Zobrazeno 1 - 10
of 10
pro vyhledávání: '"Célia Deville"'
Autor:
Nane C. Kuznik, Valeria Solozobova, Irene I. Lee, Nicole Jung, Linxiao Yang, Karin Nienhaus, Emmanuel A. Ntim, Jaice T. Rottenberg, Claudia Muhle-Goll, Amrish Rajendra Kumar, Ravindra Peravali, Simone Gräßle, Victor Gourain, Célia Deville, Laura Cato, Antje Neeb, Marco Dilger, Christina A. Cramer von Clausbruch, Carsten Weiss, Bruno Kieffer, G. Ulrich Nienhaus, Myles Brown, Stefan Bräse, Andrew C.B. Cato
Publikováno v:
iScience, Vol 25, Iss 5, Pp 104175- (2022)
Summary: BAG1 is a family of polypeptides with a conserved C-terminal BAG domain that functions as a nucleotide exchange factor for the molecular chaperone HSP70. BAG1 proteins also control several signaling processes including proteostasis, apoptosi
Externí odkaz:
https://doaj.org/article/ef7d174a265a47ad8c77177cd0835a85
Publikováno v:
Cell Reports, Vol 27, Iss 12, Pp 3433-3446.e4 (2019)
Summary: AAA+ proteins form asymmetric hexameric rings that hydrolyze ATP and thread substrate proteins through a central channel via mobile substrate-binding pore loops. Understanding how ATPase and threading activities are regulated and intertwined
Externí odkaz:
https://doaj.org/article/1437e116bee14ff49e614571aa503d64
Autor:
Robert Fagiewicz, Corinne Crucifix, Torben Klos, Célia Deville, Bruno Kieffer, Yves Nominé, Johan Busselez, Paola Rossolillo, Helgo Schmidt
SUMMARYCargo adaptors are crucial in coupling motor proteins with their respective cargos and regulatory proteins. BicD2 is a prominent example within the cargo adaptor family. BicD2 is able to recruit the microtubule motor dynein to RNA, viral parti
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::e380a4b9be5bf7d92e4479a5c04f5773
https://doi.org/10.1101/2022.01.05.474964
https://doi.org/10.1101/2022.01.05.474964
Autor:
Célia Deville, Ewen Lescop, Ali Badache, Carine van Heijenoort, Ying-Hui Wang, Dominique Durand, François Bontems, Nelly Morellet, Françoise Guerlesquin, Louise Pinet, Nadine Assrir
Publikováno v:
Biophysical Journal
Biophysical Journal, 2021, 120 (10), pp.1869-1882. ⟨10.1016/j.bpj.2021.03.005⟩
Biophysical Journal, Biophysical Society, 2021, 120 (10), pp.1869-1882. ⟨10.1016/j.bpj.2021.03.005⟩
Biophys J
Biophysical Journal, 2021, 120 (10), pp.1869-1882. ⟨10.1016/j.bpj.2021.03.005⟩
Biophysical Journal, Biophysical Society, 2021, 120 (10), pp.1869-1882. ⟨10.1016/j.bpj.2021.03.005⟩
Biophys J
ErbB2 (or HER2) is a receptor tyrosine kinase overexpressed in some breast cancers, associated with poor prognosis. Treatments targeting the receptor extracellular and kinase domains have greatly improved disease outcome in the last twenty years. In
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a92a53d86450c505d485d68976c40675
https://hal.science/hal-03095358
https://hal.science/hal-03095358
Autor:
Dominique Durand, Célia Deville, Louise Pinet, Tâp Ha-Duong, Maud Chan-Yao-Chong, Carine van Heijenoort
Publikováno v:
Biophysical Journal
Biophysical Journal, Biophysical Society, 2019, 116 (7), pp.1216-1227. ⟨10.1016/j.bpj.2019.02.015⟩
Biophysical Journal, Biophysical Society, 2019, 116 (7), pp.1216--1227. ⟨10.1016/j.bpj.2019.02.015⟩
Biophysical Journal, 2019, 116 (7), pp.1216--1227. ⟨10.1016/j.bpj.2019.02.015⟩
Biophysical Journal, Biophysical Society, 2019, 116 (7), pp.1216-1227. ⟨10.1016/j.bpj.2019.02.015⟩
Biophysical Journal, Biophysical Society, 2019, 116 (7), pp.1216--1227. ⟨10.1016/j.bpj.2019.02.015⟩
Biophysical Journal, 2019, 116 (7), pp.1216--1227. ⟨10.1016/j.bpj.2019.02.015⟩
International audience; Because of their large conformational heterogeneity, structural characterization of intrinsically disordered proteins (IDPs) is very challenging using classical experimental methods alone. In this study, we use NMR and small-a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5783fca92b33e4465ed2fc7c7e247e8a
https://hal.archives-ouvertes.fr/hal-02393047
https://hal.archives-ouvertes.fr/hal-02393047
Publikováno v:
Cytoskeleton. 70:686-705
Many actin-binding proteins (ABPs) use complex multidomain architectures to integrate and coordinate multiple signals and interactions with the dynamic remodeling of actin cytoskeleton. In these proteins, small segments that are intrinsically disorde
Autor:
Undine Mechold, Sabrina Montluc, Louis Renault, Véronique Henriot, Christophe Velours, Dorothée Raoux-Barbot, Daniel Ladant, Alexander Belyy, Célia Deville, Lina Worpenberg
Publikováno v:
PLoS ONE
PLoS ONE, Public Library of Science, 2018, 13 (11), pp.e0206133. ⟨10.1371/journal.pone.0206133⟩
PLoS ONE, Vol 13, Iss 11, p e0206133 (2018)
PLoS ONE, 2018, 13 (11), pp.e0206133. ⟨10.1371/journal.pone.0206133⟩
PLoS ONE, Public Library of Science, 2018, 13 (11), pp.e0206133. ⟨10.1371/journal.pone.0206133⟩
PLoS ONE, Vol 13, Iss 11, p e0206133 (2018)
PLoS ONE, 2018, 13 (11), pp.e0206133. ⟨10.1371/journal.pone.0206133⟩
International audience; Several bacterial pathogens produce nucleotidyl cyclase toxins to manipulate eukaryotic host cells. Inside host cells they are activated by endogenous cofactors to produce high levels of cyclic nucleotides (cNMPs). The ExoY to
Autor:
Louis Renault, Christine Girard-Blanc, Célia Deville, François Bontems, Naïma Nhiri, Stéphane Petres, Carine van Heijenoort, Nadine Assrir, Eric Jacquet
Publikováno v:
FEBS Letters
FEBS Letters, 2016, 590 (20), pp.3690-3699. ⟨10.1002/1873-3468.12423⟩
FEBS Letters, Wiley, 2016, 590 (20), pp.3690-3699. 〈10.1002/1873-3468.12423〉
FEBS Letters, Wiley, 2016, 590 (20), pp.3690-3699. ⟨10.1002/1873-3468.12423⟩
FEBS Letters, 2016, 590 (20), pp.3690-3699. ⟨10.1002/1873-3468.12423⟩
FEBS Letters, Wiley, 2016, 590 (20), pp.3690-3699. 〈10.1002/1873-3468.12423〉
FEBS Letters, Wiley, 2016, 590 (20), pp.3690-3699. ⟨10.1002/1873-3468.12423⟩
International audience; Understanding the structural basis of actin cytoskeleton remodeling requires stabilization of actin monomers, oligomers, and filaments in complex with partner proteins, using various biochemical strategies. Here, we report a d
Autor:
Félix A. Rey, Thomas Krey, Julia Chamot-Rooke, Christian Malosse, Célia Deville, Christine Girard-Blanc, Pablo Guardado-Calvo, Eric Guittet, François Bontems, Ieva Vasiliauskaite, Scott A. Jeffers, Stéphane Petres, Christina Sizun, Annalisa Meola, Carine van Heijenoort
Publikováno v:
Journal of Structural Biology
Journal of Structural Biology, Elsevier, 2014, 188 (1), pp.71-78. ⟨10.1016/j.jsb.2014.08.002⟩
Journal of Structural Biology, 2014, 188 (1), pp.71-78. ⟨10.1016/j.jsb.2014.08.002⟩
Journal of Structural Biology, Elsevier, 2014, 188 (1), pp.71-78. ⟨10.1016/j.jsb.2014.08.002⟩
Journal of Structural Biology, 2014, 188 (1), pp.71-78. ⟨10.1016/j.jsb.2014.08.002⟩
International audience; Nuclear magnetic resonance spectroscopy is a powerful tool to study structural and functional properties of proteins, provided that they can be enriched in stable isotopes such as (15)N, (13)C and (2)H. This is usually easy an
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::61c35b59588d92465841fd7af2ae02cf
https://hal.archives-ouvertes.fr/hal-01077147
https://hal.archives-ouvertes.fr/hal-01077147
Autor:
Dorothée Raoux-Barbot, Alexander Belyy, Lina Worpenberg, Sabrina Montluc, Celia Deville, Véronique Henriot, Christophe Velours, Daniel Ladant, Louis Renault, Undine Mechold
Publikováno v:
PLoS ONE, Vol 13, Iss 11, p e0206133 (2018)
Several bacterial pathogens produce nucleotidyl cyclase toxins to manipulate eukaryotic host cells. Inside host cells they are activated by endogenous cofactors to produce high levels of cyclic nucleotides (cNMPs). The ExoY toxin from Pseudomonas aer
Externí odkaz:
https://doaj.org/article/8dc762d320cd495f99a7a21786bb3364