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Volumn 55, Issue 2, 2007, Pages 467-474

Proteomic response to intracellular proteins of Monascus pilosus grown under phosphate-limited complex medium with different growth rates and pigment production

Author keywords

Food pigments; Monascus pilosus; Protein extraction; Proteomics

Indexed keywords

MONASCUS; MONASCUS PILOSUS;

EID: 34047229539     PISSN: 00218561     EISSN: None     Source Type: Journal    
DOI: 10.1021/jf0622937     Document Type: Article
Times cited : (17)

References (52)
  • 1
    • 0029985406 scopus 로고    scopus 로고
    • Inhibitory effect of oral administration of Monascus pigment on tumor promotion in two-stage carcinogenesis in mouse skin
    • Yasukawa, K.; Takahashi, M.; Yamanouchi, S.; Takido, M. Inhibitory effect of oral administration of Monascus pigment on tumor promotion in two-stage carcinogenesis in mouse skin. Oncology 1996, 53, 247-249.
    • (1996) Oncology , vol.53 , pp. 247-249
    • Yasukawa, K.1    Takahashi, M.2    Yamanouchi, S.3    Takido, M.4
  • 2
    • 0024780638 scopus 로고
    • Food colorants: Anthocyanins
    • Francis, F. J. Food colorants: anthocyanins. Crit. Rev. Food Sci. Nutr. 1989, 28, 273-314.
    • (1989) Crit. Rev. Food Sci. Nutr , vol.28 , pp. 273-314
    • Francis, F.J.1
  • 3
    • 0037467070 scopus 로고    scopus 로고
    • Color characteristics of Monascus pigments derived by fermentation with various amino acids
    • Jung, H.; Kim, C.; Kim, K.; Shin, C. S. Color characteristics of Monascus pigments derived by fermentation with various amino acids. J. Agric. Food Chem. 2003, 51, 1302-1306.
    • (2003) J. Agric. Food Chem , vol.51 , pp. 1302-1306
    • Jung, H.1    Kim, C.2    Kim, K.3    Shin, C.S.4
  • 4
    • 0037014305 scopus 로고    scopus 로고
    • Wild, D.; Toth, G.; Humpf, H. U. New Monascus metabolite isolated from red yeast rice (angkak, red koji). J. Agric. Food Chem. 2002, 50, 3999-4002.
    • Wild, D.; Toth, G.; Humpf, H. U. New Monascus metabolite isolated from red yeast rice (angkak, red koji). J. Agric. Food Chem. 2002, 50, 3999-4002.
  • 5
    • 0036381499 scopus 로고    scopus 로고
    • A combined solid-state and submerged cultivation integrated with adsorptive product extraction for production of Monascus red pigments
    • Hsu, F. L.; Wang, P. M.; Lu, S. Y.; Wu, W. T. A combined solid-state and submerged cultivation integrated with adsorptive product extraction for production of Monascus red pigments. Bioprocess Biosyst. Eng. 2002, 25, 165-168.
    • (2002) Bioprocess Biosyst. Eng , vol.25 , pp. 165-168
    • Hsu, F.L.1    Wang, P.M.2    Lu, S.Y.3    Wu, W.T.4
  • 6
    • 0035041513 scopus 로고    scopus 로고
    • Effect of yeast extract on growth kinetics of Monascus purpureus
    • Pereira, D. G.; Kilikian, B. V. Effect of yeast extract on growth kinetics of Monascus purpureus. Appl. Biochem. Biotechnol. 2001, 91-93, 311-316.
    • (2001) Appl. Biochem. Biotechnol , vol.91-93 , pp. 311-316
    • Pereira, D.G.1    Kilikian, B.V.2
  • 7
    • 85003571657 scopus 로고    scopus 로고
    • Solid substrate fermentation of Monascus purpureus: Growth, carbon balance, and consistency analysis
    • Rosenblitt, A.; Agosin, E.; Delgado, J.; Perez-Correa, R. Solid substrate fermentation of Monascus purpureus: growth, carbon balance, and consistency analysis. Biotechnol. Prog. 2000, 16, 152-162.
    • (2000) Biotechnol. Prog , vol.16 , pp. 152-162
    • Rosenblitt, A.1    Agosin, E.2    Delgado, J.3    Perez-Correa, R.4
  • 8
    • 0037255627 scopus 로고    scopus 로고
    • Production of the secondary metabolites gamma-aminobutyric acid and monacolin K by Monascus
    • Su, Y. C.; Wang, J. J.; Lin, T. T.; Pan, T. M. Production of the secondary metabolites gamma-aminobutyric acid and monacolin K by Monascus. J. Ind. Microbiol. Biotechnol. 2003, 30, 41-46.
    • (2003) J. Ind. Microbiol. Biotechnol , vol.30 , pp. 41-46
    • Su, Y.C.1    Wang, J.J.2    Lin, T.T.3    Pan, T.M.4
  • 9
    • 0346057821 scopus 로고    scopus 로고
    • Improvement of monacolin K, gamma-aminobutyric acid and citrinin production ratio as a function of environmental conditions of Monascus purpureus NTU 601
    • Wang, J. J.; Lee, C. L.; Pan, T. M. Improvement of monacolin K, gamma-aminobutyric acid and citrinin production ratio as a function of environmental conditions of Monascus purpureus NTU 601. J. Ind. Microbiol. Biotechnol. 2003, 30, 669-676.
    • (2003) J. Ind. Microbiol. Biotechnol , vol.30 , pp. 669-676
    • Wang, J.J.1    Lee, C.L.2    Pan, T.M.3
  • 10
    • 8444237432 scopus 로고    scopus 로고
    • Modified mutation method for screening low citrinin-producing strains of Monascus purpureus on rice culture
    • Wang, J. J.; Lee, C. L.; Pan, T. M. Modified mutation method for screening low citrinin-producing strains of Monascus purpureus on rice culture. J. Agric. Food Chem. 2004, 52, 6977-6982.
    • (2004) J. Agric. Food Chem , vol.52 , pp. 6977-6982
    • Wang, J.J.1    Lee, C.L.2    Pan, T.M.3
  • 11
    • 0034095399 scopus 로고    scopus 로고
    • Growth, pigment production and protease activity of Monascus purpureus as affected by salt, sodium nitrite, polyphosphate and various sugars
    • Tseng, Y. Y.; Chen, M. T.; Lin, C. F. Growth, pigment production and protease activity of Monascus purpureus as affected by salt, sodium nitrite, polyphosphate and various sugars. J. Appl. Microbiol. 2000, 88, 31-37.
    • (2000) J. Appl. Microbiol , vol.88 , pp. 31-37
    • Tseng, Y.Y.1    Chen, M.T.2    Lin, C.F.3
  • 12
    • 0001356283 scopus 로고
    • Isolation and cultural conditions of Monascus sp. for the production of pigment in a submerged culture
    • Lin, C. F. Isolation and cultural conditions of Monascus sp. for the production of pigment in a submerged culture. J. Ferment. Technol. 1973, 51, 407-414.
    • (1973) J. Ferment. Technol , vol.51 , pp. 407-414
    • Lin, C.F.1
  • 13
    • 1542615443 scopus 로고    scopus 로고
    • Two-dimensional gel electrophoresis pattern (pH 6-11) and identification of water-soluble barley seed and malt proteins by mass spectrometry
    • Bak-Jensen, K. S.; Laugesen, S.; Roepstorff, P.; Svensson, B. Two-dimensional gel electrophoresis pattern (pH 6-11) and identification of water-soluble barley seed and malt proteins by mass spectrometry. Proteomics 2004, 4, 728-742.
    • (2004) Proteomics , vol.4 , pp. 728-742
    • Bak-Jensen, K.S.1    Laugesen, S.2    Roepstorff, P.3    Svensson, B.4
  • 14
    • 14644395537 scopus 로고    scopus 로고
    • Comparative proteome analysis of Saccharomyces cerevisiae grown in chemostat cultures limited for glucose or ethanol
    • Kolkman, A.; Olsthoorn, M. M.; Heeremans, C. E.; Heck, A. J.; Slijper, M. Comparative proteome analysis of Saccharomyces cerevisiae grown in chemostat cultures limited for glucose or ethanol. Mol. Cell. Proteomics 2005, 4, 1-11.
    • (2005) Mol. Cell. Proteomics , vol.4 , pp. 1-11
    • Kolkman, A.1    Olsthoorn, M.M.2    Heeremans, C.E.3    Heck, A.J.4    Slijper, M.5
  • 15
    • 3543095175 scopus 로고    scopus 로고
    • Quantitative proteome profiling during the fermentation process of pleiotropic Bacillus subtilis mutants
    • Antelmann, H.; Sapolsky, R.; Miller, B.; Ferrari, E.; Chotani, G.; Weyler, W.; Gaertner, A.; Hecker, M. Quantitative proteome profiling during the fermentation process of pleiotropic Bacillus subtilis mutants. Proteomics 2004, 4, 2408-2424.
    • (2004) Proteomics , vol.4 , pp. 2408-2424
    • Antelmann, H.1    Sapolsky, R.2    Miller, B.3    Ferrari, E.4    Chotani, G.5    Weyler, W.6    Gaertner, A.7    Hecker, M.8
  • 16
    • 10644274361 scopus 로고    scopus 로고
    • Towards a comprehensive understanding of Bacillus subtilis cell physiology by physiological proteomics
    • Hecker, M.; Volker, U. Towards a comprehensive understanding of Bacillus subtilis cell physiology by physiological proteomics. Proteomics 2004, 4, 3727-3750.
    • (2004) Proteomics , vol.4 , pp. 3727-3750
    • Hecker, M.1    Volker, U.2
  • 18
    • 0036637702 scopus 로고    scopus 로고
    • Comparison of lysis methods and preparation protocols for one- and two-dimensional electrophoresis of Aspergillus oryzae intracellular proteins
    • Nandakumar, M. P.; Marten, M. R. Comparison of lysis methods and preparation protocols for one- and two-dimensional electrophoresis of Aspergillus oryzae intracellular proteins. Electrophoresis 2002, 23, 2216-2222.
    • (2002) Electrophoresis , vol.23 , pp. 2216-2222
    • Nandakumar, M.P.1    Marten, M.R.2
  • 19
    • 4544330114 scopus 로고    scopus 로고
    • Identification of phospholipase B from Dictyostelium discoideum reveals a new lipase family present in mammals, flies and nematodes, but not yeast
    • Morgan, C. P.; Insall, R.; Haynes, L.; Cockcroft, S. Identification of phospholipase B from Dictyostelium discoideum reveals a new lipase family present in mammals, flies and nematodes, but not yeast. Biochem. J. 2004, 382, 441-449.
    • (2004) Biochem. J , vol.382 , pp. 441-449
    • Morgan, C.P.1    Insall, R.2    Haynes, L.3    Cockcroft, S.4
  • 20
    • 0028917303 scopus 로고
    • Cross-species identification of proteins separated by two-dimensional gel electrophoresis using matrix-assisted laser desorption ionisation/time-of-flight mass spectrometry and amino acid composition
    • Cordwell, S. J.; Wilkins, M. R.; Cerpa-Poljak, A.; Gooley, A. A.; Duncan, M.; Williams, K. L.; Humphery-Smith, I. Cross-species identification of proteins separated by two-dimensional gel electrophoresis using matrix-assisted laser desorption ionisation/time-of-flight mass spectrometry and amino acid composition. Electrophoresis 1995, 16, 438-443.
    • (1995) Electrophoresis , vol.16 , pp. 438-443
    • Cordwell, S.J.1    Wilkins, M.R.2    Cerpa-Poljak, A.3    Gooley, A.A.4    Duncan, M.5    Williams, K.L.6    Humphery-Smith, I.7
  • 21
    • 0031557882 scopus 로고    scopus 로고
    • Cross-species protein identification using amino acid composition, peptide mass fingerprinting, isoelectric point and molecular mass: A theoretical evaluation
    • Wilkins, M. R.; Williams, K. L. Cross-species protein identification using amino acid composition, peptide mass fingerprinting, isoelectric point and molecular mass: a theoretical evaluation. J. Theor. Biol. 1997, 186, 7-15.
    • (1997) J. Theor. Biol , vol.186 , pp. 7-15
    • Wilkins, M.R.1    Williams, K.L.2
  • 22
    • 0035350894 scopus 로고    scopus 로고
    • Mass spectrometry allows direct identification of proteins in large genomes
    • Kuster, B.; Mortensen, P.; Andersen, J. S.; Mann, M. Mass spectrometry allows direct identification of proteins in large genomes. Proteomics 2001, 1, 641-650.
    • (2001) Proteomics , vol.1 , pp. 641-650
    • Kuster, B.1    Mortensen, P.2    Andersen, J.S.3    Mann, M.4
  • 23
    • 0025946331 scopus 로고
    • Effect of nutrition of Monascus sp. on formation of red pigments
    • Lin, T. F.; Demain, A. L. Effect of nutrition of Monascus sp. on formation of red pigments. Appl. Microbiol. Biotechnol. 1991, 36, 70-75.
    • (1991) Appl. Microbiol. Biotechnol , vol.36 , pp. 70-75
    • Lin, T.F.1    Demain, A.L.2
  • 24
    • 0034599528 scopus 로고    scopus 로고
    • Dell'Angelica, E. C.; Puertollano, R.; Mullins, C.; Aguilar, R. C.; Vargas, J. D.; Hartnell, L. M.; Bonifacino, J. S. GGAs: a family of ADP ribosylation factor-binding proteins related to adaptors and associated with the Golgi complex. J. Cell Biol. 2000, 149, 81-94.
    • Dell'Angelica, E. C.; Puertollano, R.; Mullins, C.; Aguilar, R. C.; Vargas, J. D.; Hartnell, L. M.; Bonifacino, J. S. GGAs: a family of ADP ribosylation factor-binding proteins related to adaptors and associated with the Golgi complex. J. Cell Biol. 2000, 149, 81-94.
  • 25
    • 0032584676 scopus 로고    scopus 로고
    • Zhang, C. J.; Cavenagh, M. M.; Kahn, R. A. A family of Arf effectors defined as suppressors of the loss of Arf function in the yeast Saccharomyces cerevisiae. J. Biol. Chem. 1998, 273, 19792-19796.
    • Zhang, C. J.; Cavenagh, M. M.; Kahn, R. A. A family of Arf effectors defined as suppressors of the loss of Arf function in the yeast Saccharomyces cerevisiae. J. Biol. Chem. 1998, 273, 19792-19796.
  • 26
    • 0029411666 scopus 로고
    • Novel aspects of the regulation of a cDNA (Arf1) from Chlamydomonas with high sequence identity to animal ADP-ribosylation factor 1
    • Memon, A. R.; Hwang, S.; Deshpande, N.; Thompson, G. A., Jr.; Herrin, D. L. Novel aspects of the regulation of a cDNA (Arf1) from Chlamydomonas with high sequence identity to animal ADP-ribosylation factor 1. Plant Mol. Biol. 1995, 29, 567-577.
    • (1995) Plant Mol. Biol , vol.29 , pp. 567-577
    • Memon, A.R.1    Hwang, S.2    Deshpande, N.3    Thompson Jr., G.A.4    Herrin, D.L.5
  • 28
    • 0021913732 scopus 로고
    • Protein synthesis during transition and stationary phases under glucose limitation in Saccharomyces cerevisiae
    • Boucherie, H. Protein synthesis during transition and stationary phases under glucose limitation in Saccharomyces cerevisiae. J. Bacteriol. 1985, 161, 385-392.
    • (1985) J. Bacteriol , vol.161 , pp. 385-392
    • Boucherie, H.1
  • 29
    • 0344256526 scopus 로고    scopus 로고
    • Starvation and temperature upshift cause an increase-in the enzymatically active cell wall-associated glyceraldehyde-3-phosphate dehydrogenase protein in yeast
    • Delgado, M. L.; Gil, M. L.; Gozalbo, D. Starvation and temperature upshift cause an increase-in the enzymatically active cell wall-associated glyceraldehyde-3-phosphate dehydrogenase protein in yeast. FEMS Yeast Res. 2003, 4, 297-303.
    • (2003) FEMS Yeast Res , vol.4 , pp. 297-303
    • Delgado, M.L.1    Gil, M.L.2    Gozalbo, D.3
  • 30
    • 0032819504 scopus 로고    scopus 로고
    • Purification of a biologically active recombinant glyceraldehyde 3-phosphate dehydrogenase from Candida albicans
    • Villamon, E.; Gozalbo, D.; Martinez, J. P.; Gil, M. L. Purification of a biologically active recombinant glyceraldehyde 3-phosphate dehydrogenase from Candida albicans. FEMS Microbiol. Lett. 1999, 179, 61-65.
    • (1999) FEMS Microbiol. Lett , vol.179 , pp. 61-65
    • Villamon, E.1    Gozalbo, D.2    Martinez, J.P.3    Gil, M.L.4
  • 31
    • 0027371487 scopus 로고
    • Identification and characterization of stationary phase-inducible genes in Escherichia coli
    • Weichart, D.; Lange, R.; Henneberg, N.; Hengge-Aronis, R. Identification and characterization of stationary phase-inducible genes in Escherichia coli. Mol. Microbiol. 1993, 10, 407-420.
    • (1993) Mol. Microbiol , vol.10 , pp. 407-420
    • Weichart, D.1    Lange, R.2    Henneberg, N.3    Hengge-Aronis, R.4
  • 32
    • 0019970038 scopus 로고
    • Phosphate-controlled gene expression in Escherichia coli K12 using Mudl-directed lacZ fusions
    • Wanner, B. L.; McSharry, R. Phosphate-controlled gene expression in Escherichia coli K12 using Mudl-directed lacZ fusions. J. Mol. Biol. 1982, 158, 347-363.
    • (1982) J. Mol. Biol , vol.158 , pp. 347-363
    • Wanner, B.L.1    McSharry, R.2
  • 33
    • 85047683547 scopus 로고    scopus 로고
    • Similarity of the Escherichia coli proteome upon completion of different biopharmaceutical fermentation processes
    • Champion, K. M.; Nishihara, J. C.; Joly, J. C.; Arnott, D. Similarity of the Escherichia coli proteome upon completion of different biopharmaceutical fermentation processes. Proteomics 2001, 1, 1133-1148.
    • (2001) Proteomics , vol.1 , pp. 1133-1148
    • Champion, K.M.1    Nishihara, J.C.2    Joly, J.C.3    Arnott, D.4
  • 34
    • 0029779668 scopus 로고    scopus 로고
    • Global analysis of proteins synthesized during phosphorus restriction in Escherichia coli
    • VanBogelen, R. A.; Olson, E. R.; Wanner, B. L.; Neidhardt, F. C. Global analysis of proteins synthesized during phosphorus restriction in Escherichia coli. J. Bacteriol. 1996, 178, 4344-4366.
    • (1996) J. Bacteriol , vol.178 , pp. 4344-4366
    • VanBogelen, R.A.1    Olson, E.R.2    Wanner, B.L.3    Neidhardt, F.C.4
  • 35
    • 0035692234 scopus 로고    scopus 로고
    • Phosphate transport and sensing in Saccharomyces cerevisiae
    • Wykoff, D. D.; O'Shea, E. K. Phosphate transport and sensing in Saccharomyces cerevisiae. Genetics 2001, 159, 1491-1499.
    • (2001) Genetics , vol.159 , pp. 1491-1499
    • Wykoff, D.D.1    O'Shea, E.K.2
  • 36
    • 0028786431 scopus 로고
    • Energetics and product formation by Saccharomyces cerevisiae grown in anaerobic chemostats under nitrogen limitation
    • Liden, G.; Persson, A.; Gustafsson, L.; Niklasson, C. Energetics and product formation by Saccharomyces cerevisiae grown in anaerobic chemostats under nitrogen limitation. Appl. Microbiol. Biotechnol. 1995, 43, 1034-1038.
    • (1995) Appl. Microbiol. Biotechnol , vol.43 , pp. 1034-1038
    • Liden, G.1    Persson, A.2    Gustafsson, L.3    Niklasson, C.4
  • 38
    • 0020490759 scopus 로고
    • Targeted deletion of a yeast enolase structural gene. Identification and isolation of yeast enolase isozymes
    • McAlister, L.; Holland, M. J. Targeted deletion of a yeast enolase structural gene. Identification and isolation of yeast enolase isozymes. J. Biol. Chem. 1982, 257, 7181-7188.
    • (1982) J. Biol. Chem , vol.257 , pp. 7181-7188
    • McAlister, L.1    Holland, M.J.2
  • 39
    • 0015238985 scopus 로고
    • A kinetic study of glycolytic enzyme synthesis in yeast
    • Maitra, P. K.; Lobo, Z. A kinetic study of glycolytic enzyme synthesis in yeast. J. Biol. Chem. 1971, 246, 475-488.
    • (1971) J. Biol. Chem , vol.246 , pp. 475-488
    • Maitra, P.K.1    Lobo, Z.2
  • 41
    • 0027267942 scopus 로고
    • Different signals control the activation of glycolysis in the yeast Saccharomyces cerevisiae
    • Boles, E.; Heinisch, J.; Zimmermann, F. K. Different signals control the activation of glycolysis in the yeast Saccharomyces cerevisiae. Yeast 1993, 9, 761-770.
    • (1993) Yeast , vol.9 , pp. 761-770
    • Boles, E.1    Heinisch, J.2    Zimmermann, F.K.3
  • 42
    • 0027170537 scopus 로고
    • Induction of pyruvate decarboxylase in glycolysis mutants of Saccharomyces cerevisiae correlates with the concentrations of three-carbon glycolytic metabolites
    • Boles, E.; Zimmermann, F. K. Induction of pyruvate decarboxylase in glycolysis mutants of Saccharomyces cerevisiae correlates with the concentrations of three-carbon glycolytic metabolites. Arch. Microbiol. 1993, 160, 324-328.
    • (1993) Arch. Microbiol , vol.160 , pp. 324-328
    • Boles, E.1    Zimmermann, F.K.2
  • 44
    • 0016418463 scopus 로고
    • Energy utilization for control
    • Hess, B. Energy utilization for control. Ciba Found. Symp. 1975, 369-392.
    • (1975) Ciba Found. Symp , pp. 369-392
    • Hess, B.1
  • 45
    • 0016258153 scopus 로고
    • Modulation of the adenylate energy charge by sustained metabolic oscillations
    • Goldbeter, A. Modulation of the adenylate energy charge by sustained metabolic oscillations. FEBS Lett. 1974, 43, 327-330.
    • (1974) FEBS Lett , vol.43 , pp. 327-330
    • Goldbeter, A.1
  • 46
    • 18844442599 scopus 로고    scopus 로고
    • A systematic high-throughput screen of a yeast deletion collection for mutants defective in PHO5 regulation
    • Huang, S.; O'Shea, E. K. A systematic high-throughput screen of a yeast deletion collection for mutants defective in PHO5 regulation. Genetics 2005, 169, 1859-1871.
    • (2005) Genetics , vol.169 , pp. 1859-1871
    • Huang, S.1    O'Shea, E.K.2
  • 47
    • 0030982112 scopus 로고    scopus 로고
    • Irreversible metabolic transitions: The glucose 6-phosphate metabolism in yeast cell-free extracts
    • Coevoet, M. A.; Hervagault, J. F. Irreversible metabolic transitions: the glucose 6-phosphate metabolism in yeast cell-free extracts. Biochem. Biophys. Res. Commun. 1997, 234, 162-166.
    • (1997) Biochem. Biophys. Res. Commun , vol.234 , pp. 162-166
    • Coevoet, M.A.1    Hervagault, J.F.2
  • 48
    • 0034661449 scopus 로고    scopus 로고
    • Purification and characterization of glutamine:fructose 6-phosphate amidotransferase from rat liver
    • Huynh, Q. K.; Gulve, E. A.; Dian, T. Purification and characterization of glutamine:fructose 6-phosphate amidotransferase from rat liver. Arch. Biochem. Biophys. 2000, 379, 307-313.
    • (2000) Arch. Biochem. Biophys , vol.379 , pp. 307-313
    • Huynh, Q.K.1    Gulve, E.A.2    Dian, T.3
  • 49
    • 0023280276 scopus 로고
    • Glucosamine synthetase from Escherichia coli: Purification, properties, and glutamine-utilizing site location
    • Badet, B.; Vermoote, P.; Haumont, P. Y.; Lederer, F.; LeGoffic, F. Glucosamine synthetase from Escherichia coli: purification, properties, and glutamine-utilizing site location. Biochemistry 1987, 26, 1940-1948.
    • (1987) Biochemistry , vol.26 , pp. 1940-1948
    • Badet, B.1    Vermoote, P.2    Haumont, P.Y.3    Lederer, F.4    LeGoffic, F.5
  • 50
    • 0036000565 scopus 로고    scopus 로고
    • Glucosamine:fructose-6-phosphate aminotransferase: Gene characterization, chitin biosynmesis and peritrophic matrix formation in Aedes aegypti
    • Kato, N.; Dasgupta, R.; Smartt, C. T.; Christensen, B. M. Glucosamine:fructose-6-phosphate aminotransferase: gene characterization, chitin biosynmesis and peritrophic matrix formation in Aedes aegypti. Insect Mol. Biol. 2002, 11, 207-216.
    • (2002) Insect Mol. Biol , vol.11 , pp. 207-216
    • Kato, N.1    Dasgupta, R.2    Smartt, C.T.3    Christensen, B.M.4
  • 51
    • 6444241905 scopus 로고    scopus 로고
    • Ram, A. F.; Arentshorst, M.; Damveld, R. A.; vanKuyk, P. A.; Klis, F. M.; van den Hondel, C. A. The cell wall stress response in Aspergillus niger involves increased expression of the glutamine:fructose-6-phosphate amidotransferase-encoding gene (gfaA) and increased deposition of chitin in the cell wall. Microbiology 2004, 150, 3315-3326.
    • Ram, A. F.; Arentshorst, M.; Damveld, R. A.; vanKuyk, P. A.; Klis, F. M.; van den Hondel, C. A. The cell wall stress response in Aspergillus niger involves increased expression of the glutamine:fructose-6-phosphate amidotransferase-encoding gene (gfaA) and increased deposition of chitin in the cell wall. Microbiology 2004, 150, 3315-3326.
  • 52
    • 0142184966 scopus 로고    scopus 로고
    • Chitin synthesis in Saccharomyces cerevisiae in response to supplementation of growth medium with glucosamine and cell wall stress
    • Bulik, D. A.; Olczak, M.; Lucero, H. A.; Osmond, B. C.; Robbins, P. W.; Specht, C. A. Chitin synthesis in Saccharomyces cerevisiae in response to supplementation of growth medium with glucosamine and cell wall stress. Eukaryotic Cell 2003, 2, 886-900.
    • (2003) Eukaryotic Cell , vol.2 , pp. 886-900
    • Bulik, D.A.1    Olczak, M.2    Lucero, H.A.3    Osmond, B.C.4    Robbins, P.W.5    Specht, C.A.6


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