Výsledky vyhledávání - "Magalie Sénéchal"

Akademický článek

A biomimetic electrostatic assistance for guiding and promoting N-terminal protein chemical modification

Autor: Nathalie Ollivier, Magalie Sénéchal, Rémi Desmet, Benoît Snella, Vangelis Agouridas, Oleg Melnyk

Publikováno v: Nature Communications, Vol 13, Iss 1, Pp 1-10 (2022)

Phosphorylation is a mechanism used by cells to promote proteins-biomolecules association. Here, the authors show the effect of the interactions between proteins equipped with positively charged arginines and peptides harbouring negatively charged ph

Externí odkaz: https://doaj.org/article/35af3717c05a41b8b1e9a8f432c76bde

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Akademický článek

Activation of a helper and not regulatory human CD4+ T cell response by oncolytic H-1 parvovirus.

Autor: Olivier Moralès, Audrey Richard, Nathalie Martin, Dhafer Mrizak, Magalie Sénéchal, Céline Miroux, Véronique Pancré, Jean Rommelaere, Perrine Caillet-Fauquet, Yvan de Launoit, Nadira Delhem

Publikováno v: PLoS ONE, Vol 7, Iss 2, p e32197 (2012)

BACKGROUND:H-1 parvovirus (H-1 PV), a rodent autonomous oncolytic parvovirus, has emerged as a novel class of promising anticancer agents, because of its ability to selectively find and destroy malignant cells. However, to probe H-1 PV multimodal ant

Externí odkaz: https://doaj.org/article/8f6e0b61610c4cbcb06ab756bcccf42c

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Total Chemical Synthesis of All SUMO-2/3 Dimer Combinations

Autor: Jennifer Bouchenna, Jérôme Vicogne, Magalie Sénéchal, Oleg Melnyk, Hervé Drobecq

Publikováno v: Bioconjugate Chemistry
Bioconjugate Chemistry, American Chemical Society, 2019, 30 (11), pp.2967-2973. ⟨10.1021/acs.bioconjchem.9b00661⟩
Bioconjugate Chemistry, 2019, 30 (11), pp.2967-2973. ⟨10.1021/acs.bioconjchem.9b00661⟩

International audience; One hallmark of protein chemical synthesis is its capacity to access proteins that living systems can hardly produce. This is typically the case for proteins harboring post-translational modifications such as ubiquitin or ubiq

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f46e74ce0fb5fb0016ee8fdc240f0e9c
https://doi.org/10.1021/acs.bioconjchem.9b00661

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The Problem of Aspartimide Formation During Protein Chemical Synthesis Using SEA-Mediated Ligation

Autor: Jérôme Vicogne, Hervé Drobecq, Magalie Sénéchal, Jennifer Bouchenna, Oleg Melnyk

Publikováno v: Peptide and Protein Engineering
Peptide and Protein Engineering, pp.13-28, 2020, 978-1-0716-0720-6. ⟨10.1007/978-1-0716-0720-6_2⟩
Springer Protocols Handbooks ISBN: 9781071607190

Aspartimide formation often complicates the solid phase synthesis of peptides. Much less discussed is the potential occurrence of this side-reaction during the coupling of peptide segments using chemoselective peptide bond forming reactions such as t

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::36d9f5a3bd1bf6d20f89e66d118e49c7
https://hal.science/hal-02995426

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The Role of the Conserved SUMO-2/3 Cysteine Residue on Domain Structure Investigated Using Protein Chemical Synthesis

Autor: Jennifer Bouchenna, Oleg Melnyk, Nicolas Stankovic-Valentin, Jérôme Vicogne, Magalie Sénéchal, Hervé Drobecq

Publikováno v: Bioconjugate Chemistry
Bioconjugate Chemistry, 2019, 30 (10), pp.2684-2696. ⟨10.1021/acs.bioconjchem.9b00598⟩
Bioconjugate Chemistry, American Chemical Society, 2019, 30 (10), pp.2684-2696. ⟨10.1021/acs.bioconjchem.9b00598⟩

International audience; While the semi or total synthesis of ubiquitin or polyubiquitin conjugates has attracted a lot of attention the past decade, the preparation of small ubiquitin-like modifier (SUMO) conjugates is much less developed. We describ

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c640246653ff862516b03c48d2cd7776
https://pubmed.ncbi.nlm.nih.gov/31532181

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A Central Cysteine Residue Is Essential for the Thermal Stability and Function of SUMO-1 Protein and SUMO-1 Peptide-Protein Conjugates

Autor: Jean-Michel Saliou, Alexandra Mougel, Hervé Drobecq, Rémi Desmet, Oleg Melnyk, Magalie Sénéchal, Emmanuelle Boll, Jean-Jacques Lacapère, Jérôme Vicogne

Publikováno v: Bioconjugate Chemistry
Bioconjugate Chemistry, American Chemical Society, 2016, 27 (6), pp.1540-1546. ⟨10.1021/acs.bioconjchem.6b00211⟩
Bioconjugate Chemistry, 2016, 27 (6), pp.1540-1546. ⟨10.1021/acs.bioconjchem.6b00211⟩

International audience; SUMOylation constitutes a major post-translational modification (PTM) used by the eukaryote cellular machinery to modulate protein interactions of the targeted proteins. The small ubiquitin-like modifier-1 (SUMO-1) features a

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::500b9a29da324dbe758caf511cc3bbae
https://pubmed.ncbi.nlm.nih.gov/27195426

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Solution structure of the N-terminal transactivation domain of ERM modified by SUMO-1

Autor: Magalie Sénéchal, Vincent Villeret, Coralie Bompard, Didier Monté, Frédérique Dewitte, Alexis Verger, Jean-Luc Baert, Yvan de Launoit, Carine Van Lint, Zoé Lens

Publikováno v: Biochemical and biophysical research communications. 399(1)

ERM is a member of the PEA3 group of the Ets transcription factor family that plays important roles in development and tumorigenesis. The PEA3s share an N-terminal transactivation domain (TADn) whose activity is inhibited by small ubiquitin-like modi

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a89f1945cf796ca505884e7d808c6eac
https://pubmed.ncbi.nlm.nih.gov/20647002

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Crystallization and preliminary X-ray diffraction analysis of the peptidylprolyl isomerase Par27 of Bordetella pertussis

Autor: Bernard Clantin, Magalie Sénéchal, Coralie Bompard, Alexandre Wohlkönig, Vincent Villeret, Hélène Hodak, Françoise Jacob-Dubuisson

Proteins with both peptidylprolyl isomerase (PPIase) and chaperone activities play a crucial role in protein folding in the periplasm of Gram-negative bacteria. Few such proteins have been structurally characterized and to date only the crystal struc

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b33081bbdd210453523eb0662dac06fb
https://europepmc.org/articles/PMC2531267/

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The peptidyl-prolyl isomerase and chaperone Par27 of Bordetella pertussis as the prototype for a new group of parvulins

Autor: Magalie Sénéchal, Françoise Jacob-Dubuisson, Alexandre Wohlkonig, Hervé Drobecq, Isabelle Landrieu, Jean-Michel Wieruszeski, Hélène Hodak, Marc Jamin, Caroline Smet-Nocca, Camille Locht

Publikováno v: Journal of Molecular Biology
Journal of Molecular Biology, Elsevier, 2008, 376 (2), pp.414-26. ⟨10.1016/j.jmb.2007.10.088⟩
Journal of Molecular Biology, 2008, 376 (2), pp.414-26. ⟨10.1016/j.jmb.2007.10.088⟩

Proteins that pass through the periplasm in an unfolded state are highly sensitive to proteolysis and aggregation and, therefore, often require protection by chaperone-like proteins. The periplasm of Gram-negative bacteria is well equipped with ATP-i

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2c1982bfb54c832a386b83ada541f0a9
https://hal.archives-ouvertes.fr/hal-00273348

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