Zobrazeno 1 - 10
of 18
pro vyhledávání: '"Marie-Pierre Castanié-Cornet"'
Autor:
Lisa Zuily, Nora Lahrach, Rosi Fassler, Olivier Genest, Peter Faller, Olivier Sénèque, Yann Denis, Marie-Pierre Castanié-Cornet, Pierre Genevaux, Ursula Jakob, Dana Reichmann, Marie-Thérèse Giudici-Orticoni, Marianne Ilbert
Publikováno v:
mBio, Vol 13, Iss 2 (2022)
ABSTRACT Copper is well known for its antimicrobial and antiviral properties. Under aerobic conditions, copper toxicity relies in part on the production of reactive oxygen species (ROS), especially in the periplasmic compartment. However, copper is s
Externí odkaz:
https://doaj.org/article/d2b88acbd8ca489194f154fe226ef8b8
Autor:
Bruno Fauvet, Andrija Finka, Marie-Pierre Castanié-Cornet, Anne-Marie Cirinesi, Pierre Genevaux, Manfredo Quadroni, Pierre Goloubinoff
Publikováno v:
Frontiers in Molecular Biosciences, Vol 8 (2021)
In eukaryotes, the 90-kDa heat shock proteins (Hsp90s) are profusely studied chaperones that, together with 70-kDa heat shock proteins (Hsp70s), control protein homeostasis. In bacteria, however, the function of Hsp90 (HtpG) and its collaboration wit
Externí odkaz:
https://doaj.org/article/970197eb0bba44c6bea6a1507738f3d2
Autor:
Andrija Finka, Manfredo Quadroni, Pierre Goloubinoff, Bruno Fauvet, Pierre Genevaux, Anne-Marie Cirinesi, Marie-Pierre Castanié-Cornet
Publikováno v:
Frontiers in Molecular Biosciences
Frontiers in Molecular Biosciences, Frontiers Media, 2021, 8 (14), pp.2914-2928.e7. ⟨10.3389/fmolb.2021.653073⟩
Frontiers in Molecular Biosciences, Vol 8 (2021)
Frontiers in molecular biosciences, vol. 8, pp. 653073
Frontiers in Molecular Biosciences, Frontiers Media, 2021, 8 (14), pp.2914-2928.e7. ⟨10.3389/fmolb.2021.653073⟩
Frontiers in Molecular Biosciences, Vol 8 (2021)
Frontiers in molecular biosciences, vol. 8, pp. 653073
In eukaryotes, the 90-kDa heat shock proteins (Hsp90s) are profusely studied chaperones that, together with 70-kDa heat shock proteins (Hsp70s), control protein homeostasis. In bacteria, however, the function of Hsp90 (HtpG) and its collaboration wit
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::fa8debf440f38a0ffbd1b5695617ef1d
https://hal.archives-ouvertes.fr/hal-03364316
https://hal.archives-ouvertes.fr/hal-03364316
Autor:
Roland Barriot, Pierre Genevaux, Gwennaele Fichant, Justine Latour, Marie-Pierre Castanié-Cornet
Publikováno v:
Journal of Molecular Biology
Journal of Molecular Biology, Elsevier, 2020, 432 (13), pp.3771-3789. ⟨10.1016/j.jmb.2020.04.014⟩
Journal of Molecular Biology, Elsevier, 2020, 432 (13), pp.3771-3789. ⟨10.1016/j.jmb.2020.04.014⟩
Molecular chaperones maintain cellular protein homeostasis by acting at almost every step in protein biogenesis pathways. The DnaK/HSP70 chaperone has been associated with almost every known essential chaperone functions in bacteria. To act as a bona
Autor:
Reynald Gillet, Elisabetta Mileo, Patricia Bordes, Chantal Iobbi-Nivol, Marie-Thérèse Giudici-Orticoni, Alessandro Barducci, Marie-Pierre Castanié-Cornet, Cyrille Garnier, Brigitte Gontero, Pierre Goloubinoff, Pierre Genevaux, Françoise Ochsenbein, Olivier Genest, Marianne Ilbert, Gilbert Richarme
Publikováno v:
Biochimie
Biochimie, Elsevier, 2018, 151, pp.159-165. ⟨10.1016/j.biochi.2018.06.004⟩
Biochimie, 2018, 151, pp.159-165. ⟨10.1016/j.biochi.2018.06.004⟩
Biochimie, Elsevier, 2018, 151, pp.159-165. ⟨10.1016/j.biochi.2018.06.004⟩
Biochimie, 2018, 151, pp.159-165. ⟨10.1016/j.biochi.2018.06.004⟩
International audience; The "Bioenergetique et Ingenierie des Proteines (BIP)" laboratory, CNRS (France), organized its first French workshop on molecular chaperone proteins and protein folding in November 2017. The goal of this workshop was to gathe
Autor:
Sneha Kumar, F. Ulrich Hartl, Manajit Hayer-Hartl, Marie-Pierre Castanié-Cornet, Pierre Genevaux, Liang Zhao
Publikováno v:
Molecular Cell
Molecular Cell, Elsevier, 2021, 81 (14), pp.2914-2928.e7. ⟨10.1016/j.molcel.2021.05.016⟩
Molecular Cell, Elsevier, 2021, 81 (14), pp.2914-2928.e7. ⟨10.1016/j.molcel.2021.05.016⟩
Summary Molecular chaperones assist with protein folding by interacting with nascent polypeptide chains (NCs) during translation. Whether the ribosome can sense chaperone defects and, in response, abort translation of misfolding NCs has not yet been
Autor:
Manfredo Quadroni, Bruno Fauvet, Pierre Genevaux, Marie-Pierre Castanié-Cornet, Andrija Finka, Anne-Marie Cirinesi, Pierre Goloubinoff
Whereas in eukaryotic cells, the Hsp90s are profusely-studied molecular chaperones controlling protein homeostasis together with Hsp70s, in bacteria, the function of Hsp90 (HtpG) and its collaboration with Hsp70 (DnaK) remains unknown. To uncover phy
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::fc398ecf9e563c9551e35a25cb99267e
https://doi.org/10.1101/451989
https://doi.org/10.1101/451989
Autor:
Ambre Sala, Michèle Coddeville, Lionel Mourey, Sara Ayala, Marie-Pierre Castanié-Cornet, Nawel Slama, Samuel Tranier, Anne-Marie Cirinesi, Patricia Bordes, Pierre Genevaux
Publikováno v:
Proceedings of the National Academy of Sciences of the United States of America. 114(47)
SecB chaperones assist protein export in bacteria. However, certain SecB family members have diverged to become specialized toward the control of toxin-antitoxin (TA) systems known to promote bacterial adaptation to stress and persistence. In such tr
Autor:
Joen Luirink, Marie Pierre Castanié-Cornet, Nicolas Bruel, Gregory Koningstein, Anne Marie Cirinesi, Costa Georgopoulos, Pierre Genevaux
Publikováno v:
Journal of Biological Chemistry, 287, 44435-44446. American Society for Biochemistry and Molecular Biology Inc.
Journal of Biological Chemistry
Journal of Biological Chemistry, American Society for Biochemistry and Molecular Biology, 2012, 287 (53), pp.44435-46
Bruel, N, Castanié-Cornet, M P, Cirinesi, A M, Koningstein, G M, Georgopoulos, C, Luirink, J & Genevaux, P 2012, ' Hsp 33 Controls Elongation Factor-Tu Stability and allows Escherichia coli growth in the absence of the major DnaK and Trigger Factor Chaperones ', Journal of Biological Chemistry, vol. 287, pp. 44435-44446 . https://doi.org/10.1074/jbc.M112.418525
Journal of Biological Chemistry
Journal of Biological Chemistry, American Society for Biochemistry and Molecular Biology, 2012, 287 (53), pp.44435-46
Bruel, N, Castanié-Cornet, M P, Cirinesi, A M, Koningstein, G M, Georgopoulos, C, Luirink, J & Genevaux, P 2012, ' Hsp 33 Controls Elongation Factor-Tu Stability and allows Escherichia coli growth in the absence of the major DnaK and Trigger Factor Chaperones ', Journal of Biological Chemistry, vol. 287, pp. 44435-44446 . https://doi.org/10.1074/jbc.M112.418525
Intracellular de novo protein folding is assisted by cellular networks of molecular chaperones. In Escherichia coli, cooperation between the chaperones trigger factor (TF) and DnaK is central to this process. Accordingly, the simultaneous deletion of
Autor:
Anne Francez-Charlot, Annie Conter, Claude Gutierrez, Alice Boulanger, Marie-Pierre Castanié-Cornet, Kaymeuang Cam
Publikováno v:
Journal of Bacteriology. 187:3282-3286
Transcription of the Escherichia coli osmB gene is induced by several stress conditions. osmB is expressed from two promoters, osmBp1 and osmBp2 . The downstream promoter, osmBp2 , is induced after osmotic shock or upon entry into stationary phase in