A cationic motif upstream Engrailed2 homeodomain controls cell internalization through selective interaction with heparan sulfates

Autor: Sébastien Cardon, Yadira P. Hervis, Gérard Bolbach, Chrystel Lopin-Bon, Jean-Claude Jacquinet, Françoise Illien, Astrid Walrant, Delphine Ravault, Bingwei He, Laura Molina, Fabienne Burlina, Olivier Lequin, Alain Joliot, Ludovic Carlier, Sandrine Sagan

Publikováno v: Nature Communications, Vol 14, Iss 1, Pp 1-13 (2023)

Abstract Engrailed2 (En2) is a transcription factor that transfers from cell to cell through unconventional pathways. The poorly understood internalization mechanism of this cationic protein is proposed to require an initial interaction with cell-sur

Externí odkaz: https://doaj.org/article/c684e2cdb0ba43a69d9c0fdf51449845

Synthesis of oligosaccharides of the linkage region of proteoglycans using regioselective glycosylation

Autor: Chrystel Lopin-Bon, Sylvie Fournel-Gigleux, Sandrine Gulberti, Benjamin Ayela, Hélène Ledru

Publikováno v: Organic and Biomolecular Chemistry
Organic and Biomolecular Chemistry, Royal Society of Chemistry, 2020, 18 (25), pp.4831-4842. ⟨10.1039/d0ob00783h⟩
Organic & Biomolecular Chemistry
Organic & Biomolecular Chemistry, 2020, 18 (25), pp.4831-4842. ⟨10.1039/d0ob00783h⟩

Proteoglycans (PGs) are complex macromolecules that are composed of glycosaminoglycan (GAG) chains covalently attached to a core protein through a tetrasaccharide linker. Biosynthesis of PGs is complex and involves a large number of glycosyltranferas

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::aa32e99bb1c0977b30a962a0af15d202
https://doi.org/10.1039/d0ob00783h

Synthetic Modifications of the Linkage Region of Proteoglycans and Impact on CSGalNAcT‐1

Autor: Benjamin Ayela, Floriane Heis, Thomas Poisson, Xavier Pannecoucke, Sylvie Fournel‐Gigleux, Sandrine Gulberti, Chrystel Lopin‐Bon

Publikováno v: European Journal of Organic Chemistry
European Journal of Organic Chemistry, 2022, 2022 (2), pp.e202101422. ⟨10.1002/ejoc.202101422⟩

International audience; Multi-step synthesis of a library of variously modified disaccharides and trisaccharides of the linkage region of proteoglycans (PGs) having a d-galactose modified at position C-2, C-4 or C-6 position by replacing the hydroxyl

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f17acaaa9335537b35c9a07e8676042a
https://doi.org/10.1002/ejoc.202101422

A cationic motif in Engrailed-2 homeoprotein controls its internalization via selective cell-surface glycosaminoglycans interactions

Autor: Alain Joliot, Astrid Walrant, Françoise Illien, Sandrine Sagan, Olivier Lequin, Gérard Bolbach, Fabienne Burlina, Jean-Claude Jacquinet, Delphine Ravault, Laura Molina, Yadira P. Hervis, Bingwei He, Sébastien Cardon, Ludovic Carlier, Chrystel Lopin-Bon

Engrailed-2 (En2) is a transcription factor that possesses as most homeoproteins the unique and intriguing property to transfer from cell to cell through unconventional pathways. The internalization mechanism of this cationic protein is far from bein

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::52988369e5be299a35415f6ab50205d4
https://hal.archives-ouvertes.fr/hal-03429466

Kinetic theory of hyaluronan cleavage by bovine testicular hyaluronidase in standard and crowded environments

Autor: Francesco Piazza, Rouba Nasreddine, Lucija Orlic, Chrystel Lopin-Bon, Josef Hamacek, Reine Nehmé

Publikováno v: Biochimica et Biophysica Acta (BBA)-General Subjects
Biochimica et Biophysica Acta (BBA)-General Subjects, Elsevier, 2021, 1865 (3), pp.129837. ⟨10.1016/j.bbagen.2020.129837⟩
Biochimica et Biophysica Acta (BBA)-General Subjects, 2021, 1865 (3), pp.129837. ⟨10.1016/j.bbagen.2020.129837⟩

In this paper, we introduce a comprehensive kinetic model describing the enzymatic cleavage of hyaluronan (HA) by bovine testicular hyaluronidase (BTH). Our theory focuses specifically on the late stage of the hydrolysis, where the concentrations of

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5e9e7bde715832674da591b3b8c05a89
https://pubmed.ncbi.nlm.nih.gov/33378708