Zobrazeno 1 - 10
of 20
pro vyhledávání: '"Elodie, Crublet"'
Autor:
Faustine Henot, Elisa Rioual, Adrien Favier, Pavel Macek, Elodie Crublet, Pierre Josso, Bernhard Brutscher, Matthias Frech, Pierre Gans, Claire Loison, Jerome Boisbouvier
Publikováno v:
Nature Communications, Vol 13, Iss 1, Pp 1-13 (2022)
To refold client proteins, HSP90 chaperone undergoes large structural rearrangements. Here the authors use NMR and molecular simulation and reveal structure and dynamics of a key functionally relevant metastable state of human HSP90α N-terminal doma
Externí odkaz:
https://doaj.org/article/a0e415192adb4a8f825b0f4fa98dd24f
Publikováno v:
Biochemical Society Transactions. 50:1555-1567
The study of protein structure, dynamics and function by NMR spectroscopy commonly requires samples that have been enriched (‘labelled') with the stable isotopes 13C and/or 15N. The standard approach is to uniformly label a protein with one or both
Autor:
Micheline Guillotte, Alexandre Juillerat, Sébastien Igonet, Audrey Hessel, Stéphane Petres, Elodie Crublet, Cécile Le Scanf, Anita Lewit-Bentley, Graham A Bentley, Inès Vigan-Womas, Odile Mercereau-Puijalon
Publikováno v:
PLoS ONE, Vol 10, Iss 7, p e0134292 (2015)
Adhesion of Plasmodium falciparum-infected red blood cells (iRBC) to human erythrocytes (i.e. rosetting) is associated with severe malaria. Rosetting results from interactions between a subset of variant PfEMP1 (Plasmodium falciparum erythrocyte memb
Externí odkaz:
https://doaj.org/article/cff3771abc2046d38bc0f9436991bc3e
Autor:
Elodie Crublet, Rime Kerfah, Ricarda Törner, Matthias Frech, Faustine Henot, Pierre Gans, Pavel Macek, Olivier Hamelin, Jérôme Boisbouvier
Publikováno v:
Journal of Biomolecular NMR
Journal of Biomolecular NMR, Springer Verlag, 2021, 75 (6-7), pp.221-232. ⟨10.1007/s10858-021-00370-0⟩
Journal of Biomolecular NMR, 2021, 75 (6-7), pp.221-232. ⟨10.1007/s10858-021-00370-0⟩
Journal of Biomolecular NMR, Springer Verlag, 2021, 75 (6-7), pp.221-232. ⟨10.1007/s10858-021-00370-0⟩
Journal of Biomolecular NMR, 2021, 75 (6-7), pp.221-232. ⟨10.1007/s10858-021-00370-0⟩
International audience; Methyl moieties are highly valuable probes for quantitative NMR studies of large proteins. Hence, their assignment is of the utmost interest to obtain information on both interactions and dynamics of proteins in solution. Here
Autor:
Rime Kerfah, Emeric Miclet, Pierre Gans, Céline Juillan-Binard, Elodie Crublet, Alicia Vallet, Rachel Lenoir-Capello, Lionel Imbert, Jérôme Boisbouvier, Hubert Mayerhofer, Rida Awad, Isabel Ayala
Publikováno v:
Methods in Molecular Biology ISBN: 9781071608913
Methods in Molecular Biology
Methods in Molecular Biology, 2021, 2199, pp.127-149. ⟨10.1007/978-1-0716-0892-0_8⟩
Methods in Molecular Biology-Structural Genomics
Structural Genomics-General Applications
Methods in Molecular Biology, Humana Press/Springer Imprint, 2021, 2199, pp.127-149. ⟨10.1007/978-1-0716-0892-0_8⟩
Methods in Molecular Biology
Methods in Molecular Biology, 2021, 2199, pp.127-149. ⟨10.1007/978-1-0716-0892-0_8⟩
Methods in Molecular Biology-Structural Genomics
Structural Genomics-General Applications
Methods in Molecular Biology, Humana Press/Springer Imprint, 2021, 2199, pp.127-149. ⟨10.1007/978-1-0716-0892-0_8⟩
International audience; The cell-free synthesis is an efficient strategy to produce in large scale protein samples for structural investigations. In vitro synthesis allows for significant reduction of production time, simplification of purification s
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::71677b64694f2c37e6793ea04a003290
https://doi.org/10.1007/978-1-0716-0892-0_8
https://doi.org/10.1007/978-1-0716-0892-0_8
Autor:
Lionel, Imbert, Rachel, Lenoir-Capello, Elodie, Crublet, Alicia, Vallet, Rida, Awad, Isabel, Ayala, Celine, Juillan-Binard, Hubert, Mayerhofer, Rime, Kerfah, Pierre, Gans, Emeric, Miclet, Jerome, Boisbouvier
Publikováno v:
Methods in molecular biology (Clifton, N.J.). 2199
The cell-free synthesis is an efficient strategy to produce in large scale protein samples for structural investigations. In vitro synthesis allows for significant reduction of production time, simplification of purification steps and enables product
Autor:
Giacomo Bastianelli, Anthony Bouillon, Christophe Nguyen, Elodie Crublet, Stéphane Pêtres, Olivier Gorgette, Dung Le-Nguyen, Jean-Christophe Barale, Michael Nilges
Publikováno v:
PLoS ONE, Vol 6, Iss 7, p e21812 (2011)
BACKGROUND: Psalmopeotoxin I (PcFK1), a protein of 33 aminoacids derived from the venom of the spider Psalmopoeus Cambridgei, is able to inhibit the growth of Plasmodium falciparum malaria parasites with an IC50 in the low micromolar range. PcFK1 was
Externí odkaz:
https://doaj.org/article/9aea6e5faaf34cb19d66cc6fa0250c4a
Autor:
Guillaume Mas, Pierre Gans, Paul Schanda, Elisa Colas Debled, Guy Schoehn, Pavel Macek, Christine Moriscot, Jérôme Boisbouvier, Jia-Ying Guan, Elodie Crublet
Publikováno v:
Science Advances
Science Advances, American Association for the Advancement of Science (AAAS), 2018, 4 (9), pp.eaau4196. ⟨10.1126/sciadv.aau4196⟩
Science Advances, 2018, 4 (9), pp.eaau4196. ⟨10.1126/sciadv.aau4196⟩
Science Advances, American Association for the Advancement of Science (AAAS), 2018, 4 (9), pp.eaau4196. ⟨10.1126/sciadv.aau4196⟩
Science Advances, 2018, 4 (9), pp.eaau4196. ⟨10.1126/sciadv.aau4196⟩
International audience; Chaperonins are ubiquitous protein assemblies present in bacteria, eukaryota, and archaea, facilitating the folding of proteins, preventing protein aggregation, and thus participating in maintaining protein homeostasis in the
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::532d6bfb69448aa3bd9fbb0dd8ccdd80
https://hal.archives-ouvertes.fr/hal-01912129
https://hal.archives-ouvertes.fr/hal-01912129
Autor:
Pavel Macek, Guy Schoehn, Rime Kerfah, Elodie Crublet, Jérôme Boisbouvier, Elisabetta Boeri Erba, Christine Moriscot, Carlos Amero
Publikováno v:
Science Advances
Science Advances, American Association for the Advancement of Science (AAAS), 2017, 3 (4), pp.e1601601. ⟨10.1126/sciadv.1601601⟩
Science Advances, 2017, 3 (4), pp.e1601601. ⟨10.1126/sciadv.1601601⟩
Science Advances, American Association for the Advancement of Science (AAAS), 2017, 3 (4), pp.e1601601. ⟨10.1126/sciadv.1601601⟩
Science Advances, 2017, 3 (4), pp.e1601601. ⟨10.1126/sciadv.1601601⟩
Real-time NMR, EM, and native MS studies revealed intermediates and parallel pathways in the assembly of a dodecameric peptidase.
The spontaneous formation of biological higher-order structures from smaller building blocks, called self-assembly,
The spontaneous formation of biological higher-order structures from smaller building blocks, called self-assembly,
Autor:
Paul Schanda, Pavel Macek, Vilius Kurauskas, Diego F. Gauto, Elodie Crublet, Rime Kerfah, Jérôme Boisbouvier
Publikováno v:
Chemical Communications
Chemical Communications, Royal Society of Chemistry, 2016, 52, pp.9558-9561. ⟨10.1039/C6CC04484K⟩
Chemical Communications, 2016, 52, pp.9558-9561. ⟨10.1039/C6CC04484K⟩
Chemical Communications, Royal Society of Chemistry, 2016, 52, pp.9558-9561. ⟨10.1039/C6CC04484K⟩
Chemical Communications, 2016, 52, pp.9558-9561. ⟨10.1039/C6CC04484K⟩
International audience; Solid-state NMR spectroscopy allows the characterization of structure, interactions and dynamics of insoluble and/or very large proteins. Sensitivity and resolution are often major challenges for obtaining atomic-resolution in
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a49700a96d8d0c5f2b00b381817a3835
https://hal.archives-ouvertes.fr/hal-01353309/document
https://hal.archives-ouvertes.fr/hal-01353309/document