Zobrazeno 1 - 10 of 33 pro vyhledávání: '"Guillermo Mulliert"'
1
Akademický článek
Biochemical and Structural Characterization of Chi-Class Glutathione Transferases: A Snapshot on the Glutathione Transferase Encoded by sll0067 Gene in the Cyanobacterium Synechocystis sp. Strain PCC 6803
Autor: Eva Mocchetti, Laura Morette, Guillermo Mulliert, Sandrine Mathiot, Benoît Guillot, François Dehez, Franck Chauvat, Corinne Cassier-Chauvat, Céline Brochier-Armanet, Claude Didierjean, Arnaud Hecker
Publikováno v: Biomolecules, Vol 12, Iss 10, p 1466 (2022)
Glutathione transferases (GSTs) constitute a widespread superfamily of enzymes notably involved in detoxification processes and/or in specialized metabolism. In the cyanobacterium Synechocsytis sp. PCC 6803, SynGSTC1, a chi-class GST (GSTC), is thoug
Externí odkaz: https://doaj.org/article/4216006f688645b5bb441db324171ea0
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3
Akademický článek
Matrix metalloproteinase 9 polymorphism and outcome after myocardial infarction
Autor: Sophie Rodius, Guillermo Mulliert, Francisco Azuaje, Yvan Devaux, Daniel R. Wagner
Publikováno v: Cardiogenetics, Vol 1, Iss 1, Pp e5-e5 (2011)
Matrix metalloproteinase 9 (MMP9) is functionally implicated in the process of infarct healing. Several genetic variation of the MMP9 gene have been described, among which the MMP9 Arg668Gln polymorphism. In the present study, we assessed whether thi
Externí odkaz: https://doaj.org/article/83e1f0cfa03d4872b1cfe37638345453
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4
The structure of Trametes versicolor glutathione transferase Omega 3S bound to its conjugation product glutathionyl-phenethylthiocarbamate reveals plasticity of its active site
Autor: Thomas Perrot, Mélanie Morel-Rouhier, Mathieu Schwartz, Claude Didierjean, Eric Gelhaye, Frédérique Favier, Guillermo Mulliert
Publikováno v: Protein Science
Protein Science, Wiley, 2019, 28 (6), pp.1143-1150. ⟨10.1002/pro.3620⟩
Protein Sci
Trametes versicolor glutathione transferase Omega 3S (TvGSTO3S) catalyzes the conjugation of isothiocyanates (ITC) with glutathione (GSH).Previously, this isoform was investigated in depth both biochemically and structurally. Structural analysis of c
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::56acc52bbb0a5aca7f3046529d134094
https://hal.archives-ouvertes.fr/hal-02311418
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6
Trametes versicolor glutathione transferase Xi 3, a dual Cys-GST with catalytic specificities of both Xi and Omega classes
Autor: Guillermo Mulliert, Mathieu Schwartz, Thomas Roret, Claude Didierjean, Frédérique Favier, Aurélie Deroy, Thomas Perrot, Mélanie Morel-Rouhier, Eric Gelhaye
Publikováno v: FEBS Letters
FEBS Letters, Wiley, 2018, 592 (18), pp.3163-3172. ⟨10.1002/1873-3468.13224⟩
Glutathione transferases (GSTs) from the Xi and Omega classes have a catalytic cysteine residue, which gives them reductase activities. Until now, they have been assigned distinct substrates. While Xi GSTs specifically reduce glutathionyl-(hydro)quin
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0f4e476c3352ddc75bb5ba7c1df75e2c
https://hal.archives-ouvertes.fr/hal-01959634/document
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7
Identification of Key Functional Residues in the Active Site of Human β1,4-Galactosyltransferase 7
Autor: Rafael Oriol, Ibtissam Talhaoui, Guillermo Mulliert, Sandrine Gulberti, Catherine Bui, Michael W.H. Coughtrie, Mohamed Ouzzine, Patrick Netter, Sylvie Fournel-Gigleux
Publikováno v: Journal of Biological Chemistry
Journal of Biological Chemistry, American Society for Biochemistry and Molecular Biology, 2010, 285 (48), pp.37342-37358. ⟨10.1074/jbc.m110.151951⟩
Glycosaminoglycans (GAGs) play a central role in many pathophysiological events, and exogenous xyloside substrates of β1,4-galactosyltransferase 7 (β4GalT7), a major enzyme of GAG biosynthesis, have interesting biomedical applications. To predict f
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::17464ddba0599e6ef3e8efab81d6f7e8
https://doi.org/10.1074/jbc.m110.151951
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9
Identification by FT-ICR-MS of Camelus dromedarius α-lactalbumin variants as the result of nonenzymatic deamidation of Asn-16 and Asn-45
Autor: Jean-Michel Girardet, Abderrahmane Mati, Saliha Si Ahmed Zennia, Joëlle Vinh, Giovanni Chiappetta, Yann Verdier, Guillermo Mulliert, Laurent Miclo, Franck Saulnier
Publikováno v: Food Chemistry
Food Chemistry, Elsevier, 2015, 187, pp.305-313. ⟨10.1016/j.foodchem.2015.04.036⟩
International audience; Nonenzymatic deamidation of asparaginyl residues can occur spontaneously under physiological conditions principally when a glycyl residue is at the carboxyl side of Asn and leads to formation of aspartyl and isoaspartyl residu
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b0b534d810bc687a4e4307a48af6215c
https://hal.univ-lorraine.fr/hal-01522025
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10
Modifications of the Glycosaminoglycan-Linkage Region of Proteoglycans: Phosphorylation and Sulfation Determine the Activity of the Human ß1,4-Galactosyltransferase 7 and ß1,3-Glucuronosyltransferase I
Autor: Patrick Netter, Magali Fondeur, Jean-Claude Jacquinet, Sylvie Fournel-Gigleux, Sandrine Gulberti, Guillermo Mulliert, Virginie Lattard, Jacques Magdalou, Mohamed Ouzzine
Publikováno v: The Scientific World Journal, Vol 5, Pp 510-514 (2005)
The Scientific World Journal
Sandrine Gulberti, Virginie Lattard, Magali Fondeur, Jean-Claude Jacquinet, Guillermo Mulliert, Patrick Netter, Jacques Magdalou, Mohamed Ouzzine, and Sylvie Fournel-Gigleux* UMR 7561 CNRS-Universite Henri Poincare Nancy I, Faculte de Medecine, BP 18
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::92f6c51edacc7882e9bf3c544bbc58e9
https://doi.org/10.1100/tsw.2005.65
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