메뉴 건너뛰기




Volumn 73, Issue 19, 2007, Pages 6241-6253

Characteristics of Gloeophyllum trabeum alcohol oxidase, an extracellular source of H2O2 in brown rot decay of wood

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; COTTON FIBERS; DNA; ELECTRON MICROSCOPY; MOLECULAR MASS; POLYPEPTIDES; PROTEINS;

EID: 35148832513     PISSN: 00992240     EISSN: None     Source Type: Journal    
DOI: 10.1128/AEM.00977-07     Document Type: Article
Times cited : (108)

References (60)
  • 1
    • 0021947993 scopus 로고
    • Methanol formation during lignin degradation by Phanerochaete chrysosporium
    • Ander, P., and K. E. Eriksson. 1985. Methanol formation during lignin degradation by Phanerochaete chrysosporium. Appl. Microbiol. Biotechnol. 21:96-102.
    • (1985) Appl. Microbiol. Biotechnol , vol.21 , pp. 96-102
    • Ander, P.1    Eriksson, K.E.2
  • 2
    • 0345487002 scopus 로고    scopus 로고
    • Electron and fluorescence microscopy of extracellular glucan and aryl-alcohol oxidase during wheat-straw degradation by Pleurotus eryngii
    • Barrasa, J. M., A. Gutiérrez, V. Escaso, F. Guillén, M. J. Martinez, and A. T. Martinez. 1998. Electron and fluorescence microscopy of extracellular glucan and aryl-alcohol oxidase during wheat-straw degradation by Pleurotus eryngii. Appl. Environ. Microbiol. 64:325-332.
    • (1998) Appl. Environ. Microbiol , vol.64 , pp. 325-332
    • Barrasa, J.M.1    Gutiérrez, A.2    Escaso, V.3    Guillén, F.4    Martinez, M.J.5    Martinez, A.T.6
  • 3
    • 0018540477 scopus 로고
    • Purification and properties of alcohol oxidase from Poria contigua
    • Bringer, S., B. Sprey, and H. Sham. 1979. Purification and properties of alcohol oxidase from Poria contigua. Eur. J. Biochem. 101:563-570.
    • (1979) Eur. J. Biochem , vol.101 , pp. 563-570
    • Bringer, S.1    Sprey, B.2    Sham, H.3
  • 4
    • 0345062300 scopus 로고    scopus 로고
    • Expression analysis of a cytosolic glutamine synthetase gene in cotyledons of Scots pine seedlings: Developmental, light regulation and spatial distribution of specific transcripts
    • Canton, F. R., M. F. Suarez, M. Jose-Estanyol, and F. M. Canovas. 1999. Expression analysis of a cytosolic glutamine synthetase gene in cotyledons of Scots pine seedlings: developmental, light regulation and spatial distribution of specific transcripts. Plant Mol. Biol. 40:623-634.
    • (1999) Plant Mol. Biol , vol.40 , pp. 623-634
    • Canton, F.R.1    Suarez, M.F.2    Jose-Estanyol, M.3    Canovas, F.M.4
  • 5
    • 0347761163 scopus 로고    scopus 로고
    • Differential stress-induced regulation of two quinone reductases in the brown-rot basidiomycete Gloeophyllum trabeum
    • Cohen, R., M. R. Suzuki, and K. E. Hammel. 2004. Differential stress-induced regulation of two quinone reductases in the brown-rot basidiomycete Gloeophyllum trabeum. Appl. Environ. Microbiol. 70:324-331.
    • (2004) Appl. Environ. Microbiol , vol.70 , pp. 324-331
    • Cohen, R.1    Suzuki, M.R.2    Hammel, K.E.3
  • 6
    • 0028267037 scopus 로고
    • Use of electron microscopy for aiding our understanding of wood biodegradation
    • Daniel, G. 1994. Use of electron microscopy for aiding our understanding of wood biodegradation. FEMS Microbiol. Rev. 13:199-233.
    • (1994) FEMS Microbiol. Rev , vol.13 , pp. 199-233
    • Daniel, G.1
  • 7
    • 0028340896 scopus 로고
    • 2 during wood degradation by Phanerochaete chrysosporium, Trametes versicolor, and Oudemansiella mucida
    • 2 during wood degradation by Phanerochaete chrysosporium, Trametes versicolor, and Oudemansiella mucida. Appl. Environ. Microbiol. 60:2524-2532.
    • (1994) Appl. Environ. Microbiol , vol.60 , pp. 2524-2532
    • Daniel, G.1    Volc, J.2    Kubátová, E.3
  • 8
    • 0026443134 scopus 로고
    • 2-producing enzyme pyranose oxidase in Phanerochaete chrysosporium grown under liquid culture conditions
    • 2-producing enzyme pyranose oxidase in Phanerochaete chrysosporium grown under liquid culture conditions. Appl. Environ. Microbiol. 58:3667-3676.
    • (1992) Appl. Environ. Microbiol , vol.58 , pp. 3667-3676
    • Daniel, G.1    Volc, J.2    Kubátová, E.3    Nilsson, T.4
  • 9
    • 9244250633 scopus 로고    scopus 로고
    • Cryo-FE-SEM and TEM immuno-techniques reveal new details for understanding white rot decay of lignocellulose
    • Daniel, G., J. Volc, and M.-L. Niku-Paavola. 2004. Cryo-FE-SEM and TEM immuno-techniques reveal new details for understanding white rot decay of lignocellulose. C. R. Biol. 327:861-871.
    • (2004) C. R. Biol , vol.327 , pp. 861-871
    • Daniel, G.1    Volc, J.2    Niku-Paavola, M.-L.3
  • 10
    • 0000934679 scopus 로고
    • Intra- and extracellular localization of lignin peroxidase during degradation of solid wood and wood fragments by Phanerochaete chrysosporium by using transmission electron microscopy and immunogold labeling
    • Daniel, G., T. Nilsson, and B. Pettersson. 1989. Intra- and extracellular localization of lignin peroxidase during degradation of solid wood and wood fragments by Phanerochaete chrysosporium by using transmission electron microscopy and immunogold labeling. Appl. Environ. Microbiol. 55:871-881.
    • (1989) Appl. Environ. Microbiol , vol.55 , pp. 871-881
    • Daniel, G.1    Nilsson, T.2    Pettersson, B.3
  • 11
    • 0028324235 scopus 로고
    • Production, purification and characterization of an alcohol oxidase of the ligninolytic fungus Peniophora gigantea
    • Danneel, H.-J., A. Reichert, and F. Giffhorn. 1994. Production, purification and characterization of an alcohol oxidase of the ligninolytic fungus Peniophora gigantea. J. Biotechnol. 33:33-41.
    • (1994) J. Biotechnol , vol.33 , pp. 33-41
    • Danneel, H.-J.1    Reichert, A.2    Giffhorn, F.3
  • 12
    • 0017154853 scopus 로고
    • A sensitive fluorescent method fort he detection of glycoprotein in Polyacrylamide gels
    • Eckhardt, A. E., C. E. Hayes, and J. Goldstein. 1976. A sensitive fluorescent method fort he detection of glycoprotein in Polyacrylamide gels. Anal. Biochem. 73:192-197.
    • (1976) Anal. Biochem , vol.73 , pp. 192-197
    • Eckhardt, A.E.1    Hayes, C.E.2    Goldstein, J.3
  • 13
    • 0030615451 scopus 로고    scopus 로고
    • Enoki, A., S. Itakura, and H. Tanaka. 1997. The involvement of extracellular substances for reducing molecular oxygen to hydroxyl radical and ferric iron to ferrous iron in wood degradation by wood decay fungi. I. Biotechnol. 53:265-272.
    • Enoki, A., S. Itakura, and H. Tanaka. 1997. The involvement of extracellular substances for reducing molecular oxygen to hydroxyl radical and ferric iron to ferrous iron in wood degradation by wood decay fungi. I. Biotechnol. 53:265-272.
  • 14
    • 0001167774 scopus 로고
    • Methanol oxidase of Phanerochaete chrysosporium
    • Eriksson, K. E., and A. Nishida. 1988. Methanol oxidase of Phanerochaete chrysosporium. Methods Enzymol. 161:322-326.
    • (1988) Methods Enzymol , vol.161 , pp. 322-326
    • Eriksson, K.E.1    Nishida, A.2
  • 15
    • 0005515389 scopus 로고
    • Microbial and enzymatic degradation of wood and wood components
    • Springer, Berlin, Germany
    • Eriksson, K.-E., R. A. Blanchette, and P. Ander. 1990. Microbial and enzymatic degradation of wood and wood components, p. 407. In Springer series in wood science. Springer, Berlin, Germany.
    • (1990) Springer series in wood science , pp. 407
    • Eriksson, K.-E.1    Blanchette, R.A.2    Ander, P.3
  • 16
    • 0036187745 scopus 로고    scopus 로고
    • Lignin demethylation and polysaccharide decomposition in spruce sapwood degraded by brown rot fungi
    • Filley, T. R., G. D. Cody, B. Goodell, J. Jellison, C. Noser, and A. Ostrofsky. 2002. Lignin demethylation and polysaccharide decomposition in spruce sapwood degraded by brown rot fungi. Org. Geochem. 33:111-124.
    • (2002) Org. Geochem , vol.33 , pp. 111-124
    • Filley, T.R.1    Cody, G.D.2    Goodell, B.3    Jellison, J.4    Noser, C.5    Ostrofsky, A.6
  • 17
    • 5244332657 scopus 로고
    • Wood decay by basidiomycetes: Extracellular tripartite membranous structures
    • Foisner, R., K. Messner, H. Stachelberger, and M. Röhr. 1985. Wood decay by basidiomycetes: extracellular tripartite membranous structures. Trans. Br. Mycol. Soc. 85:257-266.
    • (1985) Trans. Br. Mycol. Soc , vol.85 , pp. 257-266
    • Foisner, R.1    Messner, K.2    Stachelberger, H.3    Röhr, M.4
  • 18
    • 49349106270 scopus 로고    scopus 로고
    • Brown-rot fungal degradation of wood: Our evolving view
    • B. Goodell, D. D. Nicholas, and T. P. Schultz ed, ACS, Washington, DC
    • Goodell, B. 2003. Brown-rot fungal degradation of wood: our evolving view, p. 97-119. In B. Goodell, D. D. Nicholas, and T. P. Schultz (ed.), Wood deterioration and preservation: advances in our changing world. ACS series 845. ACS, Washington, DC.
    • (2003) Wood deterioration and preservation: Advances in our changing world. ACS series , vol.845 , pp. 97-119
    • Goodell, B.1
  • 19
    • 0342547343 scopus 로고    scopus 로고
    • Low molecular weight chelators and phenolic compounds isolated from wood decay and their role in the fungal biodegradation of wood
    • Goodell, B., J. Jellison, J. Liu, G. Daniel, A. Paszczynski, F. Fekete, S. Krishnamurty, L. Jun, and G. Xu. 1997. Low molecular weight chelators and phenolic compounds isolated from wood decay and their role in the fungal biodegradation of wood. J. Biotechnol. 53:133-162.
    • (1997) J. Biotechnol , vol.53 , pp. 133-162
    • Goodell, B.1    Jellison, J.2    Liu, J.3    Daniel, G.4    Paszczynski, A.5    Fekete, F.6    Krishnamurty, S.7    Jun, L.8    Xu, G.9
  • 20
    • 0021267821 scopus 로고
    • Alcohol oxidase assembles post-translation all into the peroxisome of Candida boidinii
    • Goodman, J. M., C. W. Scott, P. W. Donahue, and J. P. Atheron. 1984. Alcohol oxidase assembles post-translation all into the peroxisome of Candida boidinii. J. Biol. Chem. 259:8485-8493.
    • (1984) J. Biol. Chem , vol.259 , pp. 8485-8493
    • Goodman, J.M.1    Scott, C.W.2    Donahue, P.W.3    Atheron, J.P.4
  • 21
    • 0031103592 scopus 로고    scopus 로고
    • Mechanism of brown rot decay: Paradigm or paradox
    • Green, F., and T. L. Highley. 1997. Mechanism of brown rot decay: paradigm or paradox. Int. Biodeter. Biodegr. 39:113-124.
    • (1997) Int. Biodeter. Biodegr , vol.39 , pp. 113-124
    • Green, F.1    Highley, T.L.2
  • 22
    • 0026458087 scopus 로고
    • Immunoscanning electron microscopic localization of extracellular polysaccharidases within the fibrillar sheath of the brown rot fungus Postia placenta
    • Green, F., M. J. Larsen, L. Murmanis, and T. L. Highley. 1992. Immunoscanning electron microscopic localization of extracellular polysaccharidases within the fibrillar sheath of the brown rot fungus Postia placenta. Can. J. Bot. 38:898-904.
    • (1992) Can. J. Bot , vol.38 , pp. 898-904
    • Green, F.1    Larsen, M.J.2    Murmanis, L.3    Highley, T.L.4
  • 23
    • 1542344022 scopus 로고    scopus 로고
    • Routing of Hansenula polymorpha alcohol oxidase: An alternative peroxisomal protein-sorting machinery
    • Gunkel, K., R. van Dijk, M. Veenhuis, and I. J. van der Klei. 2004. Routing of Hansenula polymorpha alcohol oxidase: an alternative peroxisomal protein-sorting machinery. Mol. Biol. Cell 15:1347-1355.
    • (2004) Mol. Biol. Cell , vol.15 , pp. 1347-1355
    • Gunkel, K.1    van Dijk, R.2    Veenhuis, M.3    van der Klei, I.J.4
  • 26
    • 0000663716 scopus 로고
    • Electron microscopy of cellulose decomposition by brown rot fungi
    • Highley, T. L., L. Murmanis, and J. G. Palmer. 1983. Electron microscopy of cellulose decomposition by brown rot fungi. Holzforschung 37:271-277.
    • (1983) Holzforschung , vol.37 , pp. 271-277
    • Highley, T.L.1    Murmanis, L.2    Palmer, J.G.3
  • 27
    • 0036121162 scopus 로고    scopus 로고
    • A Penicillium chrysogenum gene (aox) identified by specific induction upon shifting pH encodes for a protein which shows high homology to fungal alcohol oxidases
    • Holzmann, K., E. Schreiner, and H. Schwalb. 2002. A Penicillium chrysogenum gene (aox) identified by specific induction upon shifting pH encodes for a protein which shows high homology to fungal alcohol oxidases. Curr. Genet. 40:339-344.
    • (2002) Curr. Genet , vol.40 , pp. 339-344
    • Holzmann, K.1    Schreiner, E.2    Schwalb, H.3
  • 28
    • 0031032498 scopus 로고    scopus 로고
    • A mechanism for production of hydroxyl radicals by the brown-rot fungus Coniophora puteana: Fe(III) reduction by cellobiose dehydrogenase and Fe(II) oxidation at a distance from the hyphae
    • Hyde, S. M., and P. Wood. 1997. A mechanism for production of hydroxyl radicals by the brown-rot fungus Coniophora puteana: Fe(III) reduction by cellobiose dehydrogenase and Fe(II) oxidation at a distance from the hyphae. Microbiology 143:259-266.
    • (1997) Microbiology , vol.143 , pp. 259-266
    • Hyde, S.M.1    Wood, P.2
  • 29
    • 0014403212 scopus 로고
    • Alcohol oxidase, a flavoprotein from several basidiomycete species: Crystallization by fractional precipitation with polyethylene glycol
    • Janssen, F. W., and W. Ruelius. 1968. Alcohol oxidase, a flavoprotein from several basidiomycete species: crystallization by fractional precipitation with polyethylene glycol. Biochim. Biophys. Acta 151:330-342.
    • (1968) Biochim. Biophys. Acta , vol.151 , pp. 330-342
    • Janssen, F.W.1    Ruelius, W.2
  • 30
    • 0035379763 scopus 로고    scopus 로고
    • Pathways for extracellular Fenton chemistry in the brown rot basidiomycete Gloeophyllum trabeum
    • Jensen, Jr., K. A., C. J. Houtman, Z. C. Ryan, and K. E. Hammel. 2001. Pathways for extracellular Fenton chemistry in the brown rot basidiomycete Gloeophyllum trabeum. Appl. Environ. Microbiol. 67:2705-2711.
    • (2001) Appl. Environ. Microbiol , vol.67 , pp. 2705-2711
    • Jensen Jr., K.A.1    Houtman, C.J.2    Ryan, Z.C.3    Hammel, K.E.4
  • 31
    • 0036269033 scopus 로고    scopus 로고
    • An NADH:quinone oxidoreductase active during biodegradation by the brown-rot basidiomycete Gloeophyllum trabeum
    • Jensen, K. A., Jr., Z. C. Ryan, A. V. Wymelenberg, D. Cullen, and K. E. Hammel. 2002. An NADH:quinone oxidoreductase active during biodegradation by the brown-rot basidiomycete Gloeophyllum trabeum. Appl. Environ. Microbiol. 68:2699-2703.
    • (2002) Appl. Environ. Microbiol , vol.68 , pp. 2699-2703
    • Jensen Jr., K.A.1    Ryan, Z.C.2    Wymelenberg, A.V.3    Cullen, D.4    Hammel, K.E.5
  • 32
    • 0032985079 scopus 로고    scopus 로고
    • Biodegradative mechanisms of the brown rot basidiomycete Gloeophyllum trabeum: Evidence for an extracellular hydroquinone-driven Fenton reaction
    • Kerem, Z., K. A. Jensen, Jr., and K. E. Hammel. 1999. Biodegradative mechanisms of the brown rot basidiomycete Gloeophyllum trabeum: evidence for an extracellular hydroquinone-driven Fenton reaction. FEBS Lett. 446: 49-54.
    • (1999) FEBS Lett , vol.446 , pp. 49-54
    • Kerem, Z.1    Jensen Jr., K.A.2    Hammel, K.E.3
  • 33
    • 0027242188 scopus 로고
    • 2-producing enzyme from the lignin-degrading basidiomycete Phanerochaete chrysosporium
    • 2-producing enzyme from the lignin-degrading basidiomycete Phanerochaete chrysosporium. Proc. Natl. Acad. Sci. USA 90:7411-7413.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 7411-7413
    • Kersten, P.J.1    Cullen, D.2
  • 34
    • 0014483314 scopus 로고
    • Production of alcohol oxidase by several basidiomycetes
    • Kerwin, R. M., and H. W. Ruelius. 1969. Production of alcohol oxidase by several basidiomycetes. Appl. Microbiol. 17:347-351.
    • (1969) Appl. Microbiol , vol.17 , pp. 347-351
    • Kerwin, R.M.1    Ruelius, H.W.2
  • 35
    • 84941838891 scopus 로고
    • Characteristics of cotton cellulose depolymerized by a brown-rot fungus, by acid, or chemical oxidants
    • Kirk, T. K., R. Ibach, M. D. Mozuch, A. H. Conner, and T. L. Highley. 1991. Characteristics of cotton cellulose depolymerized by a brown-rot fungus, by acid, or chemical oxidants. Holzforschung 45:230-244.
    • (1991) Holzforschung , vol.45 , pp. 230-244
    • Kirk, T.K.1    Ibach, R.2    Mozuch, M.D.3    Conner, A.H.4    Highley, T.L.5
  • 36
    • 19644376590 scopus 로고    scopus 로고
    • Purification and characterization of intracellular and extracellular, thermostable and alkali-tolerant alcohol oxidases produced by a thermophilic fungus, Thermoascus aurantiacus NBRC 31693
    • Ko, H.-S., Y. Yokoyama, N. Ohno, M. Okadome, S. Amachi, H. Shinoyama, and T. Fujii. 2005. Purification and characterization of intracellular and extracellular, thermostable and alkali-tolerant alcohol oxidases produced by a thermophilic fungus, Thermoascus aurantiacus NBRC 31693. J. Biosci. Bioeng. 99:348-353.
    • (2005) J. Biosci. Bioeng , vol.99 , pp. 348-353
    • Ko, H.-S.1    Yokoyama, Y.2    Ohno, N.3    Okadome, M.4    Amachi, S.5    Shinoyama, H.6    Fujii, T.7
  • 37
    • 0002958405 scopus 로고
    • Hydrogen peroxide and iron: A proposed system for decomposition of wood by brown-rot basidiomycetes
    • Koenigs, J. W. 1974. Hydrogen peroxide and iron: a proposed system for decomposition of wood by brown-rot basidiomycetes. Wood Fiber Sci. 6:66-79.
    • (1974) Wood Fiber Sci , vol.6 , pp. 66-79
    • Koenigs, J.W.1
  • 38
    • 17544395540 scopus 로고
    • Molecular cloning and characterization of a gene coding for methanol oxidase in Hansenula polymorpha
    • Ledeboer, A. M., L. Edens, J. Maat, C. Visser, J. W. Bos, and C. T. Verrips. 1985. Molecular cloning and characterization of a gene coding for methanol oxidase in Hansenula polymorpha. Nucleic Acids Res. 13:3063-3082.
    • (1985) Nucleic Acids Res , vol.13 , pp. 3063-3082
    • Ledeboer, A.M.1    Edens, L.2    Maat, J.3    Visser, C.4    Bos, J.W.5    Verrips, C.T.6
  • 39
    • 0038066884 scopus 로고
    • Some oxidations involving the free hydroxyl radical
    • Merz, J. H., and W. A. Waters. 1949. Some oxidations involving the free hydroxyl radical. J. Chem. Soc. 1949:15S-25S.
    • (1949) J. Chem. Soc , vol.1949
    • Merz, J.H.1    Waters, W.A.2
  • 40
    • 0011069907 scopus 로고
    • Extracellular glucan production by Postia (=Poria) placenta
    • Micales, J. A., A. L. Richter, and T. L. Highley. 1990. Extracellular glucan production by Postia (=Poria) placenta. Mater. Org. 24:259-269.
    • (1990) Mater. Org , vol.24 , pp. 259-269
    • Micales, J.A.1    Richter, A.L.2    Highley, T.L.3
  • 41
    • 0037117777 scopus 로고    scopus 로고
    • Production of small molecular weight catalysts and the mechanism of trinitrotoluene degradation by several Gloeophyllum species
    • Newcombe, D., A. Paszczynski, W. Gajewska, M. Kroger, G. Feis, and R. Crawford. 2002. Production of small molecular weight catalysts and the mechanism of trinitrotoluene degradation by several Gloeophyllum species. Enzyme Microb. Technol. 30:506-517.
    • (2002) Enzyme Microb. Technol , vol.30 , pp. 506-517
    • Newcombe, D.1    Paszczynski, A.2    Gajewska, W.3    Kroger, M.4    Feis, G.5    Crawford, R.6
  • 44
    • 27644453559 scopus 로고    scopus 로고
    • Alcohol oxidase: A complex peroxisomal, oligomeric flavoprotein
    • Ozimek, P., M. Veenhuis, and I. J. van der Klei. 2005. Alcohol oxidase: a complex peroxisomal, oligomeric flavoprotein. FEMS Yeast Res. 5:975-983.
    • (2005) FEMS Yeast Res , vol.5 , pp. 975-983
    • Ozimek, P.1    Veenhuis, M.2    van der Klei, I.J.3
  • 45
    • 0033013291 scopus 로고    scopus 로고
    • De novo synthesis of 4,5-dimethoxycatechol and 2,5-dimethoxyhydroquinone by the brown rot fungus Gloeophyllum trabeum
    • Paszczynski, A., R. Crawford, D. Funk, and B. Goodell. 1999. De novo synthesis of 4,5-dimethoxycatechol and 2,5-dimethoxyhydroquinone by the brown rot fungus Gloeophyllum trabeum. Appl. Environ. Microbiol. 65:674-679.
    • (1999) Appl. Environ. Microbiol , vol.65 , pp. 674-679
    • Paszczynski, A.1    Crawford, R.2    Funk, D.3    Goodell, B.4
  • 46
    • 0026011630 scopus 로고
    • Involvement of an extracellular glucan sheath during degradation of Populus wood by Phanerochaete chrysosporium
    • Ruel, K., and J.-P. Joseleau. 1991. Involvement of an extracellular glucan sheath during degradation of Populus wood by Phanerochaete chrysosporium. Appl. Environ. Microbiol. 57:374-384.
    • (1991) Appl. Environ. Microbiol , vol.57 , pp. 374-384
    • Ruel, K.1    Joseleau, J.-P.2
  • 47
    • 0034129589 scopus 로고    scopus 로고
    • Hydroxylated metabolites of 2,4-dichlorophenol imply a Fenton-type reaction in Gloeophyllum striatum
    • Schlosser, D., K. Fahr, W. Karl, and H.-G. Wetzstein. 2000. Hydroxylated metabolites of 2,4-dichlorophenol imply a Fenton-type reaction in Gloeophyllum striatum. Appl. Environ. Microbiol. 66:2479-2483.
    • (2000) Appl. Environ. Microbiol , vol.66 , pp. 2479-2483
    • Schlosser, D.1    Fahr, K.2    Karl, W.3    Wetzstein, H.-G.4
  • 48
    • 0035111498 scopus 로고    scopus 로고
    • Alcohol oxidase is a novel pathogenicity factor for Cladosporium fulvum, but aldehyde dehydrogenase is dispensable
    • Segers, G., N. Bradshaw, D. Archer, K. Blissett, and R. P. Oliver. 2001. Alcohol oxidase is a novel pathogenicity factor for Cladosporium fulvum, but aldehyde dehydrogenase is dispensable. Mol. Plant-Microbe Interact. 14:367-377.
    • (2001) Mol. Plant-Microbe Interact , vol.14 , pp. 367-377
    • Segers, G.1    Bradshaw, N.2    Archer, D.3    Blissett, K.4    Oliver, R.P.5
  • 49
    • 0035895943 scopus 로고    scopus 로고
    • A novel alcohol oxidase/RNA-binding protein with affinity for mycovirus double-stranded RNA from the filamentous fungus Helminthosporium (Cochliobolus) victoriae: Molecular and functional characterization
    • Soldevila, A. I., and S. A. Ghabrial. 2001. A novel alcohol oxidase/RNA-binding protein with affinity for mycovirus double-stranded RNA from the filamentous fungus Helminthosporium (Cochliobolus) victoriae: molecular and functional characterization. J. Biol. Chem. 276:4652-4661.
    • (2001) J. Biol. Chem , vol.276 , pp. 4652-4661
    • Soldevila, A.I.1    Ghabrial, S.A.2
  • 51
    • 22944444556 scopus 로고    scopus 로고
    • Identification of four alcohol oxidases from methylotropic yeasts
    • Szamecz, B., G. Urbán, R. Rubiera, J. Kucsera, and L. Dorgai. 2005. Identification of four alcohol oxidases from methylotropic yeasts. Yeast 22:669-676.
    • (2005) Yeast , vol.22 , pp. 669-676
    • Szamecz, B.1    Urbán, G.2    Rubiera, R.3    Kucsera, J.4    Dorgai, L.5
  • 52
    • 0142104391 scopus 로고    scopus 로고
    • Effect of pH and oxalate on hydroquinone-derived hydroxyl radical formation during brown rot wood degradation
    • Varela, E., and M. Tien. 2003. Effect of pH and oxalate on hydroquinone-derived hydroxyl radical formation during brown rot wood degradation. Appl. Environ. Microbiol. 69:6025-6031.
    • (2003) Appl. Environ. Microbiol , vol.69 , pp. 6025-6031
    • Varela, E.1    Tien, M.2
  • 53
    • 0036965556 scopus 로고    scopus 로고
    • A peptide-mediated and hydroxyl radical HO·-involved oxidative degradation of cellulose by brown-rot fungi
    • Wang, W., and P. J. Gao. 2002. A peptide-mediated and hydroxyl radical HO·-involved oxidative degradation of cellulose by brown-rot fungi. Biodegradation 13:383-394.
    • (2002) Biodegradation , vol.13 , pp. 383-394
    • Wang, W.1    Gao, P.J.2
  • 54
    • 0037422225 scopus 로고    scopus 로고
    • Function and mechanism of a low-molecular-weight peptide produced by Gloeophyllum trabeum in biodegradation of cellulose
    • Wang, W., and P. J. Gao. 2003. Function and mechanism of a low-molecular-weight peptide produced by Gloeophyllum trabeum in biodegradation of cellulose. J. Biotechnol. 101:119-130.
    • (2003) J. Biotechnol , vol.101 , pp. 119-130
    • Wang, W.1    Gao, P.J.2
  • 55
    • 0031439260 scopus 로고    scopus 로고
    • Peroxisomal targeting, import, and assembly of alcohol oxidase in Pichia pastoris
    • Waterham, H. R., K. A. Russell, Y. Vries, and J. M. Cregg. 1997. Peroxisomal targeting, import, and assembly of alcohol oxidase in Pichia pastoris. J. Cell Biol. 139:1419-1431.
    • (1997) J. Cell Biol , vol.139 , pp. 1419-1431
    • Waterham, H.R.1    Russell, K.A.2    Vries, Y.3    Cregg, J.M.4
  • 56
    • 34250489053 scopus 로고
    • Über die Eigenschaften eines neuen Chromogens für die Blutzuckerbestimmung nach der GOD/POD Methode
    • Werner, W., H. G. Rey, and H. Z. Wielinger. 1970. Über die Eigenschaften eines neuen Chromogens für die Blutzuckerbestimmung nach der GOD/POD Methode. Z. Anal. Chem. 252:224-228.
    • (1970) Z. Anal. Chem , vol.252 , pp. 224-228
    • Werner, W.1    Rey, H.G.2    Wielinger, H.Z.3
  • 57
    • 0023041821 scopus 로고
    • Prediction of the occurrence of the ADP-binding βαβ-fold in proteins, using an amino acid sequence fingerprint
    • Wierenga, R. K., P. Terpstra, and W. G. Hol. 1986. Prediction of the occurrence of the ADP-binding βαβ-fold in proteins, using an amino acid sequence fingerprint. J. Mol. Biol. 187:101-107.
    • (1986) J. Mol. Biol , vol.187 , pp. 101-107
    • Wierenga, R.K.1    Terpstra, P.2    Hol, W.G.3
  • 58
    • 0035957847 scopus 로고    scopus 로고
    • Mechanisms of wood degradation by brown-rot fungi: Chelator-mediated cellulose degradation and binding of iron by cellulose
    • Xu, G., and B. Goodell. 2001. Mechanisms of wood degradation by brown-rot fungi: chelator-mediated cellulose degradation and binding of iron by cellulose. J. Biotechnol. 87:43-57.
    • (2001) J. Biotechnol , vol.87 , pp. 43-57
    • Xu, G.1    Goodell, B.2
  • 59
    • 0001038767 scopus 로고
    • Equilibrium ultracentrifugation of dilute solutions
    • Yphantis, D. A. 1964. Equilibrium ultracentrifugation of dilute solutions. Biochemistry 3:297-317.
    • (1964) Biochemistry , vol.3 , pp. 297-317
    • Yphantis, D.A.1
  • 60
    • 0024382642 scopus 로고
    • Enzymatic method for measuring the absolute values of oxygen concentration
    • Yomo, T., I. Urabe, and H. Okada. 1989. Enzymatic method for measuring the absolute values of oxygen concentration. Anal. Biochem. 179:124-126.
    • (1989) Anal. Biochem , vol.179 , pp. 124-126
    • Yomo, T.1    Urabe, I.2    Okada, H.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.