The world's first wiki where authorship really matters (Nature Genetics, 2008). Due credit and reputation for authors. Imagine a global collaborative knowledge base for original thoughts. Search thousands of articles and collaborate with scientists around the globe.

wikigene or wiki gene protein drug chemical gene disease author authorship tracking collaborative publishing evolutionary knowledge reputation system wiki2.0 global collaboration genes proteins drugs chemicals diseases compound
Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
MeSH Review


Welcome! If you are familiar with the subject of this article, you can contribute to this open access knowledge base by deleting incorrect information, restructuring or completely rewriting any text. Read more.

Disease relevance of Phanerochaete


High impact information on Phanerochaete


Biological context of Phanerochaete


Anatomical context of Phanerochaete


Associations of Phanerochaete with chemical compounds


Gene context of Phanerochaete


Analytical, diagnostic and therapeutic context of Phanerochaete


  1. The trpC gene of Phanerochaete chrysosporium is unique in containing an intron but nevertheless maintains the order of functional domains seen in other fungi. Schrank, A., Tempelaars, C., Sims, P.F., Oliver, S.G., Broda, P. Mol. Microbiol. (1991) [Pubmed]
  2. Heterologous expression of active manganese peroxidase from Phanerochaete chrysosporium using the baculovirus expression system. Pease, E.A., Aust, S.D., Tien, M. Biochem. Biophys. Res. Commun. (1991) [Pubmed]
  3. Enhanced production of manganese peroxidase from immobilized Phanerochaete chrysosporium due to the increased autolysis of chlamydospore-like cells. Chung, E., Oh, J., Hwang, S., Ahn, I.S., Yoon, Y.J. Biotechnol. Lett. (2005) [Pubmed]
  4. Cloning and sequencing of a cDNA for a ligninase from Phanerochaete chrysosporium. Tien, M., Tu, C.P. Nature (1987) [Pubmed]
  5. Oxidation of persistent environmental pollutants by a white rot fungus. Bumpus, J.A., Tien, M., Wright, D., Aust, S.D. Science (1985) [Pubmed]
  6. Biodegradation of nitroaromatic compounds. Spain, J.C. Annu. Rev. Microbiol. (1995) [Pubmed]
  7. cAMP-mediated differential regulation of lignin peroxidase and manganese-dependent peroxidase production in the white-rot basidiomycete Phanerochaete chrysosporium. Boominathan, K., Reddy, C.A. Proc. Natl. Acad. Sci. U.S.A. (1992) [Pubmed]
  8. Ring fission of anthracene by a eukaryote. Hammel, K.E., Green, B., Gai, W.Z. Proc. Natl. Acad. Sci. U.S.A. (1991) [Pubmed]
  9. Phosphorylation of lignin peroxidases from Phanerochaete chrysosporium. Identification of mannose 6-phosphate. Kuan, I.C., Tien, M. J. Biol. Chem. (1989) [Pubmed]
  10. Kinetics of inter-domain electron transfer in flavocytochrome cellobiose dehydrogenase from the white-rot fungus Phanerochaete chrysosporium. Igarashi, K., Momohara, I., Nishino, T., Samejima, M. Biochem. J. (2002) [Pubmed]
  11. Polarimetry and 13C n.m.r. show that the hydrolyses of beta-D-glucopyranosyl fluoride by beta(1-->3)-glucanases from Phanerochaete chrysosporium and Sporotrichum dimorphosporum have opposite stereochemistries. Copa-Patiño, J.L., Zhang, Y., Padmaperuma, B., Marsden, I., Broda, P., Sinnott, M.L. Biochem. J. (1993) [Pubmed]
  12. Reverse transcription-PCR analysis of the regulation of the manganese peroxidase gene family. Gettemy, J.M., Ma, B., Alic, M., Gold, M.H. Appl. Environ. Microbiol. (1998) [Pubmed]
  13. Cellobiose dehydrogenase from Phanerochaete chrysosporium is encoded by two allelic variants. Li, B., Nagalla, S.R., Renganathan, V. Appl. Environ. Microbiol. (1997) [Pubmed]
  14. Plasma membrane dependent reduction of 2,4,6-trinitrotoluene by Phanerochaete chrysosporium. Stahl, J.D., Aust, S.D. Biochem. Biophys. Res. Commun. (1993) [Pubmed]
  15. Evidence that cellobiose oxidase from Phanerochaete chrysosporium is primarily an Fe(III) reductase. Kinetic comparison with neutrophil NADPH oxidase and yeast flavocytochrome b2. Kremer, S.M., Wood, P.M. Eur. J. Biochem. (1992) [Pubmed]
  16. Cellobiose dehydrogenase from the fungi Phanerochaete chrysosporium and Humicola insolens. A flavohemoprotein from Humicola insolens contains 6-hydroxy-FAD as the dominant active cofactor. Igarashi, K., Verhagen, M.F., Samejima, M., Schülein, M., Eriksson, K.E., Nishino, T. J. Biol. Chem. (1999) [Pubmed]
  17. Steady-state and transient-state kinetic studies on the oxidation of 3,4-dimethoxybenzyl alcohol catalyzed by the ligninase of Phanerocheate chrysosporium Burds. Tien, M., Kirk, T.K., Bull, C., Fee, J.A. J. Biol. Chem. (1986) [Pubmed]
  18. Iodide as the mediator for the reductive reactions of peroxidases. Shah, M.M., Aust, S.D. J. Biol. Chem. (1993) [Pubmed]
  19. Comparison of lignin peroxidase, horseradish peroxidase and laccase in the oxidation of methoxybenzenes. Kersten, P.J., Kalyanaraman, B., Hammel, K.E., Reinhammar, B., Kirk, T.K. Biochem. J. (1990) [Pubmed]
  20. Cytochrome P450 oxidoreductase gene and its differentially terminated cDNAs from the white rot fungus Phanerochaete chrysosporium. Yadav, J.S., Loper, J.C. Curr. Genet. (2000) [Pubmed]
  21. Cloning of Phanerochaete chrysosporium leu2 by complementation of bacterial auxotrophs and transformation of fungal auxotrophs. Zapanta, L.S., Hattori, T., Rzetskaya, M., Tien, M. Appl. Environ. Microbiol. (1998) [Pubmed]
  22. Crystal structure of the fungal peroxidase from Arthromyces ramosus at 1.9 A resolution. Structural comparisons with the lignin and cytochrome c peroxidases. Kunishima, N., Fukuyama, K., Matsubara, H., Hatanaka, H., Shibano, Y., Amachi, T. J. Mol. Biol. (1994) [Pubmed]
  23. Cloning of several lignin peroxidase (LIP)-encoding genes: sequence analysis of the LIP6 gene from the white-rot basidiomycete, Phanerochaete chrysosporium. Zhang, Y.Z., Reddy, C.A., Rasooly, A. Gene (1991) [Pubmed]
  24. Purification and characterization of glucose oxidase from ligninolytic cultures of Phanerochaete chrysosporium. Kelley, R.L., Reddy, C.A. J. Bacteriol. (1986) [Pubmed]
  25. Cloning and analysis of Pycnoporus cinnabarinus cellobiose dehydrogenase. Moukha, S.M., Dumonceaux, T.J., Record, E., Archibald, F.S. Gene (1999) [Pubmed]
WikiGenes - Universities