Zobrazeno 1 - 10
of 49
pro vyhledávání: '"Marchand CH"'
Autor:
Martins, L, Knuesting, J, Bariat, L, Dard, A, Freibert, SA, Marchand, CH, Young, D, Dung, NHT, Debures, A, Saez-Vasquez, J, Lemaire, SD, Lill, R, Messens, J, Riondet, C
Living organisms use a large panel of mechanisms to protect themselves from environmental stress. Particularly, heat stress induces misfolding and aggregation of proteins which are guarded by chaperone systems. Here, we examine the function the gluta
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=od______3848::4bfffa60a3fba465c989646b3fa3e45d
https://biblio.vub.ac.be/vubir/redox-response-of-ironsulfur-glutaredoxin-grxs17-activates-its-holdase-activity-to-protect-plants-from-heat-stress(6260d22e-0c3d-495f-93d7-1d4dbd3c0631).html
https://biblio.vub.ac.be/vubir/redox-response-of-ironsulfur-glutaredoxin-grxs17-activates-its-holdase-activity-to-protect-plants-from-heat-stress(6260d22e-0c3d-495f-93d7-1d4dbd3c0631).html
Autor:
Merienne Camille, Marchand Chloe, Filali Samira, Salmon Damien, Pivot Christine, Pirot Fabrice
Publikováno v:
Pharmaceutical Technology in Hospital Pharmacy, Vol 5, Iss 1, Pp 1552-99 (2020)
Stability of low amoxicillin oral dosage form (5 mg) used in reintroduction drug test was not fully documented. Furthermore, the impact of (1) salt moiety of amoxicillin and (2) amoxicillin – excipient interactions upon the antibiotic formulation s
Externí odkaz:
https://doaj.org/article/6068a9ee6b1c4c6e8c240b3e0bafba0f
Autor:
Maes Alexandre, Martinez Xavier, Druart Karen, Laurent Benoist, Guégan Sean, Marchand Christophe H., Lemaire Stéphane D., Baaden Marc
Publikováno v:
Journal of Integrative Bioinformatics, Vol 15, Iss 2, Pp I1-7 (2018)
Proteomic and transcriptomic technologies resulted in massive biological datasets, their interpretation requiring sophisticated computational strategies. Efficient and intuitive real-time analysis remains challenging. We use proteomic data on 1417 pr
Externí odkaz:
https://doaj.org/article/983a449d1cf2448aaf03035e2aeb3ba0
Autor:
Marchand, Ch., Foggia, A.
Publikováno v:
IEEE Transactions on Magnetics; 1983, Vol. 19 Issue 6, p2647-2649, 3p
Akademický článek
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Autor:
Mariette Bedhomme, Christophe H. Marchand, Laure Michelet, Stéphane D. Lemaire, Xing-Huang Gao, Mathieu Moslonka-Lefebvre, Paulette Decottignies, Mirko Zaffagnini
Publikováno v:
Journal of Biological Chemistry. 284:36282-36291
Post-translational modification of protein cysteine residues is emerging as an important regulatory and signaling mechanism. We have identified numerous putative targets of redox regulation in the unicellular green alga Chlamydomonas reinhardtii. One
Autor:
Stéphane D. Lemaire, María Esther Pérez-Pérez, Christophe H. Marchand, José L. Crespo, Mirko Zaffagnini
Autophagy is a membrane-trafficking process whereby double-membrane vesicles called autophagosomes engulf and deliver intracellular material to the vacuole for degradation. Atg4 is a cysteine protease with an essential function in autophagosome forma
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::bd9f33deec995e5611f594d3834dd96b
Autor:
Christophe H. Marchand, Xing-Huang Gao, Samuel Morisse, Stéphane D. Lemaire, Mirko Zaffagnini
Aims: Protein S-nitrosylation, a post-translational modification (PTM) consisting of the covalent binding of nitric oxide (NO) to a cysteine thiol moiety, plays a major role in cell signaling and is recognized to be involved in numerous physiological
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4ee74e42f3c01fd4df04ee42ac4f6341
https://europepmc.org/articles/PMC4158989/
https://europepmc.org/articles/PMC4158989/
Glutathionylation in the photosynthetic model organism Chlamydomonas reinhardtii: a proteomic survey
Autor:
Mariette Bedhomme, Stéphane D. Lemaire, Mirko Zaffagnini, Hayam Groni, Christophe H. Marchand, Carine Puppo, Brigitte Gontero, Paulette Decottignies, Corinne Cassier-Chauvat
Publikováno v:
Molecular and Cellular Proteomics
Molecular and Cellular Proteomics, 2012, 11 (2), pp.M111.014142. ⟨10.1074/mcp.M111.014142⟩
Molecular and Cellular Proteomics, American Society for Biochemistry and Molecular Biology, 2012, 11 (2), pp.M111.014142. ⟨10.1074/mcp.M111.014142⟩
Molecular and Cellular Proteomics (MCP Online)
Molecular and Cellular Proteomics (MCP Online), American Society for Biochemistry and Molecular Biology, 2012, 11 (2), pp.M111.014142. 〈10.1074/mcp.M111.014142〉
Molecular and Cellular Proteomics, 2012, 11 (2), pp.M111.014142. ⟨10.1074/mcp.M111.014142⟩
Molecular and Cellular Proteomics, American Society for Biochemistry and Molecular Biology, 2012, 11 (2), pp.M111.014142. ⟨10.1074/mcp.M111.014142⟩
Molecular and Cellular Proteomics (MCP Online)
Molecular and Cellular Proteomics (MCP Online), American Society for Biochemistry and Molecular Biology, 2012, 11 (2), pp.M111.014142. 〈10.1074/mcp.M111.014142〉
International audience; Protein glutathionylation is a redox post-translational modification occurring under oxidative stress conditions and playing a major role in cell regulation and signaling. This modification has been mainly studied in nonphotos
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4e5056071c0a4634f874728c1312cdea
https://hal.science/hal-01183584
https://hal.science/hal-01183584
Autor:
Stéphane D. Lemaire, Jérémy Couturier, Mariette Bedhomme, Christophe H. Marchand, Nicolas Rouhier, Paolo Trost, Mirko Zaffagnini, Mattia Adamo
Publikováno v:
Biochemical Journal
Biochemical Journal, Portland Press, 2012, 445, pp.337-347. ⟨10.1042/BJ20120505⟩
Biochemical Journal, 2012, 445, pp.337-347. ⟨10.1042/BJ20120505⟩
Biochemical Journal, Portland Press, 2012, 445, pp.337-347. ⟨10.1042/BJ20120505⟩
Biochemical Journal, 2012, 445, pp.337-347. ⟨10.1042/BJ20120505⟩
Plants contain both cytosolic and chloroplastic GAPDHs (glyceraldehyde-3-phosphate dehydrogenases). In Arabidopsis thaliana, cytosolic GAPDH is involved in the glycolytic pathway and is represented by two differentially expressed isoforms (GapC1 and
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5ffeb54a4d7fad0553abbb5b0cd7e466
https://hal.archives-ouvertes.fr/hal-01268311
https://hal.archives-ouvertes.fr/hal-01268311