메뉴 건너뛰기




Volumn 31, Issue 10, 2014, Pages 1277-1286

Spatial and temporal control of fungal natural product synthesis

Author keywords

[No Author keywords available]

Indexed keywords

BIOLOGICAL PRODUCT;

EID: 84907156522     PISSN: 02650568     EISSN: 14604752     Source Type: Journal    
DOI: 10.1039/c4np00083h     Document Type: Article
Times cited : (63)

References (87)
  • 1
    • 84876002671 scopus 로고    scopus 로고
    • Natural products: A continuing source of novel drug leads
    • G. M. Cragg D. J. Newman Natural products: a continuing source of novel drug leads Biochim. Biophys. Acta 2013 1830 3670 3695
    • (2013) Biochim. Biophys. Acta , vol.1830 , pp. 3670-3695
    • Cragg, G.M.1    Newman, D.J.2
  • 2
    • 0000378637 scopus 로고
    • On the antibacterial action of cultures of a Penicillium, with special reference to their use in the isolation of B. Influenzae
    • A. Fleming On the antibacterial action of cultures of a Penicillium, with special reference to their use in the isolation of B. influenzae Br. J. Exp. Pathol. 1929 10 226 236
    • (1929) Br. J. Exp. Pathol. , vol.10 , pp. 226-236
    • Fleming, A.1
  • 3
    • 33947694781 scopus 로고    scopus 로고
    • Natural products of filamentous fungi: Enzymes, genes, and their regulation
    • D. Hoffmeister N. Keller Natural products of filamentous fungi: enzymes, genes, and their regulation Nat. Prod. Rep. 2007 24 393 416
    • (2007) Nat. Prod. Rep. , vol.24 , pp. 393-416
    • Hoffmeister, D.1    Keller, N.2
  • 4
    • 77954663320 scopus 로고    scopus 로고
    • Self-protection against gliotoxin-A component of the gliotoxin biosynthetic cluster, gliT, completely protects Aspergillus fumigatus against exogenous gliotoxin
    • M. Schrettl S. Carberry K. Kavanagh H. Haas G. Jones J. O'Brien A. Nolan J. Stephens O. Fenelon S. Doyle Self-protection against gliotoxin-A component of the gliotoxin biosynthetic cluster, gliT, completely protects Aspergillus fumigatus against exogenous gliotoxin PLoS Pathog. 2010 6 e1000952
    • (2010) PLoS Pathog. , vol.6 , pp. 1000952
    • Schrettl, M.1    Carberry, S.2    Kavanagh, K.3    Haas, H.4    Jones, G.5    O'Brien, J.6    Nolan, A.7    Stephens, J.8    Fenelon, O.9    Doyle, S.10
  • 5
    • 0031079973 scopus 로고    scopus 로고
    • Metabolic Pathway Gene Clusters in Filamentous Fungi
    • N. Keller T. Hohn Metabolic Pathway Gene Clusters in Filamentous Fungi Fungal Genet. Biol. 1997 21 17 29
    • (1997) Fungal Genet. Biol. , vol.21 , pp. 17-29
    • Keller, N.1    Hohn, T.2
  • 6
    • 84871292787 scopus 로고    scopus 로고
    • Regulation of fungal secondary metabolism
    • A. A. Brakhage Regulation of fungal secondary metabolism Nat. Rev. Microbiol. 2013 11 21 32
    • (2013) Nat. Rev. Microbiol. , vol.11 , pp. 21-32
    • Brakhage, A.A.1
  • 7
    • 79959769183 scopus 로고    scopus 로고
    • Transcriptional regulatory elements in fungal secondary metabolism
    • W. Yin N. P. Keller Transcriptional regulatory elements in fungal secondary metabolism J. Microbiol. 2011 49 329 339
    • (2011) J. Microbiol. , vol.49 , pp. 329-339
    • Yin, W.1    Keller, N.P.2
  • 8
    • 77955428831 scopus 로고    scopus 로고
    • Secondary metabolism in fungi: Does chromosomal location matter?
    • J. M. Palmer N. P. Keller Secondary metabolism in fungi: does chromosomal location matter? Curr. Opin. Microbiol. 2010 13 431 436
    • (2010) Curr. Opin. Microbiol. , vol.13 , pp. 431-436
    • Palmer, J.M.1    Keller, N.P.2
  • 9
    • 0033817260 scopus 로고    scopus 로고
    • The evolution of secondary metabolism-A unifying model
    • R. D. Firn C. G. Jones The evolution of secondary metabolism-A unifying model Mol. Microbiol. 2000 37 989 994
    • (2000) Mol. Microbiol. , vol.37 , pp. 989-994
    • Firn, R.D.1    Jones, C.G.2
  • 10
    • 0034887171 scopus 로고    scopus 로고
    • Polyketide biosynthesis: A millennium review
    • J. Staunton K. J. Weissman Polyketide biosynthesis: a millennium review Nat. Prod. Rep. 2001 18 380 416
    • (2001) Nat. Prod. Rep. , vol.18 , pp. 380-416
    • Staunton, J.1    Weissman, K.J.2
  • 11
    • 0021894235 scopus 로고
    • Carotenoid synthesis in Neurospora crassa
    • W. Rau U. Mitzka-Schnabel Carotenoid synthesis in Neurospora crassa Methods Enzymol. 1985 110 253 267
    • (1985) Methods Enzymol. , vol.110 , pp. 253-267
    • Rau, W.1    Mitzka-Schnabel, U.2
  • 12
    • 0035021637 scopus 로고    scopus 로고
    • Structure, synthesis, and biosynthesis of fumonisin B1 and related compounds
    • J. W. ApSimon Structure, synthesis, and biosynthesis of fumonisin B1 and related compounds Environ. Health Perspect. 2001 109 suppl. 2 245 249
    • (2001) Environ. Health Perspect. , vol.109 , pp. 245-249
    • Apsimon, J.W.1
  • 15
    • 78650208991 scopus 로고    scopus 로고
    • Compartmentalization and molecular traffic in secondary metabolism: A new understanding of established cellular processes
    • L. V. Roze A. Chanda J. E. Linz Compartmentalization and molecular traffic in secondary metabolism: a new understanding of established cellular processes Fungal Genet. Biol. 2011 48 35 48
    • (2011) Fungal Genet. Biol. , vol.48 , pp. 35-48
    • Roze, L.V.1    Chanda, A.2    Linz, J.E.3
  • 16
    • 23044485041 scopus 로고    scopus 로고
    • Fundamental contribution of beta-oxidation to polyketide mycotoxin production in planta
    • L. A. Maggio-Hall R. A. Wilson N. P. Keller Fundamental contribution of beta-oxidation to polyketide mycotoxin production in planta Mol. Plant-Microbe Interact. 2005 18 783 793
    • (2005) Mol. Plant-Microbe Interact. , vol.18 , pp. 783-793
    • Maggio-Hall, L.A.1    Wilson, R.A.2    Keller, N.P.3
  • 18
    • 0030448870 scopus 로고    scopus 로고
    • Pyruvate metabolism in Saccharomyces cerevisiae
    • J. T. Pronk H. Yde Steensma J. P. Van Dijken Pyruvate metabolism in Saccharomyces cerevisiae Yeast 1996 12 1607 1633
    • (1996) Yeast , vol.12 , pp. 1607-1633
    • Pronk, J.T.1    Yde Steensma, H.2    Van Dijken, J.P.3
  • 19
    • 0028989612 scopus 로고
    • A second branched-chain alpha-keto acid dehydrogenase gene cluster (bkdFGH) from Streptomyces avermitilis: Its relationship to avermectin biosynthesis and the construction of a bkdF mutant suitable for the production of novel antiparasitic avermectins
    • C. D. Denoya R. W. Fedechko E. W. Hafner H. A. McArthur M. R. Morgenstern D. D. Skinner K. Stutzman-Engwall R. G. Wax W. C. Wernau A second branched-chain alpha-keto acid dehydrogenase gene cluster (bkdFGH) from Streptomyces avermitilis: its relationship to avermectin biosynthesis and the construction of a bkdF mutant suitable for the production of novel antiparasitic avermectins J. Bacteriol. 1995 177 3504 3511
    • (1995) J. Bacteriol. , vol.177 , pp. 3504-3511
    • Denoya, C.D.1    Fedechko, R.W.2    Hafner, E.W.3    McArthur, H.A.4    Morgenstern, M.R.5    Skinner, D.D.6    Stutzman-Engwall, K.7    Wax, R.G.8    Wernau, W.C.9
  • 20
    • 57649157673 scopus 로고    scopus 로고
    • Branched-chain amino acid catabolism provides precursors for the Type II polyketide antibiotic, actinorhodin, via pathways that are nutrient dependent
    • K. Stirrett C. Denoya J. Westpheling Branched-chain amino acid catabolism provides precursors for the Type II polyketide antibiotic, actinorhodin, via pathways that are nutrient dependent J. Ind. Microbiol. Biotechnol. 2009 36 129 137
    • (2009) J. Ind. Microbiol. Biotechnol. , vol.36 , pp. 129-137
    • Stirrett, K.1    Denoya, C.2    Westpheling, J.3
  • 21
    • 84904967255 scopus 로고    scopus 로고
    • Co-ordination between BrlA regulation and secretion of the oxidoreductase FmqD directs selective accumulation of fumiquinazoline C to conidial tissues in Aspergillus fumigatus
    • F. Y. Lim B. Ames C. T. Walsh N. P. Keller Co-ordination between BrlA regulation and secretion of the oxidoreductase FmqD directs selective accumulation of fumiquinazoline C to conidial tissues in Aspergillus fumigatus Cell. Microbiol. 2014 16 1267 1283
    • (2014) Cell. Microbiol. , vol.16 , pp. 1267-1283
    • Lim, F.Y.1    Ames, B.2    Walsh, C.T.3    Keller, N.P.4
  • 22
    • 34547675748 scopus 로고    scopus 로고
    • The Arabidopsis MATE transporter TT12 acts as a vacuolar flavonoid/H+ -Antiporter active in proanthocyanidin-Accumulating cells of the seed coat
    • K. Marinova L. Pourcel B. Weder M. Schwarz D. Barron J. M. Routaboul I. Debeaujon M. Klein The Arabidopsis MATE transporter TT12 acts as a vacuolar flavonoid/H+ -Antiporter active in proanthocyanidin-Accumulating cells of the seed coat Plant Cell 2007 19 2023 2038
    • (2007) Plant Cell , vol.19 , pp. 2023-2038
    • Marinova, K.1    Pourcel, L.2    Weder, B.3    Schwarz, M.4    Barron, D.5    Routaboul, J.M.6    Debeaujon, I.7    Klein, M.8
  • 23
    • 33846581959 scopus 로고    scopus 로고
    • New insight into the structures and formation of anthocyanic vacuolar inclusions in flower petals
    • H. Zhang L. Wang S. Deroles R. Bennett K. Davies New insight into the structures and formation of anthocyanic vacuolar inclusions in flower petals BMC Plant Biol. 2006 6 29
    • (2006) BMC Plant Biol. , vol.6 , pp. 29
    • Zhang, H.1    Wang, L.2    Deroles, S.3    Bennett, R.4    Davies, K.5
  • 24
    • 44949127129 scopus 로고    scopus 로고
    • Alkaloid biosynthesis: Metabolism and trafficking
    • J. Ziegler P. J. Facchini Alkaloid biosynthesis: metabolism and trafficking Annu. Rev. Plant Biol. 2008 59 735 769
    • (2008) Annu. Rev. Plant Biol. , vol.59 , pp. 735-769
    • Ziegler, J.1    Facchini, P.J.2
  • 25
    • 77953486651 scopus 로고    scopus 로고
    • Contribution of peroxisomes to secondary metabolism and pathogenicity in the fungal plant pathogen Alternaria alternata
    • A. Imazaki A. Tanaka Y. Harimoto M. Yamamoto K. Akimitsu P. Park T. Tsuge Contribution of peroxisomes to secondary metabolism and pathogenicity in the fungal plant pathogen Alternaria alternata Eukaryotic Cell 2010 9 682 694
    • (2010) Eukaryotic Cell , vol.9 , pp. 682-694
    • Imazaki, A.1    Tanaka, A.2    Harimoto, Y.3    Yamamoto, M.4    Akimitsu, K.5    Park, P.6    Tsuge, T.7
  • 26
    • 80052805066 scopus 로고    scopus 로고
    • The significance of peroxisomes in secondary metabolite biosynthesis in filamentous fungi
    • M. Bartoszewska L. Opalinski M. Veenhuis I. J. van der Klei The significance of peroxisomes in secondary metabolite biosynthesis in filamentous fungi Biotechnol. Lett. 2011 33 1921 1931
    • (2011) Biotechnol. Lett. , vol.33 , pp. 1921-1931
    • Bartoszewska, M.1    Opalinski, L.2    Veenhuis, M.3    Van Der Klei, I.J.4
  • 27
    • 67349265180 scopus 로고    scopus 로고
    • Purification of a vesicle-vacuole fraction functionally linked to aflatoxin synthesis in Aspergillus parasiticus
    • A. Chanda L. V. Roze A. Pastor M. K. Frame J. E. Linz Purification of a vesicle-vacuole fraction functionally linked to aflatoxin synthesis in Aspergillus parasiticus J. Microbiol. Methods 2009 78 28 33
    • (2009) J. Microbiol. Methods , vol.78 , pp. 28-33
    • Chanda, A.1    Roze, L.V.2    Pastor, A.3    Frame, M.K.4    Linz, J.E.5
  • 29
    • 84859833488 scopus 로고    scopus 로고
    • Role of peroxisomes in the biosynthesis and secretion of beta-lactams and other secondary metabolites
    • J. F. Martin R. V. Ullan C. Garcia-Estrada Role of peroxisomes in the biosynthesis and secretion of beta-lactams and other secondary metabolites J. Ind. Microbiol. Biotechnol. 2012 39 367 382
    • (2012) J. Ind. Microbiol. Biotechnol. , vol.39 , pp. 367-382
    • Martin, J.F.1    Ullan, R.V.2    Garcia-Estrada, C.3
  • 30
    • 77349092837 scopus 로고    scopus 로고
    • Peroxisome diversity and evolution
    • T. Gabaldon Peroxisome diversity and evolution Philos. Trans. R. Soc., B 2010 365 765 773
    • (2010) Philos. Trans. R. Soc., B , vol.365 , pp. 765-773
    • Gabaldon, T.1
  • 31
    • 84905790777 scopus 로고    scopus 로고
    • The versatility of peroxisome function in filamentous fungi
    • I. J. Van der Klei M. Veenhuis The versatility of peroxisome function in filamentous fungi Subcell. Biochem. 2013 69 135 152
    • (2013) Subcell. Biochem. , vol.69 , pp. 135-152
    • Van Der Klei, I.J.1    Veenhuis, M.2
  • 32
    • 38749103478 scopus 로고    scopus 로고
    • Making two organelles from one: Woronin body biogenesis by peroxisomal protein sorting
    • F. Liu S. K. Ng Y. Lu W. Low J. Lai G. Jedd Making two organelles from one: Woronin body biogenesis by peroxisomal protein sorting J. Cell Biol. 2008 180 325 339
    • (2008) J. Cell Biol. , vol.180 , pp. 325-339
    • Liu, F.1    Ng, S.K.2    Lu, Y.3    Low, W.4    Lai, J.5    Jedd, G.6
  • 33
    • 34247340584 scopus 로고    scopus 로고
    • Functional analysis of lipid metabolism in Magnaporthe grisea reveals a requirement for peroxisomal fatty acid beta-oxidation during appressorium-mediated plant infection
    • Z. Y. Wang D. M. Soanes M. J. Kershaw N. J. Talbot Functional analysis of lipid metabolism in Magnaporthe grisea reveals a requirement for peroxisomal fatty acid beta-oxidation during appressorium-mediated plant infection Mol. Plant-Microbe Interact. 2007 20 475 491
    • (2007) Mol. Plant-Microbe Interact. , vol.20 , pp. 475-491
    • Wang, Z.Y.1    Soanes, D.M.2    Kershaw, M.J.3    Talbot, N.J.4
  • 34
    • 33745204227 scopus 로고    scopus 로고
    • Peroxisomal carnitine acetyl transferase is required for elaboration of penetration hyphae during plant infection by Magnaporthe grisea
    • G. K. Bhambra Z. Y. Wang D. M. Soanes G. E. Wakley N. J. Talbot Peroxisomal carnitine acetyl transferase is required for elaboration of penetration hyphae during plant infection by Magnaporthe grisea Mol. Microbiol. 2006 61 46 60
    • (2006) Mol. Microbiol. , vol.61 , pp. 46-60
    • Bhambra, G.K.1    Wang, Z.Y.2    Soanes, D.M.3    Wakley, G.E.4    Talbot, N.J.5
  • 35
    • 33748785145 scopus 로고    scopus 로고
    • Multiple contributions of peroxisomal metabolic function to fungal pathogenicity in Colletotrichum lagenarium
    • M. Asakura T. Okuno Y. Takano Multiple contributions of peroxisomal metabolic function to fungal pathogenicity in Colletotrichum lagenarium Appl. Environ. Microbiol. 2006 72 6345 6354
    • (2006) Appl. Environ. Microbiol. , vol.72 , pp. 6345-6354
    • Asakura, M.1    Okuno, T.2    Takano, Y.3
  • 37
    • 0033837581 scopus 로고    scopus 로고
    • Structural and functional complexity of the genomic region controlling AK-toxin biosynthesis and pathogenicity in the Japanese pear pathotype of Alternaria alternata
    • A. Tanaka T. Tsuge Structural and functional complexity of the genomic region controlling AK-toxin biosynthesis and pathogenicity in the Japanese pear pathotype of Alternaria alternata Mol. Plant-Microbe Interact. 2000 13 975 986
    • (2000) Mol. Plant-Microbe Interact. , vol.13 , pp. 975-986
    • Tanaka, A.1    Tsuge, T.2
  • 38
    • 61949235019 scopus 로고    scopus 로고
    • Contribution of peroxisomes to penicillin biosynthesis in Aspergillus nidulans
    • P. Sprote A. A. Brakhage M. J. Hynes Contribution of peroxisomes to penicillin biosynthesis in Aspergillus nidulans Eukaryotic Cell 2009 8 421 423
    • (2009) Eukaryotic Cell , vol.8 , pp. 421-423
    • Sprote, P.1    Brakhage, A.A.2    Hynes, M.J.3
  • 40
    • 69249213571 scopus 로고    scopus 로고
    • Functional analysis and subcellular localization of two geranylgeranyl diphosphate synthases from Penicillium paxilli
    • S. Saikia B. Scott Functional analysis and subcellular localization of two geranylgeranyl diphosphate synthases from Penicillium paxilli Mol. Genet. Genomics 2009 282 257 271
    • (2009) Mol. Genet. Genomics , vol.282 , pp. 257-271
    • Saikia, S.1    Scott, B.2
  • 41
    • 84899960978 scopus 로고    scopus 로고
    • Complex regulation of secondary metabolism controlling pathogenicity in the phytopathogenic fungus Alternaria alternata
    • S. Takaoka M. Kurata Y. Harimoto R. Hatta M. Yamamoto K. Akimitsu T. Tsuge Complex regulation of secondary metabolism controlling pathogenicity in the phytopathogenic fungus Alternaria alternata New Phytol. 2014 202 1297 1309
    • (2014) New Phytol. , vol.202 , pp. 1297-1309
    • Takaoka, S.1    Kurata, M.2    Harimoto, Y.3    Hatta, R.4    Yamamoto, M.5    Akimitsu, K.6    Tsuge, T.7
  • 42
    • 8644220677 scopus 로고    scopus 로고
    • Siderophore biosynthesis but not reductive iron assimilation is essential for Aspergillus fumigatus virulence
    • M. Schrettl E. Bignell C. Kragl C. Joechl T. Rogers H. N. Arst K. Haynes H. Haas Siderophore biosynthesis but not reductive iron assimilation is essential for Aspergillus fumigatus virulence J. Exp. Med. 2004 200 1213 1219
    • (2004) J. Exp. Med. , vol.200 , pp. 1213-1219
    • Schrettl, M.1    Bignell, E.2    Kragl, C.3    Joechl, C.4    Rogers, T.5    Arst, H.N.6    Haynes, K.7    Haas, H.8
  • 44
    • 23944524422 scopus 로고    scopus 로고
    • The Aspergillus fumigatus siderophore biosynthetic gene SidA, encoding l-ornithine N5-oxygenase, is required for virulence
    • A. H. Hissen A. N. Wan M. L. Warwas L. J. Pinto M. M. Moore The Aspergillus fumigatus siderophore biosynthetic gene SidA, encoding l-ornithine N5-oxygenase, is required for virulence Infect. Immun. 2005 73 5493 5503
    • (2005) Infect. Immun. , vol.73 , pp. 5493-5503
    • Hissen, A.H.1    Wan, A.N.2    Warwas, M.L.3    Pinto, L.J.4    Moore, M.M.5
  • 45
    • 1542313759 scopus 로고    scopus 로고
    • Subcellular localization of aflatoxin biosynthetic enzymes Nor-1, Ver-1, and OmtA in time-dependent fractionated colonies of Aspergillus parasiticus
    • L. W. Lee C. H. Chiou K. L. Klomparens J. W. Cary J. E. Linz Subcellular localization of aflatoxin biosynthetic enzymes Nor-1, Ver-1, and OmtA in time-dependent fractionated colonies of Aspergillus parasiticus Arch. Microbiol. 2004 181 204 214
    • (2004) Arch. Microbiol. , vol.181 , pp. 204-214
    • Lee, L.W.1    Chiou, C.H.2    Klomparens, K.L.3    Cary, J.W.4    Linz, J.E.5
  • 46
    • 54949153108 scopus 로고    scopus 로고
    • Functional expression and subcellular localization of the aflatoxin pathway enzyme Ver-1 fused to enhanced green fluorescent protein
    • S. Y. Hong J. E. Linz Functional expression and subcellular localization of the aflatoxin pathway enzyme Ver-1 fused to enhanced green fluorescent protein Appl. Environ. Microbiol. 2008 74 6385 6396
    • (2008) Appl. Environ. Microbiol. , vol.74 , pp. 6385-6396
    • Hong, S.Y.1    Linz, J.E.2
  • 47
    • 67349123336 scopus 로고    scopus 로고
    • Functional expression and sub-cellular localization of the early aflatoxin pathway enzyme Nor-1 in Aspergillus parasiticus
    • S. Y. Hong J. E. Linz Functional expression and sub-cellular localization of the early aflatoxin pathway enzyme Nor-1 in Aspergillus parasiticus Mycol. Res. 2009 113 591 601
    • (2009) Mycol. Res. , vol.113 , pp. 591-601
    • Hong, S.Y.1    Linz, J.E.2
  • 48
    • 4544304346 scopus 로고    scopus 로고
    • Distribution and sub-cellular localization of the aflatoxin enzyme versicolorin B synthase in time-fractionated colonies of Aspergillus parasiticus
    • C. H. Chiou L. W. Lee S. A. Owens J. H. Whallon K. L. Klomparens C. A. Townsend J. E. Linz Distribution and sub-cellular localization of the aflatoxin enzyme versicolorin B synthase in time-fractionated colonies of Aspergillus parasiticus Arch. Microbiol. 2004 182 67 79
    • (2004) Arch. Microbiol. , vol.182 , pp. 67-79
    • Chiou, C.H.1    Lee, L.W.2    Owens, S.A.3    Whallon, J.H.4    Klomparens, K.L.5    Townsend, C.A.6    Linz, J.E.7
  • 49
    • 0033020288 scopus 로고    scopus 로고
    • Compartmentalization and transport in beta-lactam antibiotic biosynthesis by filamentous fungi
    • M. van de Kamp A. J. Driessen W. N. Konings Compartmentalization and transport in beta-lactam antibiotic biosynthesis by filamentous fungi Antonie van Leeuwenhoek 1999 75 41 78
    • (1999) Antonie Van Leeuwenhoek , vol.75 , pp. 41-78
    • Van De Kamp, M.1    Driessen, A.J.2    Konings, W.N.3
  • 50
    • 84876681040 scopus 로고    scopus 로고
    • Strategies for strain improvement in Fusarium fujikuroi: Overexpression and localization of key enzymes of the isoprenoid pathway and their impact on gibberellin biosynthesis
    • S. Albermann P. Linnemannstons B. Tudzynski Strategies for strain improvement in Fusarium fujikuroi: overexpression and localization of key enzymes of the isoprenoid pathway and their impact on gibberellin biosynthesis Appl. Microbiol. Biotechnol. 2013 97 2979 2995
    • (2013) Appl. Microbiol. Biotechnol. , vol.97 , pp. 2979-2995
    • Albermann, S.1    Linnemannstons, P.2    Tudzynski, B.3
  • 51
    • 0036230983 scopus 로고    scopus 로고
    • Vacuoles and the fungal lifestyle
    • R. W. S. Weber Vacuoles and the fungal lifestyle Mycologist 2002 16 10 20
    • (2002) Mycologist , vol.16 , pp. 10-20
    • Weber, R.W.S.1
  • 52
    • 84877155775 scopus 로고    scopus 로고
    • Cellular development associated with induced mycotoxin synthesis in the filamentous fungus Fusarium graminearum
    • J. Menke J. Weber K. Broz H. C. Kistler Cellular development associated with induced mycotoxin synthesis in the filamentous fungus Fusarium graminearum PLoS One 2013 8 e63077
    • (2013) PLoS One , vol.8 , pp. 63077
    • Menke, J.1    Weber, J.2    Broz, K.3    Kistler, H.C.4
  • 53
    • 84901246161 scopus 로고    scopus 로고
    • Fungal physiology: Reaching the right location
    • S. Molloy Fungal physiology: Reaching the right location Nat. Rev. Microbiol. 2014 12 396 397
    • (2014) Nat. Rev. Microbiol. , vol.12 , pp. 396-397
    • Molloy, S.1
  • 54
    • 0036752689 scopus 로고    scopus 로고
    • Initial characterization of a type i fatty acid synthase and polyketide synthase multienzyme complex NorS in the biosynthesis of aflatoxin B(1)
    • C. M. Watanabe C. A. Townsend Initial characterization of a type I fatty acid synthase and polyketide synthase multienzyme complex NorS in the biosynthesis of aflatoxin B(1) Chem. Biol. 2002 9 981 988
    • (2002) Chem. Biol. , vol.9 , pp. 981-988
    • Watanabe, C.M.1    Townsend, C.A.2
  • 55
    • 84872262471 scopus 로고    scopus 로고
    • Genetic control of asexual sporulation in filamentous fungi
    • H. S. Park J. H. Yu Genetic control of asexual sporulation in filamentous fungi Curr. Opin. Microbiol. 2012 15 669 677
    • (2012) Curr. Opin. Microbiol. , vol.15 , pp. 669-677
    • Park, H.S.1    Yu, J.H.2
  • 56
    • 33750964698 scopus 로고    scopus 로고
    • Structure determination of inonotsuoxides A and B and in vivo anti-tumor promoting activity of inotodiol from the sclerotia of Inonotus obliquus
    • T. Nakata T. Yamada S. Taji H. Ohishi S. Wada H. Tokuda K. Sakuma R. Tanaka Structure determination of inonotsuoxides A and B and in vivo anti-tumor promoting activity of inotodiol from the sclerotia of Inonotus obliquus Bioorg. Med. Chem. 2007 15 257 264
    • (2007) Bioorg. Med. Chem. , vol.15 , pp. 257-264
    • Nakata, T.1    Yamada, T.2    Taji, S.3    Ohishi, H.4    Wada, S.5    Tokuda, H.6    Sakuma, K.7    Tanaka, R.8
  • 57
    • 0029856862 scopus 로고    scopus 로고
    • Sclerotiamide: A new member of the paraherquamide class with potent antiinsectan activity from the sclerotia of Aspergillus sclerotiorum
    • A. C. Whyte J. B. Gloer D. T. Wicklow P. F. Dowdw Sclerotiamide: a new member of the paraherquamide class with potent antiinsectan activity from the sclerotia of Aspergillus sclerotiorum J. Nat. Prod. 1996 59 1093 1095
    • (1996) J. Nat. Prod. , vol.59 , pp. 1093-1095
    • Whyte, A.C.1    Gloer, J.B.2    Wicklow, D.T.3    Dowdw, P.F.4
  • 61
    • 0025010497 scopus 로고
    • Isolation and molecular characterization of the Aspergillus nidulans wA gene
    • M. E. Mayorga W. E. Timberlake Isolation and molecular characterization of the Aspergillus nidulans wA gene Genetics 1990 126 73 79
    • (1990) Genetics , vol.126 , pp. 73-79
    • Mayorga, M.E.1    Timberlake, W.E.2
  • 62
    • 0032693329 scopus 로고    scopus 로고
    • A developmentally regulated gene cluster involved in conidial pigment biosynthesis in Aspergillus fumigatus
    • H. Tsai M. Wheeler Y. Chang K. Kwon-Chung A developmentally regulated gene cluster involved in conidial pigment biosynthesis in Aspergillus fumigatus J. Bacteriol. 1999 181 6469 6477
    • (1999) J. Bacteriol. , vol.181 , pp. 6469-6477
    • Tsai, H.1    Wheeler, M.2    Chang, Y.3    Kwon-Chung, K.4
  • 63
  • 64
    • 0024299512 scopus 로고
    • BrlA is necessary and sufficient to direct conidiophore development in Aspergillus nidulans
    • T. H. Adams M. T. Boylan W. E. Timberlake BrlA is necessary and sufficient to direct conidiophore development in Aspergillus nidulans Cell 1988 54 353 362
    • (1988) Cell , vol.54 , pp. 353-362
    • Adams, T.H.1    Boylan, M.T.2    Timberlake, W.E.3
  • 65
    • 84892146979 scopus 로고    scopus 로고
    • Penicillium decumbens BrlA extensively regulates secondary metabolism and functionally associates with the expression of cellulase genes
    • Y. Qin L. Bao M. Gao M. Chen Y. Lei G. Liu Y. Qu Penicillium decumbens BrlA extensively regulates secondary metabolism and functionally associates with the expression of cellulase genes Appl. Microbiol. Biotechnol. 2013 97 10453 10467
    • (2013) Appl. Microbiol. Biotechnol. , vol.97 , pp. 10453-10467
    • Qin, Y.1    Bao, L.2    Gao, M.3    Chen, M.4    Lei, Y.5    Liu, G.6    Qu, Y.7
  • 66
    • 0023404245 scopus 로고
    • Isolation and physical characterization of three essential conidiation genes from Aspergillus nidulans
    • M. T. Boylan P. M. Mirabito C. E. Willett C. R. Zimmerman W. E. Timberlake Isolation and physical characterization of three essential conidiation genes from Aspergillus nidulans Mol. Cell. Biol. 1987 7 3113 3118
    • (1987) Mol. Cell. Biol. , vol.7 , pp. 3113-3118
    • Boylan, M.T.1    Mirabito, P.M.2    Willett, C.E.3    Zimmerman, C.R.4    Timberlake, W.E.5
  • 68
    • 84864097219 scopus 로고    scopus 로고
    • Genome-based cluster deletion reveals an endocrocin biosynthetic pathway in Aspergillus fumigatus
    • F. Y. Lim Y. Hou Y. Chen J. H. Oh I. Lee T. S. Bugni N. P. Keller Genome-based cluster deletion reveals an endocrocin biosynthetic pathway in Aspergillus fumigatus Appl. Environ. Microbiol. 2012 78 4117 4125
    • (2012) Appl. Environ. Microbiol. , vol.78 , pp. 4117-4125
    • Lim, F.Y.1    Hou, Y.2    Chen, Y.3    Oh, J.H.4    Lee, I.5    Bugni, T.S.6    Keller, N.P.7
  • 70
    • 38849095118 scopus 로고    scopus 로고
    • Association of ergot alkaloids with conidiation in Aspergillus fumigatus
    • C. M. Coyle S. C. Kenaley W. R. Rittenour D. G. Panaccione Association of ergot alkaloids with conidiation in Aspergillus fumigatus Mycologia 2007 99 804 811
    • (2007) Mycologia , vol.99 , pp. 804-811
    • Coyle, C.M.1    Kenaley, S.C.2    Rittenour, W.R.3    Panaccione, D.G.4
  • 72
    • 67651120253 scopus 로고    scopus 로고
    • Effect of competition on the production and activity of secondary metabolites in Aspergillus species
    • L. Losada O. Ajayi J. C. Frisvad J. J. Yu W. C. Nierman Effect of competition on the production and activity of secondary metabolites in Aspergillus species Med. Mycol. 2009 47 S88 S96
    • (2009) Med. Mycol. , vol.47 , pp. 88-S96
    • Losada, L.1    Ajayi, O.2    Frisvad, J.C.3    Yu, J.J.4    Nierman, W.C.5
  • 73
    • 15244354736 scopus 로고    scopus 로고
    • Aspergillus fumigatus suppresses the human cellular immune response via gliotoxin-mediated apoptosis of monocytes
    • M. Stanzani E. Orciuolo R. Lewis D. Kontoyiannis S. Martins L. St John K. Komanduri Aspergillus fumigatus suppresses the human cellular immune response via gliotoxin-mediated apoptosis of monocytes Blood 2005 105 2258 2265
    • (2005) Blood , vol.105 , pp. 2258-2265
    • Stanzani, M.1    Orciuolo, E.2    Lewis, R.3    Kontoyiannis, D.4    Martins, S.5    St John, L.6    Komanduri, K.7
  • 78
    • 73949113518 scopus 로고    scopus 로고
    • Aspergillus fumigatus inhibits angiogenesis through the production of gliotoxin and other secondary metabolites
    • R. Ben-Ami R. E. Lewis K. Leventakos D. P. Kontoyiannis Aspergillus fumigatus inhibits angiogenesis through the production of gliotoxin and other secondary metabolites Blood 2009 114 5393 5399
    • (2009) Blood , vol.114 , pp. 5393-5399
    • Ben-Ami, R.1    Lewis, R.E.2    Leventakos, K.3    Kontoyiannis, D.P.4
  • 79
    • 22044435268 scopus 로고    scopus 로고
    • Fumigaclavine C, an fungal metabolite, improves experimental colitis in mice via downregulating Th1 cytokine production and matrix metalloproteinase activity
    • X. F. Wu M. J. Fei R. G. Shu R. X. Tan Q. Xu Fumigaclavine C, an fungal metabolite, improves experimental colitis in mice via downregulating Th1 cytokine production and matrix metalloproteinase activity Int. Immunopharmacol. 2005 5 1543 1553
    • (2005) Int. Immunopharmacol. , vol.5 , pp. 1543-1553
    • Wu, X.F.1    Fei, M.J.2    Shu, R.G.3    Tan, R.X.4    Xu, Q.5
  • 80
    • 3042553356 scopus 로고    scopus 로고
    • Fumigaclavine C improves concanavalin A-induced liver injury in mice mainly via inhibiting TNF-Alpha production and lymphocyte adhesion to extracellular matrices
    • Y. Zhao J. Liu J. Wang L. Wang H. Yin R. Tan Q. Xu Fumigaclavine C improves concanavalin A-induced liver injury in mice mainly via inhibiting TNF-Alpha production and lymphocyte adhesion to extracellular matrices J. Pharm. Pharmacol. 2004 56 775 782
    • (2004) J. Pharm. Pharmacol. , vol.56 , pp. 775-782
    • Zhao, Y.1    Liu, J.2    Wang, J.3    Wang, L.4    Yin, H.5    Tan, R.6    Xu, Q.7
  • 81
    • 84856643514 scopus 로고    scopus 로고
    • Proteomic and biochemical evidence support a role for transport vesicles and endosomes in stress response and secondary metabolism in Aspergillus parasiticus
    • J. E. Linz A. Chanda S. Y. Hong D. A. Whitten C. Wilkerson L. V. Roze Proteomic and biochemical evidence support a role for transport vesicles and endosomes in stress response and secondary metabolism in Aspergillus parasiticus J. Proteome Res. 2012 11 767 775
    • (2012) J. Proteome Res. , vol.11 , pp. 767-775
    • Linz, J.E.1    Chanda, A.2    Hong, S.Y.3    Whitten, D.A.4    Wilkerson, C.5    Roze, L.V.6
  • 82
    • 0023501173 scopus 로고
    • Biosynthesis of benzylpenicillin by Penicillium chrysogenum and its Golgi apparatus
    • W. Kurylowicz W. Kurzatkowski J. Kurzatkowski Biosynthesis of benzylpenicillin by Penicillium chrysogenum and its Golgi apparatus Arch. Immunol. Ther. Exp. 1987 35 699 724
    • (1987) Arch. Immunol. Ther. Exp. , vol.35 , pp. 699-724
    • Kurylowicz, W.1    Kurzatkowski, W.2    Kurzatkowski, J.3
  • 83
    • 0027518445 scopus 로고
    • Subcellular compartmentation of penicillin biosynthesis in Penicillium chrysogenum. The amino acid precursors are derived from the vacuole
    • T. Lendenfeld D. Ghali M. Wolschek E. M. Kubicek-Pranz C. P. Kubicek Subcellular compartmentation of penicillin biosynthesis in Penicillium chrysogenum. The amino acid precursors are derived from the vacuole J. Biol. Chem. 1993 268 665 671
    • (1993) J. Biol. Chem. , vol.268 , pp. 665-671
    • Lendenfeld, T.1    Ghali, D.2    Wolschek, M.3    Kubicek-Pranz, E.M.4    Kubicek, C.P.5
  • 86
    • 0035732760 scopus 로고    scopus 로고
    • Structure and localization of cyclosporin synthetase, the key enzyme of cyclosporin biosynthesis in Tolypocladium inflatum
    • M. Hoppert C. Gentzsch K. Schorgendorfer Structure and localization of cyclosporin synthetase, the key enzyme of cyclosporin biosynthesis in Tolypocladium inflatum Arch. Microbiol. 2001 176 285 293
    • (2001) Arch. Microbiol. , vol.176 , pp. 285-293
    • Hoppert, M.1    Gentzsch, C.2    Schorgendorfer, K.3
  • 87
    • 78649816006 scopus 로고    scopus 로고
    • Colocalization of amanitin and a candidate toxin-processing prolyl oligopeptidase in Amanita basidiocarps
    • H. Luo H. E. Hallen-Adams J. S. Scott-Craig J. D. Walton Colocalization of amanitin and a candidate toxin-processing prolyl oligopeptidase in Amanita basidiocarps Eukaryotic Cell 2010 9 1891 1900
    • (2010) Eukaryotic Cell , vol.9 , pp. 1891-1900
    • Luo, H.1    Hallen-Adams, H.E.2    Scott-Craig, J.S.3    Walton, J.D.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.