Zobrazeno 1 - 10
of 33
pro vyhledávání: '"Jean Chaudiere"'
Autor:
Jean Chaudière
Publikováno v:
International Journal of Molecular Sciences, Vol 24, Iss 12, p 10109 (2023)
Selenocysteine is a catalytic residue at the active site of all selenoenzymes in bacteria and mammals, and it is incorporated into the polypeptide backbone by a co-translational process that relies on the recoding of a UGA termination codon into a se
Externí odkaz:
https://doaj.org/article/b8377d73226b42869f84281c93b5ce95
Autor:
Jia-Rong Zhang, Claudine Trossat-Magnin, Katell Bathany, Luc Negroni, Serge Delrot, Jean Chaudière
Publikováno v:
Molecules, Vol 27, Iss 3, p 1047 (2022)
Twelve polyphenols from three distinct families (dihydroflavonols, flavan-3-ols, and flavanones) were studied as potential substrates of anthocyanidin synthase from Vitis vinifera (VvANS). Only flavan-3-ols of (2R,3S) configuration having either a ca
Externí odkaz:
https://doaj.org/article/54488813a913466988b219e6ebccde71
Publikováno v:
Journal of Agricultural and Food Chemistry
Journal of Agricultural and Food Chemistry, American Chemical Society, 2019, 67 (13), pp.3595-3604. ⟨10.1021/acs.jafc.8b06968⟩
Journal of Agricultural and Food Chemistry, American Chemical Society, 2019, 67 (13), pp.3595-3604. ⟨10.1021/acs.jafc.8b06968⟩
International audience; Anthocyanidin synthase from Vitis vinifera (VvANS) catalyzes the in vitro transformation of the natural isomer of leucocyanidin, 2R,3S,4S-cis-leucocyanidin, into 2R,4S-flavan-3,3,4-triol ([M + H]+, m/z 323) and quercetin. The
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b810ff93854da5039cbaf646cdb6d91e
https://hal.inrae.fr/hal-02623939
https://hal.inrae.fr/hal-02623939
Autor:
Jia-rong Zhang, Béatrice Langlois d'Estaintot, Katell Bathany, Jean Chaudiere, James Tolchard
Publikováno v:
Journal of Agricultural and Food Chemistry
Journal of Agricultural and Food Chemistry, American Chemical Society, 2018, 66 (1), pp.351-358
Journal of Agricultural and Food Chemistry, American Chemical Society, 2018, 66 (1), pp.351-358. ⟨10.1021/acs.jafc.7b04380⟩
Journal of Agricultural and Food Chemistry, American Chemical Society, 2018, 66 (1), pp.351-358
Journal of Agricultural and Food Chemistry, American Chemical Society, 2018, 66 (1), pp.351-358. ⟨10.1021/acs.jafc.7b04380⟩
(+)-2,3-trans-3,4-cis-Leucocyanidin was produced by acidic epimerization of (+)-2,3-trans-3,4-trans-leucocyanidin synthesized by reduction of (+)-dihydroquercetin with NaBH4, and structures of the two stereoisomers purified by C18- and phenyl-reverse
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d6e77bb831592e0c692522485c958c5c
https://hal.archives-ouvertes.fr/hal-03160315
https://hal.archives-ouvertes.fr/hal-03160315
Autor:
Mahmoud Gargouri, Thierry Granier, Jean-Marie Schmitter, Claude Manigand, Bernard Gallois, Chloé Maugé, Béatrice Langlois d'Estaintot, Jean Chaudiere
Publikováno v:
Journal of Molecular Biology. 397:1079-1091
Leucoanthocyanidin reductase (LAR) catalyzes the NADPH-dependent reduction of 2R,3S,4S-flavan-3,4-diols into 2R,3S-flavan-3-ols, a subfamily of flavonoids that is important for plant survival and for human nutrition. LAR1 from Vitis vinifera has been
Autor:
Katell Bathany, Claude Manigand, Chloé Maugé, Jean Chaudiere, Bernard Gallois, Mahmoud Gargouri, Jean-Marie Schmitter
Publikováno v:
Biological Chemistry. 391:219-227
Anthocyanidin reductase (ANR) from Vitis vinifera catalyzes an NADPH-dependent double reduction of anthocyanidins producing a mixture of (2S,3R)- and (2S,3S)-flavan-3-ols. At pH 7.5 and 30°C, the first hydride transfer to anthocyanidin is irreversib
Autor:
Chloé Maugé, Olivier Cala, Bernard Gallois, Jean Chaudiere, Thierry Granier, Mahmoud Gargouri, Claude Manigand, Katell Bathany, Isabelle Pianet, Béatrice Langlois d'Estaintot
Publikováno v:
Acta Crystallographica Section D Biological Crystallography. 65:989-1000
Together with leucoanthocyanidin reductase, anthocyanidin reductase (ANR) is one of the two enzymes of the flavonoid-biosynthesis pathway that produces the flavan-3-ol monomers required for the formation of proanthocyanidins or condensed tannins. It
Autor:
Béatrice Langlois d'Estaintot, Pierre Petit, Bernard Gallois, Claude Manigand, Jean Chaudiere, Thierry Granier, Nadia Trabelsi
Publikováno v:
Acta Crystallographica Section D Biological Crystallography. 64:883-891
Dihydroflavonol 4-reductase (DFR) is a key enzyme of the flavonoid biosynthesis pathway which catalyses the NADPH-dependent reduction of 2R,3R-trans-dihydroflavonols to leucoanthocyanidins. The latter are the precursors of anthocyans and condensed ta
Autor:
M. Piciotti, Michel Clément, Jean-Marie Bourre, Georges Durand, Gérard Pascal, Huguette Lafont, Michelle Bonneil, Gilles Nalbone, Jean Chaudiere, Odile Dumont
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::c35772f2ad8cef2a4906f528b2961dd4
https://doi.org/10.1159/000419283
https://doi.org/10.1159/000419283
Autor:
Jean Chaudiere, R. Ferrari-Iliou
Publikováno v:
Food and Chemical Toxicology. 37:949-962
Intracellular antioxidants include low molecular weight scavengers of oxidizing species, and enzymes which degrade superoxide and hydroperoxides. Such antioxidants systems prevent the uncontrolled formation of free radicals and activated oxygen speci