Výsledky vyhledávání - "Guy Branlant"

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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Structural diversity in the recognition between reduced thioredoxin and its oxidized enzyme partners

Autor: Arnaud Gruez, Guy Branlant

Publikováno v: BioMolecular Concepts. 3:141-150

Thioredoxins (Trx) are ubiquitous proteins that are conserved in all living organisms from archaea to humans. These small proteins display various cellular roles, including functioning as reductases in redox processes. All Trxs share a similar, chara

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::13da5a7add430c325a261fd9b8c90fba
https://doi.org/10.1515/bmc.2011.056

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Methylmalonate-semialdehyde Dehydrogenase from Bacillus subtilis

Autor: Claire Stines-Chaumeil, Guy Branlant, François Talfournier

Publikováno v: Journal of Biological Chemistry. 286:21971-21981

Methylmalonate-semialdehyde dehydrogenase (MSDH) belongs to the CoA-dependent aldehyde dehydrogenase subfamily. It catalyzes the NAD-dependent oxidation of methylmalonate semialdehyde (MMSA) to propionyl-CoA via the acylation and deacylation steps. M

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::8b419ea2e38ff009fafa83fc0ebe28fd
https://doi.org/10.1074/jbc.m110.213280

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Thioredoxin 2 fromEscherichia coliis not involvedin vivoin the recycling process of methionine sulfoxide reductase activities

Autor: Guy Branlant, Alexandre Kriznik, Sandrine Boschi-Muller, Christophe Jacob

Publikováno v: FEBS Letters
FEBS Letters, Wiley, 2011, 585 (12), pp.1905-1909. ⟨10.1016/j.febslet.2011.04.070⟩

Thioredoxins (Trx) 1 and 2, and three methionine sulfoxide reductases (Msr) whose activities are Trx-dependent, are expressed in Escherichia coli. A metB1 trxA mutant was shown to be unable to grow on methionine sulfoxide (Met-O) suggesting that Trx2

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3d1cce5f50a4ec3d7b5dcc62b48a643c
https://doi.org/10.1016/j.febslet.2011.04.070

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Solution Structure and Backbone Dynamics of the Cysteine 103 to Serine Mutant of the N-Terminal Domain of DsbD from Neisseria meningitides

Autor: Marc Quinternet, Manh-Thong Cung, Laure Selme, Marie-Christine Averlant-Petit, Pascale Tsan, Christophe Jacob, Guy Branlant, Chrystel Beaufils, Sandrine Boschi-Muller

Publikováno v: Biochemistry
Biochemistry, American Chemical Society, 2008, 47 (48), pp.12710-20. ⟨10.1021/bi801343c⟩

International audience; The DsbD protein is essential for electron transfer from the cytoplasm to the periplasm of Gram-negative bacteria. Its N-terminal domain dispatches electrons coming from cytoplasmic thioredoxin (Trx), via its central transmemb

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0961b6374a8e9e51ac3c48cdeac7e6a4
https://doi.org/10.1021/bi801343c

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A Structural Analysis of the Catalytic Mechanism of Methionine Sulfoxide Reductase A from Neisseria meningitidis

Autor: Frédérique Favier, André Aubry, Brice Kauffmann, Fanomezana M. Ranaivoson, Guy Branlant, Mathias Antoine, Sandrine Boschi-Muller

Publikováno v: Journal of Molecular Biology
Journal of Molecular Biology, Elsevier, 2008, 377 (1), pp.268-280. ⟨10.1016/j.jmb.2008.01.021⟩

The methionine sulfoxide reductases (Msrs) are thioredoxin-dependent oxidoreductases that catalyse the reduction of the sulfoxide function of the oxidized methionine residues. These enzymes have been shown to regulate the life span of a wide range of

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::afe3d756dc69ae44c8629546075c2596
https://doi.org/10.1016/j.jmb.2008.01.021

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Characterization of the Amino Acids Involved in Substrate Specificity of Methionine Sulfoxide Reductase A

Autor: Sandrine Boschi-Muller, Mathias Antoine, Adeline Gand, Guy Branlant

Publikováno v: Journal of Biological Chemistry
Journal of Biological Chemistry, American Society for Biochemistry and Molecular Biology, 2007, 282 (28), pp.20484-20491. ⟨10.1074/jbc.M702350200⟩

International audience; Methionine sulfoxide reductases (Msrs) are ubiquitous enzymes that catalyze the thioredoxin-dependent reduction of methionine sulfoxide (MetSO) back to methionine. In vivo, Msrs are essential in protecting cells against oxidat

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::673759918b90f589eebeac2dc820741e
https://doi.org/10.1074/jbc.m702350200

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Evidence That Glutathione and the Glutathione System Efficiently Recycle 1-Cys Sulfiredoxin In Vivo

Autor: Samia Boukhenouna, Michel B. Toledano, Guy Branlant, Christophe Jacob, Hortense Mazon, Sophie Rahuel-Clermont

Publikováno v: Antioxidants and Redox Signaling
Antioxidants and Redox Signaling, Mary Ann Liebert, 2015, 22 (9), pp.731-743. ⟨10.1089/ars.2014.5998⟩
Antioxidants and Redox Signaling, 2015, 22 (9), pp.731-743. ⟨10.1089/ars.2014.5998⟩

International audience; Aims: Typical 2-Cys peroxiredoxins (2-Cys Prxs) are Cys peroxidases that undergo inactivation by hyperoxidation of the catalytic Cys, a modification reversed by ATP-dependent reduction by sulfiredoxin (Srx). Such an attribute

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e9af7a6c5b1cc4ed7c013cb2e49f7d0b
https://europepmc.org/articles/PMC4361365/

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Insights into the role of the metal binding site in methionine-R-sulfoxide reductases B

Autor: Sandrine Boschi-Muller, Guy Branlant, Daniel Burnel, Hong Yu, Alexandre Olry

Publikováno v: Protein Science. 14:2828-2837

Methionine sulfoxide reductases B (MsrBs) catalyze the reduction of methionine-R-sulfoxide via a three-step chemical mechanism including a reductase step, formation of an intradisulfide bond followed by a thioredoxin recycling process. Fifty percent

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::5ab23b0a90ccfebd70953729ccb719fc
https://doi.org/10.1110/ps.051711105

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Thermal Destabilization of Non-phosphorylating Glyceraldehyde-3-phosphate Dehydrogenase from Streptococcus mutans upon Phosphate Binding in the Active Site

Autor: Guy Branlant, Victor N. Orlov, Stéphane Marchal, Denis Arutyunov, Vladimir I. Muronetz, Sophie Rahuel-Clermont

Publikováno v: Journal of Biological Chemistry
Journal of Biological Chemistry, American Society for Biochemistry and Molecular Biology, 2005, 280 (19), pp.18590-18597. ⟨10.1074/jbc.M414110200⟩
Journal of Biological Chemistry, 2005, 280 (19), pp.18590-18597. ⟨10.1074/jbc.M414110200⟩

International audience; Catalysis by the NADP-dependent non-phosphorylating glyceraldehyde-3-phosphate dehydrogenase (GAPN) from Streptococcus mutans, a member of the aldehyde dehydrogenase (ALDH) family, relies on a local conformational reorganizati

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::bd0baaa8a8adc4fdaded1e93e7f94ae1
https://doi.org/10.1074/jbc.m414110200

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