N
Nicole Hugouvieux-Cotte-Pattat
Researcher at University of Lyon
Publications - 54
Citations - 2708
Nicole Hugouvieux-Cotte-Pattat is an academic researcher from University of Lyon. The author has contributed to research in topics: Pectate lyase & Pectobacterium chrysanthemi. The author has an hindex of 29, co-authored 50 publications receiving 2513 citations. Previous affiliations of Nicole Hugouvieux-Cotte-Pattat include Centre national de la recherche scientifique.
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Journal ArticleDOI
Regulation of pectinolysis in erwinia chrysanthemi
TL;DR: The regulation of pel genes requires several regulatory systems, including the KdgR repressor, which mediates the induction of all the pectinolysis genes in the presence of pectin catabolites.
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The secretome of the plant pathogenic bacterium Erwinia chrysanthemi
TL;DR: A proteomic analysis to create a reference map of the E. chrysanthemi secretome revealed that the type II Out system mediates secretion of the esterase FaeD and of the Avr‐like protein AvrL, homologous to an avirulence protein of Xanthomonas campestris.
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Bacterial pectate lyases, structural and functional diversity.
TL;DR: Pectate lyases are enzymes involved in plant cell wall degradation that cleave pectin using a β-elimination mechanism, specific for acidic polysaccharides, and are mainly produced by plant pathogens and plant-associated organisms, and only rarely by animals.
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Comparative analysis of the five major Erwinia chrysanthemi pectate lyases: enzyme characteristics and potential inhibitors.
TL;DR: In Erwinia chrysanthemi 3937, pectate lyase activity mainly results from the cumulative action of five major isoenzymes, PelA to PelE, and it is demonstrated that two compounds present in plant tissues, epicatechin and salicylic acid, inhibit the pECTate lyases.
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N-Sulfonyl homoserine lactones as antagonists of bacterial quorum sensing.
Sandra Castang,Bernard Chantegrel,Christian Deshayes,Rene Dolmazon,Patrice Gouet,Richard Haser,Sylvie Reverchon,William Nasser,Nicole Hugouvieux-Cotte-Pattat,Alain Doutheau +9 more
TL;DR: A series of 11 new analogues of N-acylhomoserine lactones in which the carboxamide bond was replaced by a sulfonamide one, has been synthesised and molecular modeling suggests that the latter prevent a cascade of structural rearrangements necessary for the formation of the active LuxR dimer.