Výsledky vyhledávání - "Sophie Rahuel-Clermont"

Akademický článek

Anti-Inflammatory Activity of Bryophytes Extracts in LPS-Stimulated RAW264.7 Murine Macrophages

Autor: Raíssa Volpatto Marques, Stefania Enza Sestito, Frédéric Bourgaud, Sissi Miguel, Frédéric Cailotto, Pascal Reboul, Jean-Yves Jouzeau, Sophie Rahuel-Clermont, Sandrine Boschi-Muller, Henrik Toft Simonsen, David Moulin

Publikováno v: Molecules, Vol 27, Iss 6, p 1940 (2022)

Bryophytes produce rare and bioactive compounds with a broad range of therapeutic potential, and many species are reported in ethnomedicinal uses. However, only a few studies have investigated their potential as natural anti-inflammatory drug candida

Externí odkaz: https://doaj.org/article/d94e0c4bbfff4d85904afe3381ad78cc

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Redox-based sensing controls bacterial chemotaxis to copper

Autor: Gwennaëlle Louis, Pauline Cherry, Catherine Michaux, Sophie Rahuel-Clermont, Marc Dieu, Françoise Tilquin, Laurens Maertens, Rob Van Houdt, Patricia Renard, Eric Perpete, Jean-Yves Matroule

Chemotaxis is a widespread strategy used by unicellular and multicellular living organisms to maintain their fitness in stressful environments. In bacteria, the control of chemotaxis relies on the sensing of environmental changes by chemoreceptors, w

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::9a478ef7dfac302d302a2ab6e65cc261
https://doi.org/10.1101/2022.06.29.497744

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Splice variants of protein disulfide isomerase - identification, distribution and functional characterization in the rat

Autor: Thomas Chetot, Xavier Serfaty, Léna Carret, Alexandre Kriznik, null Sophie-Rahuel-Clermont, Lucie Grand, Maïwenn Jacolot, Florence Popowycz, Etienne Benoit, Véronique Lambert, Virginie Lattard

Publikováno v: Biochimica et biophysica acta. General subjects. 1867(2)

Protein Disulfide Isomerase (PDI) enzyme is an emerging therapeutic target in oncology and hematology. Although PDI reductase activity has been studied with isolated fragments of the protein, natural structural variations affecting reductase activity

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::98376d0294770d0d873408cf8ca53a7b
https://pubmed.ncbi.nlm.nih.gov/36423740

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Probing the mechanism of the peroxiredoxin decamer interaction with its reductase sulfiredoxin from the single molecule to the solution scale

Autor: Audrey Beaussart, Florent Canonico, Hortense Mazon, Jorge Hidalgo, Sarah Cianférani, Hélène Le Cordier, Alexandre Kriznik, Sophie Rahuel-Clermont

Publikováno v: Nanoscale Horizons
Nanoscale Horizons, 2022, 7 (5), pp.515-525. ⟨10.1039/d2nh00037g⟩

Peroxiredoxins from the Prx1 subfamily (Prx) are highly regulated multifunctional proteins involved in oxidative stress response, redox signaling and cell protection. Prx is a homodimer that associates into a decamer. The monomer C-terminus plays int

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2732e62e206c7ffac71323df5258d406
https://pubmed.ncbi.nlm.nih.gov/35234779

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Screening of natural extract libraries for anti-inflammatory properties

Autor: David MOULIN, Sophie Rahuel-Clermont

Publikováno v: 2nd International Conference on Biomolecules and the Bioeconomy
2nd International Conference on Biomolecules and the Bioeconomy, Nov 2021, Nancy, France
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International audience

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=dedup_wf_001::7293cb76b997be6577e877a16e0e344c
https://hal.univ-lorraine.fr/hal-03516993

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Dynamics of a key conformational transition in the mechanism of peroxiredoxin sulfinylation

Autor: Alexandre Kriznik, Samia Boukhenouna, Marouane Libiad, Hélène Le Cordier, Sophie Rahuel-Clermont, Michel B. Toledano

Publikováno v: ACS Catalysis
ACS Catalysis, American Chemical Society, 2020, 10 (5), pp.3326-3339. ⟨10.1021/acscatal.9b04471⟩
ACS Catalysis, 2020, 10 (5), pp.3326-3339. ⟨10.1021/acscatal.9b04471⟩

International audience; Peroxiredoxins from the Prx1 subfamily (Prx) are moonlighting peroxidases that operate in peroxide signaling and are regulated by sulfinylation. Prxs offer a major model of protein−thiol oxidative modification. They react wi

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8383c1d6550ef4c908d4bff2989b4416
https://hal.univ-lorraine.fr/hal-02473398/document

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Parsing protein sulfinic acid switches

Autor: Sophie Rahuel-Clermont, Michel B. Toledano

Publikováno v: Nature Chemical Biology
Nature Chemical Biology, Nature Publishing Group, 2018, 14 (11), pp.991-993. ⟨10.1038/s41589-018-0151-z⟩
Nature Chemical Biology, 2018, 14 (11), pp.991-993. ⟨10.1038/s41589-018-0151-z⟩

The proteome-wide application of a probe that selectively labels cysteine residues oxidized to the sulfinic acid form reveals the mammalian S-sulfinylome and uncovers novel substrates of the sulfinyl reductase sulfiredoxin, opening yet unexplored rea

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3c4689fa3cc6d8ab17a7d35a1657292d
https://pubmed.ncbi.nlm.nih.gov/30327557

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A scaffold protein that chaperones a cysteine-sulfenic acid in H2O2 signaling

Autor: Benoît D'Autréaux, Alexandre Kriznik, Antoine Bersweiler, Agnès Delaunay-Moisan, Sophie Rahuel-Clermont, Gemma Belli, Michel B. Toledano, Hortense Mazon

Publikováno v: Nature Chemical Biology
Nature Chemical Biology, Nature Publishing Group, 2017, 13 (8), pp.909-915. 〈10.1038/nCHeMBIO.2412〉
Recercat. Dipósit de la Recerca de Catalunya
instname
Repositorio Abierto de la UdL
Universitad de Lleida
Nature Chemical Biology, 2017, 13 (8), pp.909-915. ⟨10.1038/nCHeMBIO.2412⟩
Recercat: Dipósit de la Recerca de Catalunya
Varias* (Consorci de Biblioteques Universitáries de Catalunya, Centre de Serveis Científics i Acadèmics de Catalunya)
Nature Chemical Biology, Nature Publishing Group, 2017, 13 (8), pp.909-915. ⟨10.1038/nCHeMBIO.2412⟩

In Saccharomyces cerevisiae, Yap1 regulates an H2O2-inducible transcriptional response that controls cellular H2O2 homeostasis. H2O2 activates Yap1 by oxidation through the intermediacy of the thiol-peroxidase Orp1. Upon reacting with H2O2, Orp1 cata

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9c59a4074835802b719224b2231e1de7
https://hal.univ-lorraine.fr/hal-01652643/document

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Retinoic acid biosynthesis catalyzed by retinal dehydrogenases relies on a rate-limiting conformational transition associated with substrate recognition

Autor: Sophie Rahuel-Clermont, Guy Branlant, François Talfournier, Raphael Bchini, Vasilis Vasiliou

Publikováno v: Chemico-Biological Interactions
Chemico-Biological Interactions, Elsevier, 2013, 202 (1-3, SI), pp.78-84. ⟨10.1016/j.cbi.2012.11.019⟩

International audience; Retinoic acid (RA), a metabolite of vitamin A, exerts pleiotropic ă effects throughout life in vertebrate organisms. Thus, RA action must be ă tightly regulated through the coordinated action of biosynthetic and ă degrading

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::eafd519d94f8fa16020a207a2bf14661
https://doi.org/10.1016/j.cbi.2012.11.019

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