Výsledky vyhledávání - "Jean-Charles Gaudin"

Akademický článek

Critical structural elements for the antigenicity of wheat allergen LTP1 (Tri a 14) revealed by site-directed mutagenesis

Autor: Hamza Mameri, Jean-Charles Gaudin, Virginie Lollier, Olivier Tranquet, Chantal Brossard, Manon Pietri, Didier Marion, Fanny Codreanu-Morel, Etienne Beaudouin, Frank Wien, Yann Gohon, Pierre Briozzo, Sandra Denery-Papini

Publikováno v: Scientific Reports, Vol 12, Iss 1, Pp 1-17 (2022)

Abstract Lipid transfer proteins (LTPs) were identified as allergens in a large variety of pollens and foods, including cereals. LTPs belong to the prolamin superfamily and display an α-helical fold, with a bundle of four α-helices held together by

Externí odkaz: https://doaj.org/article/5d3afccf01ad4560a154f73ad26cbe92

Zobrazit plný text záznamu

Plný text ve formátu HTML

Akademický článek

Wheat DOF transcription factors TaSAD and WPBF regulate glutenin gene expression in cooperation with SPA.

Autor: Marielle Merlino, Jean-Charles Gaudin, Mireille Dardevet, Pierre Martre, Catherine Ravel, Julie Boudet

Publikováno v: PLoS ONE, Vol 18, Iss 6, p e0287645 (2023)

Grain storage proteins (GSPs) quantity and composition determine the end-use value of wheat flour. GSPs consists of low-molecular-weight glutenins (LMW-GS), high-molecular-weight glutenins (HMW-GS) and gliadins. GSP gene expression is controlled by a

Externí odkaz: https://doaj.org/article/b4cf0295e83740c397ec3c98529fd388

Zobrazit plný text záznamu

Plný text ve formátu HTML

Akademický článek

A chimeric IgE that mimics IgE from patients allergic to acid-hydrolyzed wheat proteins is a novel tool for in vitro allergenicity assessment of functionalized glutens.

Autor: Olivier Tranquet, Jean-Charles Gaudin, Sarita Patil, Johanna Steinbrecher, Kayoko Matsunaga, Reiko Teshima, Shinobu Sakai, Colette Larré, Sandra Denery-Papini

Publikováno v: PLoS ONE, Vol 12, Iss 11, p e0187415 (2017)

Acid-hydrolyzed wheat proteins (acid-HWPs) have been shown to provoke severe allergic reactions in Europe and Japan that are distinct from classical wheat allergies. Acid-HWPs were shown to contain neo-epitopes induced by the deamidation of gluten pr

Externí odkaz: https://doaj.org/article/5184bdbd2330459b85263163afa0c6a5

Zobrazit plný text záznamu

A chimeric IgE that mimics IgE from patients allergic to acid-hydrolyzed wheat proteins is a novel tool for in vitro allergenicity assessment of functionalized glutens

Autor: Colette Larré, Reiko Teshima, Olivier Tranquet, Sandra Denery-Papini, Kayoko Matsunaga, Jean Charles Gaudin, Sarita U. Patil, Johanna Steinbrecher, Shinobu Sakai

Publikováno v: PLoS ONE, Vol 12, Iss 11, p e0187415 (2017)
PLoS ONE
PLoS ONE, Public Library of Science, 2017, 12 (11), ⟨10.1371/journal.pone.0187415⟩
Plos One 11 (12), . (2017)

International audience; Background Acid-hydrolyzed wheat proteins (acid-HWPs) have been shown to provoke severe allergic reactions in Europe and Japan that are distinct from classical wheat allergies. Acid-HWPs were shown to contain neo-epitopes indu

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a7482001c3d4f27a7f735fc43bf7052c
http://europepmc.org/articles/PMC5678878?pdf=render

Zobrazit plný text záznamu

Allergy to Goat/Sheep’s Milk with Good Tolerance to Cow’s Milk but Not to Cow’s Milk Cheese: Identification of 1-105 Peptide from -Casein as the Molecular Basis of Reactivity toward Cow’s Milk Cheese for Two Patients

Autor: Sandra Denery-Papini, Martine Drouet, Marion Beaumesnil, Jean-Charles Gaudin

Publikováno v: Research in immunology
Research in immunology, Elsevier, 2013, pp.1-7. ⟨10.5171/2013.168397⟩
Research in Immunology, 1-7. (2013)

International audience; In Europe, a new population of patients developing anaphylaxis to goat’s/sheep’s milk associated to tolerance to cow’s milk has recently appeared. Nevertheless, among these patients, some show allergic reactions to cow�

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b7381e9e7c12f8c6b344f1297e0afe31
https://doi.org/10.5171/2013.168397

Zobrazit plný text záznamu

MS Analysis and Molecular Characterization of Botrytis cinerea Protease Prot-2. Use in Bioactive Peptides Production

Autor: Nayssene Aissaoui, Ferid Abidi, Thomas Haertlé, Mohamed Nejib Marzouki, Jean-Marc Chobert, Jean-Charles Gaudin

Publikováno v: Applied Biochemistry and Biotechnology
Applied Biochemistry and Biotechnology, Humana Press, 2013, 170 (2), pp.231-247. ⟨10.1007/s12010-013-0186-2⟩

Prot-2 protease previously purified to homogeneity from Botrytis cinerea showed potentiality to be used in detergency and for production of bioactive peptides. To extend the characterization of Prot-2 protease, antifungal and antibacterial assays wer

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a26a252b5c586f04f8a60f225746c7fc
https://doi.org/10.1007/s12010-013-0186-2

Zobrazit plný text záznamu

Wheat gliadins modified by deamidation are more efficient than native gliadins in inducing a Th2 response in Balb/c mice experimentally sensitized to wheat allergens

Autor: Colette Larré, Chantal Brossard, Pascal Gourbeyre, Marie Bodinier, Sandra Denery-Papini, Jean-Charles Gaudin

Publikováno v: Molecular Nutrition and Food Research
Molecular Nutrition and Food Research, Wiley-VCH Verlag, 2012, 56 (2), pp.336-344. ⟨10.1002/mnfr.201100353⟩

International audience; Scope: Wheat gluten proteins such as gliadins constitute major food allergens. Gluten can be modified industrially by deamidation which increases its solubility and enhances its use as a food ingredient. Sensitization to deami

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3938d4c6c7caff62cdbfbe294ee3d605
https://doi.org/10.1002/mnfr.201100353

Zobrazit plný text záznamu

Modifications of the charges at the N-terminus of bovine β-casein: Consequences on its structure and its micellisation

Autor: Monique A.V. Axelos, Stéphane Gangnard, V. K. Fedotov, Jean-Marc Chobert, Thomas Haertlé, Yuri F. Zuev, Jean-Charles Gaudin, Yvan Choiset

Publikováno v: Food Hydrocolloids
Food Hydrocolloids, Elsevier, 2007, 21 (2), pp.180-190. ⟨10.1016/j.foodhyd.2006.03.007⟩

Due to the combination of flexibility and amphiphilicity, in solution β -casein ( β -CN) acts as a surfactant molecule. It undergoes self-association and forms “micellar-like” aggregates in aqueous media. The aim of our study was to understand

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5b7d84750508a0c493e629d6dcbd3e02
https://doi.org/10.1016/j.foodhyd.2006.03.007

Zobrazit plný text záznamu

Vyhledávací nástroje:

Upřesnit hledání