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Volumn 5, Issue , 2010, Pages

Proteomic changes associated with deletion of the Magnaporthe oryzae conidial morphology-regulating gene COM1

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIA (MICROORGANISMS); MAGNAPORTHE; MAGNAPORTHE ORYZAE;

EID: 77958601896     PISSN: None     EISSN: 17456150     Source Type: Journal    
DOI: 10.1186/1745-6150-5-61     Document Type: Article
Times cited : (23)

References (82)
  • 1
    • 0004080812 scopus 로고
    • Wallingford: Commonwealth Agricultural Bureaux
    • Ou SH. Rice Diseases 1985, Wallingford: Commonwealth Agricultural Bureaux.
    • (1985) Rice Diseases
    • Ou, S.H.1
  • 2
    • 37049179013 scopus 로고
    • A mechanism for surface attachment in spores of a plant pathogenic fungus
    • 10.1126/science.239.4837.288, 17769992
    • Hamer J, Howard RJ, Chumley FG, Valent B. A mechanism for surface attachment in spores of a plant pathogenic fungus. Science 1988, 239:288-290. 10.1126/science.239.4837.288, 17769992.
    • (1988) Science , vol.239 , pp. 288-290
    • Hamer, J.1    Howard, R.J.2    Chumley, F.G.3    Valent, B.4
  • 3
    • 66149185406 scopus 로고    scopus 로고
    • Interaction transcriptome analysis identifies Magnaporthe oryzae BAS1-4 as biotrophy-associated secreted proteins in rice blast disease
    • 10.1105/tpc.107.055228, 2685627, 19357089
    • Mosquera G, Giraldo MC, Khang CH, Coughlan S, Valent B. Interaction transcriptome analysis identifies Magnaporthe oryzae BAS1-4 as biotrophy-associated secreted proteins in rice blast disease. Plant Cell 2009, 21:1273-1290. 10.1105/tpc.107.055228, 2685627, 19357089.
    • (2009) Plant Cell , vol.21 , pp. 1273-1290
    • Mosquera, G.1    Giraldo, M.C.2    Khang, C.H.3    Coughlan, S.4    Valent, B.5
  • 4
    • 0242693135 scopus 로고    scopus 로고
    • On the trail of a cereal killer: Exploring the biology of Magnaporthe oryzae
    • 10.1146/annurev.micro.57.030502.090957, 14527276
    • Talbot NJ. On the trail of a cereal killer: Exploring the biology of Magnaporthe oryzae. Annu Rev Microbiol 2003, 57:177-202. 10.1146/annurev.micro.57.030502.090957, 14527276.
    • (2003) Annu Rev Microbiol , vol.57 , pp. 177-202
    • Talbot, N.J.1
  • 5
    • 0242627729 scopus 로고
    • Mutations at the Smo genetic locus affect the shape of diverse cell types in the rice blast fungus
    • 1203707, 17246498
    • Hamer JE, Valent B, Chumley FG. Mutations at the Smo genetic locus affect the shape of diverse cell types in the rice blast fungus. Genetics 1989, 122:351-361. 1203707, 17246498.
    • (1989) Genetics , vol.122 , pp. 351-361
    • Hamer, J.E.1    Valent, B.2    Chumley, F.G.3
  • 6
    • 0029189336 scopus 로고
    • Genetic analysis of sporulation in Magnaporthe oryzae by chemical and insertional mutagenesis
    • Shi Z, Leung H. Genetic analysis of sporulation in Magnaporthe oryzae by chemical and insertional mutagenesis. Mol Plant-Microbe Interact 1995, 8:949-959.
    • (1995) Mol Plant-Microbe Interact , vol.8 , pp. 949-959
    • Shi, Z.1    Leung, H.2
  • 7
    • 0032098394 scopus 로고    scopus 로고
    • Acropetal: a genetic locus required for conidiophore architecture and pathogenicity in the rice blast fungus
    • 10.1006/fgbi.1998.1053, 9742203
    • Lau GW, Hamer JE. Acropetal: a genetic locus required for conidiophore architecture and pathogenicity in the rice blast fungus. Fungal Genet Biol 1998, 24:228-239. 10.1006/fgbi.1998.1053, 9742203.
    • (1998) Fungal Genet Biol , vol.24 , pp. 228-239
    • Lau, G.W.1    Hamer, J.E.2
  • 8
    • 1942440044 scopus 로고    scopus 로고
    • Two PKA kinase genes, CHM1 and MST20, have distinct functions in Magnaporthe oryzae
    • 10.1094/MPMI.2004.17.5.547, 15141959
    • Li L, Xue CY, Bruno K, Nishimura M, Xu JR. Two PKA kinase genes, CHM1 and MST20, have distinct functions in Magnaporthe oryzae. Mol Plant-Microbe Interact 2004, 17:547-556. 10.1094/MPMI.2004.17.5.547, 15141959.
    • (2004) Mol Plant-Microbe Interact , vol.17 , pp. 547-556
    • Li, L.1    Xue, C.Y.2    Bruno, K.3    Nishimura, M.4    Xu, J.R.5
  • 9
    • 73949110688 scopus 로고    scopus 로고
    • A novel protein Com1 is required for normal conidium morphology and full virulence in Magnaporthe oryzae
    • 10.1094/MPMI-23-1-0112, 19958144
    • Yang J, Zhao XY, Sun J, Kang ZS, Ding SL, Xu JR, Peng YL. A novel protein Com1 is required for normal conidium morphology and full virulence in Magnaporthe oryzae. Mol Plant-Microbe Interact 2010, 23(1):112-123. 10.1094/MPMI-23-1-0112, 19958144.
    • (2010) Mol Plant-Microbe Interact , vol.23 , Issue.1 , pp. 112-123
    • Yang, J.1    Zhao, X.Y.2    Sun, J.3    Kang, Z.S.4    Ding, S.L.5    Xu, J.R.6    Peng, Y.L.7
  • 10
    • 0025007276 scopus 로고
    • Genetic mapping with dispersed repeated sequences in the rice blast fungus: Mapping the SMO locus
    • 10.1007/BF00264458, 1980141
    • Hamer JE, Givan S. Genetic mapping with dispersed repeated sequences in the rice blast fungus: Mapping the SMO locus. Mol Gen Genet 1990, 223:487-495. 10.1007/BF00264458, 1980141.
    • (1990) Mol Gen Genet , vol.223 , pp. 487-495
    • Hamer, J.E.1    Givan, S.2
  • 11
    • 60349106351 scopus 로고    scopus 로고
    • A proteomic analysis of powdery mildew (Blumeria graminis f. sp. hordei) conidiospores
    • 10.1111/j.1364-3703.2008.00524.x, 19236571
    • Noir S, Colby T, Harzen A, Schmidt J, Panstruga R. A proteomic analysis of powdery mildew (Blumeria graminis f. sp. hordei) conidiospores. Mol Plant Pathol 2009, 10(2):223-236. 10.1111/j.1364-3703.2008.00524.x, 19236571.
    • (2009) Mol Plant Pathol , vol.10 , Issue.2 , pp. 223-236
    • Noir, S.1    Colby, T.2    Harzen, A.3    Schmidt, J.4    Panstruga, R.5
  • 13
    • 8744313768 scopus 로고    scopus 로고
    • Proteome analysis of rice blast fungus (Magnaporthe grisea) proteome during appressorium formation
    • 10.1002/pmic.200400969, 15378734
    • Kim ST, Yu S, Kim SG, Kang SY, Hwang DH, Jang YS, Kang KY. Proteome analysis of rice blast fungus (Magnaporthe grisea) proteome during appressorium formation. Proteomics 2004, 4:3579-3587. 10.1002/pmic.200400969, 15378734.
    • (2004) Proteomics , vol.4 , pp. 3579-3587
    • Kim, S.T.1    Yu, S.2    Kim, S.G.3    Kang, S.Y.4    Hwang, D.H.5    Jang, Y.S.6    Kang, K.Y.7
  • 14
    • 0024397415 scopus 로고
    • The structure and regulation of protein phosphatase
    • 10.1146/annurev.bi.58.070189.002321, 2549856
    • Cohen P. The structure and regulation of protein phosphatase. Ann Rev Biochem 1989, 58:453-508. 10.1146/annurev.bi.58.070189.002321, 2549856.
    • (1989) Ann Rev Biochem , vol.58 , pp. 453-508
    • Cohen, P.1
  • 15
    • 0025915688 scopus 로고
    • Cloning, nucleotide sequence, and regulation of met 14, the gene encoding the APS kinase of Saccharomyces cerevisiae
    • 10.1007/BF00264218, 1654509
    • Korch C, Mountain HA, Bystrom AS. Cloning, nucleotide sequence, and regulation of met 14, the gene encoding the APS kinase of Saccharomyces cerevisiae. Mol Gen Genet 1991, 229:96-108. 10.1007/BF00264218, 1654509.
    • (1991) Mol Gen Genet , vol.229 , pp. 96-108
    • Korch, C.1    Mountain, H.A.2    Bystrom, A.S.3
  • 16
    • 0034654011 scopus 로고    scopus 로고
    • Acetylation: a regulatory modification to rival phosphorylation?
    • 10.1093/emboj/19.6.1176, 305658, 10716917
    • Kouzarides T. Acetylation: a regulatory modification to rival phosphorylation?. EMBO J 2000, 19:1176-1179. 10.1093/emboj/19.6.1176, 305658, 10716917.
    • (2000) EMBO J , vol.19 , pp. 1176-1179
    • Kouzarides, T.1
  • 18
    • 17044392996 scopus 로고    scopus 로고
    • Role of protein methylation I regulation of transcription
    • 10.1210/er.2004-0008, 15479858
    • Lee DY, Teyssier C, Strahl BD, Stallcup MR. Role of protein methylation I regulation of transcription. Endocr Rev 2005, 26:147-170. 10.1210/er.2004-0008, 15479858.
    • (2005) Endocr Rev , vol.26 , pp. 147-170
    • Lee, D.Y.1    Teyssier, C.2    Strahl, B.D.3    Stallcup, M.R.4
  • 19
    • 0024789886 scopus 로고
    • Role of melanin in appressorium formation
    • Howard RJ, Ferrari MA. Role of melanin in appressorium formation. Exp Mycol 1989, 13:403-418.
    • (1989) Exp Mycol , vol.13 , pp. 403-418
    • Howard, R.J.1    Ferrari, M.A.2
  • 20
    • 0000008358 scopus 로고
    • Genetic analysis of melanin-deficient nonpathogenic mutants of Magnaporthe grisea
    • Chumley FG, Valent B. Genetic analysis of melanin-deficient nonpathogenic mutants of Magnaporthe grisea. Mol Plant-Microbe Interact 1990, 3:135-143.
    • (1990) Mol Plant-Microbe Interact , vol.3 , pp. 135-143
    • Chumley, F.G.1    Valent, B.2
  • 21
    • 0032948367 scopus 로고    scopus 로고
    • Targeted disruption of a melanin biosynthesis gene affects conidial development and UV tolerance in the Japanese pear pathotype of Alternaria alternate
    • 10.1094/MPMI.1999.12.1.59, 9885194
    • Kawamura C, Tsujimoto T, Tsuge T. Targeted disruption of a melanin biosynthesis gene affects conidial development and UV tolerance in the Japanese pear pathotype of Alternaria alternate. Mol Plant-Microbe Interact 1999, 12(1):59-63. 10.1094/MPMI.1999.12.1.59, 9885194.
    • (1999) Mol Plant-Microbe Interact , vol.12 , Issue.1 , pp. 59-63
    • Kawamura, C.1    Tsujimoto, T.2    Tsuge, T.3
  • 22
    • 0000772612 scopus 로고
    • Biosynthesis and function of fungal melanin
    • Bell AA, Wheeler MH. Biosynthesis and function of fungal melanin. Ann Rev Phytopathol 1986, 24:411-451.
    • (1986) Ann Rev Phytopathol , vol.24 , pp. 411-451
    • Bell, A.A.1    Wheeler, M.H.2
  • 23
    • 0029816544 scopus 로고    scopus 로고
    • Breaking and entering: host penetration by the fungal rice blast pathogen Magnaporthe grisea
    • Howard RJ, Valent B. Breaking and entering: host penetration by the fungal rice blast pathogen Magnaporthe grisea. Ann Rev Microbiol 1996, 50:491-512.
    • (1996) Ann Rev Microbiol , vol.50 , pp. 491-512
    • Howard, R.J.1    Valent, B.2
  • 24
    • 0033578680 scopus 로고    scopus 로고
    • Optical measurements of invasive forces exerted by appressoria of a plant pathogenic fungus
    • 10.1126/science.285.5435.1896, 10489364
    • Bechinger C, Giebel KF, Schnell M, Leiderer P, Deising HB, Bastmeyer M. Optical measurements of invasive forces exerted by appressoria of a plant pathogenic fungus. Science 1999, 285:1896-1899. 10.1126/science.285.5435.1896, 10489364.
    • (1999) Science , vol.285 , pp. 1896-1899
    • Bechinger, C.1    Giebel, K.F.2    Schnell, M.3    Leiderer, P.4    Deising, H.B.5    Bastmeyer, M.6
  • 25
    • 0033532642 scopus 로고    scopus 로고
    • Design of scytalone dehydratase inhibitors as rice blast fungicides: derivatives of norephedrine
    • Basarab GS, Jordan DB, Gehret TC, Schwartz RS, Wawrzak Z. Design of scytalone dehydratase inhibitors as rice blast fungicides: derivatives of norephedrine. Bioorg Med Chem Lett 1999, 9:613-1618.
    • (1999) Bioorg Med Chem Lett , vol.9 , pp. 613-1618
    • Basarab, G.S.1    Jordan, D.B.2    Gehret, T.C.3    Schwartz, R.S.4    Wawrzak, Z.5
  • 26
    • 0034713887 scopus 로고    scopus 로고
    • Tight-binding inhibitors of scytalone dehydratase: effects of site-directed mutations
    • 10.1021/bi000467m, 10913266
    • Jordan DB, Basarab GS, Steffens JJ, Schwartz RS, Doughty JG. Tight-binding inhibitors of scytalone dehydratase: effects of site-directed mutations. Biochemistry 2000, 39:8593-8602. 10.1021/bi000467m, 10913266.
    • (2000) Biochemistry , vol.39 , pp. 8593-8602
    • Jordan, D.B.1    Basarab, G.S.2    Steffens, J.J.3    Schwartz, R.S.4    Doughty, J.G.5
  • 27
    • 0034053461 scopus 로고    scopus 로고
    • Stereochemistry of the enolization of scytalone by scytalone dehydratase
    • 10.1021/bi991839y, 10694394
    • Jordan DB, Zheng YJ, Lockett BA, Basarab GS. Stereochemistry of the enolization of scytalone by scytalone dehydratase. Biochemistry 2000, 39:2276-2282. 10.1021/bi991839y, 10694394.
    • (2000) Biochemistry , vol.39 , pp. 2276-2282
    • Jordan, D.B.1    Zheng, Y.J.2    Lockett, B.A.3    Basarab, G.S.4
  • 28
    • 0000066402 scopus 로고    scopus 로고
    • Biological activity of carpropamid (KTU 3616): a new fungicide for rice blast disease
    • Kurahashi Y, Sakawa S, Kinbara T, Tanaka K, Kagabu S. Biological activity of carpropamid (KTU 3616): a new fungicide for rice blast disease. J Pestic Sci 1997, 22:108-112.
    • (1997) J Pestic Sci , vol.22 , pp. 108-112
    • Kurahashi, Y.1    Sakawa, S.2    Kinbara, T.3    Tanaka, K.4    Kagabu, S.5
  • 29
    • 0031100230 scopus 로고    scopus 로고
    • Carpropamid, an anti-rice blast fungicide, inhibits scytalone dehydratase activity and appressorial penetration in Colletotrichum lagenarium
    • Tsuji G, Takeda T, Furusawa I, Horino O, Kubo Y. Carpropamid, an anti-rice blast fungicide, inhibits scytalone dehydratase activity and appressorial penetration in Colletotrichum lagenarium. Pestic Biochem Physiol 1997, 57:211-219.
    • (1997) Pestic Biochem Physiol , vol.57 , pp. 211-219
    • Tsuji, G.1    Takeda, T.2    Furusawa, I.3    Horino, O.4    Kubo, Y.5
  • 30
    • 0032516487 scopus 로고    scopus 로고
    • Cryogenic X-ray crystal analysis for the complex of scytalone dehydratase of a rice blast fungus and its tight-binding inhibitor, carpropamid: the structural basis of tight-binding inhibition
    • 10.1021/bi980321b, 9665698
    • Nakasako M, Motoyama T, Kurahashi Y. Cryogenic X-ray crystal analysis for the complex of scytalone dehydratase of a rice blast fungus and its tight-binding inhibitor, carpropamid: the structural basis of tight-binding inhibition. Biochemistry 1998, 37:9931-9939. 10.1021/bi980321b, 9665698.
    • (1998) Biochemistry , vol.37 , pp. 9931-9939
    • Nakasako, M.1    Motoyama, T.2    Kurahashi, Y.3
  • 32
    • 0030237580 scopus 로고    scopus 로고
    • Confirmation of a link between fungal pigmentation, turgor pressure, and pathogenicity using a new method of turgor measurement
    • Money NP, Howard RJ. Confirmation of a link between fungal pigmentation, turgor pressure, and pathogenicity using a new method of turgor measurement. Fungal Genet Biol 1996, 20:217-227.
    • (1996) Fungal Genet Biol , vol.20 , pp. 217-227
    • Money, N.P.1    Howard, R.J.2
  • 33
    • 33745505185 scopus 로고    scopus 로고
    • Actin microfilaments in fungi
    • Walker SK, Garrill A. Actin microfilaments in fungi. Mycologist 2006, 20:26-31.
    • (2006) Mycologist , vol.20 , pp. 26-31
    • Walker, S.K.1    Garrill, A.2
  • 34
    • 0033040628 scopus 로고    scopus 로고
    • The Arp2/3 complex: a multifunctional actin organizer
    • 10.1016/S0955-0674(99)80014-3, 10047519
    • Machesky LM, Gould KL. The Arp2/3 complex: a multifunctional actin organizer. Curr Opin Cell Biol 1999, 11:117-121. 10.1016/S0955-0674(99)80014-3, 10047519.
    • (1999) Curr Opin Cell Biol , vol.11 , pp. 117-121
    • Machesky, L.M.1    Gould, K.L.2
  • 35
    • 0030670302 scopus 로고    scopus 로고
    • Mammalian actin-related protein 2/3 complex localizes to regions of lamellipodia protrusion and is composed of evolutionarily conserved proteins
    • 1218893, 9359840
    • Machesky LM, Reeves E, Wientjes F, Mattheyse FJ, Grogan A, Totty NF, Burlingame AL, Hsuan JJ, Segal AW. Mammalian actin-related protein 2/3 complex localizes to regions of lamellipodia protrusion and is composed of evolutionarily conserved proteins. Biochem J 1997, 328:105-112. 1218893, 9359840.
    • (1997) Biochem J , vol.328 , pp. 105-112
    • Machesky, L.M.1    Reeves, E.2    Wientjes, F.3    Mattheyse, F.J.4    Grogan, A.5    Totty, N.F.6    Burlingame, A.L.7    Hsuan, J.J.8    Segal, A.W.9
  • 36
    • 0033231935 scopus 로고    scopus 로고
    • The world according to Arp: regulation of actin nucleation by the Arp2/3 complex
    • 10.1016/S0962-8924(99)01651-7, 10511705
    • Welch MD. The world according to Arp: regulation of actin nucleation by the Arp2/3 complex. Trends Cell Biol 1999, 9:423-427. 10.1016/S0962-8924(99)01651-7, 10511705.
    • (1999) Trends Cell Biol , vol.9 , pp. 423-427
    • Welch, M.D.1
  • 37
    • 0347994991 scopus 로고    scopus 로고
    • Cytoskeleton and motor proteins in filamentous fungi
    • 10.1016/j.mib.2003.10.009, 14662360
    • Xiang X, Plamann M. Cytoskeleton and motor proteins in filamentous fungi. Curr Opin Microbiol 2003, 6:628-633. 10.1016/j.mib.2003.10.009, 14662360.
    • (2003) Curr Opin Microbiol , vol.6 , pp. 628-633
    • Xiang, X.1    Plamann, M.2
  • 38
    • 0033594955 scopus 로고    scopus 로고
    • Genetic dissection of the budding yeast Arp2/3 complex: a comparison of the in vivo and structural roles of individual subunits
    • 10.1073/pnas.96.13.7288, 22078, 10377407
    • Winter DC, Choe EY, Li R. Genetic dissection of the budding yeast Arp2/3 complex: a comparison of the in vivo and structural roles of individual subunits. Proc Natl Acad Sci USA 1999, 96:7288-7293. 10.1073/pnas.96.13.7288, 22078, 10377407.
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 7288-7293
    • Winter, D.C.1    Choe, E.Y.2    Li, R.3
  • 40
    • 0024961780 scopus 로고
    • Genomic organization of the glyceraldehyde-3-phosphate dehydrogenase gene family of Caenorhabditis elegans
    • 10.1016/0022-2836(89)90490-7, 2716055
    • Huang XY, Barrios LA, Vonkhorporn P, Honda S, Albertson DG, Hecht RM. Genomic organization of the glyceraldehyde-3-phosphate dehydrogenase gene family of Caenorhabditis elegans. J Mol Biol 1989, 206:411-424. 10.1016/0022-2836(89)90490-7, 2716055.
    • (1989) J Mol Biol , vol.206 , pp. 411-424
    • Huang, X.Y.1    Barrios, L.A.2    Vonkhorporn, P.3    Honda, S.4    Albertson, D.G.5    Hecht, R.M.6
  • 41
    • 0347753321 scopus 로고    scopus 로고
    • Housekeeping enzymes as virulence factors for pathogens
    • 10.1078/1438-4221-00283, 14760970
    • Pancholi V, Chhatwal GS. Housekeeping enzymes as virulence factors for pathogens. Int J Med Microbiol 2003, 293:391-401. 10.1078/1438-4221-00283, 14760970.
    • (2003) Int J Med Microbiol , vol.293 , pp. 391-401
    • Pancholi, V.1    Chhatwal, G.S.2
  • 42
    • 0034949123 scopus 로고    scopus 로고
    • Enzymes on microbial pathogens and Trichomonas vaginalis: molecular mimicry and functional diversity
    • 10.1046/j.1462-5822.2001.00126.x, 11422079
    • Alderete JF, Millsap KW, Lehker MW, Benchimol M. Enzymes on microbial pathogens and Trichomonas vaginalis: molecular mimicry and functional diversity. Cell Microbiol 2001, 3:359-370. 10.1046/j.1462-5822.2001.00126.x, 11422079.
    • (2001) Cell Microbiol , vol.3 , pp. 359-370
    • Alderete, J.F.1    Millsap, K.W.2    Lehker, M.W.3    Benchimol, M.4
  • 43
    • 0035949681 scopus 로고    scopus 로고
    • A physiological role for oxalic acid biosynthesis in the wood-rotting basidiomycete Fomitopsis palustris
    • 10.1073/pnas.191389598, 58694, 11553780
    • Munir E, Yoon JJ, Tokimatsu T, Hattori T, Shimada M. A physiological role for oxalic acid biosynthesis in the wood-rotting basidiomycete Fomitopsis palustris. Proc Natl Acad Sci USA 2001, 98:11126-11130. 10.1073/pnas.191389598, 58694, 11553780.
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 11126-11130
    • Munir, E.1    Yoon, J.J.2    Tokimatsu, T.3    Hattori, T.4    Shimada, M.5
  • 44
    • 0023976071 scopus 로고
    • Evidence for a cytoplasmic pathway of oxalate biosynthesis in Aspergillus niger
    • 202517, 3132096
    • Kubicek CP, Schreferl-Kunar G, Wöhrer W, Röhr M. Evidence for a cytoplasmic pathway of oxalate biosynthesis in Aspergillus niger. Appl Environ Microbiol 1988, 54:633-637. 202517, 3132096.
    • (1988) Appl Environ Microbiol , vol.54 , pp. 633-637
    • Kubicek, C.P.1    Schreferl-Kunar, G.2    Wöhrer, W.3    Röhr, M.4
  • 45
    • 84900146155 scopus 로고    scopus 로고
    • Botrytis cinerea perturbs redox processes as an attack strategy in plants
    • Dordrecht: Kluwer Academic Publishers, Elad Y, Williamson B, Tudzynski P, Delen N
    • Lyon GD, Goodman BA, Williamson B. Botrytis cinerea perturbs redox processes as an attack strategy in plants. Botrytis: Biology, Pathology and Control 2004, 119-141. Dordrecht: Kluwer Academic Publishers, Elad Y, Williamson B, Tudzynski P, Delen N.
    • (2004) Botrytis: Biology, Pathology and Control , pp. 119-141
    • Lyon, G.D.1    Goodman, B.A.2    Williamson, B.3
  • 46
    • 0035461311 scopus 로고    scopus 로고
    • ATP synthase--a marvelous rotary engine of the cell
    • 10.1038/35089509, 11533724
    • Yoshida M, Muneyuki E, Hisabori T. ATP synthase--a marvelous rotary engine of the cell. Nat Rev Mol Cell Biol 2001, 2:669-677. 10.1038/35089509, 11533724.
    • (2001) Nat Rev Mol Cell Biol , vol.2 , pp. 669-677
    • Yoshida, M.1    Muneyuki, E.2    Hisabori, T.3
  • 47
    • 44949089613 scopus 로고    scopus 로고
    • ATP25, a new nuclear gene of Saccharomyces cerevisiae required for expression and assembly of the Atp9p subunit of mitochondrial ATPase
    • 10.1091/mbc.E07-08-0746, 2291438, 18216280
    • Zeng X, Barros MH, Shulman T, Tzagoloff A. ATP25, a new nuclear gene of Saccharomyces cerevisiae required for expression and assembly of the Atp9p subunit of mitochondrial ATPase. Mol Biol Cell 2008, 19:1366-1377. 10.1091/mbc.E07-08-0746, 2291438, 18216280.
    • (2008) Mol Biol Cell , vol.19 , pp. 1366-1377
    • Zeng, X.1    Barros, M.H.2    Shulman, T.3    Tzagoloff, A.4
  • 48
    • 56949088879 scopus 로고    scopus 로고
    • Vacuoles and fungal biology
    • 10.1016/j.mib.2008.09.017, 18935977
    • Veses V, Richards A, Gow NAR. Vacuoles and fungal biology. Curr Opin Microbiol 2008, 11:503-510. 10.1016/j.mib.2008.09.017, 18935977.
    • (2008) Curr Opin Microbiol , vol.11 , pp. 503-510
    • Veses, V.1    Richards, A.2    Gow, N.A.R.3
  • 49
    • 3342953763 scopus 로고    scopus 로고
    • Crystal structures of human glutaryl-CoA dehydrogenases with and without an alternate substrate: structural bases of dehydrogenation and decarboxylation reactions
    • 10.1021/bi049290c, 15274622
    • Fu Z, Wang M, Paschke R, Rao S, Frerman FE, Kim JP. Crystal structures of human glutaryl-CoA dehydrogenases with and without an alternate substrate: structural bases of dehydrogenation and decarboxylation reactions. Biochemistry 2004, 43:9674-9684. 10.1021/bi049290c, 15274622.
    • (2004) Biochemistry , vol.43 , pp. 9674-9684
    • Fu, Z.1    Wang, M.2    Paschke, R.3    Rao, S.4    Frerman, F.E.5    Kim, J.P.6
  • 50
  • 51
    • 0033947041 scopus 로고    scopus 로고
    • A group of expressed cDNA sequences from the wheat fungal leaf blotch pathogen, Mycosphaerella graminicola (Septoria tritici)
    • 10.1006/fgbi.2000.1186, 10919380
    • Keon J, Bailey A, Hargreaves J. A group of expressed cDNA sequences from the wheat fungal leaf blotch pathogen, Mycosphaerella graminicola (Septoria tritici). Fungal Genet Biol 2000, 29:118-133. 10.1006/fgbi.2000.1186, 10919380.
    • (2000) Fungal Genet Biol , vol.29 , pp. 118-133
    • Keon, J.1    Bailey, A.2    Hargreaves, J.3
  • 52
    • 0021111556 scopus 로고
    • Separation and properties of five distinct acyl-CoA dehydrogenases from rat liver mitochondria
    • Ikeda Y, Dabrowski C, Tanaka K. Separation and properties of five distinct acyl-CoA dehydrogenases from rat liver mitochondria. J Biol Chem 1983, 258:1066-1076.
    • (1983) J Biol Chem , vol.258 , pp. 1066-1076
    • Ikeda, Y.1    Dabrowski, C.2    Tanaka, K.3
  • 53
    • 1042266637 scopus 로고    scopus 로고
    • Fungal metabolic model for 3-methylcrotonyl-CoA carboxylase deficiency
    • 10.1074/jbc.M310055200, 14612443
    • Rodríguez JM, Ruíz-Sala P, Ugarte M, Peñalva MA. Fungal metabolic model for 3-methylcrotonyl-CoA carboxylase deficiency. J Biol Chem 2004, 279:4578-4587. 10.1074/jbc.M310055200, 14612443.
    • (2004) J Biol Chem , vol.279 , pp. 4578-4587
    • Rodríguez, J.M.1    Ruíz-Sala, P.2    Ugarte, M.3    Peñalva, M.A.4
  • 54
    • 0026036047 scopus 로고
    • Enzymes depending on the pterin molybdenum cofactor: sequence families, spectroscopic properties of molybdenum and possible cofactor-binding domains
    • 10.1016/S0005-2728(05)80100-8, 2015248
    • Wootton JC, Nicotson RE, Cock JM, Walters DE, Burke JF, Doyle WA, Bray RC. Enzymes depending on the pterin molybdenum cofactor: sequence families, spectroscopic properties of molybdenum and possible cofactor-binding domains. Biochim Biophys Acta 1991, 1057:157-185. 10.1016/S0005-2728(05)80100-8, 2015248.
    • (1991) Biochim Biophys Acta , vol.1057 , pp. 157-185
    • Wootton, J.C.1    Nicotson, R.E.2    Cock, J.M.3    Walters, D.E.4    Burke, J.F.5    Doyle, W.A.6    Bray, R.C.7
  • 55
    • 0040559975 scopus 로고    scopus 로고
    • Disruption of phacA, an Aspergillus nidulans gene encoding a novel Cytochrome P450 monooxygenase catalyzing phenylacetate 2-hydroxylation, results in penicillin overproduction
    • 10.1074/jbc.274.21.14545, 10329644
    • Mingot JM, Peňalva MA, Fernǎndez-Caňón JM. Disruption of phacA, an Aspergillus nidulans gene encoding a novel Cytochrome P450 monooxygenase catalyzing phenylacetate 2-hydroxylation, results in penicillin overproduction. J Biol Chem 1999, 274(21):14545-14550. 10.1074/jbc.274.21.14545, 10329644.
    • (1999) J Biol Chem , vol.274 , Issue.21 , pp. 14545-14550
    • Mingot, J.M.1    Peňalva, M.A.2    Fernǎndez-Caňón, J.M.3
  • 56
    • 0032826299 scopus 로고    scopus 로고
    • Serine/threonine protein kinases and phosphatases in filamentious fungi
    • 10.1006/fgbi.1999.1118, 10328981
    • Dickman MB, Yarden O. Serine/threonine protein kinases and phosphatases in filamentious fungi. Fungal Genet Biol 1999, 26:99-117. 10.1006/fgbi.1999.1118, 10328981.
    • (1999) Fungal Genet Biol , vol.26 , pp. 99-117
    • Dickman, M.B.1    Yarden, O.2
  • 57
    • 0027143725 scopus 로고
    • Protein serine/threonine phosphatases: structure, regulation, and functions in cell growth
    • Mumby MC, Walter G. Protein serine/threonine phosphatases: structure, regulation, and functions in cell growth. Physiol Rev 1993, 73:673-699.
    • (1993) Physiol Rev , vol.73 , pp. 673-699
    • Mumby, M.C.1    Walter, G.2
  • 58
    • 0028359957 scopus 로고
    • Protein phosphatase 2A - a 'menage a trois'
    • 10.1016/0962-8924(94)90219-4, 14731592
    • Mayer-Jaekel RE, Hemmings BA. Protein phosphatase 2A - a 'menage a trois'. Trends Cell Biol 1994, 4:287-291. 10.1016/0962-8924(94)90219-4, 14731592.
    • (1994) Trends Cell Biol , vol.4 , pp. 287-291
    • Mayer-Jaekel, R.E.1    Hemmings, B.A.2
  • 59
    • 0032896632 scopus 로고    scopus 로고
    • The B regulatory subunit of protein phosphatase 2A is required for completion of macroconidiation and other developmental processes in Neurospora crassa
    • 10.1046/j.1365-2958.1999.01161.x, 9987122
    • Yatzkan E, Yarden O. The B regulatory subunit of protein phosphatase 2A is required for completion of macroconidiation and other developmental processes in Neurospora crassa. Mol Microbiol 1999, 31(1):197-209. 10.1046/j.1365-2958.1999.01161.x, 9987122.
    • (1999) Mol Microbiol , vol.31 , Issue.1 , pp. 197-209
    • Yatzkan, E.1    Yarden, O.2
  • 60
    • 84907130863 scopus 로고
    • Nutritional studies on Paracoccidioides brasiliensis: the role of organic sulfur in dimorphism
    • Paris S, Durán-González S, Mariat F. Nutritional studies on Paracoccidioides brasiliensis: the role of organic sulfur in dimorphism. Sabouraudia 1985, 23:85-92.
    • (1985) Sabouraudia , vol.23 , pp. 85-92
    • Paris, S.1    Durán-González, S.2    Mariat, F.3
  • 61
    • 4043115069 scopus 로고    scopus 로고
    • Identification of genes preferentially expressed in the pathogenic yeast phase of Paracoccidioides brasiliensis, using suppression subtraction hybridization and differential macroarray analysis
    • 10.1007/s00438-004-1016-6, 15138890
    • Marques ER, Ferreira ME, Drummond RD, Felix JM, Menossi M, Savoldi M, Travassos LR, Puccia R, Batista WL, Carvalho KC, Goldman MHS, Goldman GH. Identification of genes preferentially expressed in the pathogenic yeast phase of Paracoccidioides brasiliensis, using suppression subtraction hybridization and differential macroarray analysis. Mol Genet Genomics 2004, 271:667-677. 10.1007/s00438-004-1016-6, 15138890.
    • (2004) Mol Genet Genomics , vol.271 , pp. 667-677
    • Marques, E.R.1    Ferreira, M.E.2    Drummond, R.D.3    Felix, J.M.4    Menossi, M.5    Savoldi, M.6    Travassos, L.R.7    Puccia, R.8    Batista, W.L.9    Carvalho, K.C.10    Goldman, M.H.S.11    Goldman, G.H.12
  • 62
    • 0002705479 scopus 로고    scopus 로고
    • S-adenosylmethionine-dependent methyltransferase
    • Cambridge: Cambridge University Press, Carmel R, Jacobsen D
    • Clarke S, Banfield K. S-adenosylmethionine-dependent methyltransferase. Homocysteine in health and disease 2001, 63-78. Cambridge: Cambridge University Press, Carmel R, Jacobsen D.
    • (2001) Homocysteine in health and disease , pp. 63-78
    • Clarke, S.1    Banfield, K.2
  • 63
    • 0038374971 scopus 로고    scopus 로고
    • Many paths to methyltransfer: a chronicle of convergence
    • 10.1016/S0968-0004(03)00090-2, 2758044, 12826405
    • Schubert HL, Blumenthal RM, Cheng X. Many paths to methyltransfer: a chronicle of convergence. Trends Biochem Sci 2003, 28:329-335. 10.1016/S0968-0004(03)00090-2, 2758044, 12826405.
    • (2003) Trends Biochem Sci , vol.28 , pp. 329-335
    • Schubert, H.L.1    Blumenthal, R.M.2    Cheng, X.3
  • 64
    • 0037213362 scopus 로고    scopus 로고
    • The on-off story of protein palmitoylation
    • 2003, 10.1016/S0962-8924(02)00008-9, 12480338
    • Bijlmakers MJE, Marsh M. The on-off story of protein palmitoylation. Trends Cell Biol 2003, 13(1):32-42. 2003, 10.1016/S0962-8924(02)00008-9, 12480338.
    • (2003) Trends Cell Biol , vol.13 , Issue.1 , pp. 32-42
    • Bijlmakers, M.J.E.1    Marsh, M.2
  • 65
    • 33745623380 scopus 로고    scopus 로고
    • Palmitoylation by the DHHC protein Pfa4 regulates the ER exit of Chs3
    • 10.1083/jcb.200602049, 2064155, 16818716
    • Lam KKY, Davey M, Sun B, Roth AF, Davis NG, Conibear E. Palmitoylation by the DHHC protein Pfa4 regulates the ER exit of Chs3. J Cell Biol 2006, 174(1):19-25. 10.1083/jcb.200602049, 2064155, 16818716.
    • (2006) J Cell Biol , vol.174 , Issue.1 , pp. 19-25
    • Lam, K.K.Y.1    Davey, M.2    Sun, B.3    Roth, A.F.4    Davis, N.G.5    Conibear, E.6
  • 66
    • 33747586510 scopus 로고    scopus 로고
    • Improving the accuracy of protein secondary structure prediction using structural alignment
    • Montgomerie S, Sundararaj S, Gallin WJ, Wishart DS. Improving the accuracy of protein secondary structure prediction using structural alignment. BMC Bioinformat 2006, 7:301.
    • (2006) BMC Bioinformat , vol.7 , pp. 301
    • Montgomerie, S.1    Sundararaj, S.2    Gallin, W.J.3    Wishart, D.S.4
  • 67
    • 33947118612 scopus 로고    scopus 로고
    • Mouse homologue of yeast Prp19 interacts with mouse SUG1, the regulatory subunit of 26S proteasome
    • 10.1016/j.bbrc.2007.02.134, 17349974
    • Sihn CR, Cho SY, Lee JH, Lee TR, Kim SH. Mouse homologue of yeast Prp19 interacts with mouse SUG1, the regulatory subunit of 26S proteasome. Biochem Biophys Res Commun 2007, 356(1):175-80. 10.1016/j.bbrc.2007.02.134, 17349974.
    • (2007) Biochem Biophys Res Commun , vol.356 , Issue.1 , pp. 175-180
    • Sihn, C.R.1    Cho, S.Y.2    Lee, J.H.3    Lee, T.R.4    Kim, S.H.5
  • 68
    • 0028972077 scopus 로고
    • Gene RPA43 in Saccharomyces cerevisiae encodes an essential subunit of RNA polymerase I
    • 10.1074/jbc.270.41.24252, 7592632
    • Thuriaux P, Mariotte S, Buhler JM, Sentenac A, Vu L, Lee BS, Nomura M. Gene RPA43 in Saccharomyces cerevisiae encodes an essential subunit of RNA polymerase I. J Biol Chem 1995, 270(41):24252-24257. 10.1074/jbc.270.41.24252, 7592632.
    • (1995) J Biol Chem , vol.270 , Issue.41 , pp. 24252-24257
    • Thuriaux, P.1    Mariotte, S.2    Buhler, J.M.3    Sentenac, A.4    Vu, L.5    Lee, B.S.6    Nomura, M.7
  • 69
    • 0031944397 scopus 로고    scopus 로고
    • Nuclear protein import, but not mRNA export, is defective in all Saccharomyces cerevisiae mutants that produce temperature-sensitive forms of the Ran GTPase homologue Gsp1p
    • 10.1007/s004380050690, 9604885
    • Oki M, Noguchi E, Hayashi N, Nishimoto T. Nuclear protein import, but not mRNA export, is defective in all Saccharomyces cerevisiae mutants that produce temperature-sensitive forms of the Ran GTPase homologue Gsp1p. Mol Gen Genet 1998, 257:624-634. 10.1007/s004380050690, 9604885.
    • (1998) Mol Gen Genet , vol.257 , pp. 624-634
    • Oki, M.1    Noguchi, E.2    Hayashi, N.3    Nishimoto, T.4
  • 70
    • 0039115156 scopus 로고    scopus 로고
    • Transport into and out of the cell nucleus
    • 10.1093/emboj/17.10.2721, 1170612, 9582265
    • Görlich D. Transport into and out of the cell nucleus. EMBO J 1998, 17:2721-2727. 10.1093/emboj/17.10.2721, 1170612, 9582265.
    • (1998) EMBO J , vol.17 , pp. 2721-2727
    • Görlich, D.1
  • 71
    • 0033598989 scopus 로고    scopus 로고
    • Transport of proteins and RNAs in an out of the nucleus
    • 10.1016/S0092-8674(00)81666-9, 10619422
    • Nakielny S, Dreyfuss G. Transport of proteins and RNAs in an out of the nucleus. Cell 1999, 99:677-690. 10.1016/S0092-8674(00)81666-9, 10619422.
    • (1999) Cell , vol.99 , pp. 677-690
    • Nakielny, S.1    Dreyfuss, G.2
  • 72
    • 0033111170 scopus 로고    scopus 로고
    • Switching affinities in nuclear trafficking
    • 10.1038/7529, 10201390
    • Stewart M, Rhodes D. Switching affinities in nuclear trafficking. Nature Struct Biol 1999, 6:301-304. 10.1038/7529, 10201390.
    • (1999) Nature Struct Biol , vol.6 , pp. 301-304
    • Stewart, M.1    Rhodes, D.2
  • 73
    • 0034487424 scopus 로고    scopus 로고
    • Roles of molecular chaperones in cytoplasmic protein folding
    • 10.1006/scdb.1999.0347, 10736260
    • Agashe VR, Hartl FU. Roles of molecular chaperones in cytoplasmic protein folding. Semin Cell Dev Biol 2000, 11:15-25. 10.1006/scdb.1999.0347, 10736260.
    • (2000) Semin Cell Dev Biol , vol.11 , pp. 15-25
    • Agashe, V.R.1    Hartl, F.U.2
  • 74
    • 0032489016 scopus 로고    scopus 로고
    • The Hsp70 and Hsp60 chaperone machines
    • 10.1016/S0092-8674(00)80928-9, 9476895
    • Bukau B, Horwich AL. The Hsp70 and Hsp60 chaperone machines. Cell 1998, 92:351-366. 10.1016/S0092-8674(00)80928-9, 9476895.
    • (1998) Cell , vol.92 , pp. 351-366
    • Bukau, B.1    Horwich, A.L.2
  • 75
    • 0034924812 scopus 로고    scopus 로고
    • Folding of newly translated proteins in vivo: the role of molecular chaperones
    • 10.1146/annurev.biochem.70.1.603, 11395418
    • Frydman J. Folding of newly translated proteins in vivo: the role of molecular chaperones. Annu Rev Biochem 2001, 70:603-647. 10.1146/annurev.biochem.70.1.603, 11395418.
    • (2001) Annu Rev Biochem , vol.70 , pp. 603-647
    • Frydman, J.1
  • 76
    • 33745762927 scopus 로고    scopus 로고
    • Molecular chaperones of the Hsp110 family act as nucleotide exchange factors of Hsp70s
    • 10.1038/sj.emboj.7601138, 1478182, 16688212
    • Dragovic Z, Broadley SA, Shomura Y, Bracher A, Hartl FU. Molecular chaperones of the Hsp110 family act as nucleotide exchange factors of Hsp70s. EMBO J 2006, 25:2519-2528. 10.1038/sj.emboj.7601138, 1478182, 16688212.
    • (2006) EMBO J , vol.25 , pp. 2519-2528
    • Dragovic, Z.1    Broadley, S.A.2    Shomura, Y.3    Bracher, A.4    Hartl, F.U.5
  • 77
    • 0021342031 scopus 로고
    • Mutants of Saccharomyces. cerevisiae defective in the maintenance of minichromosomes
    • 1224244, 6323245
    • Maine GT, Sinha P, Tye BK. Mutants of Saccharomyces. cerevisiae defective in the maintenance of minichromosomes. Genetics 1984, 106(3):365-385. 1224244, 6323245.
    • (1984) Genetics , vol.106 , Issue.3 , pp. 365-385
    • Maine, G.T.1    Sinha, P.2    Tye, B.K.3
  • 78
    • 33746218931 scopus 로고    scopus 로고
    • A MADS-box protein interacts with a mating-type protein and is required for fruiting body development in the homothallic ascomycete Sordaria macrospora
    • 10.1128/EC.00086-06, 1489284, 16835449
    • Nolting N, Pöggeler S. A MADS-box protein interacts with a mating-type protein and is required for fruiting body development in the homothallic ascomycete Sordaria macrospora. Eukaryot Cell 2006, 5:1043-1056. 10.1128/EC.00086-06, 1489284, 16835449.
    • (2006) Eukaryot Cell , vol.5 , pp. 1043-1056
    • Nolting, N.1    Pöggeler, S.2
  • 79
    • 0000192534 scopus 로고
    • Temporal sequence of cytological events in rice leaves infected with Pyricularia oryzae
    • Peng Y, Shishiyama J. Temporal sequence of cytological events in rice leaves infected with Pyricularia oryzae. Can J Bot 1988, 66:730-735.
    • (1988) Can J Bot , vol.66 , pp. 730-735
    • Peng, Y.1    Shishiyama, J.2
  • 81
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • 10.1016/0003-2697(76)90527-3, 942051
    • Bradford MM. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 1976, 72:248-254. 10.1016/0003-2697(76)90527-3, 942051.
    • (1976) Anal Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 82
    • 13444262384 scopus 로고    scopus 로고
    • CDD: a conserved domain database for protein classification
    • 10.1093/nar/gki069, 540023, 15608175
    • Marchler-Bauer A, Anderson JB, Cherukuri PF, DeWeese-Scott C. CDD: a conserved domain database for protein classification. Nucleic Acids Res 2005, 33:D192-196. 10.1093/nar/gki069, 540023, 15608175.
    • (2005) Nucleic Acids Res , vol.33
    • Marchler-Bauer, A.1    Anderson, J.B.2    Cherukuri, P.F.3    DeWeese-Scott, C.4


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