Publisher Correction: Structural insights into chaperone addiction of toxin-antitoxin systems

Autor: Valérie Guillet, Patricia Bordes, Cécile Bon, Julien Marcoux, Virginie Gervais, Ambre Julie Sala, Suzana Dos Reis, Nawel Slama, Israel Mares-Mejía, Anne-Marie Cirinesi, Laurent Maveyraud, Pierre Genevaux, Lionel Mourey

Publikováno v: Nature Communications, Vol 10, Iss 1, Pp 1-1 (2019)

The original version of this Article contained errors in Figures 1 and 4. In Fig. 1b, the Mtb-SecBTA sequence was displayed incorrectly. In the inset panel within Fig. 4c, the y-axis of the graph incorrectly read (Q.Rg)2 × I(Q)//(0), and should have

Externí odkaz: https://doaj.org/article/86663963fbab4cdd99bfffa04d5c24c2

Structural insights into chaperone addiction of toxin-antitoxin systems

Autor: Pierre Genevaux, Laurent Maveyraud, Suzana Dos Reis, Anne-Marie Cirinesi, Ambre Sala, Valérie Guillet, Virginie Gervais, Israel Mares-Mejía, Patricia Bordes, Nawel Slama, Lionel Mourey, Julien Marcoux, Cécile Bon

Publikováno v: Nature Communications
Nature Communications, Nature Publishing Group, 2019, 10 (1), ⟨10.1038/s41467-019-08747-4⟩
Nature Communications, Vol 10, Iss 1, Pp 1-15 (2019)
'Nature Communications ', vol: 10, pages: 782-1-1-782-15 (2019)

SecB chaperones assist protein export by binding both unfolded proteins and the SecA motor. Certain SecB homologs can also control toxin-antitoxin (TA) systems known to modulate bacterial growth in response to stress. In such TA-chaperone (TAC) syste

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::39ffc20d2cb092a770b9d121eaed91f7
https://hal.archives-ouvertes.fr/hal-02346695

Discovery of Novel Inhibitors of Amyloid β-Peptide 1–42 Aggregation

Autor: Salvador Ventura, Alba Espargaró, Javier Sancho, José Alberto Carrodeguas, L. López, Marie-Lise Maddelein, Suzana Dos-Reis

Publikováno v: Journal of Medicinal Chemistry
Journal of Medicinal Chemistry, American Chemical Society, 2012, 55 (22), pp.9521-9530. ⟨10.1021/jm301186p⟩

Alzheimer's disease, characterized by deposits of amyloid β-peptide (Aβ), is the most common neurodegenerative disease, but it still lacks a specific treatment. We have discovered five chemically unrelated inhibitors of the in vitro aggregation of

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::def9eb936bad4773a5af9c47af7e5260
https://doi.org/10.1021/jm301186p

The sequences appended to the amyloid core region of the HET-s prion protein determine higher-order aggregate organization in vivo

Autor: Sven J. Saupe, Suzana Dos Reis, Jean-Marie Schmitter, Martine Sabourin, Bénédicte Coulary-Salin, Axelle Balguerie, Stéphane Chaignepain

Publikováno v: Journal of Cell Science. 117:2599-2610

The [Het-s] prion of the fungus Podospora anserina propagates as a self-perpetuating amyloid form of the HET-s protein. This protein triggers a cell death reaction termed heterokaryon incompatibility when interacting with the HET-S protein, an alleli

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::74d6d4742dc41f88a620fe6200342a49
https://doi.org/10.1242/jcs.01116

Domain organization and structure-function relationship of the HET-s prion protein of Podospora anserina

Autor: Katell Bathany, Bénédicte Coulary-Salin, Suzana Dos Reis, Stéphane Chaignepain, Vincent Forge, Axelle Balguerie, Ioan Lascu, Jean-Marie Schmitter, Sven J. Saupe, Roland Riek, Christiane Ritter

Publikováno v: The EMBO Journal. 22:2071-2081

The [Het-s] infectious element of the fungus Podospora anserina is a prion protein involved in a genetically controlled cell death reaction termed heterokaryon incompatibility. Previous analyses indicate that [Het-s] propagates as a self-perpetuating

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c30ec14d729f7598700388b26d818060
https://doi.org/10.1093/emboj/cdg213