메뉴 건너뛰기




Volumn 8, Issue 5, 1997, Pages 554-560

Production of recombinant proteins by methylotrophic yeasts

Author keywords

[No Author keywords available]

Indexed keywords

ANTIBODY; BLOOD CLOTTING INHIBITOR; CYTOKINE; ENZYME; FIBRINOLYTIC AGENT; GHILANTEN; HEPATITIS B VACCINE; HIRUDIN DERIVATIVE; HORMONE; HYBRID PROTEIN; MU OPIATE RECEPTOR; PROTEINASE INHIBITOR; RECOMBINANT PROTEIN; SEROTONIN RECEPTOR; SIGNAL PEPTIDE; VACCINE;

EID: 0030725815     PISSN: 09581669     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0958-1669(97)80028-6     Document Type: Article
Times cited : (182)

References (58)
  • 1
    • 0001023204 scopus 로고    scopus 로고
    • Expression of heterologous gene products in yeast
    • Edited by Cleland JL, Craik CS. New York: Wiley Liss
    • Pichuantes S, Nguyen AT, Franzusoff A: Expression of heterologous gene products in yeast. In Protein Engineering: Principles and Practice. Edited by Cleland JL, Craik CS. New York: Wiley Liss; 1996:129-161. Overview of industrially and pharmaceutically relevant components and methods of heterologous gene expression in yeast.
    • (1996) Protein Engineering: Principles and Practice , pp. 129-161
    • Pichuantes, S.1    Nguyen, A.T.2    Franzusoff, A.3
  • 2
    • 0004048061 scopus 로고    scopus 로고
    • Berlin: Springer
    • Wolf K (Ed): Nonconventional Yeasts in Biotechnology. A Handbook. Berlin: Springer; 1996. A compilation of methods and components of biotechnological applications of 10 non-Saccharomyces yeasts. The book contains, among others, chapters on Pichia pastoris and Hansenula polymorpha (see also [52,53]).
    • (1996) Nonconventional Yeasts in Biotechnology. A Handbook
    • Wolf, K.1
  • 3
    • 0030272554 scopus 로고    scopus 로고
    • The expression of recombinant proteins in yeasts
    • Sudbery PE: The expression of recombinant proteins in yeasts. Curr Opin Biotechnol 1996, 7:517-524.
    • (1996) Curr Opin Biotechnol , vol.7 , pp. 517-524
    • Sudbery, P.E.1
  • 4
    • 0031010051 scopus 로고    scopus 로고
    • Applications of yeasts in gene expression studies: A comparison of Saccharomyces cerevisiae, Hansenula polymorpha and Kluyveromyces lactis - A review
    • Gellissen G, Hollenberg CP: Applications of yeasts in gene expression studies: a comparison of Saccharomyces cerevisiae, Hansenula polymorpha and Kluyveromyces lactis - a review. Gene 1997, 190:87-97.
    • (1997) Gene , vol.190 , pp. 87-97
    • Gellissen, G.1    Hollenberg, C.P.2
  • 5
    • 0030272217 scopus 로고    scopus 로고
    • Quality and authenticity of heterologous proteins synthesized in yeast
    • Eckart MR, Bussineau CM: Quality and authenticity of heterologous proteins synthesized in yeast Curr Opin Biotechnol 1996, 7:525-530.
    • (1996) Curr Opin Biotechnol , vol.7 , pp. 525-530
    • Eckart, M.R.1    Bussineau, C.M.2
  • 6
    • 0028801044 scopus 로고
    • Advances in the use of Pichia pastoris for high-level gene expression
    • Romanos M: Advances in the use of Pichia pastoris for high-level gene expression. Curr Opin Biotechnol 1995, 6:527-533.
    • (1995) Curr Opin Biotechnol , vol.6 , pp. 527-533
    • Romanos, M.1
  • 7
    • 0030600453 scopus 로고    scopus 로고
    • Inducible expression of a heterologous protein in Hansenula polymorpha using the alcohol oxidase 1 promoter of Pichia pastoris
    • •], demonstrates an efficient expression of heterologous proteins in H. polymorpha driven by the P. pastoris-derived alcohol oxidase 1 (AOX1) promoter. The AOX1-promotor has all the cis-acting elements necessary for proper regulation (induction by methanol and derepression under glycerol limitation) in H. polymorpha.
    • (1996) Gene , vol.177 , pp. 163-167
    • Raschke, W.C.1    Neiditch, B.R.2    Hendricks, M.3    Cregg, J.M.4
  • 10
    • 0028187499 scopus 로고
    • Heterologous gene expression in C1 compound-utilizing yeasts
    • Edited by Murooka Y, Imanaka T. New York: Dekker
    • Gellissen G: Heterologous gene expression in C1 compound-utilizing yeasts. In Recombinant Microbes for industrial and Agricultural Applications. Edited by Murooka Y, Imanaka T. New York: Dekker; 1994:787-796.
    • (1994) Recombinant Microbes for Industrial and Agricultural Applications , pp. 787-796
    • Gellissen, G.1
  • 11
    • 0028827506 scopus 로고
    • Review: Methylotrophic yeasts as factories for the production of foreign proteins
    • Faber KN, Harder W, Ab G, Veenhuis M: Review: methylotrophic yeasts as factories for the production of foreign proteins. Yeast 1995, 11:1331-1344.
    • (1995) Yeast , vol.11 , pp. 1331-1344
    • Faber, K.N.1    Harder, W.2    Ab, G.3    Veenhuis, M.4
  • 12
    • 0030608045 scopus 로고    scopus 로고
    • High-level secretion of fungal glucoamylase using the Candida boidinii gene expression system
    • Sakai Y, Akiyama M, Kondoh H, Shibano Y, Kato N: High-level secretion of fungal glucoamylase using the Candida boidinii gene expression system. Biochim Biophys Acta 1996, 1308:81-87. Describes the high-yield production of a secreted heterologous enzyme in gram ranges. The C. boidinii system exhibits properties similar to those described for the two established methylotrophs.
    • (1996) Biochim Biophys Acta , vol.1308 , pp. 81-87
    • Sakai, Y.1    Akiyama, M.2    Kondoh, H.3    Shibano, Y.4    Kato, N.5
  • 13
    • 0029780708 scopus 로고    scopus 로고
    • Methylotrophic yeast Hansenula polymorpha as production organism for recombinant pharmaceuticals
    • Gellissen G, Melber K: Methylotrophic yeast Hansenula polymorpha as production organism for recombinant pharmaceuticals. Drug Res 1996, 46:943-948. A brief review on H. polymorpha as a production organism for recombinant pharmaceuticals focusing on hirudin and a H. polymorpha-derived hepatitis B vaccine. The review includes a list of FDA-approved recombinant drugs.
    • (1996) Drug Res , vol.46 , pp. 943-948
    • Gellissen, G.1    Melber, K.2
  • 15
    • 0028081167 scopus 로고
    • High-level secretion and very efficient isotopic labelling of tick anticoagulant peptide (TAP) expressed in the methylotrophic yeast, Pichia pastoris
    • Laroche Y, Storme V, de Meutter J, Messens J, Lauwereys M: High-level secretion and very efficient isotopic labelling of tick anticoagulant peptide (TAP) expressed in the methylotrophic yeast, Pichia pastoris. Bio-Technology 1994, 12:1119-1124.
    • (1994) Bio-Technology , vol.12 , pp. 1119-1124
    • Laroche, Y.1    Storme, V.2    De Meutter, J.3    Messens, J.4    Lauwereys, M.5
  • 17
    • 0030250768 scopus 로고    scopus 로고
    • Overexpression in Pichia pastoris and crystallization of an elicitor protein secreted by the phytopathogenic fungus, Phytophora cryptogea
    • O'Donohue MJ, Boissy G, Huet J-C, Nespoulous C, Brunie S, Pernollet J-C: Overexpression in Pichia pastoris and crystallization of an elicitor protein secreted by the phytopathogenic fungus, Phytophora cryptogea. Protein Expr Purif 1996, 8:254-261. This study presents a convincing example of the high-yield secretion of an interesting protein obtained in crystallization quality. Former approaches to produce this protein in an appropriate quality in an E. coli host had failed.
    • (1996) Protein Expr Purif , vol.8 , pp. 254-261
    • O'Donohue, M.J.1    Boissy, G.2    Huet, J.-C.3    Nespoulous, C.4    Brunie, S.5    Pernollet, J.-C.6
  • 18
    • 0030022151 scopus 로고    scopus 로고
    • Biochemical characterization of the recombinant Boophilus microplus Bm86 antigen expressed by transformed Pichia pastoris cells
    • Montesino R, Cremata J, Rodriguez M, Besada V, Falcón V, de la Fuente J: Biochemical characterization of the recombinant Boophilus microplus Bm86 antigen expressed by transformed Pichia pastoris cells. Biotechnol Appl Biochem 1996, 23:23-28.
    • (1996) Biotechnol Appl Biochem , vol.23 , pp. 23-28
    • Montesino, R.1    Cremata, J.2    Rodriguez, M.3    Besada, V.4    Falcón, V.5    De La Fuente, J.6
  • 20
    • 0030475733 scopus 로고    scopus 로고
    • Production and purification of recombinant hirudin expressed in the methylotrophic yeast Pichia pastoris
    • Rosenfeld SA, Nadeau D, Tirado J, Hollis GF, Knabb RM, Jia S: Production and purification of recombinant hirudin expressed in the methylotrophic yeast Pichia pastoris. Protein Expr Purif 1996, 8:476-482.
    • (1996) Protein Expr Purif , vol.8 , pp. 476-482
    • Rosenfeld, S.A.1    Nadeau, D.2    Tirado, J.3    Hollis, G.F.4    Knabb, R.M.5    Jia, S.6
  • 22
    • 0029443619 scopus 로고
    • Expression of a synthetic gene encoding the anticoagulant-antimetastatic protein ghilanten by the methylotrophic yeast Pichia pastoris
    • Brankamp RG, Sreekrishna K, Smith PL, Blankenship DT, Cardin AD: Expression of a synthetic gene encoding the anticoagulant-antimetastatic protein ghilanten by the methylotrophic yeast Pichia pastoris. Protein Expr Purif 1995, 6:813-820.
    • (1995) Protein Expr Purif , vol.6 , pp. 813-820
    • Brankamp, R.G.1    Sreekrishna, K.2    Smith, P.L.3    Blankenship, D.T.4    Cardin, A.D.5
  • 24
    • 0029990729 scopus 로고    scopus 로고
    • Secretion of a variant of human single-chain urokinase-type plasminogen activator without an N-glycosylation site in the methylotrophic yeast, Pichia pastoris and characterization of the secreted product
    • Tsujikawa M, Okabayashi K, Morita M, Tanabe T: Secretion of a variant of human single-chain urokinase-type plasminogen activator without an N-glycosylation site in the methylotrophic yeast, Pichia pastoris and characterization of the secreted product Yeast 1996, 12:541-553.
    • (1996) Yeast , vol.12 , pp. 541-553
    • Tsujikawa, M.1    Okabayashi, K.2    Morita, M.3    Tanabe, T.4
  • 26
    • 0028785213 scopus 로고
    • A disruption-replacement approach for the targeted integration of foreign genes in Hansenula polymorpha
    • Agaphonov MO, Beburov MY, Ter-Avanesyan MD, Smirnov VN: A disruption-replacement approach for the targeted integration of foreign genes in Hansenula polymorpha. Yeast 1995, 11:1241-1247.
    • (1995) Yeast , vol.11 , pp. 1241-1247
    • Agaphonov, M.O.1    Beburov, M.Y.2    Ter-Avanesyan, M.D.3    Smirnov, V.N.4
  • 27
    • 0029940930 scopus 로고    scopus 로고
    • Foreign gene expression in Hansenula polymorpha. A system for the synthesis of small functional peptides
    • Faber KN, Westra S, Waterham HR, Keizer-Gunnink I, Harder W, Veenhuis GA: Foreign gene expression in Hansenula polymorpha. A system for the synthesis of small functional peptides. Appl Microbiol Biotechnol 1996, 45:72-79. Describes the targeting of heterologous proteins to the peroxisome. Fusion to the amino oxidase stabilizes an otherwise unstable protein.
    • (1996) Appl Microbiol Biotechnol , vol.45 , pp. 72-79
    • Faber, K.N.1    Westra, S.2    Waterham, H.R.3    Keizer-Gunnink, I.4    Harder, W.5    Veenhuis, G.A.6
  • 28
    • 0030614539 scopus 로고    scopus 로고
    • A bioactive designer cytokine for human hematopoietic progenitor cell expansion
    • Fischer M, Goldschmitt J, Peschel C, Brakenhoff JPG, Kallen K-J, Wollmer A, Grötzinger J, Rose-John S: A bioactive designer cytokine for human hematopoietic progenitor cell expansion. Nat Biotechnol 1997, 15:142-145. The efficient production of a fusion protein consisting of interleukin-6 and a soluble form of its receptor is described. The fusion protein turned out to be fully active at 100-1000 lower concentration than the unlinked proteins in expanding gp130-expressing human haematopoietic progenitor cells. This publication opens new approaches to treating blood cell deficiencies.
    • (1997) Nat Biotechnol , vol.15 , pp. 142-145
    • Fischer, M.1    Goldschmitt, J.2    Peschel, C.3    Brakenhoff, J.P.G.4    Kallen, K.-J.5    Wollmer, A.6    Grötzinger, J.7    Rose-John, S.8
  • 29
    • 0029863568 scopus 로고    scopus 로고
    • High-yield expression and secretion of the ovine pregnancy recognition hormone interferon-tau by Pichia pastoris
    • Vanheeke G, Ott TL, Strauss A, Ammaturo D, Bazer FW: High-yield expression and secretion of the ovine pregnancy recognition hormone interferon-tau by Pichia pastoris. J Interferon Cytokine Res 1996, 16:119-126.
    • (1996) J Interferon Cytokine Res , vol.16 , pp. 119-126
    • Vanheeke, G.1    Ott, T.L.2    Strauss, A.3    Ammaturo, D.4    Bazer, F.W.5
  • 30
    • 0030591760 scopus 로고    scopus 로고
    • Intracellular production of a major cytomegalovirus antigenic protein in the methylotrophic yeast Pichia pastoris
    • Battista MC, Bergamini G, Campanini F, Landini MP, Ripalti A: Intracellular production of a major cytomegalovirus antigenic protein in the methylotrophic yeast Pichia pastoris. Gene 1996, 176:197-201.
    • (1996) Gene , vol.176 , pp. 197-201
    • Battista, M.C.1    Bergamini, G.2    Campanini, F.3    Landini, M.P.4    Ripalti, A.5
  • 31
    • 0029839368 scopus 로고    scopus 로고
    • Cloning and expression in yeast Pichia pastoris of a biologically active form of Cyn d 1, the major allergen of Bermuda grass pollen
    • Smith PM, Suphioglu C, Griffith IJ, Theriault K, Knox RB, Singh MB: Cloning and expression in yeast Pichia pastoris of a biologically active form of Cyn d 1, the major allergen of Bermuda grass pollen. J Allergy Clin Immunol 1996, 98:331-343.
    • (1996) J Allergy Clin Immunol , vol.98 , pp. 331-343
    • Smith, P.M.1    Suphioglu, C.2    Griffith, I.J.3    Theriault, K.4    Knox, R.B.5    Singh, M.B.6
  • 33
    • 0013514028 scopus 로고    scopus 로고
    • Production of Fv fragment of monoclonal antibody from recombinant yeast Pichia pastoris
    • Ando K, Arunwanich P, Kai K, Shinkai M, Honda H, Kobayashi T: Production of Fv fragment of monoclonal antibody from recombinant yeast Pichia pastoris. J Chem Eng Japan 1996, 29:390-392.
    • (1996) J Chem Eng Japan , vol.29 , pp. 390-392
    • Ando, K.1    Arunwanich, P.2    Kai, K.3    Shinkai, M.4    Honda, H.5    Kobayashi, T.6
  • 34
    • 0028944846 scopus 로고
    • Generation of rabbit monoclonal antibody fragments from a combinatorial phage display library and their production in the yeast Pichia pastoris
    • Ridder R, Schmitz R, Legay F, Gram H: Generation of rabbit monoclonal antibody fragments from a combinatorial phage display library and their production in the yeast Pichia pastoris. Bio-Technology 1995, 13:255-260.
    • (1995) Bio-Technology , vol.13 , pp. 255-260
    • Ridder, R.1    Schmitz, R.2    Legay, F.3    Gram, H.4
  • 35
    • 0029560973 scopus 로고
    • 5A serotonin receptor in the methylotrophic yeast Pichia pastoris: Pharmacological charcterization and localization
    • 5A serotonin receptor in the methylotrophic yeast Pichia pastoris: pharmacological charcterization and localization. FEBS Lett 1995, 377:451-456.
    • (1995) FEBS Lett , vol.377 , pp. 451-456
    • Weiß, H.M.1    Haase, W.2    Michel, H.3    Reiländer, H.4
  • 36
    • 0030574052 scopus 로고    scopus 로고
    • Expression and pharmacological characterization of the human μ-opioid receptor in the methylotrophic yeast Pichia pastoris
    • Talmont F, Sidobre S, Demange P, Milon A, Emorine LJ: Expression and pharmacological characterization of the human μ-opioid receptor in the methylotrophic yeast Pichia pastoris. FEBS Lett 1996, 394:268-272.
    • (1996) FEBS Lett , vol.394 , pp. 268-272
    • Talmont, F.1    Sidobre, S.2    Demange, P.3    Milon, A.4    Emorine, L.J.5
  • 37
    • 0030974549 scopus 로고    scopus 로고
    • Expression of trimeric CD40 ligand in Pichia pastoris: Use of a rapid method to detect high-level expressing transformants
    • McGrew JT, Leiske D, Dell B, Klinke R, Krasts D, Wee SF, Abbott N, Armitage R, Harrington K: Expression of trimeric CD40 ligand in Pichia pastoris: use of a rapid method to detect high-level expressing transformants. Gene 1997, 187:193-200.
    • (1997) Gene , vol.187 , pp. 193-200
    • McGrew, J.T.1    Leiske, D.2    Dell, B.3    Klinke, R.4    Krasts, D.5    Wee, S.F.6    Abbott, N.7    Armitage, R.8    Harrington, K.9
  • 38
    • 0030444332 scopus 로고    scopus 로고
    • Expression, purification, and characterization of recombinant alpha-N-acetylgalactosaminidase produced in the yeast Pichia pastoris
    • Zhu A, Monahan C, Wang ZK, Goldstein J: Expression, purification, and characterization of recombinant alpha-N-acetylgalactosaminidase produced in the yeast Pichia pastoris. Protein Expr Purif 1996, 8:456-462.
    • (1996) Protein Expr Purif , vol.8 , pp. 456-462
    • Zhu, A.1    Monahan, C.2    Wang, Z.K.3    Goldstein, J.4
  • 39
    • 0029865393 scopus 로고    scopus 로고
    • Characterization of recombinant alpha-galactosidase for use in seroconversion from blood-group B to blood group O of human erythrocytes
    • Zhu A, Leng L, Monahan C, Zhang ZF, Hurst R, Lenny L, Goldstein J: Characterization of recombinant alpha-galactosidase for use in seroconversion from blood-group B to blood group O of human erythrocytes. Arch Biochem Biophys 1996, 327:324-329.
    • (1996) Arch Biochem Biophys , vol.327 , pp. 324-329
    • Zhu, A.1    Leng, L.2    Monahan, C.3    Zhang, Z.F.4    Hurst, R.5    Lenny, L.6    Goldstein, J.7
  • 40
    • 0028828190 scopus 로고
    • High-level expression and purification of coffee bean α-galactosidase produced in the yeast Pichia pastoris
    • Zhu A, Monahan C, Zhang Z, Hurst R, Leng L, Goldstein J: High-level expression and purification of coffee bean α-galactosidase produced in the yeast Pichia pastoris. Arch Biochem Biophys 1995, 324:65-70.
    • (1995) Arch Biochem Biophys , vol.324 , pp. 65-70
    • Zhu, A.1    Monahan, C.2    Zhang, Z.3    Hurst, R.4    Leng, L.5    Goldstein, J.6
  • 41
    • 9344252854 scopus 로고    scopus 로고
    • Cloning, expression and characterization of a blood group B active recombinant alpha-D-galactosidase from soybean (glycine-max)
    • Davis MO, Hata DJ, Johnson SA, Walker JC, Smith DS: Cloning, expression and characterization of a blood group B active recombinant alpha-D-galactosidase from soybean (glycine-max). Biochem Mol Biol Int 1996, 39:471-485.
    • (1996) Biochem Mol Biol int , vol.39 , pp. 471-485
    • Davis, M.O.1    Hata, D.J.2    Johnson, S.A.3    Walker, J.C.4    Smith, D.S.5
  • 42
    • 0030250653 scopus 로고    scopus 로고
    • Overexpression, purification and characterization of recombinant barley α-amylase-1 and 2 secreted by the methylotrophic yeast Pichia pastoris
    • Juge N, Andersen JS, Tull D, Roepstorff P, Svensson B: Overexpression, purification and characterization of recombinant barley α-amylase-1 and 2 secreted by the methylotrophic yeast Pichia pastoris. Protein Expr Purif 1996, 8:204-214.
    • (1996) Protein Expr Purif , vol.8 , pp. 204-214
    • Juge, N.1    Andersen, J.S.2    Tull, D.3    Roepstorff, P.4    Svensson, B.5
  • 43
    • 0343989849 scopus 로고    scopus 로고
    • Biochemical responses of recombinant strains of Hansenula polymorpha on oversynthesis of homologous dihydroxyacetone kinase and bacterial β-galactosidase
    • Velkov VV, Matys VY, Solokov: Biochemical responses of recombinant strains of Hansenula polymorpha on oversynthesis of homologous dihydroxyacetone kinase and bacterial β-galactosidase. Appl Biochem Microbiol 1996, 32:100-105.
    • (1996) Appl Biochem Microbiol , vol.32 , pp. 100-105
    • Velkov, V.V.1    Matys, V.Y.2    Solokov3
  • 44
    • 0343113395 scopus 로고    scopus 로고
    • Expression of the major bean proteins from Theobrama cacao (Cocoa) in the yeasts Hansenula polymorpha and Saccharomyces cerevisiae
    • Yavuz MÖ, Ashton SMV, Deakin ED, Spencer ME, Sudbery PE: Expression of the major bean proteins from Theobrama cacao (Cocoa) in the yeasts Hansenula polymorpha and Saccharomyces cerevisiae. J Biotechnol 1996, 46:43-54.
    • (1996) J Biotechnol , vol.46 , pp. 43-54
    • Yavuz, M.Ö.1    Ashton, S.M.V.2    Deakin, E.D.3    Spencer, M.E.4    Sudbery, P.E.5
  • 45
    • 0029866204 scopus 로고    scopus 로고
    • Efficient expression of the gene for spinach phosphoribulokinase in Pichia pastoris and utilization of the recombinant enzyme to explore the role of regulatory cysteinyl residues by site-directed mutagenesis
    • Brandes HK, Hartman FC, Lu TYS, Larimer FW: Efficient expression of the gene for spinach phosphoribulokinase in Pichia pastoris and utilization of the recombinant enzyme to explore the role of regulatory cysteinyl residues by site-directed mutagenesis. J Biol Chem 1996, 271:6490-6496.
    • (1996) J Biol Chem , vol.271 , pp. 6490-6496
    • Brandes, H.K.1    Hartman, F.C.2    Lu, T.Y.S.3    Larimer, F.W.4
  • 46
    • 0029595212 scopus 로고
    • High-level production of spinach glycolate oxidase in the methylotrophix yeast Pichia pastoris - Engineering a biocatalyst
    • Payne MS, Petrillo KL, Gavagan JE, Wagner LW, DiCosimo R, Anton DL: High-level production of spinach glycolate oxidase in the methylotrophix yeast Pichia pastoris - engineering a biocatalyst Gene 1995, 167:215-219.
    • (1995) Gene , vol.167 , pp. 215-219
    • Payne, M.S.1    Petrillo, K.L.2    Gavagan, J.E.3    Wagner, L.W.4    DiCosimo, R.5    Anton, D.L.6
  • 47
    • 0029813916 scopus 로고    scopus 로고
    • Recombinant Hansenula polymorpha as a biocatalyst: Coexpression of the spinach glycolate oxidase (GO) and the S. cerevisiae catalase T (CTT1) gene
    • Gellissen G, Piontek M, Dahlems U, Jenzelewski V, Gavagan JE, DiCosimo R, Anton DL, Janowicz ZA: Recombinant Hansenula polymorpha as a biocatalyst: coexpression of the spinach glycolate oxidase (GO) and the S. cerevisiae catalase T (CTT1) gene. Appl Microbiol Biotechnol 1996, 46:46-54. Two enzyme genes are integrated in anticipated fixed copy number ratios. A recombinant peroxisomal and a cytoplasmic enzyme are co-produced. This is a strategy to use recombinant H. polymorpha strains as biocatalyst.
    • (1996) Appl Microbiol Biotechnol , vol.46 , pp. 46-54
    • Gellissen, G.1    Piontek, M.2    Dahlems, U.3    Jenzelewski, V.4    Gavagan, J.E.5    Dicosimo, R.6    Anton, D.L.7    Janowicz, Z.A.8
  • 48
    • 0028589448 scopus 로고
    • Increase in copy number of an integrated vector during continuous culture of Hansenula polymorpha expressing functional hemoglobin
    • Gilbert SC, van Urk H, Greefield DM, McAvoy MJ, Denton KA, Coghlan D, Jones GD, Mead DJ: Increase in copy number of an integrated vector during continuous culture of Hansenula polymorpha expressing functional hemoglobin. Yeast 1994, 10:1569-1580.
    • (1994) Yeast , vol.10 , pp. 1569-1580
    • Gilbert, S.C.1    Van Urk, H.2    Greefield, D.M.3    McAvoy, M.J.4    Denton, K.A.5    Coghlan, D.6    Jones, G.D.7    Mead, D.J.8
  • 49
    • 0029829267 scopus 로고    scopus 로고
    • The methylotrophic yeast Pichia pastoris synthesizes a functionally active chromophore precursor of the plant photoreceptor phytochrome
    • Wu S-H, Lagarias JC: The methylotrophic yeast Pichia pastoris synthesizes a functionally active chromophore precursor of the plant photoreceptor phytochrome. Proc Natl Acad Sci USA 1996, 93:8989-8994.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 8989-8994
    • Wu, S.-H.1    Lagarias, J.C.2
  • 50
    • 0029790768 scopus 로고    scopus 로고
    • Drosophila melanogaster angiotensin-l-converting enzyme expressed in Pichia pastoris resembles the C-domain of the mammalian homolog and does not require glycosylation for secretion and enzymatic activity
    • Williams TA, Michaud A, Houard X, Chauvet MT, Soubrier F, Corvol P: Drosophila melanogaster angiotensin-l-converting enzyme expressed in Pichia pastoris resembles the C-domain of the mammalian homolog and does not require glycosylation for secretion and enzymatic activity. Biochem J 1996, 318:125-131.
    • (1996) Biochem J , vol.318 , pp. 125-131
    • Williams, T.A.1    Michaud, A.2    Houard, X.3    Chauvet, M.T.4    Soubrier, F.5    Corvol, P.6
  • 52
    • 0000296246 scopus 로고    scopus 로고
    • Hansenula polymorpha (Pichia angusta)
    • Edited by Wolf K. Heidelberg: Springer
    • Hansen H, Hollenberg CP: Hansenula polymorpha (Pichia angusta). In Nonconventional Yeasts in Biotechnology. Edited by Wolf K. Heidelberg: Springer; 1996:293-311.
    • (1996) Nonconventional Yeasts in Biotechnology , pp. 293-311
    • Hansen, H.1    Hollenberg, C.P.2
  • 55
    • 0029743974 scopus 로고    scopus 로고
    • A novel autonomously replicating sequence (ARS) for multiple integration in the yeast Hansenula polymorpha DL1
    • Sohn JH, Choi ES, Kim CH, Agaphonov MO, Ter-Avanesyan MD, Rhee JS, Rhee SK: A novel autonomously replicating sequence (ARS) for multiple integration in the yeast Hansenula polymorpha DL1. J Bacteriol 1996, 178:4420-4428.
    • (1996) J Bacteriol , vol.178 , pp. 4420-4428
    • Sohn, J.H.1    Choi, E.S.2    Kim, C.H.3    Agaphonov, M.O.4    Ter-Avanesyan, M.D.5    Rhee, J.S.6    Rhee, S.K.7
  • 58
    • 0028940737 scopus 로고
    • Plasmid reorganization during integrative transformation in Hansenula polymorpha
    • Bogdanova AI, Agaphonov MO, Ter-Avanesyan MD: Plasmid reorganization during integrative transformation in Hansenula polymorpha. Yeast 1995, 11:343-353.
    • (1995) Yeast , vol.11 , pp. 343-353
    • Bogdanova, A.I.1    Agaphonov, M.O.2    Ter-Avanesyan, M.D.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.