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Volumn 64, Issue 9, 1998, Pages 3202-3208

Role of endoproteolytic dibasic proprotein processing in maturation of secretory proteins in Trichoderma reesei

Author keywords

[No Author keywords available]

Indexed keywords

BINDING PROTEIN; CALCIUM; CELLULOSE 1,4 BETA CELLOBIOSIDASE; ENZYME; FLUORIDE; FUNGAL PROTEIN; HYBRID PROTEIN; PHLEOMYCIN; PROTEINASE; SECRETORY PROTEIN; SERINE PROTEINASE INHIBITOR; SULFONIC ACID DERIVATIVE; XYLAN ENDO 1,3 BETA XYLOSIDASE;

EID: 0031684924     PISSN: 00992240     EISSN: None     Source Type: Journal    
DOI: 10.1128/aem.64.9.3202-3208.1998     Document Type: Article
Times cited : (37)

References (52)
  • 1
    • 0028086427 scopus 로고
    • Strategies for improvirtg heterologous protein production from filamentous fungi
    • Archer, D. B., D. J. Jeenes, and D. A. Mackenzie. 1994, Strategies for improvirtg heterologous protein production from filamentous fungi Antonic Leeuwenhoek 65:245-250.
    • (1994) Antonic Leeuwenhoek , vol.65 , pp. 245-250
    • Archer, D.B.1    Jeenes, D.J.2    Mackenzie, D.A.3
  • 2
    • 0021668869 scopus 로고
    • Isolation of cellulolytic enzymes from Trichoderma reesei QM 9414
    • Bhikhabhai, R., G. Johansson, and G. Petterson. 1984. Isolation of cellulolytic enzymes from Trichoderma reesei QM 9414. J. Appl. Biochem:6:336-345.
    • (1984) J. Appl. Biochem , vol.6 , pp. 336-345
    • Bhikhabhai, R.1    Johansson, G.2    Petterson, G.3
  • 3
    • 0017184389 scopus 로고
    • A rapid arid sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M. M. 1976, A rapid arid sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72:248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 4
    • 0029097268 scopus 로고
    • Effects of leader sequences upon heterologous expression of restrictocm in Aspergillus nidulans and Aspergillus niger
    • Brandhorst, T., and W. R. Kenealy. 1995. Effects of leader sequences upon heterologous expression of restrictocm 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
  • 5
    • 0026532760 scopus 로고
    • Structural and enzymatic characterization of a purified prohormone-processing enzyme: Secreted soluble Kex2 protease
    • Brenner, C., and R. S. Fuller. 1992. Structural and enzymatic characterization of a purified prohormone-processing enzyme: secreted soluble Kex2 protease. Proc. Natl. Acad. Sci. USA 89:922-926.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 922-926
    • Brenner, C.1    Fuller, R.S.2
  • 6
    • 0027508505 scopus 로고
    • Secretion of heterologous proteins by Aspergillus niger. Production of active human interleukin-6 in a proteasedeficient mutant by Kex2-like processing of a glucoamylase-HIL6 fusion protein
    • Broekhuijsen, M. P., I. E. Mattern, R. Contreras, J. R. Kinghorn, and C. A. M. J. J. van den Hondel. 1993. Secretion of heterologous proteins by Aspergillus niger. Production of active human interleukin-6 in a proteasedeficient 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
  • 7
    • 0025977561 scopus 로고
    • Proteolytic events in the processing of secreted proteins in fungi
    • Calmels, T. P. G., F. Martin, H. Durand, and G. Tiraby. 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
  • 8
    • 0025884805 scopus 로고
    • High efficiency transformation of Totypocladium geodes conidiospores to phleomycin resistance
    • Calmels, T. P. G., M. Parriche, H. Durand, and G. Tiraby. 1991. High efficiency transformation of Totypocladium geodes conidiospores to phleomycin resistance. Curr. Genet. 20:309-314.
    • (1991) Curr. Genet. , vol.20 , pp. 309-314
    • Calmels, T.P.G.1    Parriche, M.2    Durand, H.3    Tiraby, G.4
  • 9
    • 14744271483 scopus 로고
    • Efficient KEX2-like processing of a glucoamylase-interleukin-6 fusion protein by Aspergiilus nidulans and secretion of mature interleukin-6
    • Contreras, R., D. Carrez, J. R. Kinghorn, C. A. M. J. J. van den Hondel, and W. Fiers. 1991. Efficient KEX2-like processing of a glucoamylase-interleukin-6 fusion protein by Aspergiilus 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    Kinghorn, J.R.3    Van den Hondel, C.A.M.J.J.4    Fiers, W.5
  • 10
    • 0023653256 scopus 로고
    • Yeast KEX1 gene encodes a putative protease with a carboxypeptidase β-like function involved in killer toxin and α-factor precursor processing
    • Dmochowska, A., D. Dignard, D. Henning, D. Y. Thomas, and H. Bussey. 1987. Yeast KEX1 gene encodes a putative protease with a carboxypeptidase β-like function involved in killer toxin and α-factor precursor processing. Cell 50:573-584.
    • (1987) Cell , vol.50 , pp. 573-584
    • Dmochowska, A.1    Dignard, D.2    Henning, D.3    Thomas, D.Y.4    Bussey, H.5
  • 11
    • 0025376034 scopus 로고
    • Cassettes of the Streptoalloteichus hindustanus ble gene for transformation of lower and higher eukaryotes to phleomycin resistance
    • Drocourt, D., T. Calmels, J.-P. Reynes, M. Baron, and G. Tiraby. 1990. Cassettes of the Streptoalloteichus hindustanus ble gene for transformation of lower and higher eukaryotes to phleomycin resistance. Nucleic Acids Res. 18:4009.
    • (1990) Nucleic Acids Res. , vol.18 , pp. 4009
    • Drocourt, D.1    Calmels, T.2    Reynes, J.-P.3    Baron, M.4    Tiraby, G.5
  • 12
    • 0025394708 scopus 로고
    • A novel aspartyl. protease allowing Kex2-independent MF alpha propheromone processing in yeast
    • Egel-Mitani, M., H. P. Flygenrmg, and M. T. Hansen. 1990. A novel aspartyl. protease allowing Kex2-independent MF alpha propheromone processing in yeast. Yeast 6:127-137.
    • (1990) Yeast , vol.6 , pp. 127-137
    • Egel-Mitani, M.1    Flygenrmg, H.P.2    Hansen, M.T.3
  • 13
    • 0028012081 scopus 로고
    • Cloning, nucleotide sequence and functions of XPR6, which codes for a dibasic processing endoprotease from the yeast Yarrowia lipolytica
    • Enderlin, C. S., and D. M. Ogrydziak, 1994, Cloning, nucleotide sequence and functions of XPR6, which codes for a dibasic processing endoprotease from the yeast Yarrowia lipolytica. Yeast 10:67-79.
    • (1994) Yeast , vol.10 , pp. 67-79
    • Enderlin, C.S.1    Ogrydziak, D.M.2
  • 15
    • 3543034663 scopus 로고
    • North-Holland Publishing Co., Amsterdam, The Netherlands
    • Glaurt, A. M. 1974. Practical methods in electronical microscopy, vol. 3/I. North-Holland Publishing Co., Amsterdam, The Netherlands. 15a. Goller, S. P., and C. P. Kubicek. Unpublished data.
    • (1974) Practical Methods in Electronical Microscopy , vol.3 , Issue.1
    • Glaurt, A.M.1
  • 16
    • 3543017988 scopus 로고    scopus 로고
    • Unpublished data
    • Glaurt, A. M. 1974. Practical methods in electronical microscopy, vol. 3/I. North-Holland Publishing Co., Amsterdam, The Netherlands. 15a. Goller, S. P., and C. P. Kubicek. Unpublished data.
    • Goller, S.P.1    Kubicek, C.P.2
  • 17
    • 0031054007 scopus 로고    scopus 로고
    • Heterologous gene expression in Aspergiilus awamori: Comparison of expression levels of genes from different origins
    • Gouka, R. J., P. J. Punt, J. G. M. Hessing, and C. A. M. J. J. van den Hondel. 1997. Heterologous gene expression in Aspergiilus awamori: comparison of expression levels of genes from different origins. Appl. Microbiol. Biotechnol. 47:1-11.
    • (1997) Appl. Microbiol. Biotechnol. , vol.47 , pp. 1-11
    • Gouka, R.J.1    Punt, P.J.2    Hessing, J.G.M.3    Van den Hondel, C.A.M.J.J.4
  • 18
    • 0025634125 scopus 로고
    • Cloning of the Trichoderma reesei pyrG gene and its use as a homologous marker for a high frequency transformation system
    • Gruber, F., J. Visser, C. P. Kubicek, and L. De Graaff. 1990. Cloning of the Trichoderma reesei pyrG gene and its use as a homologous marker for a high frequency transformation system. Curr. Genet. 18:447-451.
    • (1990) Curr. Genet. , vol.18 , pp. 447-451
    • Gruber, F.1    Visser, J.2    Kubicek, C.P.3    De Graaff, L.4
  • 19
    • 0025321953 scopus 로고
    • The development of a heterologous transformation system for the cellulolytic fungus Trichoderma reesei based on a pyrG-negative mutant strain
    • Gruber, F., J. Visser, C. P. Kubicek, and L. De Graaff. 1990. The development of a heterologous transformation system for the cellulolytic fungus Trichoderma reesei based on a pyrG-negative mutant strain. Curr. Genet. 18:71-76.
    • (1990) Curr. Genet. , vol.18 , pp. 71-76
    • Gruber, F.1    Visser, J.2    Kubicek, C.P.3    De Graaff, L.4
  • 21
    • 0016422363 scopus 로고
    • Glucose-6-P dehydrogenase from bovine mammary gland
    • Julian, G. R., and F. J. Reithel. 1975. Glucose-6-P dehydrogenase from bovine mammary gland. Methods Enzymol. 41:183-188.
    • (1975) Methods Enzymol. , vol.41 , pp. 183-188
    • Julian, G.R.1    Reithel, F.J.2
  • 22
    • 0021713896 scopus 로고
    • Isolation of the putative structural gene for the lysine-arginine-cleaving endopeptidase required for the processing of yeast prepro-a-factor
    • Julius, D., A. Brake, L. Blair, R. Kunisawa, and J. Thorner. 1984. Isolation of the putative structural gene for the lysine-arginine-cleaving endopeptidase required for the processing of yeast prepro-a-factor. Cell 37:1075-1089.
    • (1984) Cell , vol.37 , pp. 1075-1089
    • Julius, D.1    Brake, A.2    Blair, L.3    Kunisawa, R.4    Thorner, J.5
  • 23
    • 0028877138 scopus 로고
    • Production of recombinant proteins in the filamentous fungus Trichoderma reesei
    • Keränen, S., and M. Penttilä. 1995. Production of recombinant 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
  • 24
    • 0025191378 scopus 로고
    • Processing of precursors by dipeptidylaminopeptidases: A case of molecular ticketing
    • Kreil, G. 1990, Processing of precursors by dipeptidylaminopeptidases: a case of molecular ticketing. Trends Biochem. Sci. 15:23-26.
    • (1990) Trends Biochem. Sci. , vol.15 , pp. 23-26
    • Kreil, G.1
  • 25
    • 0020402318 scopus 로고
    • Glucosidase excretion by Trichoderma pseudokoningii: Correlation with cell wall bound β-1.3-glucanase activities
    • Kubicek, C. P. 1982. β-Glucosidase excretion by Trichoderma pseudokoningii: correlation with cell wall bound β-1.3-glucanase activities. Arch. Microbiol. 132:349-354.
    • (1982) Arch. Microbiol. , vol.132 , pp. 349-354
    • Kubicek, C.P.1
  • 26
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacterrophage T4
    • Laemmli, U. K. 1970. Cleavage of structural proteins during the assembly of the head of bacterrophage T4. Nature 227:680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 27
    • 0019225431 scopus 로고
    • (p-Amidinophenyl)meth-anesulfonyl fluoride, an irreversible inhibitor of serine proteases
    • Laura, R., D. J. Robison, and D. H. Bing. 1980. (p-Amidinophenyl)meth-anesulfonyl fluoride, an irreversible inhibitor of serine proteases. Biochemistry 19:4859-4864.
    • (1980) Biochemistry , vol.19 , pp. 4859-4864
    • Laura, R.1    Robison, D.J.2    Bing, D.H.3
  • 28
    • 0029832663 scopus 로고    scopus 로고
    • Carbon catabolite repression of xynl (xylanase I-encoding) gene expression in Trichoderma reesei
    • Mach, R. L., J. Strauss, S. Zeilinger, M. Schindler, and C. P. Kubicek. 1996. Carbon catabolite repression of xynl (xylanase I-encoding) gene expression in Trichoderma reesei. Mol. Microbiol. 21:1273-1281.
    • (1996) Mol. Microbiol. , vol.21 , pp. 1273-1281
    • Mach, R.L.1    Strauss, J.2    Zeilinger, S.3    Schindler, M.4    Kubicek, C.P.5
  • 29
    • 0027454511 scopus 로고
    • Regulation of secreted protein production by filamentous fungi: Recent developments and perspectrves
    • MacKenzie, D. A., D. J. Jeenes, N. J. Belshaw, and D. B. Archer. 1993. Regulation of secreted protein production by filamentous fungi: recent developments and perspectrves. 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
  • 30
    • 0028177395 scopus 로고
    • Philological optimization of secreted protein production by Aspergillus niger
    • Mackenzie, D. A., L. C. G. Gendron, D. J. Jeenes, and D. B. Archer. 1994. Philological optimization of secreted protein production by Aspergillus niger. Enzyme Microb. Technol. 16:276-280.
    • (1994) Enzyme Microb. Technol. , vol.16 , pp. 276-280
    • Mackenzie, D.A.1    Gendron, L.C.G.2    Jeenes, D.J.3    Archer, D.B.4
  • 31
    • 0000992883 scopus 로고
    • Sophorose as an inducer of cellulase in Trichoderma viride
    • Mandels, M., F. W. Parrish, and E. T. Reese, 1962. Sophorose as an inducer of cellulase in Trichoderma viride. J. Bacteriol. 83:400-408.
    • (1962) J. Bacteriol. , vol.83 , pp. 400-408
    • Mandels, M.1    Parrish, F.W.2    Reese, E.T.3
  • 32
    • 0002067986 scopus 로고
    • The cellulose to cellulase fermentation
    • Mandels, M., and R. E. Andreotti. 1978. The cellulose to cellulase fermentation. Proc. Biochem. 13:6-13.
    • (1978) Proc. Biochem. , vol.13 , pp. 6-13
    • Mandels, M.1    Andreotti, R.E.2
  • 33
    • 0030579523 scopus 로고    scopus 로고
    • Secretion of active human mucus proteinase inhibitor by Aspergillus niger after KEX2-like processing of a glucoamylase-inhibitor fusion protein
    • Mikosch, T., P. Klemm, H. G. Gassen, C. A. M. J. J. van den Hondel, and M. Kemme. 1996. Secretion of active human mucus proteinase inhibitor by Aspergillus niger after KEX2-like processing of a glucoamylase-inhibitor fusion protein. J. Biotechnol, 52:97-106.
    • (1996) J. Biotechnol , vol.52 , pp. 97-106
    • Mikosch, T.1    Klemm, P.2    Gassen, H.G.3    Van den Hondel, C.A.M.J.J.4    Kemme, M.5
  • 36
    • 3543016196 scopus 로고    scopus 로고
    • Unpublished data
    • 34a.Parriche, M. Unpublished data.
    • Parriche, M.1
  • 37
    • 3543031089 scopus 로고
    • Qualitative improvement of Trichoderma reesei cellulases through genetic engineering
    • J. Coombs and G. Grassi (ed.). CPL Press, Newbury, United Kingdom
    • Parriche, M., and H. Durand, 1992. Qualitative improvement of Trichoderma reesei cellulases through genetic engineering, p. 110-118. In J. Coombs and G. Grassi (ed.), Cellulose hydrolysis and fermentation. CPL Press, Newbury, United Kingdom.
    • (1992) Cellulose Hydrolysis and Fermentation , pp. 110-118
    • Parriche, M.1    Durand, H.2
  • 38
    • 0028273292 scopus 로고
    • Protein secretiottin filamentous fungi-trying to understand a highly productive black box
    • Peberdy, J. F. 1994. Protein secretiottin filamentous fungi-trying to understand a highly productive black box. Trends Biotechnol. 12:50-57.
    • (1994) Trends Biotechnol. , vol.12 , pp. 50-57
    • Peberdy, J.F.1
  • 39
    • 0025752784 scopus 로고
    • Immunolocalization of Kex2 protease identifies a putative late Golgi compartment in the yeast Saccharomyces cerevisiae
    • Redding, K., C. Holcomb, and R. S. Fuller. 1991. Immunolocalization of Kex2 protease identifies a putative late Golgi compartment in the yeast Saccharomyces cerevisiae. J. Cell Biol. 113:527-538.
    • (1991) J. Cell Biol. , vol.113 , pp. 527-538
    • Redding, K.1    Holcomb, C.2    Fuller, R.S.3
  • 40
    • 3542997525 scopus 로고    scopus 로고
    • Personal communication
    • Saloheimo, M. Personal communication.
    • Saloheimo, M.1
  • 43
    • 0028277501 scopus 로고
    • Homology modelling of the catalytic domain of human furin. A model for the eukaryotic subtilisin-like proprotein convertases
    • Siezen, R. J., J. W. M. Creemeers, and W. J. M. van de Ven. 1994. Homology modelling of the catalytic domain of human furin. A model for the eukaryotic subtilisin-like proprotein convertases, Eur. J. Biochem. 222:255-266. 40a.Sowka, S. 1995. Diploma thesis. Technische Universität Wien, Vienna, Austria.
    • (1994) Eur. J. Biochem. , vol.222 , pp. 255-266
    • Siezen, R.J.1    Creemeers, J.W.M.2    Van de Ven, W.J.M.3
  • 44
    • 0028277501 scopus 로고
    • Diploma thesis. Technische Universität Wien, Vienna, Austria
    • Siezen, R. J., J. W. M. Creemeers, and W. J. M. van de Ven. 1994. Homology modelling of the catalytic domain of human furin. A model for the eukaryotic subtilisin-like proprotein convertases, Eur. J. Biochem. 222:255-266. 40a.Sowka, S. 1995. Diploma thesis. Technische Universität Wien, Vienna, Austria.
    • (1995)
    • Sowka, S.1
  • 45
    • 77957010982 scopus 로고
    • Citrate synthase
    • Srere, P. A. 1969. Citrate synthase. Methods Enzymol. 13:3-11.
    • (1969) Methods Enzymol. , vol.13 , pp. 3-11
    • Srere, P.A.1
  • 46
    • 0023132478 scopus 로고
    • Homologous domains in Trichodenna reesei cellulolytic enzymes: Gene sequence and expression of cellobiohydrolase II
    • Teeri, T. T., P. Lehtovaara, S. Kaupinnen, I. Salovuori, and J. Knowles. 1987. Homologous domains in Trichodenna reesei cellulolytic enzymes: gene sequence and expression of cellobiohydrolase II. Gene 51:43-52.
    • (1987) Gene , vol.51 , pp. 43-52
    • Teeri, T.T.1    Lehtovaara, P.2    Kaupinnen, S.3    Salovuori, I.4    Knowles, J.5
  • 47
    • 0025945724 scopus 로고
    • Kex2-line endoproteases PC2. and PC3 accurately cleave a model of prohormone in mammalian cells: Evidence for a common core of neuroendocrine processing enzymes
    • Thomas, L., R. Leduc, B. A. Tnorne, S. P. Smeekens, D. F. Steiner, and G. Thomas. 1991, Kex2-line endoproteases PC2. and PC3 accurately cleave a model of prohormone in mammalian cells: evidence for a common core of neuroendocrine processing enzymes, Proc. Natl. Acad. Sci. USA 88:5297-5301.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 5297-5301
    • Thomas, L.1    Leduc, R.2    Tnorne, B.A.3    Smeekens, S.P.4    Steiner, D.F.5    Thomas, G.6
  • 49
    • 0343004772 scopus 로고
    • The major xylanase of Trichoderma reesei: Purification and production of monoclonal antibodies
    • J. Visser, G. Beldman, M. A. Kusters-van Someren, and A. G. J. Voragen (ed). Elsevier, Amsterdam, The Netherlands
    • Törrönen, A., K. A. Affenzeller, F. Hofer, T. A. Myohanen, D. Blaas, A. M. Harkki, and C. P. Kubicek. 1992. The major xylanase of Trichoderma reesei: purification and production of monoclonal antibodies, p. 501-504. In J. Visser, G. Beldman, M. A. Kusters-van Someren, and A. G. J. Voragen (ed), Xylans and xylanases. Elsevier, Amsterdam, The Netherlands.
    • (1992) Xylans and Xylanases , pp. 501-504
    • Törrönen, A.1    Affenzeller, K.A.2    Hofer, F.3    Myohanen, T.A.4    Blaas, D.5    Harkki, A.M.6    Kubicek, C.P.7
  • 50
    • 0026605105 scopus 로고
    • Production of extracellular proteins by the filamentous fungus Aspergillus
    • van den Hondel, C. A. M. J. J., P. J. Punt, and R. F. M. vanGorcom. 1992. Production of extracellular proteins by the filamentous fungus Aspergillus. Antonie Leeuwenhoek 61:153-160.
    • (1992) Antonie Leeuwenhoek , vol.61 , pp. 153-160
    • Van den Hondel, C.A.M.J.J.1    Punt, P.J.2    VanGorcom, R.F.M.3
  • 51
    • 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., A. Beijersbergen, W. Musters, R. J. Gouka, C. A. M. J. J. van den Hondel, and C. T. Verrips. 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
  • 52
    • 0021943518 scopus 로고
    • Improved M13 phage cloning vectors and host strains: Nucleotide sequences of the M13mp18 and pUC19 vectors
    • Yanisch-Perron, C., J. Vieira, and J. Messing. 1985, Improved M13 phage cloning vectors and host strains: nucleotide sequences of the M13mp18 and pUC19 vectors. Gene 33:103-119.
    • (1985) Gene , vol.33 , pp. 103-119
    • Yanisch-Perron, C.1    Vieira, J.2    Messing, J.3


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