메뉴 건너뛰기




Volumn 9, Issue 12, 2010, Pages 1891-1900

Colocalization of amanitin and a candidate toxin-processing prolyl oligopeptidase in Amanita basidiocarps

Author keywords

[No Author keywords available]

Indexed keywords

AMANITIN; FUNGAL PROTEIN; PROLYL ENDOPEPTIDASE; SERINE PROTEINASE;

EID: 78649816006     PISSN: 15359778     EISSN: None     Source Type: Journal    
DOI: 10.1128/EC.00161-10     Document Type: Article
Times cited : (38)

References (37)
  • 1
    • 65949116381 scopus 로고    scopus 로고
    • Diversity of sesquiterpene synthases in the basidiomycete Coprinus cinereus
    • Agger, S., F. Lopez-Gallego, and C. Schmidt-Dannert. 2009. Diversity of sesquiterpene synthases in the basidiomycete Coprinus cinereus. Mol. Microbiol. 72:1181-1195.
    • (2009) Mol. Microbiol , vol.72 , pp. 1181-1195
    • Agger, S.1    Lopez-Gallego, F.2    Schmidt-Dannert, C.3
  • 2
    • 77952675691 scopus 로고    scopus 로고
    • Prolyl oligopeptidase of Trypanosoma brucei hydrolyzes native collagen, peptide hormones and is active in the plasma of infected mice
    • Bastos, I. M., F. N. Motta, S. Charneau, J. M. Santana, L. Dubost, K. Augustyns, and P. Grellier. 2010. Prolyl oligopeptidase of Trypanosoma brucei hydrolyzes native collagen, peptide hormones and is active in the plasma of infected mice. Microbes Infect. 12:457-466.
    • (2010) Microbes Infect , vol.12 , pp. 457-466
    • Bastos, I.M.1    Motta, F.N.2    Charneau, S.3    Santana, J.M.4    Dubost, L.5    Augustyns, K.6    Grellier, P.7
  • 4
    • 0037022279 scopus 로고    scopus 로고
    • Structural basis of transcription: Alpha-amanitin-RNA polymerase II cocrystal at 2.8 A resolution
    • Bushnell, D. A., P. Cramer, and R. D. Kornberg. 2002. Structural basis of transcription: alpha-amanitin-RNA polymerase II cocrystal at 2.8 A resolution. Proc. Natl. Acad. Sci. U. S. A. 99:1218-1222.
    • (2002) Proc. Natl. Acad. Sci. U. S. A , vol.99 , pp. 1218-1222
    • Bushnell, D.A.1    Cramer, P.2    Kornberg, R.D.3
  • 7
    • 0026579853 scopus 로고
    • Simultaneous assay for amatoxins and phallotoxins in Amanita phalloides Fr. by high-performance liquid chromatography
    • Enjalbert, F., C. Gallion, F. Jehl, H. Monteil, and H. Faulstich. 1992. Simultaneous assay for amatoxins and phallotoxins in Amanita phalloides Fr. by high-performance liquid chromatography. J. Chromatogr. 598:227-236.
    • (1992) J. Chromatogr , vol.598 , pp. 227-236
    • Enjalbert, F.1    Gallion, C.2    Jehl, F.3    Monteil, H.4    Faulstich, H.5
  • 8
    • 0032727275 scopus 로고    scopus 로고
    • Distribution of the amatoxins and phallotoxins in Amanita phalloides. Influence of the tissues and the collection site
    • Enjalbert, F., G. Cassanas, S. L. Salhi, C. Guinchard, and J.-P. Chaumont. 1999. Distribution of the amatoxins and phallotoxins in Amanita phalloides. Influence of the tissues and the collection site. C. R. Hebd. Seances Acad. Sci. III 322:855-862.
    • (1999) C. R. Hebd. Seances Acad. Sci , vol.3 , Issue.322 , pp. 855-862
    • Enjalbert, F.1    Cassanas, G.2    Salhi, S.L.3    Guinchard, C.4    Chaumont, J.-P.5
  • 9
    • 69549111337 scopus 로고    scopus 로고
    • Antibiotics for emerging pathogens
    • Fischbach, M. A., and C. T. Walsh. 2009. Antibiotics for emerging pathogens. Science 325:1089-1093.
    • (2009) Science , vol.325 , pp. 1089-1093
    • Fischbach, M.A.1    Walsh, C.T.2
  • 11
    • 0141595150 scopus 로고    scopus 로고
    • Taxonomy and toxicity of Conocybe lactea and related species
    • Hallen, H. E., R. Watling, and G. C. Adams. 2003. Taxonomy and toxicity of Conocybe lactea and related species. Mycol. Res. 107:969-979.
    • (2003) Mycol. Res , vol.107 , pp. 969-979
    • Hallen, H.E.1    Watling, R.2    Adams, G.C.3
  • 12
    • 0030047867 scopus 로고    scopus 로고
    • The presence and antifeedant function of toxin-producing secretory cells on hyphae of the lawn-inhabiting agaric Conocybe lactea
    • Hutchison, L. J., S. E. Madzia, and G. L. Barron. 1996. The presence and antifeedant function of toxin-producing secretory cells on hyphae of the lawn-inhabiting agaric Conocybe lactea. Can. J. Bot. 74:431-434.
    • (1996) Can. J. Bot , vol.74 , pp. 431-434
    • Hutchison, L.J.1    Madzia, S.E.2    Barron, G.L.3
  • 14
    • 0022617548 scopus 로고
    • Purification of amatoxin-specific antibodies from rabbit sera by affinity chromatography, their characterization and use in toxicological studies
    • Kirchner, K., and H. Faulstich. 1986. Purification of amatoxin-specific antibodies from rabbit sera by affinity chromatography, their characterization and use in toxicological studies. Toxicon 24:273-283.
    • (1986) Toxicon , vol.24 , pp. 273-283
    • Kirchner, K.1    Faulstich, H.2
  • 16
    • 18044396993 scopus 로고    scopus 로고
    • A role for intra- and intercellular translocation in natural product biosynthesis
    • Kutchan, T. M. 2005. A role for intra- and intercellular translocation in natural product biosynthesis. Curr. Opin. Plant Biol. 8:292-300.
    • (2005) Curr. Opin. Plant Biol , vol.8 , pp. 292-300
    • Kutchan, T.M.1
  • 17
    • 0013660206 scopus 로고
    • How to identify mushrooms to genus
    • Mad River Press, Eureka, CA
    • Largent, D. L., and D. Johnson. 1977. How to identify mushrooms to genus. III. Microscopic features, p. 71-88. Mad River Press, Eureka, CA.
    • (1977) III. Microscopic Features , pp. 71-88
    • Largent, D.L.1    Johnson, D.2
  • 18
    • 67650594524 scopus 로고    scopus 로고
    • Processing of the phalloidin proprotein by prolyl oligopeptidase from the mushroom Conocybe albipes
    • Luo, H., H. E. Hallen-Adams, and J. D. Walton. 2009. Processing of the phalloidin proprotein by prolyl oligopeptidase from the mushroom Conocybe albipes. J. Biol. Chem. 284:18070-18077.
    • (2009) J. Biol. Chem , vol.284 , pp. 18070-18077
    • Luo, H.1    Hallen-Adams, H.E.2    Walton, J.D.3
  • 19
    • 35048844271 scopus 로고    scopus 로고
    • Tryptathionine bridges in peptide synthesis
    • May, J. P., and D. M. Perrin. 2007. Tryptathionine bridges in peptide synthesis. Pept. Sci. 88:714-724.
    • (2007) Pept. Sci , vol.88 , pp. 714-724
    • May, J.P.1    Perrin, D.M.2
  • 20
    • 67649604461 scopus 로고    scopus 로고
    • Ribosomal peptide natural products: Bridging the ribosomal and nonribosomal worlds
    • McIntosh, J. A., M. S. Donia, and E. W. Schmidt. 2009. Ribosomal peptide natural products: bridging the ribosomal and nonribosomal worlds. Nat. Prod. Rep. 26:537-559.
    • (2009) Nat. Prod. Rep , vol.26 , pp. 537-559
    • McIntosh, J.A.1    Donia, M.S.2    Schmidt, E.W.3
  • 21
    • 77955875685 scopus 로고    scopus 로고
    • Amatoxin and phallotoxin concentration in Amanita bisporigera spores
    • McKnight, T. A., K. B. McKnight, and M. C. Skeels. 2010. Amatoxin and phallotoxin concentration in Amanita bisporigera spores. Mycologia 102:763-765.
    • (2010) Mycologia , vol.102 , pp. 763-765
    • McKnight, T.A.1    McKnight, K.B.2    Skeels, M.C.3
  • 22
    • 64049118903 scopus 로고    scopus 로고
    • Reduced genomic potential for secreted plant cell-walldegrading enzymes in the ectomycorrhizal fungus Amanita bisporigera, based on the secretome of Trichoderma reesei
    • Nagendran, S., H. E. Hallen-Adams, J. M. Paper, N. Aslam, and J. D. Walton. 2009. Reduced genomic potential for secreted plant cell-walldegrading enzymes in the ectomycorrhizal fungus Amanita bisporigera, based on the secretome of Trichoderma reesei. Fung. Genet. Biol. 46:427-435.
    • (2009) Fung. Genet. Biol , vol.46 , pp. 427-435
    • Nagendran, S.1    Hallen-Adams, H.E.2    Paper, J.M.3    Aslam, N.4    Walton, J.D.5
  • 23
    • 36549088142 scopus 로고    scopus 로고
    • Defensive role of cystidia against Collembola in thebasidiomycetes Russula bella and Strobilurus ohshimae
    • Nakamori, T., and A. Suzuki. 2007. Defensive role of cystidia against Collembola in thebasidiomycetes Russula bella and Strobilurus ohshimae. Mycol. Res. 111:1345-1351.
    • (2007) Mycol. Res , vol.111 , pp. 1345-1351
    • Nakamori, T.1    Suzuki, A.2
  • 24
    • 72449148123 scopus 로고    scopus 로고
    • Peptidomics of prolyl endopeptidase in the central nervous system
    • Nolte, W. M., D. M. Tagore, W. S. Lane, and A. Saghatelian. 2009. Peptidomics of prolyl endopeptidase in the central nervous system. Biochemistry 48:11971-11981.
    • (2009) Biochemistry , vol.48 , pp. 11971-11981
    • Nolte, W.M.1    Tagore, D.M.2    Lane, W.S.3    Saghatelian, A.4
  • 25
    • 74049115080 scopus 로고    scopus 로고
    • Follow the leader: The use of leader peptides to guide natural product biosynthesis
    • Oman, T. J., and W. A. van der Donk. 2010. Follow the leader: the use of leader peptides to guide natural product biosynthesis. Nat. Chem. Biol. 6:9-18.
    • (2010) Nat. Chem. Biol , vol.6 , pp. 9-18
    • Oman, T.J.1    van der Donk, W.A.2
  • 26
    • 78650208991 scopus 로고    scopus 로고
    • Compartmentalization and molecular traffic in secondary metabolism: A new understanding of established cellular processes
    • in press. doi:10.1016/ j.fgb.2010.05.006
    • Roze, L. V., A. Chanda, and J. E. Linz. Compartmentalization and molecular traffic in secondary metabolism: a new understanding of established cellular processes. Fungal Genet. Biol., in press. doi:10.1016/ j.fgb.2010.05.006.
    • Fungal Genet. Biol
    • Roze, L.V.1    Chanda, A.2    Linz, J.E.3
  • 27
    • 55149109662 scopus 로고    scopus 로고
    • Characterization of the atromentin biosynthesis genes and enzymes in the homobasidiomycete Tapinella panuoides
    • Schneider, P., S. Bouhired, and D. Hoffmeister. 2008. Characterization of the atromentin biosynthesis genes and enzymes in the homobasidiomycete Tapinella panuoides. Fungal Genet. Biol. 45:1487-1496.
    • (2008) Fungal Genet. Biol , vol.45 , pp. 1487-1496
    • Schneider, P.1    Bouhired, S.2    Hoffmeister, D.3
  • 28
    • 0025576522 scopus 로고
    • Endopolygalacturonase is not required for pathogenicity of Cochliobolus carbonum on maize
    • Scott-Craig, J. S., D. G. Panaccione, F. Cervone, and J. D. Walton. 1990. Endopolygalacturonase is not required for pathogenicity of Cochliobolus carbonum on maize. Plant Cell 2:1191-1200.
    • (1990) Plant Cell , vol.2 , pp. 1191-1200
    • Scott-Craig, J.S.1    Panaccione, D.G.2    Cervone, F.3    Walton, J.D.4
  • 29
    • 41949135032 scopus 로고    scopus 로고
    • Structure, function and biological relevance of prolyl oligopeptidase
    • Szeltner, Z., and L. Polgár. 2008. Structure, function and biological relevance of prolyl oligopeptidase. Curr. Protein Pept. Sci. 9:96-107.
    • (2008) Curr. Protein Pept. Sci , vol.9 , pp. 96-107
    • Szeltner, Z.1
  • 31
    • 77649305354 scopus 로고    scopus 로고
    • Natural products version 2.0: Connecting genes to molecules
    • Walsh, C. T., and M. A. Fischbach. 2010. Natural products version 2.0: connecting genes to molecules. J. Am. Chem. Soc. 132:2469-2493.
    • (2010) J. Am. Chem. Soc , vol.132 , pp. 2469-2493
    • Walsh, C.T.1    Fischbach, M.A.2
  • 32
    • 0033762670 scopus 로고    scopus 로고
    • Horizontal gene transfer and the evolution of secondary metabolite gene clusters in fungi: An hypothesis
    • Walton, J. D. 2000. Horizontal gene transfer and the evolution of secondary metabolite gene clusters in fungi: an hypothesis. Fungal Genet. Biol. 30:167-171.
    • (2000) Fungal Genet. Biol , vol.30 , pp. 167-171
    • Walton, J.D.1
  • 34
    • 33644887475 scopus 로고    scopus 로고
    • Genes expressed in a turrid venom duct: Divergence and similarity to conotoxins
    • Watkins, M., D. R. Hillyard, and B. M. Olivera. 2006. Genes expressed in a turrid venom duct: divergence and similarity to conotoxins. J. Mol. Evol. 62:247-256.
    • (2006) J. Mol. Evol , vol.62 , pp. 247-256
    • Watkins, M.1    Hillyard, D.R.2    Olivera, B.M.3
  • 35
    • 22144450632 scopus 로고    scopus 로고
    • Characterization of the ferrichrome A biosynthetic gene cluster in the homobasidiomycete Omphalotus olearius
    • Welzel, K., K. Eisfeld, L. Antelo, T. Anke, and H. Anke. 2005. Characterization of the ferrichrome A biosynthetic gene cluster in the homobasidiomycete Omphalotus olearius. FEMS Microbiol. Lett. 249:157-163.
    • (2005) FEMS Microbiol. Lett , vol.249 , pp. 157-163
    • Welzel, K.1    Eisfeld, K.2    Antelo, L.3    Anke, T.4    Anke, H.5
  • 37
    • 27444445936 scopus 로고    scopus 로고
    • Production and characterization of amanitin toxins from a pure culture of Amanita exitialis
    • Zhang, P., Z. Chen, J. Hu, B. Ei, Z. Zhang, and W. Hu. 2005. Production and characterization of amanitin toxins from a pure culture of Amanita exitialis. FEMS Microbiol. Lett. 252:223-228.
    • (2005) FEMS Microbiol. Lett , vol.252 , pp. 223-228
    • Zhang, P.1    Chen, Z.2    Hu, J.3    Ei, B.4    Zhang, Z.5    Hu, W.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.