2
  • 69
    • 85033504317 scopus 로고    scopus 로고
    • 1995. A Fungal Protein Disulfide Isomerase. Patent WO 95/00636
    • Hjort, C. M. 1995. A Fungal Protein Disulfide Isomerase. Patent WO 95/00636.
    • Hjort, C.M.1
  • 70
    • 0028365549 scopus 로고
    • Engineering the assembly pathway of the baculovirus-insect cell expression system
    • Hsu, T. A., Eiden, J. J., and Betenbaugh, M. J. 1994. Engineering the assembly pathway of the baculovirus-insect cell expression system. Ann. N.Y. Acad. Sci. 721: 208-217.
    • (1994) Ann. N.Y. Acad. Sci. , vol.721 , pp. 208-217
    • Hsu, T.A.1    Eiden, J.J.2    Betenbaugh, M.J.3
  • 71
    • 0029027219 scopus 로고
    • Cloning, nucleotide sequence, and expression of tef-1, the gene encoding translation elongation factor 1-alpha (EF-1-alpha) of Neurospora crassa
    • Ichiishi, A. and Inoue, H. 1995. Cloning, nucleotide sequence, and expression of tef-1, the gene encoding translation elongation factor 1-alpha (EF-1-alpha) of Neurospora crassa. Jpn. J. Genet. 70: 273-287.
    • (1995) Jpn. J. Genet. , vol.70 , pp. 273-287
    • Ichiishi, A.1    Inoue, H.2
  • 73
    • 0030036051 scopus 로고    scopus 로고
    • The glucose repressor gene cre1 of Trichoderma: Isolation and expression of a full-length and a truncated mutant form
    • Ilmén, M., Thrane, C., and Penttilä, M. 1996a The glucose repressor gene cre1 of Trichoderma: isolation and expression of a full-length and a truncated mutant form. Mol. Gen. Genet. 251: 451-460.
    • (1996) Mol. Gen. Genet. , vol.251 , pp. 451-460
    • Ilmén, M.1    Thrane, C.2    Penttilä, M.3
  • 74
    • 0030480099 scopus 로고    scopus 로고
    • Functional analysis of the cellobiohydrolase I promoter of the filamentous fungus Trichoderma reesei
    • Ilmén, M., Onnela, M.-L., Klemsdal, S., Keränen, S., and Penttilä, M. 1996b. Functional analysis of the cellobiohydrolase I promoter of the filamentous fungus Trichoderma reesei. Mol. Gen. Genet. 253: 303-314.
    • (1996) Mol. Gen. Genet. , vol.253 , pp. 303-314
    • Ilmén, M.1    Onnela, M.-L.2    Klemsdal, S.3    Keränen, S.4    Penttilä, M.5
  • 75
    • 0029881045 scopus 로고    scopus 로고
    • Sequences attaching loops of nuclear and mitochondrial DNA to underlying structures in human cells: The role of transcription units
    • Jackson, D. A., Bartlett, J., and Cook, P. R. 1996. Sequences attaching loops of nuclear and mitochondrial DNA to underlying structures in human cells: the role of transcription units. Nucl. Acids Res. 24: 1212-1219.
    • (1996) Nucl. Acids Res. , vol.24 , pp. 1212-1219
    • Jackson, D.A.1    Bartlett, J.2    Cook, P.R.3
  • 76
    • 0029618309 scopus 로고
    • The structural basis of nuclear function
    • Jackson, D. A. and Cook, P. R. 1995. The structural basis of nuclear function. Int. Rev. Cytol. 162A: 125-149.
    • (1995) Int. Rev. Cytol. , vol.162 A , pp. 125-149
    • Jackson, D.A.1    Cook, P.R.2
  • 77
    • 0028921010 scopus 로고
    • The Schizosaccharomyces pombe homologue of the chaperone calnexin is essential for viability
    • Jannatipour, M. and Rokeach, L. A. 1995. The Schizosaccharomyces pombe homologue of the chaperone calnexin is essential for viability. J. Biol. Chem. 270: 4845-4853.
    • (1995) J. Biol. Chem. , vol.270 , pp. 4845-4853
    • Jannatipour, M.1    Rokeach, L.A.2
  • 78
    • 0028093358 scopus 로고
    • Nitrogen, carbon, and pH regulation of extracellular acidic proteases of Aspergillus niger
    • Jarai, G. and Buxton, F. 1994. Nitrogen, carbon, and pH regulation of extracellular acidic proteases of Aspergillus niger. Curr. Genet. 26: 238-244.
    • (1994) Curr. Genet. , vol.26 , pp. 238-244
    • Jarai, G.1    Buxton, F.2
  • 79
    • 0028268699 scopus 로고
    • Cloning and characterization of the pepD gene of Aspergillus niger which codes for a subtilisin-like protease
    • Jarai, G., Kirchherr, D., and Buxton, F. P. 1994a. Cloning and characterization of the pepD gene of Aspergillus niger which codes for a subtilisin-like protease. Gene 139: 51-57.
    • (1994) Gene , vol.139 , pp. 51-57
    • Jarai, G.1    Kirchherr, D.2    Buxton, F.P.3
  • 80
    • 0028068165 scopus 로고
    • Cloning and characterization of the pepE gene of Aspergillus niger encoding a new aspartic protease and regulation of pepE and pepC
    • Jarai, G., van den Hombergh, H., and Buxton, F. P. 1994b. Cloning and characterization of the pepE gene of Aspergillus niger encoding a new aspartic protease and regulation of pepE and pepC. Gene 145: 171-178.
    • (1994) Gene , vol.145 , pp. 171-178
    • Jarai, G.1    Van Den Hombergh, H.2    Buxton, F.P.3
  • 81
    • 0028500342 scopus 로고
    • Transcriptional and post-transcriptional events affect the production of secreted hen egg white lysozyme by Aspergillus niger
    • Jeenes, D. J., MacKenzie, D. A., and Archer, D. B. 1994. Transcriptional and post-transcriptional events affect the production of secreted hen egg white lysozyme by Aspergillus niger. Transgenic Res. 3: 297-303.
    • (1994) Transgenic Res. , vol.3 , pp. 297-303
    • Jeenes, D.J.1    MacKenzie, D.A.2    Archer, D.B.3
  • 83
    • 0027411139 scopus 로고
    • A truncated glucoamylase gene fusion for heterologous protein secretion from Aspergillus niger
    • Jeenes, D. J., Marczinke, B., MacKenzie, D. A. and Archer, D. B.1993. A truncated glucoamylase gene fusion for heterologous protein secretion from Aspergillus niger. FEMS Microbiol. Lett. 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
  • 84
    • 0030787806 scopus 로고    scopus 로고
    • Isolation and characterization of a novel stress-inducible PDI-family gene from Aspergillus niger
    • Jeenes, D. J., Pfaller, R., and Archer, D. B. 1997. Isolation and characterization of a novel stress-inducible PDI-family gene from Aspergillus niger. Gene 193: 151-156.
    • (1997) Gene , vol.193 , pp. 151-156
    • Jeenes, D.J.1    Pfaller, R.2    Archer, D.B.3
  • 85
    • 0027367915 scopus 로고
    • Transformation of Trichoderma reesei with the Hormoconis resinae glucoamylase P (gamP) gene: Production of a heterologous glucoamylase by Trichoderma reesei
    • Joutsjoki, V. V., Torkkeli, T. K., and Nevalainen, K. M. 1993. Transformation of Trichoderma reesei with the Hormoconis resinae glucoamylase P (gamP) gene: production of a heterologous glucoamylase by Trichoderma reesei. Curr. Genet. 24: 223-228.
    • (1993) Curr. Genet. , vol.24 , pp. 223-228
    • Joutsjoki, V.V.1    Torkkeli, T.K.2    Nevalainen, K.M.3
  • 87
    • 0029010002 scopus 로고
    • Insertion into Aspergillus nidulans of functional UDP-GlcNAc-a-3-D-mannoside β-1,2-N-acetylglucosaminyl-transferase-I, the enzyme catalyzing the first comitted step from oligomannose to hybrid and complex N-glycans
    • Kalsner, I., Hintz, W., Reid, L. S., and Schachter, H. 1995. Insertion into Aspergillus nidulans of functional UDP-GlcNAc-a-3-D-mannoside β-1,2-N-acetylglucosaminyl-transferase-I, the enzyme catalyzing the first comitted step from oligomannose to hybrid and complex N-glycans. Glycoconj. J. 12: 360-370.
    • (1995) Glycoconj. J. , vol.12 , pp. 360-370
    • Kalsner, I.1    Hintz, W.2    Reid, L.S.3    Schachter, H.4
  • 88
    • 0029885397 scopus 로고    scopus 로고
    • Molecular cloning and determination of the nucleotide sequence of a gene encoding an acid-stable α-amylase from Aspergillus kawachi
    • Kaneko, A., Sudo, S., Takayasau-Sakamoto, Y., Tamura, G., Ishikawa, T., and Ohba, T. 1996. Molecular cloning and determination of the nucleotide sequence of a gene encoding an acid-stable α-amylase from Aspergillus kawachi. J. Ferment. Bioeng. 81: 292-298.
    • (1996) J. Ferment. Bioeng. , vol.81 , pp. 292-298
    • Kaneko, A.1    Sudo, S.2    Takayasau-Sakamoto, Y.3    Tamura, G.4    Ishikawa, T.5    Ohba, T.6
  • 89
    • 0027138808 scopus 로고
    • High-frequency one-step gene replacement in Trichoderma reesei. I. Endoglucanase I overproduction
    • Karhunen, T., Mäntylä, A., Nevalainen, K. M., and Suominen, P. L. 1993. High-frequency one-step gene replacement in Trichoderma reesei. I. Endoglucanase I overproduction. Mol. Gen. Genet. 241: 515-522.
    • (1993) Mol. Gen. Genet. , vol.241 , pp. 515-522
    • Karhunen, T.1    Mäntylä, A.2    Nevalainen, K.M.3    Suominen, P.L.4
  • 90
    • 0029940951 scopus 로고    scopus 로고
    • Mutations affecting extracellular protease production in the filamentous fungus Aspergillus nidulans
    • Katz, M. E., Flynn, P. K., van Kuyk, P. A., and Cheetham, B. F. 1996. Mutations affecting extracellular protease production in the filamentous fungus Aspergillus nidulans. Mol. Gen. Genet. 250: 715-724.
    • (1996) Mol. Gen. Genet. , vol.250 , pp. 715-724
    • Katz, M.E.1    Flynn, P.K.2    Van Kuyk, P.A.3    Cheetham, B.F.4
  • 92
    • 0028311699 scopus 로고
    • Carbon catabolite repression
    • Martinelli, S. D. and Kinghorn, J. R. (Eds.), Elsevier, Amsterdam
    • Kelly, J. 1994. Carbon catabolite repression. In: Aspergillus: 50 Years On, Martinelli, S. D. and Kinghorn, J. R. (Eds.), pp.355-367, Elsevier, Amsterdam.
    • (1994) Aspergillus: 50 Years on , pp. 355-367
    • Kelly, J.1
  • 93
    • 0028877138 scopus 로고
    • Production of recobinant proteins in the filamentous fungus Trichoderma reesei
    • Keränen, S. and Penttilä, M. 1995. Production of recobinant proteins in the filamentous fungus Trichoderma reesei. Curr. Opin. Biotechnol. 6: 534-537.
    • (1995) Curr. Opin. Biotechnol. , vol.6 , pp. 534-537
    • Keränen, S.1    Penttilä, M.2
  • 94
    • 0028801931 scopus 로고
    • Calnexin and BiP act as sequential molecular chaperones during thyroglobulin folding in the endoplasmic reticulum
    • Kim, P. S. and Arvan, P. 1995. Calnexin and BiP act as sequential molecular chaperones during thyroglobulin folding in the endoplasmic reticulum. J. Cell Biol. 128: 29-38.
    • (1995) J. Cell Biol. , vol.128 , pp. 29-38
    • Kim, P.S.1    Arvan, P.2
  • 95
    • 0028143066 scopus 로고
    • Cloning and characterization of two structurally and functionally divergent rhamnogalaturonases from Aspergillus aculeatus
    • Kofod, L. V., Kauppinen, S., Christgau, S., Andersen, L. N., Heldt-Hansen, H. P., Dörreich, K., and Dalboge, H. 1994. Cloning and characterization of two structurally and functionally divergent rhamnogalaturonases from Aspergillus aculeatus. J. Biol. Chem. 269: 29182-29189.
    • (1994) J. Biol. Chem. , vol.269 , pp. 29182-29189
    • Kofod, L.V.1    Kauppinen, S.2    Christgau, S.3    Andersen, L.N.4    Heldt-Hansen, H.P.5    Dörreich, K.6    Dalboge, H.7
  • 96
    • 0030897340 scopus 로고    scopus 로고
    • Calreticulin
    • Krause, K.-H. and Michalak, M. 1997. Calreticulin. Cell 88: 439-443.
    • (1997) Cell , vol.88 , pp. 439-443
    • Krause, K.-H.1    Michalak, M.2
  • 97
    • 0025728711 scopus 로고
    • Mannosyl-phospho-dolichol synthase from Trichoderma reesei is activated by protein kinase dependent phosphorylation in vitro
    • Kruszewska, J., Palamarczyk, G., and Kubicek, C. P. 1991. Mannosyl-phospho-dolichol synthase from Trichoderma reesei is activated by protein kinase dependent phosphorylation in vitro. FEMS Microbiol. Lett. 80: 81-85.
    • (1991) FEMS Microbiol. Lett. , vol.80 , pp. 81-85
    • Kruszewska, J.1    Palamarczyk, G.2    Kubicek, C.P.3
  • 99
    • 14444280363 scopus 로고    scopus 로고
    • Multiple molecular chaperones complex with misfolded large oligomeric glycoproteins in the endoplasmic reticulum
    • Kuznetsov, G., Chen, L. B., and Nigam, S. K. 1997. Multiple molecular chaperones complex with misfolded large oligomeric glycoproteins in the endoplasmic reticulum. J. Biol. Chem. 272: 3057-3063.
    • (1997) J. Biol. Chem. , vol.272 , pp. 3057-3063
    • Kuznetsov, G.1    Chen, L.B.2    Nigam, S.K.3
  • 100
    • 0028882680 scopus 로고
    • Efficient expression and secretion of Aspergillus niger polygalacturonase in Saccharomyces cerevisiae
    • Lang, C. and Looman, A. C. 1995. Efficient expression and secretion of Aspergillus niger polygalacturonase in Saccharomyces cerevisiae. Appl. Microbiol. Biotechnol. 44: 147-156.
    • (1995) Appl. Microbiol. Biotechnol. , vol.44 , pp. 147-156
    • Lang, C.1    Looman, A.C.2
  • 101
    • 0028850651 scopus 로고
    • Expression in Aspergillus niger of the starch-binding domain of glucoamylase - Comparison with the proteolytically produced starch-binding domain
    • Le Gal-Coëffet, M. F., Jacks, A. J., Sorimachi, K., Williamson, M. P., Williamson, G., and Archer, D. B. 1995. Expression in Aspergillus niger of the starch-binding domain of glucoamylase - comparison with the proteolytically produced starch-binding domain. Eur. J. Biochem. 233: 561-567.
    • (1995) Eur. J. Biochem. , vol.233 , pp. 561-567
    • Le Gal-Coëffet, M.F.1    Jacks, A.J.2    Sorimachi, K.3    Williamson, M.P.4    Williamson, G.5    Archer, D.B.6
  • 102
    • 8044239621 scopus 로고    scopus 로고
    • Cloning, characterization and overexpression of a gene (pdiA) encoding protein disulfide isomerase of Aspergillus oryzae
    • Lee, B. R., Yamada, O., Kitamoto, K., and Takahashi, K. 1996. Cloning, characterization and overexpression of a gene (pdiA) encoding protein disulfide isomerase of Aspergillus oryzae. J. Ferment. Bioeng. 82: 538-543.
    • (1996) J. Ferment. Bioeng. , vol.82 , pp. 538-543
    • Lee, B.R.1    Yamada, O.2    Kitamoto, K.3    Takahashi, K.4
  • 103
    • 0002900153 scopus 로고
    • Fungal enzymes
    • Arora, D. K., Elander, R. P. and Mukerji, K. G. (Eds.), Marcel Dekker Inc., New York
    • Lowe, D. A. 1992. Fungal enzymes. In: Handbook of Applied Mycology. Fungal Biotechnology. Arora, D. K., Elander, R. P. and Mukerji, K. G. (Eds.), pp. 681-706, Marcel Dekker Inc., New York.
    • (1992) Handbook of Applied Mycology. Fungal Biotechnology , pp. 681-706
    • Lowe, D.A.1
  • 104
    • 0029986859 scopus 로고    scopus 로고
    • Identification, cloning and analysis of the Aspergillus niger gene pacC, a wide domain regulatory gene responsive to ambient pH
    • MacCabe, A. P., van den Hombergh, J. P. T. W., Tilburn, J., Arst, H. N., and Visser, J. 1996. Identification, cloning and analysis of the Aspergillus niger gene pacC, a wide domain regulatory gene responsive to ambient pH. Mol. Gen. Genet. 250: 367-374.
    • (1996) Mol. Gen. Genet. , vol.250 , pp. 367-374
    • MacCabe, A.P.1    Van Den Hombergh, J.P.T.W.2    Tilburn, J.3    Arst, H.N.4    Visser, J.5
  • 105
    • 0029832663 scopus 로고    scopus 로고
    • Carbon catabolite repression of xylanase I (xyn1) gene expression in Trichoderma reesei
    • Mach, R. L., Strauss, J., Zeilinger, S., Schindler, M., and Kubicek, C. P. 1996. Carbon catabolite repression of xylanase I (xyn1) gene expression in Trichoderma reesei. Mol. Microblol. 21: 1273-1281.
    • (1996) Mol. Microblol. , vol.21 , pp. 1273-1281
    • Mach, R.L.1    Strauss, J.2    Zeilinger, S.3    Schindler, M.4    Kubicek, C.P.5
  • 106
    • 0027454511 scopus 로고
    • Regulation of secreted protein production by filamentous fungi: Recent developments and perspectives
    • MacKenzie, D. A., Jeenes, D. J., Belshaw, N. J., and Archer, D. B. 1993. Regulation of secreted protein production by filamentous fungi: recent developments and perspectives. J. Gen. Microbiol. 139: 2295-2307.
    • (1993) J. Gen. Microbiol. , vol.139 , pp. 2295-2307
    • MacKenzie, D.A.1    Jeenes, D.J.2    Belshaw, N.J.3    Archer, D.B.4
  • 107
    • 0029919805 scopus 로고    scopus 로고
    • Cloning of cDNA for the protein disulfide isomerase from Aspergillus niger strain NNRL3 using PCR
    • Malpricht, S., Thamm, A., and Khanh, N. Q. 1996. Cloning of cDNA for the protein disulfide isomerase from Aspergillus niger strain NNRL3 using PCR. Biotechnol. Lett. 18: 445-450.
    • (1996) Biotechnol. Lett. , vol.18 , pp. 445-450
    • Malpricht, S.1    Thamm, A.2    Khanh, N.Q.3
  • 109
    • 0030957795 scopus 로고    scopus 로고
    • Structural characterization of N-linked oligosaccharides from cellobiohydrolase I secreted by the filamentous fungus Trichoderma reesei RUTC30
    • in press
    • Maras, M., de Bruyn, A., Schraml, J., Herdewijn, P., Claeyssens, M., Fiers, W., and Contreras, R. 1997. Structural characterization of N-linked oligosaccharides from cellobiohydrolase I secreted by the filamentous fungus Trichoderma reesei RUTC30. Eur. J. Biochem. in press.
    • (1997) Eur. J. Biochem.
    • Maras, M.1    De Bruyn, A.2    Schraml, J.3    Herdewijn, P.4    Claeyssens, M.5    Fiers, W.6    Contreras, R.7
  • 111
    • 0026503134 scopus 로고
    • The Golgi complex: In vitro veritas?
    • Mellman, I. and Simons, K. 1992. The Golgi complex: in vitro veritas? Cell 68: 829-840.
    • (1992) Cell , vol.68 , pp. 829-840
    • Mellman, I.1    Simons, K.2
  • 112
    • 0028170231 scopus 로고
    • Sequential interaction of the chaperones BiP and GRP94 with immunoglobulin chains in the endoplasmic reticulum
    • Melnick, J., Dul, J. L., and Argon, Y. 1994. Sequential interaction of the chaperones BiP and GRP94 with immunoglobulin chains in the endoplasmic reticulum. Nature 370: 373-375.
    • (1994) Nature , vol.370 , pp. 373-375
    • Melnick, J.1    Dul, J.L.2    Argon, Y.3
  • 113
    • 0029443088 scopus 로고
    • Characteristic expression of three amylase-encoding genes, agdA, amyB, and glaA in Aspergillus oryzae transformants containing multiple copies of the agdA gene
    • Minetoki, T., Gomi, K., Kitamoto, K., Kumagai, C., and Tamura, G. 1995. Characteristic expression of three amylase-encoding genes, agdA, amyB, and glaA in Aspergillus oryzae transformants containing multiple copies of the agdA gene. Biosci. Biotechnol. Biochem. 59: 2251-2254.
    • (1995) Biosci. Biotechnol. Biochem. , vol.59 , pp. 2251-2254
    • Minetoki, T.1    Gomi, K.2    Kitamoto, K.3    Kumagai, C.4    Tamura, G.5
  • 114
    • 0029803609 scopus 로고    scopus 로고
    • Deletion analysis of promoter elements of the Aspergillus oryzae agdA gene encoding α-glucosidase
    • Minetoki, T., Nunokawa, Y., Gomi, K., Kitamoto, K., Kumagai, C., and Tamura, G. 1996. Deletion analysis of promoter elements of the Aspergillus oryzae agdA gene encoding α-glucosidase. Curr. Genet. 30: 432-438.
    • (1996) Curr. Genet. , vol.30 , pp. 432-438
    • Minetoki, T.1    Nunokawa, Y.2    Gomi, K.3    Kitamoto, K.4    Kumagai, C.5    Tamura, G.6
  • 115
    • 0345940649 scopus 로고
    • Selective screening methods for the isolation of high yielding cellulase mutants of Trichoderma reesei
    • Brown, R. D. and Jurasec, L. (Eds.), Academic Press, San Diego
    • Montenecourt, B. S. and Eveleigh, D. E. 1979. Selective screening methods for the isolation of high yielding cellulase mutants of Trichoderma reesei. In: Hydrolysis of Cellulose: Mechanisms of Enzymatic and Acid Catalysis. Advances in Chemistry Series, Brown, R. D. and Jurasec, L. (Eds.), Vol. 181. pp. 289-301, Academic Press, San Diego.
    • (1979) Hydrolysis of Cellulose: Mechanisms of Enzymatic and Acid Catalysis. Advances in Chemistry Series , vol.181 , pp. 289-301
    • Montenecourt, B.S.1    Eveleigh, D.E.2
  • 116
    • 0027464787 scopus 로고
    • Aspergillus nidulans nuclear proteins bind to a CCAAT element and the adjacent upstream sequence in the promoter region of the starch-inducible Taka-amylase A gene
    • Nagata, O., Takashima, T., Tanaka, M., and Tsukagoshi, N. 1993. Aspergillus nidulans nuclear proteins bind to a CCAAT element and the adjacent upstream sequence in the promoter region of the starch-inducible Taka-amylase A gene. Mol. Gen. Genet. 237: 251-260.
    • (1993) Mol. Gen. Genet. , vol.237 , pp. 251-260
    • Nagata, O.1    Takashima, T.2    Tanaka, M.3    Tsukagoshi, N.4
  • 117
    • 0027765788 scopus 로고
    • Isolation of Trichoderma reesei genes highly expressed on glucose-containing media. Characterization of the tef1 gene encoding translation elongation factor 1-alpha
    • Nakari, T., Alataro, E., and Penttilä, M. 1993. Isolation of Trichoderma reesei genes highly expressed on glucose-containing media. Characterization of the tef1 gene encoding translation elongation factor 1-alpha. Gene 136: 313-318.
    • (1993) Gene , vol.136 , pp. 313-318
    • Nakari, T.1    Alataro, E.2    Penttilä, M.3
  • 118
    • 0028787878 scopus 로고
    • Production of Trichoderma reesei cellulases on glucose-containing media
    • Nakari-Setälä, T. and Penttilä, M. 1995. Production of Trichoderma reesei cellulases on glucose-containing media. Appl. Environ. Microbiol. 61: 3650-3655.
    • (1995) Appl. Environ. Microbiol. , vol.61 , pp. 3650-3655
    • Nakari-Setälä, T.1    Penttilä, M.2
  • 119
    • 0031048459 scopus 로고    scopus 로고
    • Isolation and characterisation of a gene encoding protein disulfide isomerase, pdiA, from Aspergillus niger
    • Ngiam, C., Jeenes, D. J., and Archer, D. B. 1997. Isolation and characterisation of a gene encoding protein disulfide isomerase, pdiA, from Aspergillus niger. Curr. Genet. 31: 133-138.
    • (1997) Curr. Genet. , vol.31 , pp. 133-138
    • Ngiam, C.1    Jeenes, D.J.2    Archer, D.B.3
  • 120
    • 0025970971 scopus 로고
    • Binding protein BiP is required for translocation of secretory proteins into the endoplasmic reticulum in Saccharomyces cerevisiae
    • Nguyen, T. H., Law, D. T., and Williams, D. B. 1991. Binding protein BiP is required for translocation of secretory proteins into the endoplasmic reticulum in Saccharomyces cerevisiae. Proc. Natl. Acad. Sci. U.S.A. 88: 1565-1569.
    • (1991) Proc. Natl. Acad. Sci. U.S.A. , vol.88 , pp. 1565-1569
    • Nguyen, T.H.1    Law, D.T.2    Williams, D.B.3
  • 121
  • 122
    • 0029059322 scopus 로고
    • Multiple roles of the cellulase CBHI in enhancing production of fusion antibodies by the filamentous fungus Trichoderma reesei
    • Nyyssönen, E. and Keränen, S. 1995. Multiple roles of the cellulase CBHI in enhancing production of fusion antibodies by the filamentous fungus Trichoderma reesei. Curr. Genet. 28: 71-79.
    • (1995) Curr. Genet. , vol.28 , pp. 71-79
    • Nyyssönen, E.1    Keränen, S.2
  • 124
    • 0029148258 scopus 로고
    • Activation of the Aspergillus PacC transcription factor in response to alkaline ambient pH requires proteolysis of the carboxy-terminal moiety
    • Orejas, M., Espeso, E. A., Tilburn, J., Sarkar, S., Arst, H. N., and Peñalva, M. A. 1995. Activation of the Aspergillus PacC transcription factor in response to alkaline ambient pH requires proteolysis of the carboxy-terminal moiety. Genes Dev. 9: 1622-1632.
    • (1995) Genes Dev. , vol.9 , pp. 1622-1632
    • Orejas, M.1    Espeso, E.A.2    Tilburn, J.3    Sarkar, S.4    Arst, H.N.5    Peñalva, M.A.6
  • 126
    • 0029006125 scopus 로고
    • + in Schizosaccharomyces pombe, is an essential gene which can be complemented by its soluble ER domain
    • + in Schizosaccharomyces pombe, is an essential gene which can be complemented by its soluble ER domain. EMBO J. 14: 3064-3072.
    • (1995) EMBO J. , vol.14 , pp. 3064-3072
    • Parlati, F.1    Dignard, D.2    Bergeron, J.J.M.3    Thomas, D.Y.4
  • 127
    • 0028881645 scopus 로고
    • Saccharomyces cerevisiae CNE1 encodes an endoplasmic reticulum (ER) membrane protein with sequence similarity to calnexin and calreticulin and functions as a constituent of the ER quality control apparatus
    • Parlati, F., Dominguez, M., Bergeron, J. J. M., and Thomas, D. Y. 1995b. Saccharomyces cerevisiae CNE1 encodes an endoplasmic reticulum (ER) membrane protein with sequence similarity to calnexin and calreticulin and functions as a constituent of the ER quality control apparatus. J. Biol. Chem. 270: 244-253.
    • (1995) J. Biol. Chem. , vol.270 , pp. 244-253
    • Parlati, F.1    Dominguez, M.2    Bergeron, J.J.M.3    Thomas, D.Y.4
  • 128
    • 0029890518 scopus 로고    scopus 로고
    • Molecular cloning and expression in Saccharomyces cerevisiae of two Aspergillus nidulans xylanase genes
    • Pérez-González, J. A., de Graaff, L. H., Visser, J., and Ramón, D. 1996. Molecular cloning and expression in Saccharomyces cerevisiae of two Aspergillus nidulans xylanase genes. Appl. Environ. Microbiol. 62: 2179-2182.
    • (1996) Appl. Environ. Microbiol. , vol.62 , pp. 2179-2182
    • Pérez-González, J.A.1    De Graaff, L.H.2    Visser, J.3    Ramón, D.4
  • 129
    • 0029777488 scopus 로고    scopus 로고
    • Dissection of the ability of the chicken lysozyme gene 5′ matrix attachment region to stimulate transgene expression and to dampen position effects
    • Phi-Van, L. and Sträfling, W. H. 1996. Dissection of the ability of the chicken lysozyme gene 5′ matrix attachment region to stimulate transgene expression and to dampen position effects. Biochemistry 35: 10735-10742.
    • (1996) Biochemistry , vol.35 , pp. 10735-10742
    • Phi-Van, L.1    Sträfling, W.H.2
  • 130
    • 0028232167 scopus 로고
    • Participation of the ER chaperone calnexin (p88, IP90) in the biogenesis of CFTR
    • Pind, S., Riordan, J., and Williams, D. B. 1994. Participation of the ER chaperone calnexin (p88, IP90) in the biogenesis of CFTR. J. Biol. Chem. 269: 12784-12788.
    • (1994) J. Biol. Chem. , vol.269 , pp. 12784-12788
    • Pind, S.1    Riordan, J.2    Williams, D.B.3
  • 132
    • 0025773920 scopus 로고
    • Protein targeting in yeast
    • Reid, G. A. 1991. Protein targeting in yeast. J. Gen. Microbiol. 137 (1991): 1765-1773.
    • (1991) J. Gen. Microbiol. , vol.137 , Issue.1991 , pp. 1765-1773
    • Reid, G.A.1
  • 133
    • 0026476276 scopus 로고
    • Heterologous gene expression in Aspergillus niger: A glucoamylase-porcine pancreatic prophospholipase A2 fusion protein is secreted and processed to yield mature enzyme
    • Roberts, I. N., Jeenes, D. J., MacKenzie, D. A., Wilkinson, A. P., Sumner, I. G., and Archer, D. B. 1992. Heterologous gene expression in Aspergillus niger: a glucoamylase-porcine pancreatic prophospholipase A2 fusion protein is secreted and processed to yield mature enzyme. Gene 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    Sumner, I.G.5    Archer, D.B.6
  • 134
    • 0028219869 scopus 로고
    • Protein disulfide isomerase overexpression increases secretion of foreign proteins in Saccharomyces cerevisiae
    • Robinson, A. S., Hines, V., and Wittrup, K. D. 1994. Protein disulfide isomerase overexpression increases secretion of foreign proteins in Saccharomyces cerevisiae. Bio/Technology 12: 381-384.
    • (1994) Bio/Technology , vol.12 , pp. 381-384
    • Robinson, A.S.1    Hines, V.2    Wittrup, K.D.3
  • 135
    • 0029944822 scopus 로고    scopus 로고
    • Reduction of BiP levels decreases heterologous protein secretion in Saccharomyces cerevisiae
    • Robinson, A. S., Bockhaus, J. A., Voegler, A. C., and Wittrup, K. D. 1996. Reduction of BiP levels decreases heterologous protein secretion in Saccharomyces cerevisiae. J. Biol. Chem. 271: 10017-10022.
    • (1996) J. Biol. Chem. , vol.271 , pp. 10017-10022
    • Robinson, A.S.1    Bockhaus, J.A.2    Voegler, A.C.3    Wittrup, K.D.4
  • 136
    • 0028835605 scopus 로고
    • Glucose repression in fungi
    • Ronne, H. 1995. Glucose repression in fungi. Trends Genet. 11: 12-17.
    • (1995) Trends Genet. , vol.11 , pp. 12-17
    • Ronne, H.1
  • 137
    • 0025267839 scopus 로고
    • Yeast alpha2 repressor positions nucleosomes in TRP1/ ARS1 chromatin
    • Roth, S. Y., Dean, A., and Simpson, R. T. 1990. Yeast alpha2 repressor positions nucleosomes in TRP1/ ARS1 chromatin. Mol. Cell. Biol. 10: 2247-2260.
    • (1990) Mol. Cell. Biol. , vol.10 , pp. 2247-2260
    • Roth, S.Y.1    Dean, A.2    Simpson, R.T.3
  • 138
    • 0026555196 scopus 로고
    • Molecular dissection of the secretory pathway
    • Rothman, J. E. and Orci, L. 1992. Molecular dissection of the secretory pathway. Nature 355: 409-415.
    • (1992) Nature , vol.355 , pp. 409-415
    • Rothman, J.E.1    Orci, L.2
  • 139
    • 0043156740 scopus 로고
    • Strain improvement and strain stability
    • Finkelstein, D. B. and Ball, C. (Eds.), Butterworth-Heinemann, Boston
    • Rowlands, R. T. 1992. Strain improvement and strain stability. In: Biotechnology of Filamentous Fungi. Finkelstein, D. B. and Ball, C. (Eds.), pp. 41-64, Butterworth-Heinemann, Boston.
    • (1992) Biotechnology of Filamentous Fungi , pp. 41-64
    • Rowlands, R.T.1
  • 141
    • 0028070754 scopus 로고
    • Effects of CaBP2, the rat analogue of ERp72, and of CaBP1 on the refolding of denatured reduced proteins: Comparison with protein disulfide isomerase
    • Rupp, K., Birnbach, U., Lundström, J., Van, P. N., and Soling, H. D. 1994. Effects of CaBP2, the rat analogue of ERp72, and of CaBP1 on the refolding of denatured reduced proteins: comparison with protein disulfide isomerase. J. Biol. Chem. 269: 2501-2507.
    • (1994) J. Biol. Chem. , vol.269 , pp. 2501-2507
    • Rupp, K.1    Birnbach, U.2    Lundström, J.3    Van, P.N.4    Soling, H.D.5
  • 142
    • 0027134879 scopus 로고
    • Cloning, sequencing and enhanced expression of the Trichoderma reesei endoxylanase II (pI 9) gene xln2
    • Saarelainen, R., Paloheimo, M., Fagerström, R., Suominen, P. L., and Nevalainen, K. M. H. 1993. Cloning, sequencing and enhanced expression of the Trichoderma reesei endoxylanase II (pI 9) gene xln2. Mol. Gen. Genet. 241: 497-503.
    • (1993) Mol. Gen. Genet. , vol.241 , pp. 497-503
    • Saarelainen, R.1    Paloheimo, M.2    Fagerström, R.3    Suominen, P.L.4    Nevalainen, K.M.H.5
  • 143
    • 0002029691 scopus 로고
    • Fungal enzymes used in oriental food and beverage industries
    • Kinghorn, J. R. and Turner, G. (Eds.), Blackie, London
    • Sakaguchi, K., Takagi, M., Horiuchi, H., and Gomi, K. 1992. Fungal enzymes used in oriental food and beverage industries. In: Applied Molecular Genetics of Filamentous Fungi, Kinghorn, J. R. and Turner, G. (Eds.), pp. 54-99, Blackie, London.
    • (1992) Applied Molecular Genetics of Filamentous Fungi , pp. 54-99
    • Sakaguchi, K.1    Takagi, M.2    Horiuchi, H.3    Gomi, K.4
  • 144
    • 0028361655 scopus 로고
    • A novel, small endoglucanase gene, egl5, from Trichoderma reesei isolated by expression in yeast
    • Saloheimo, A., Henrissat, B., Hoffren, A.-M., Teleman, O., and Penttilä, M. 1994. A novel, small endoglucanase gene, egl5, from Trichoderma reesei isolated by expression in yeast Mol. Microbiol. 13: 219-228.
    • (1994) Mol. Microbiol. , vol.13 , pp. 219-228
    • Saloheimo, A.1    Henrissat, B.2    Hoffren, A.-M.3    Teleman, O.4    Penttilä, M.5
  • 145
    • 0030669760 scopus 로고    scopus 로고
    • A new Trichoderma reesei cellulase: CDNA cloning and demonstration of endoglucanase activity by yeast expression
    • in press
    • Saloheimo, A., Nakari-Setälä, Tenkanen, M., and Penttilä, M. 1997. A new Trichoderma reesei cellulase: cDNA cloning and demonstration of endoglucanase activity by yeast expression. Eur. J. Biochem. in press.
    • (1997) Eur. J. Biochem.
    • Saloheimo, A.1    Nakari-Setälä2    Tenkanen, M.3    Penttilä, M.4
  • 146
    • 0029929068 scopus 로고    scopus 로고
    • Chaperone-like effect during in vitro refolding of insulin-like growth factor I using a solubilising fusion partner
    • Samuelsson, E. and Uhlen, M. 1996. Chaperone-like effect during in vitro refolding of insulin-like growth factor I using a solubilising fusion partner. Ann. N.Y. Acad. Sci. 782: 486-494.
    • (1996) Ann. N.Y. Acad. Sci. , vol.782 , pp. 486-494
    • Samuelsson, E.1    Uhlen, M.2
  • 147
    • 0026444222 scopus 로고
    • Control of gene expression in the catabolic pathways of Aspergillus nidulans: A personal and biased account
    • Scazzocchio, C. 1992. Control of gene expression in the catabolic pathways of Aspergillus nidulans: a personal and biased account. Bio/Technology 23: 43-68.
    • (1992) Bio/Technology , vol.23 , pp. 43-68
    • Scazzocchio, C.1
  • 149
    • 0029979607 scopus 로고    scopus 로고
    • Common principles of protein translocation across membranes
    • Schatz, G. and Dobberstein, B. 1996. Common principles of protein translocation across membranes. Science 271: 1519-1526.
    • (1996) Science , vol.271 , pp. 1519-1526
    • Schatz, G.1    Dobberstein, B.2
  • 150
    • 0029379684 scopus 로고
    • Filament-specific expression of a cellulase gene in the dimorphic fungus Ustilago maydis
    • Schauwecker, F., Wanner, G., and Kahmann, R. 1995. Filament-specific expression of a cellulase gene in the dimorphic fungus Ustilago maydis. Biol. Chem. Hoppe Seyler 376: 617-625.
    • (1995) Biol. Chem. Hoppe Seyler , vol.376 , pp. 617-625
    • Schauwecker, F.1    Wanner, G.2    Kahmann, R.3
  • 151
    • 0029758174 scopus 로고    scopus 로고
    • Scaffold/matrix-attached regions act upon transcription in a context-dependent manner
    • Schübeler, D., Mielke, C., Maass, K., and Bode, J. 1996. Scaffold/matrix-attached regions act upon transcription in a context-dependent manner. Biochemistry 35: 11160-11169.
    • (1996) Biochemistry , vol.35 , pp. 11160-11169
    • Schübeler, D.1    Mielke, C.2    Maass, K.3    Bode, J.4
  • 152
    • 0030886130 scopus 로고    scopus 로고
    • Role of four major cellulases in triggering of cellulase gene expression in Trichoderma reesei
    • Seiboth, B., Hakola, S., Mach, R. L., Suominen, P. L., and Kubicek, C. P. 1997. Role of four major cellulases in triggering of cellulase gene expression in Trichoderma reesei. J. Bacteriol. 179: 5318-5320.
    • (1997) J. Bacteriol. , vol.179 , pp. 5318-5320
    • Seiboth, B.1    Hakola, S.2    Mach, R.L.3    Suominen, P.L.4    Kubicek, C.P.5
  • 153
    • 0028285305 scopus 로고
    • The role of the carrier protein and disulfide formation in the folding of beta-lactamase fusion proteins in the endoplasmic reticulum of yeast
    • Simonen, M., Jamsa, E., and Makarow, M. 1994. The role of the carrier protein and disulfide formation in the folding of beta-lactamase fusion proteins in the endoplasmic reticulum of yeast. J. Biol. Chem. 269: 13887-13892.
    • (1994) J. Biol. Chem. , vol.269 , pp. 13887-13892
    • Simonen, M.1    Jamsa, E.2    Makarow, M.3
  • 154
    • 0027498957 scopus 로고
    • Characterization of the Trichoderma reesei cbh2 promoter
    • Stangl, H., Gruber, F., and Kubicek, C. P. 1993. Characterization of the Trichoderma reesei cbh2 promoter. Curr. Genet. 23: 115-122.
    • (1993) Curr. Genet. , vol.23 , pp. 115-122
    • Stangl, H.1    Gruber, F.2    Kubicek, C.P.3
  • 155
    • 0027972417 scopus 로고
    • Sequence and promoter analysis of the highly expressed TEF gene of the filamentous fungus Ashbya gossypii
    • Steiner, S. and Philippsen, P. 1994. Sequence and promoter analysis of the highly expressed TEF gene of the filamentous fungus Ashbya gossypii. Mol. Gen. Genet. 242: 263-271.
    • (1994) Mol. Gen. Genet. , vol.242 , pp. 263-271
    • Steiner, S.1    Philippsen, P.2
  • 157
    • 0029947259 scopus 로고    scopus 로고
    • Characterization of a Penicillium chrysogenum gene encoding a PacC transcription factor and its binding sites in the divergent pcbAB-pcbC promoter of the penicillin biosynthetic cluster
    • Suarez, T. and Peñalva, M. A. 1996. Characterization of a Penicillium chrysogenum gene encoding a PacC transcription factor and its binding sites in the divergent pcbAB-pcbC promoter of the penicillin biosynthetic cluster. Mol. Microbiol. 20: 529-540.
    • (1996) Mol. Microbiol. , vol.20 , pp. 529-540
    • Suarez, T.1    Peñalva, M.A.2
  • 159
    • 0027131591 scopus 로고
    • High-frequency one-step gene replacement in Trichoderma reesei. II. Effects of deletions of individual cellulase genes
    • Suominen, P. L., Mäntylä, A. L., Karhunen, T., Hakola, S., and Nevalainen, H. 1993. High-frequency one-step gene replacement in Trichoderma reesei. II. Effects of deletions of individual cellulase genes. Mol. Gen. Genet. 241: 523-530.
    • (1993) Mol. Gen. Genet. , vol.241 , pp. 523-530
    • Suominen, P.L.1    Mäntylä, A.L.2    Karhunen, T.3    Hakola, S.4    Nevalainen, H.5
  • 160
    • 0029678817 scopus 로고    scopus 로고
    • Cloning of a gene encoding a putative carbon catabolite repressor from Trichoderma reesei
    • Takashima, S., Nakamura, A., Iikura, H., Masaki, H., and Uozuma, T. 1996. Cloning of a gene encoding a putative carbon catabolite repressor from Trichoderma reesei. Biosc. Biotech. Biochem. 60: 173-176.
    • (1996) Biosc. Biotech. Biochem. , vol.60 , pp. 173-176
    • Takashima, S.1    Nakamura, A.2    Iikura, H.3    Masaki, H.4    Uozuma, T.5
  • 161
    • 0026446652 scopus 로고
    • Novel N-linked oligomannose type oligosaccharides containing an α-D-galactofuranosyl linkage found in α-D-galactosidase from Aspergillus niger
    • Takayanagi, T., Kushida, K., Idonuma, K., and Ajisaka, K. 1992. Novel N-linked oligomannose type oligosaccharides containing an α-D-galactofuranosyl linkage found in α-D-galactosidase from Aspergillus niger. Glycoconj. J. 9: 229-234.
    • (1992) Glycoconj. J. , vol.9 , pp. 229-234
    • Takayanagi, T.1    Kushida, K.2    Idonuma, K.3    Ajisaka, K.4
  • 162
    • 0028393188 scopus 로고
    • Novel structures of N-linked high mannose type oligosaccharides containing a-D-galactofuranosyl linkages in Aspergillus niger a-D-glucosidase
    • Takayanagi, T., Kimura, A., Chiba, S., and Ajisaka, K. 1994. Novel structures of N-linked high mannose type oligosaccharides containing a-D-galactofuranosyl linkages in Aspergillus niger a-D-glucosidase. Carbohyd. Res. 256: 149-158.
    • (1994) Carbohyd. Res. , vol.256 , pp. 149-158
    • Takayanagi, T.1    Kimura, A.2    Chiba, S.3    Ajisaka, K.4
  • 163
    • 0031045007 scopus 로고    scopus 로고
    • Interactions between newly synthesized glycoproteins, calnexin and a network of resident chaperones in the endoplasmic reticulum
    • Tatu, U. and Helenius, A. 1997. Interactions between newly synthesized glycoproteins, calnexin and a network of resident chaperones in the endoplasmic reticulum. J. Cell Biol. 136: 555-565.
    • (1997) J. Cell Biol. , vol.136 , pp. 555-565
    • Tatu, U.1    Helenius, A.2
  • 164
    • 0029558440 scopus 로고
    • Nucleotide sequence of the Aspergillus niger srpA gene
    • Thompson, S. A., Golightly, E. J., and Yaver, D. S. 1995. Nucleotide sequence of the Aspergillus niger srpA gene. Gene 167: 337-338.
    • (1995) Gene , vol.167 , pp. 337-338
    • Thompson, S.A.1    Golightly, E.J.2    Yaver, D.S.3
  • 165
    • 0029124761 scopus 로고
    • Cloning and characterization of the gene encoding translation elongation factor 1-alpha from Aureobasidium pullulans
    • Thornewell, S. J., Peery, R. B., and Skatrud, P. L. 1995. Cloning and characterization of the gene encoding translation elongation factor 1-alpha from Aureobasidium pullulans. Gene 162: 105-110.
    • (1995) Gene , vol.162 , pp. 105-110
    • Thornewell, S.J.1    Peery, R.B.2    Skatrud, P.L.3
  • 166
    • 0028913388 scopus 로고
    • The Aspergillus PacC zinc finger transcription factor mediates regulation of both acid- and alkaline-expressed genes by ambient pH
    • Tilburn, J., Sarkar, S., Widdick, D. A., Espeso, E. A., Orejas, M., Mungroo, J., Peñalva, M. A., and Arst, H. N. 1995. The Aspergillus PacC zinc finger transcription factor mediates regulation of both acid- and alkaline-expressed genes by ambient pH. EMBO J. 14: 779-790.
    • (1995) EMBO J. , vol.14 , pp. 779-790
    • Tilburn, J.1    Sarkar, S.2    Widdick, D.A.3    Espeso, E.A.4    Orejas, M.5    Mungroo, J.6    Peñalva, M.A.7    Arst, H.N.8
  • 167
    • 0028970369 scopus 로고
    • Repression by SSN6-TUP1 is directed by MIG1, a repressor/ activator protein
    • Treitel, M. A. and Carlson, M. 1995. Repression by SSN6-TUP1 is directed by MIG1, a repressor/ activator protein. Proc. Natl. Acad. Sci. U.S.A. 92: 3132-3136.
    • (1995) Proc. Natl. Acad. Sci. U.S.A. , vol.92 , pp. 3132-3136
    • Treitel, M.A.1    Carlson, M.2
  • 168
    • 0026948186 scopus 로고
    • Deletion analysis of the Taka-amylaseA gene promoter using a homologous transformation system in Aspergillus oryzae
    • Tsuchiya, K., Tada, S., Gomi, K., Kitamoto, K., Kumagai, C., and Tamura, G. 1992. Deletion analysis of the Taka-amylaseA gene promoter using a homologous transformation system in Aspergillus oryzae. Biosc. Biotech. Biochem. 56: 1849-1853.
    • (1992) Biosc. Biotech. Biochem. , vol.56 , pp. 1849-1853
    • Tsuchiya, K.1    Tada, S.2    Gomi, K.3    Kitamoto, K.4    Kumagai, C.5    Tamura, G.6
  • 170
    • 0002858205 scopus 로고
    • Gene organization in industrial filamentous fungi
    • Kinghorn, J. R. and Turner, G. (Eds.), Blackie Academic and Professional, Glasgow
    • Unkles, S. E. 1992. Gene organization in industrial filamentous fungi. In: Applied Molecular Genetics of Filamentous Fungi. Kinghorn, J. R. and Turner, G. (Eds.), pp.28-53, Blackie Academic and Professional, Glasgow.
    • (1992) Applied Molecular Genetics of Filamentous Fungi , pp. 28-53
    • Unkles, S.E.1
  • 172
    • 0028574789 scopus 로고
    • Cloning, characterization and expression of pepF, a gene encoding a serine carboxypeptidase from Aspergillus niger
    • van den Hombergh, J. P. T. W., Jarai, G., Buxton, F. P., and Visser, J. 1994. Cloning, characterization and expression of pepF, a gene encoding a serine carboxypeptidase from Aspergillus niger. Gene 151: 73-79.
    • (1994) Gene , vol.151 , pp. 73-79
    • Van Den Hombergh, J.P.T.W.1    Jarai, G.2    Buxton, F.P.3    Visser, J.4
  • 173
    • 0029100574 scopus 로고
    • New protease mutants in Aspergillus niger result in strongly reduced in vitro degradation of target proteins: Genetical and biochemical characterization of seven complementation groups
    • van den Hombergh, J. P. T. W., van de Vondervoort, P. J. I., van der Heijden, N. C. B. A., and Visser, J. 1995. New protease mutants in Aspergillus niger result in strongly reduced in vitro degradation of target proteins: genetical and biochemical characterization of seven complementation groups. Curr. Genet. 28: 299-308.
    • (1995) Curr. Genet. , vol.28 , pp. 299-308
    • Van Den Hombergh, J.P.T.W.1    Van De Vondervoort, P.J.I.2    Van Der Heijden, N.C.B.A.3    Visser, J.4
  • 176
    • 0030750269 scopus 로고    scopus 로고
    • Disruption of three acid proteases in Aspergillus niger - Effects on protease spectrum, intracellular proteolysis, and degradation of target proteins
    • van den Hombergh, J. P. T. W., Gelpke, M. D. S., van de Vondervoort, P. J. I., Buxton, F. P., and Visser, J. 1997b. Disruption of three acid proteases in Aspergillus niger - effects on protease spectrum, intracellular proteolysis, and degradation of target proteins. Eur. J. Biochem. 247: 605-613.
    • (1997) Eur. J. Biochem. , vol.247 , pp. 605-613
    • Van Den Hombergh, J.P.T.W.1    Gelpke, M.D.S.2    Van De Vondervoort, P.J.I.3    Buxton, F.P.4    Visser, J.5
  • 177
    • 0001852858 scopus 로고
    • Heterologous gene expression in filamentous fungi
    • Bennett, J. W. and Lasure, L. L. (Eds.), Academic Press, San Diego
    • van den Hondel, C. A. M. J. J., Punt, P. J., and van Gorcom, R. F. M. 1991. Heterologous gene expression in filamentous fungi. In: More Genetic Manipulation of Filamentous Fungi. Bennett, J. W. and Lasure, L. L. (Eds.), pp. 396-428, Academic Press, San Diego.
    • (1991) More Genetic Manipulation of Filamentous Fungi , pp. 396-428
    • Van Den Hondel, C.A.M.J.J.1    Punt, P.J.2    Van Gorcom, R.F.M.3
  • 178
    • 0028598691 scopus 로고
    • Extracellular arabinases in Aspergillus nidulans: The effect of different cre mutations on enzyme levels
    • van der Veen, P., Arst, H. N., Flipphi, M. J. A., and Visser, J. 1994. Extracellular arabinases in Aspergillus nidulans: the effect of different cre mutations on enzyme levels. Arch. Microbiol. 162: 433-440.
    • (1994) Arch. Microbiol. , vol.162 , pp. 433-440
    • Van Der Veen, P.1    Arst, H.N.2    Flipphi, M.J.A.3    Visser, J.4
  • 179
    • 0028853676 scopus 로고
    • An extreme creA mutation in Aspergillus nidulans has severe effects on D-glucose utilization
    • van der Veen, P., Ruijter, G. J. G., and Visser, J. 1995. An extreme creA mutation in Aspergillus nidulans has severe effects on D-glucose utilization. Microbiology 141: 2301-2306.
    • (1995) Microbiology , vol.141 , pp. 2301-2306
    • Van Der Veen, P.1    Ruijter, G.J.G.2    Visser, J.3
  • 180
    • 0029762302 scopus 로고    scopus 로고
    • The effect of pre- and prosequences and multicopy integration on heterologous expression of the Fusarium solani pisi cutinase gene in Aspergillus awamori
    • van Gemeren, I. A., Beijersbergen, A., Musters, W., Gouka, R. J., van den Hondel, C. A. M. J. J., and Verrips, C. T. 1996. The effect of pre- and prosequences and multicopy integration on heterologous expression of the Fusarium solani pisi cutinase gene in Aspergillus awamori. Appl. Microbiol. Biotechnol. 45: 755-763.
    • (1996) Appl. Microbiol. Biotechnol. , vol.45 , pp. 755-763
    • Van Gemeren, I.A.1    Beijersbergen, A.2    Musters, W.3    Gouka, R.J.4    Van Den Hondel, C.A.M.J.J.5    Verrips, C.T.6
  • 183
    • 0029794718 scopus 로고    scopus 로고
    • The related molecular chaperones calnexin and careticulin differentially associate with nascent T cell antigen receptor proteins within the endoplasmic reticulum
    • van Leeuwen, J. E. M. and Kearse, K. P. 1996. The related molecular chaperones calnexin and careticulin differentially associate with nascent T cell antigen receptor proteins within the endoplasmic reticulum. J. Biol. Chem. 271: 25345-25349.
    • (1996) J. Biol. Chem. , vol.271 , pp. 25345-25349
    • Van Leeuwen, J.E.M.1    Kearse, K.P.2
  • 184
    • 0030685697 scopus 로고    scopus 로고
    • Isolation and analysis of functional homologues of the secretion related SAR1 gene of Saccharomyces cerevisiae from Aspergillus niger and Trichoderma reesei
    • in press
    • Veldhuisen, G., Saloheimo, M., Fiers, M. A., Punt, P. J., Contreras, R., Penttilä, M., and van den Hondel, C. A. M. J. J. 1997. Isolation and analysis of functional homologues of the secretion related SAR1 gene of Saccharomyces cerevisiae from Aspergillus niger and Trichoderma reesei. Mol. Gen. Genet. in press.
    • (1997) Mol. Gen. Genet.
    • Veldhuisen, G.1    Saloheimo, M.2    Fiers, M.A.3    Punt, P.J.4    Contreras, R.5    Penttilä, M.6    Van Den Hondel, C.A.M.J.J.7
  • 185
    • 0027568439 scopus 로고
    • Glucoamylase overexpression in Aspergillus niger: Molecular genetic analysis of strains containing multiple copies of the glaA gene
    • Verdoes, J. C., Punt, P. J., Schrickx, J. M., van Verseveld, H. W., Stouthamer, A. H., and van den Hondel, C. A. M. J. J. 1993. Glucoamylase overexpression in Aspergillus niger: molecular genetic analysis of strains containing multiple copies of the glaA gene. Transgenic Res. 2: 84-92.
    • (1993) Transgenic Res. , vol.2 , pp. 84-92
    • Verdoes, J.C.1    Punt, P.J.2    Schrickx, J.M.3    Van Verseveld, H.W.4    Stouthamer, A.H.5    Van Den Hondel, C.A.M.J.J.6
  • 186
    • 0028068166 scopus 로고
    • The effect of multiple copies of the upstream region on expression of the Aspergillus niger glucoamylase-encoding gene
    • Verdoes, J. C., Punt, P. J., Stouthamer, A. H., and van den Hondel, C. A. M. J. J. 1994a. The effect of multiple copies of the upstream region on expression of the Aspergillus niger glucoamylase-encoding gene. Gene 145: 179-187.
    • (1994) Gene , vol.145 , pp. 179-187
    • Verdoes, J.C.1    Punt, P.J.2    Stouthamer, A.H.3    Van Den Hondel, C.A.M.J.J.4
  • 188
    • 0000253313 scopus 로고
    • Gene expression in filamentous fungi. Expression of pectinases and glucose oxidase in Aspergillus niger
    • Smith, A. (Ed.), Marcel Dekker, New York
    • Visser, J., Bussink, H. J., and Witteveen, C. 1994. Gene expression in filamentous fungi. Expression of pectinases and glucose oxidase in Aspergillus niger. In: Gene Expression in Recombinant Microorganisms, Smith, A. (Ed.), pp. 241-308, Marcel Dekker, New York.
    • (1994) Gene Expression in Recombinant Microorganisms , pp. 241-308
    • Visser, J.1    Bussink, H.J.2    Witteveen, C.3
  • 189
    • 0025339295 scopus 로고
    • Loss of BiP/GRP78 function blocks translocation of secretory proteins in yeast
    • Vogel, J. P., Misra, L. M., and Rose, M. D. 1990. Loss of BiP/GRP78 function blocks translocation of secretory proteins in yeast. J. Cell Biol. 110: 1885-1895.
    • (1990) J. Cell Biol. , vol.110 , pp. 1885-1895
    • Vogel, J.P.1    Misra, L.M.2    Rose, M.D.3
  • 190
    • 0025297583 scopus 로고
    • The signal peptide
    • von Heijne, G. 1990. The signal peptide. J. Memb. Biol. 115: 195-201.
    • (1990) J. Memb. Biol. , vol.115 , pp. 195-201
    • Von Heijne, G.1
  • 191
    • 0029134004 scopus 로고
    • Chaperone function of calreticulin when expressed in the endoplasmic reticulum as the membrane-anchored and soluble forms
    • Wada, I., Imai, S., Kai, M., Sakane, F., and Kanoh, H. 1995. Chaperone function of calreticulin when expressed in the endoplasmic reticulum as the membrane-anchored and soluble forms. J. Biol. Chem. 270: 20298-20304.
    • (1995) J. Biol. Chem. , vol.270 , pp. 20298-20304
    • Wada, I.1    Imai, S.2    Kai, M.3    Sakane, F.4    Kanoh, H.5
  • 192
    • 0029904281 scopus 로고    scopus 로고
    • Influence of the carbohydrate moiety on the stability of glycoproteins
    • Wang, C. Q., Eufemi, M., Turano, C., and Giartosio, A. 1996. Influence of the carbohydrate moiety on the stability of glycoproteins. Biochemistry 35: 7299-7307.
    • (1996) Biochemistry , vol.35 , pp. 7299-7307
    • Wang, C.Q.1    Eufemi, M.2    Turano, C.3    Giartosio, A.4
  • 193
    • 0001731191 scopus 로고
    • Heterologous gene expression in Aspergillus
    • Foundation for Biotechnical and Industrial Fermentation Research, Nevalainen, H. and Penttilä, M. (Eds.), Espoo
    • Ward, M. 1989. Heterologous gene expression in Aspergillus. In: EMBO-ALKO Workshop on Molecular Biology of Filamentous Fungi. Foundation for Biotechnical and Industrial Fermentation Research, Nevalainen, H. and Penttilä, M. (Eds.), Espoo, pp. 119-128.
    • (1989) EMBO-ALKO Workshop on Molecular Biology of Filamentous Fungi , pp. 119-128
    • Ward, M.1
  • 195
    • 0027260376 scopus 로고
    • Use of Aspergillus overproducing mutants, cured for integrated plasmid, to overproduce heterologous proteins
    • Ward, M., Wilson, L.J., and Kodama, K.H. 1993b. Use of Aspergillus overproducing mutants, cured for integrated plasmid, to overproduce heterologous proteins. Appl. Microbiol. Biotechnol. 39: 738-743.
    • (1993) Appl. Microbiol. Biotechnol. , vol.39 , pp. 738-743
    • Ward, M.1    Wilson, L.J.2    Kodama, K.H.3
  • 196
  • 197
    • 26044467671 scopus 로고
    • The cell wall and protein secretion in fungi
    • Foundation for Biotechnical and Industrial Fermentation Research, Nevalainen, H. and Penttilä, M. (Eds.), Espoo
    • Wessels, J. G. H. 1989. The cell wall and protein secretion in fungi. In: EMBO-ALKO Workshop on Molecular Biology of Filamentous Fungi. Foundation for Biotechnical and Industrial Fermentation Research, Nevalainen, H. and Penttilä, M. (Eds.), Espoo, pp. 177-186.
    • (1989) EMBO-ALKO Workshop on Molecular Biology of Filamentous Fungi , pp. 177-186
    • Wessels, J.G.H.1
  • 198
    • 0031060711 scopus 로고    scopus 로고
    • Hydrophobins: Proteins that change the nature of the fungal surface
    • Wessels, J. G. H. 1997. Hydrophobins: proteins that change the nature of the fungal surface. Adv. Microb. Physiol. 38: 1-45.
    • (1997) Adv. Microb. Physiol. , vol.38 , pp. 1-45
    • Wessels, J.G.H.1
  • 199
    • 0029828991 scopus 로고    scopus 로고
    • sec61-mediated transfer of a membrane protein from the endoplasmic reticulum to the proteasome for destruction
    • Wiertz, E. J. H. J., Tortorella, D., Bogyo, M., Yu, J., Mothes, W., Jones, T. R., Rapoport, T. A., and Ploegh, H. L. 1996. sec61-mediated transfer of a membrane protein from the endoplasmic reticulum to the proteasome for destruction. Nature 384: 432-438.
    • (1996) Nature , vol.384 , pp. 432-438
    • Wiertz, E.J.H.J.1    Tortorella, D.2    Bogyo, M.3    Yu, J.4    Mothes, W.5    Jones, T.R.6    Rapoport, T.A.7    Ploegh, H.L.8
  • 200
    • 0029268063 scopus 로고
    • Calnexin: A molecular chaperone with a taste for carbohydrate
    • Williams, D. B. 1995. Calnexin: A molecular chaperone with a taste for carbohydrate. Biochem.Cell Biol. 73: 123-132.
    • (1995) Biochem.Cell Biol. , vol.73 , pp. 123-132
    • Williams, D.B.1
  • 201
    • 0027513285 scopus 로고
    • H-dependent binding of KDEL to its receptor in vitro
    • Wilson, D. W., Lewis, M. J., and Pelham, H. R. 1993. pH-dependent binding of KDEL to its receptor in vitro. J. Biol. Chem. 268: 7465-7468.
    • (1993) J. Biol. Chem. , vol.268 , pp. 7465-7468
    • Wilson, D.W.1    Lewis, M.J.2    Pelham, H.R.3
  • 202
    • 0026511368 scopus 로고
    • Localization of glucose oxidase and catalase activities in Aspergillus niger
    • Witteveen, C. F. B., Veenhuis, M., and Visser, J. 1992. Localization of glucose oxidase and catalase activities in Aspergillus niger. Appl. Environ. Microbiol. 58: 1190-1194.
    • (1992) Appl. Environ. Microbiol. , vol.58 , pp. 1190-1194
    • Witteveen, C.F.B.1    Veenhuis, M.2    Visser, J.3
  • 203
    • 0025874638 scopus 로고
    • Localization of growth and secretion of proteins in Aspergillus niger
    • Wösten, H. A., Moukha, S. M., Sietsma, J. H., and Wessels, J. G. 1991. Localization of growth and secretion of proteins in Aspergillus niger. J. Gen. Microbiol. 137: 2017-2023.
    • (1991) J. Gen. Microbiol. , vol.137 , pp. 2017-2023
    • Wösten, H.A.1    Moukha, S.M.2    Sietsma, J.H.3    Wessels, J.G.4
  • 204
    • 0030063032 scopus 로고    scopus 로고
    • Effect of culture conditions and induction strategies on production of human interleukin-6 by a recombinant Aspergillus nidulans strain
    • Yadwad, V. B., Wilson, S., and Ward, O. P. 1996. Effect of culture conditions and induction strategies on production of human interleukin-6 by a recombinant Aspergillus nidulans strain. Mycol. Res. 100: 356-360.
    • (1996) Mycol. Res. , vol.100 , pp. 356-360
    • Yadwad, V.B.1    Wilson, S.2    Ward, O.P.3
  • 205
    • 0029820907 scopus 로고    scopus 로고
    • Different inducibility of expression of the two xylanase genes xyn1 and xyn2 in Trichoderma reesei
    • Zeilinger, S., Mach, R. L., Schindler, M., Herzog, P., and Kubicek, C. P. 1996. Different inducibility of expression of the two xylanase genes xyn1 and xyn2 in Trichoderma reesei. J. Biol. Chem. 271:25624-25629.
    • (1996) J. Biol. Chem. , vol.271 , pp. 25624-25629
    • Zeilinger, S.1    Mach, R.L.2    Schindler, M.3    Herzog, P.4    Kubicek, C.P.5
  • 206
    • 0029994384 scopus 로고    scopus 로고
    • Isolation of a dol-P-man synthase from Ustilago maydis that functions in Saccharomyces cerevisiae
    • Zimmerman, J. W., Specht, C. A., Cazares, B. X., and Robbins, P. W. 1996. Isolation of a dol-P-man synthase from Ustilago maydis that functions in Saccharomyces cerevisiae. Yeast 12: 765-771.
    • (1996) Yeast , vol.12 , pp. 765-771
    • Zimmerman, J.W.1    Specht, C.A.2    Cazares, B.X.3    Robbins, P.W.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.