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“Effect of different carbon sources on proteases secreted by the fungal pathogen Sclerotinia sclerotiorum during Phaseolus vulgaris infection”, vol. 11, pp. 2171-2181, 2012.
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Billon-Grand G, Poussereau N and Fevre M (2002). The extracellular proteases secreted in vitro and in planta by the phytopathogenic fungus Sclerotinia sclerotiorum. J. Phytopathol. 150: 507-511.
http://dx.doi.org/10.1046/j.1439-0434.2002.00782.x
Boland GJ and Hall R (1994). Index of plant hosts of Sclerotinia sclerotiorum. Can. J. Plant Pathol. 16: 93-108.
http://dx.doi.org/10.1080/07060669409500766
Bradford MM (1976). A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72: 248-254.
http://dx.doi.org/10.1016/0003-2697(76)90527-3
Clark SJ, Templeton MD and Sullivan PA (1997). A secreted aspartic proteinase from Glomerella cingulata: purification of the enzyme and molecular cloning of the cDNA. Microbiology 143: 1395-1403.
http://dx.doi.org/10.1099/00221287-143-4-1395
PMid:9141702
Cotton P, Rascle C and Fevre M (2002). Characterization of PG2, an early endoPG produced by Sclerotinia sclerotiorum, expressed in yeast. FEMS Microbiol. Lett 213: 239-244.
http://dx.doi.org/10.1111/j.1574-6968.2002.tb11312.x
PMid:12167544
Farley PC and Sullivan PA (1998). The Rhizopus oryzae secreted aspartic proteinase gene family: an analysis of gene expression. Microbiology 144: 2355-2366.
http://dx.doi.org/10.1099/00221287-144-8-2355
PMid:9720058
Hegedus DD and Rimmer SR (2005). Sclerotinia sclerotiorum: when "to be or not to be" a pathogen? FEMS Microbiol. Lett. 251: 177-184.
http://dx.doi.org/10.1016/j.femsle.2005.07.040
PMid:16112822
Jarai G and Buxton F (1994). Nitrogen, carbon, and pH regulation of extracellular acidic proteases of Aspergillus niger. Curr. Genet. 26: 238-244.
http://dx.doi.org/10.1007/BF00309554
PMid:7532112
Kim YT, Prusky D and Rollins JA (2007). An activating mutation of the Sclerotinia sclerotiorum pac1 gene increases oxalic acid production at low pH but decreases virulence. Mol. Plant. Pathol. 8: 611-622.
http://dx.doi.org/10.1111/j.1364-3703.2007.00423.x
PMid:20507525
Li R, Rimmer R, Buchwaldt L, Sharpe AG, et al. (2004). Interaction of Sclerotinia sclerotiorum with a resistant Brassica napus cultivar: expressed sequence tag analysis identifies genes associated with fungal pathogenesis. Fungal. Genet. Biol. 41: 735-753.
http://dx.doi.org/10.1016/j.fgb.2004.03.001
PMid:15219559
MacDonald F and Odds FC (1980). Inducible proteinase of Candida albicans in diagnostic serology and in the pathogenesis of systemic candidosis. J. Med. Microbiol. 13: 423-435.
http://dx.doi.org/10.1099/00222615-13-3-423
PMid:6997486
Magro P, Marciano P and Di Lenna P (1984). Oxalic acid production and its role in pathogenesis of Sclerotinia sclerotiorum. FEMS Microbiol. Lett. 24: 9-12.
http://dx.doi.org/10.1111/j.1574-6968.1984.tb01234.x
Marciano P, Di Lenna P and Magro P (1983). Oxalic acid, cell wall degrading enzymes and pH in pathogenesis and their significance in the virulence of two Sclerotinia sclerotiorum isolates on sunflower. Physiol. Plant Pathol. 22: 339- 345.
Mathieu M and Felenbok B (1994). The Aspergillus nidulans CREA protein mediates glucose repression of the ethanol regulon at various levels through competition with the ALCR-specific transactivator. EMBO J. 13: 4022-4027.
PMid:8076597 PMCid:395322
Movahedi S and Heale JB (1990). Purification and characterization of an aspartic proteinase secreted by Botrytis cinerea Pers ex. Pers in culture and in infected carrots. Physiol. Mol. Plant Pathol. 36: 289-302.
http://dx.doi.org/10.1016/0885-5765(90)90060-B
Murphy JM and Walton JD (1996). Three extracellular proteases from Cochliobolus carbonum: cloning and targeted disruption of ALP1. Mol. Plant Microbe Interact. 9: 290-297.
http://dx.doi.org/10.1094/MPMI-9-0290
PMid:8634479
Panozzo C, Cornillot E and Felenbok B (1998). The CreA repressor is the sole DNA-binding protein responsible for carbon catabolite repression of the alcA gene in Aspergillus nidulans via its binding to a couple of specific sites. J. Biol. Chem. 273: 6367-6372.
http://dx.doi.org/10.1074/jbc.273.11.6367
PMid:9497366
Paris R and Lamattina L (1999). Phytophthora infestans secretes extracellular proteases with necrosis inducing activity on potato. Eur. J. Plant Pathol. 105: 753-760.
http://dx.doi.org/10.1023/A:1008734527651
Pereira JL, Franco OL and Noronha EF (2006). Production and biochemical characterization of insecticidal enzymes from Aspergillus fumigatus toward Callosobruchus maculatus. Curr. Microbiol. 52: 430-434.
http://dx.doi.org/10.1007/s00284-005-0192-x
PMid:16732450
Poussereau N, Creton S, Billon-Grand G, Rascle C, et al. (2001a). Regulation of acp1, encoding a non-aspartyl acid protease expressed during pathogenesis of Sclerotinia sclerotiorum. Microbiology 147: 717-726.
PMid:11238979
Poussereau N, Gente S, Rascle C, Billon-Grand G, et al. (2001b). aspS encoding an unusual aspartyl protease from Sclerotinia sclerotiorum is expressed during phytopathogenesis. FEMS Microbiol. Lett. 194: 27-32.
http://dx.doi.org/10.1111/j.1574-6968.2001.tb09441.x
PMid:11150661
Riou C, Freyssinet G and Fevre M (1992). Purification and Characterization of Extracellular Pectinolytic Enzymes Produced by Sclerotinia sclerotiorum. Appl. Environ. Microbiol. 58: 578-583.
PMid:16348646 PMCid:195287
Rolland SG and Bruel CA (2008). Sulphur and nitrogen regulation of the protease-encoding ACP1 gene in the fungus Botrytis cinerea: correlation with a phospholipase D activity. Microbiology 154: 1464-1473.
http://dx.doi.org/10.1099/mic.0.2007/012005-0
PMid:18451055
Rolland S, Bruel C, Rascle C, Girard V, et al. (2009). pH controls both transcription and post-translational processing of the protease BcACP1 in the phytopathogenic fungus Botrytis cinerea. Microbiology 155: 2097-2105.
http://dx.doi.org/10.1099/mic.0.025999-0
PMid:19359322
Rollins JA (2003). The Sclerotinia sclerotiorum pac1 gene is required for sclerotial development and virulence. Mol. Plant Microbe Interact. 16: 785-795.
http://dx.doi.org/10.1094/MPMI.2003.16.9.785
PMid:12971602
Rollins JA and Dickman MB (2001). pH signaling in Sclerotinia sclerotiorum: identification of a pacC/RIM1 homolog. Appl. Environ. Microbiol. 67: 75-81.
http://dx.doi.org/10.1128/AEM.67.1.75-81.2001
PMid:11133430 PMCid:92519
Sexton AC, Cozijnsen AJ, Keniry A, Jewell E, et al. (2006). Comparison of transcription of multiple genes at three developmental stages of the plant pathogen Sclerotinia sclerotiorum. FEMS Microbiol. Lett. 258: 150-160.
http://dx.doi.org/10.1111/j.1574-6968.2006.00212.x
PMid:16630270
ten Have A, Dekkers E, Kay J, Phylip LH, et al. (2004). An aspartic proteinase gene family in the filamentous fungus Botrytis cinerea contains members with novel features. Microbiology 150: 2475-2489.
http://dx.doi.org/10.1099/mic.0.27058-0
PMid:15256589
Vautard-Mey G and Fevre M (2003). Carbon and pH modulate the expression of the fungal glucose repressor encoding genes. Curr. Microbiol. 46: 146-150.
http://dx.doi.org/10.1007/s00284-002-3838-y
PMid:12520371
“Characterization of the dry bean polygalacturonase-inhibiting protein (PGIP) gene family during Sclerotinia sclerotiorum (Sclerotiniaceae) infection”, vol. 9, pp. 994-1004, 2010.
, Agüero CB, Uratsu SL, Greve C, Powell ALT, et al. (2005). Evaluation of tolerance to Pierce's disease and Botrytis in transgenic plants of Vitis vinifera L. expressing the pear PGIP gene. Mol. Plant. Pathol. 6: 43-51.
http://dx.doi.org/10.1111/j.1364-3703.2004.00262.x
PMid:20565637
Alghisi P and Favaron F (1995). Pectin-degrading enzymes and plant-parasite interactions. Eur. J. Plant. Pathol. 101: 365-375.
http://dx.doi.org/10.1007/BF01874850
Annis SL and Goodwin PH (1997). Recent advances in the molecular genetics of plant cell wall-degrading enzymes produced by plant pathogenic fungi. Eur. J. Plant Pathol. 103: 1-14.
http://dx.doi.org/10.1023/A:1008656013255
Boland GJ and Hall R (1994). Index of plant hosts of Sclerotinia sclerotiorum. Can. J. Plant Pathol. 16: 93-108.
http://dx.doi.org/10.1080/07060669409500766
Boudart G, Charpentier M, Lafitte C, Martinez Y, et al. (2003). Elicitor activity of a fungal endopolygalacturonase in tobacco requires a functional catalytic site and cell wall localization. Plant Physiol. 131: 93-101.
http://dx.doi.org/10.1104/pp.011585
PMid:12529518 PMCid:166790
Cessna SG, Sears VE, Dickman MB and Low PS (2000). Oxalic acid, a pathogenicity factor for Sclerotinia sclerotiorum, suppresses the oxidative burst of the host plant. Plant Cell 12: 2191-2200.
PMid:11090218 PMCid:150167
Cotton P, Rascle C and Fevre M (2002). Characterization of PG2, an early endoPG produced by Sclerotinia sclerotiorum, expressed in yeast. FEMS Microbiol. Lett. 213: 239-244.
http://dx.doi.org/10.1111/j.1574-6968.2002.tb11312.x
PMid:12167544
D'Ovidio R, Raiola A, Capodicasa C, Devoto A, et al. (2004). Characterization of the complex locus of bean encoding polygalacturonase-inhibiting proteins reveals subfunctionalization for defense against fungi and insects. Plant Physiol. 135: 2424-2435.
http://dx.doi.org/10.1104/pp.104.044644
PMid:15299124 PMCid:520809
De Lorenzo G and Ferrari S (2002). Polygalacturonase-inhibiting proteins in defense against phytopathogenic fungi. Curr. Opin. Plant Biol. 5: 295-299.
http://dx.doi.org/10.1016/S1369-5266(02)00271-6
De Lorenzo G, D'Ovidio R and Cervone F (2001). The role of polygalacturonase-inhibiting proteins (PGIPs) in defense against pathogenic fungi. Annu. Rev. Phytopathol. 39: 313-335.
http://dx.doi.org/10.1146/annurev.phyto.39.1.313
PMid:11701868
Ferrari S, Vairo D, Ausubel FM, Cervone F, et al. (2003). Tandemly duplicated Arabidopsis genes that encode polygalacturonase-inhibiting proteins are regulated coordinately by different signal transduction pathways in response to fungal infection. Plant Cell 15: 93-106.
http://dx.doi.org/10.1105/tpc.005165
PMid:12509524 PMCid:143454
Fraissinet-Tachet L and Févre M (1996). Regulation by galacturonic acid of pectinolytic enzyme production by Sclerotinia sclerotiorum. Curr. Microbiol. 33: 49-53.
http://dx.doi.org/10.1007/s002849900073
PMid:8661689
Hegedus DD, Li R, Buchwaldt L, Parkin I, et al. (2008). Brassica napus possesses an expanded set of polygalacturonase inhibitor protein genes that are differentially regulated in response to Sclerotinia sclerotiorum infection, wounding and defense hormone treatment. Planta 228: 241-253.
http://dx.doi.org/10.1007/s00425-008-0733-1
PMid:18431596
Isshiki A, Akimitsu K, Yamamoto M and Yamamoto H (2001). Endopolygalacturonase is essential for citrus black rot caused by Alternaria citri but not brown spot caused by Alternaria alternata. Mol. Plant Microbe Interact. 14: 749-757.
http://dx.doi.org/10.1094/MPMI.2001.14.6.749
PMid:11386370
Kasza Z, Vagvolgyi C, Fevre M and Cotton P (2004). Molecular characterization and in planta detection of Sclerotinia sclerotiorum endopolygalacturonase genes. Curr. Microbiol. 48: 208-213.
http://dx.doi.org/10.1007/s00284-003-4166-6
PMid:15057467
Li R, Rimmer R, Yu M, Sharpe AG, et al. (2003). Two Brassica napus polygalacturonase inhibitory protein genes are expressed at different levels in response to biotic and abiotic stresses. Planta 217: 299-308.
PMid:12783338
Li R, Rimmer R, Buchwaldt L, Sharpe AG, et al. (2004). Interaction of Sclerotinia sclerotiorum with Brassica napus: cloning and characterization of endo- and exo-polygalacturonases expressed during saprophytic and parasitic modes. Fungal Genet. Biol. 41: 754-765.
http://dx.doi.org/10.1016/j.fgb.2004.03.002
PMid:15219560
Manfredini C, Sicilia F, Ferrari S, Pontiggia D, et al. (2005). Polygalacturonase-inhibiting protein 2 of Phaseolus vulgaris inhibits BcPG1, a polygalacturonase of Botrytis cinerea important for pathogenicity, and protects transgenic plants from infection. Physiol. Mol. Plant Pathol. 67: 108-115.
http://dx.doi.org/10.1016/j.pmpp.2005.10.002
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Oeser B, Heidrich PM, Muller U, Tudzynski P, et al. (2002). Polygalacturonase is a pathogenicity factor in the Claviceps purpurea/rye interaction. Fungal Genet. Biol. 36: 176-186.
http://dx.doi.org/10.1016/S1087-1845(02)00020-8
Poinssot B, Vandelle E, Bentejac M, Adrian M, et al. (2003). The endopolygalacturonase 1 from Botrytis cinerea activates grapevine defense reactions unrelated to its enzymatic activity. Mol. Plant Microbe Interact. 16: 553-564.
http://dx.doi.org/10.1094/MPMI.2003.16.6.553
PMid:12795381
Powell AL, van Kan J, ten Have A, Visser J, et al. (2000). Transgenic expression of pear PGIP in tomato limits fungal colonization. Mol. Plant Microbe Interact. 13: 942-950.
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Sicilia F, Fernandez-Recio J, Caprari C, De Lorenzo G, et al. (2005). The polygalacturonase-inhibiting protein PGIP2 of Phaseolus vulgaris has evolved a mixed mode of inhibition of endopolygalacturonase PG1 of Botrytis cinerea. Plant Physiol. 139: 1380-1388.
http://dx.doi.org/10.1104/pp.105.067546
PMid:16244152 PMCid:1283773
ten Have A, Mulder W, Visser J and van Kan JA (1998). The endopolygalacturonase gene Bcpg1 is required for full virulence of Botrytis cinerea. Mol. Plant Microbe Interact. 11: 1009-1016.
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PMid:9768518
ten Have A, Breuil WO, Wubben JP, Visser J, et al. (2001). Botrytis cinerea endopolygalacturonase genes are differentially expressed in various plant tissues. Fungal Genet. Biol. 33: 97-105.
http://dx.doi.org/10.1006/fgbi.2001.1269
PMid:11456462
Zuppini A, Navazio L, Sella L, Castiglioni C, et al. (2005). An endopolygalacturonase from Sclerotinia sclerotiorum induces calcium-mediated signaling and programmed cell death in soybean cells. Mol. Plant Microbe Interact. 18: 849-855.
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PMid:16134897
“Construction of a molecular database for soybean cultivar identification in Brazil”, vol. 9, pp. 705-720, 2010.
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