Výsledky vyhledávání - "Frédérique Dewitte"

Akademický článek

Crystal structure of human Mediator subunit MED23

Autor: Didier Monté, Bernard Clantin, Frédérique Dewitte, Zoé Lens, Prakash Rucktooa, Els Pardon, Jan Steyaert, Alexis Verger, Vincent Villeret

Publikováno v: Nature Communications, Vol 9, Iss 1, Pp 1-7 (2018)

Mediator is a large multi-subunits complex essential to the regulation of transcription by RNA pol II. Here the authors report the crystal structure of MED23—one of the largest subunits of the complex together with MED1 and MED14—revealing a comp

Externí odkaz: https://doaj.org/article/128fb504de7f40d08b3482fbcb664f49

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NMR spectroscopy of the main protease of SARS‐CoV‐2 and fragment‐based screening identify three protein hotspots and an antiviral fragment

Autor: Florence Leroux, Julie Charton, François-Xavier Cantrelle, Xavier Hanoulle, Sandrine Belouzard, Danai Moschidi, Isabelle Landrieu, Lucile Brier, Jean Dubuisson, Valérie Landry, Emmanuelle Boll, Benoit Deprez, Frédérique Dewitte

Publikováno v: Angewandte Chemie International Edition
Angewandte Chemie International Edition, In press, 60 (48), pp.25428-25435. ⟨10.1002/anie.202109965⟩
Angewandte Chemie International Edition, Wiley-VCH Verlag, In press, 60 (48), pp.25428-25435. ⟨10.1002/anie.202109965⟩
Angewandte Chemie (International Ed. in English)

The main protease (3CLp) of the SARS‐CoV‐2, the causative agent for the COVID‐19 pandemic, is one of the main targets for drug development. To be active, 3CLp relies on a complex interplay between dimerization, active site flexibility, and allo

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4b9f57c9062d78db7309da0eef562a88
https://hal.science/hal-03363607

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Solution Structure of the N-Terminal Domain of Mediator Subunit MED26 and Molecular Characterization of Its Interaction with EAF1 and TAF7

Autor: Zoé Lens, Xavier Hanoulle, Frédérique Dewitte, François-Xavier Cantrelle, Riccardo Peruzzini, Isabelle Landrieu, Marc Aumercier, Elisabeth Ferreira, Jean-Luc Baert, Vincent Villeret, Didier Monté, Alexis Verger

Publikováno v: Journal of Molecular Biology
Journal of Molecular Biology, Elsevier, 2017, 429 (20), pp.3043-3055. ⟨10.1016/j.jmb.2017.09.001⟩
Journal of Molecular Biology, 2017, 429 (20), pp.3043-3055. ⟨10.1016/j.jmb.2017.09.001⟩

International audience; MED26 is a subunit of Mediator, a large complex central to the regulation of gene transcription by RNA Polymerase II. MED26 plays a role in the switch between the initiation and elongation phases of RNA Polymerase II-mediated

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0071a4b1f0f756c7dfbed13698a6ac15
https://hal.archives-ouvertes.fr/hal-01620122

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1H, 15N and 13C assignments of the N-terminal domain of the Mediator complex subunit MED26

Autor: Isabelle Landrieu, Frédérique Dewitte, Alexis Verger, Riccardo Peruzzini, Elisabeth Ferreira, Vincent Villeret, François-Xavier Cantrelle, Zoé Lens, Jean-Luc Baert

Publikováno v: Biomolecular NMR Assignments
Biomolecular NMR Assignments, Springer, 2016, 10 (1), pp.233-236. ⟨10.1007/s12104-016-9673-z⟩
Biomolecular NMR Assignments, 2016, 10 (1), pp.233-236. ⟨10.1007/s12104-016-9673-z⟩

MED26 is a subunit of the Mediator, a very large complex involved in regulation of gene transcription by RNA Polymerase II. MED26 regulates the switch between initiation and elongation phases of the transcription. This function requires interaction o

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8e968733d1ce2b80f4da497bf5adb89f
https://hal.archives-ouvertes.fr/hal-01389830

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Single-Molecule Force Spectroscopy of Mycobacterial Adhesin-Adhesin Interactions

Autor: Yves F. Dufrêne, Camille Locht, Frédérique Dewitte, Dominique Raze, Claire Verbelen

Publikováno v: Journal of bacteriology, Vol. 189, no. 24, p. 8801-6 (2007)

The heparin-binding hemagglutinin (HBHA) is one of the few virulence factors identified for Mycobacterium tuberculosis . It is a surface-associated adhesin that expresses a number of different activities, including mycobacterial adhesion to nonphagoc

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3427d6a43ec6e77e460be3720affc4a5
https://doi.org/10.1128/jb.01299-07

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Conserved Omp85 lid-lock structure and substrate recognition in FhaC

Autor: Françoise Jacob-Dubuisson, Sebastian Hiller, Vincent Villeret, Frédérique Dewitte, Fabian Gruss, Timm Maier, Anne-Sophie Delattre, Bernard Clantin

Publikováno v: Nature Communications
Nature Communications, Nature Publishing Group, 2015, 6, pp.7452. ⟨10.1038/ncomms8452⟩
Nature Communications, 2015, 6, pp.7452. ⟨10.1038/ncomms8452⟩
'Nature Communications ', vol: 6, pages: 7452-1-7452-99 (2015)
Nature communications

Omp85 proteins mediate translocation of polypeptide substrates across and into cellular membranes. They share a common architecture comprising substrate-interacting POTRA domains, a C-terminal 16-stranded β-barrel pore and two signature motifs locat

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::05c2978f3be02de8c6dfd3774100c524
https://hal.univ-lille.fr/hal-03182009

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A salmonella type three secretion effector/chaperone complex adopts a hexameric ring-like structure

Autor: Pierre Roblin, Coralie Bompard, Vincent Villeret, Frédérique Dewitte, Emanuele G. Biondi

Publikováno v: Journal of Bacteriology
Journal of Bacteriology, American Society for Microbiology, 2015, 197 (4), pp.688-698. ⟨10.1128/JB.02294-14⟩
Journal of Bacteriology, 2015, 197 (4), pp.688-698. ⟨10.1128/JB.02294-14⟩

Many bacterial pathogens use type three secretion systems (T3SS) to inject virulence factors, named effectors, directly into the cytoplasm of target eukaryotic cells. Most of the T3SS components are conserved among plant and animal pathogens, suggest

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8bd1f3c58a5ac10e6872cf4f82e97bb6
https://hal.inrae.fr/hal-02631331

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The AP-3-dependent targeting of the melanosomal glycoprotein QNR-71 requires a di-leucine-based sorting signal

Autor: P. Martin, Simon Saule, Roland Le Borgne, Frédérique Dewitte, Nathalie Planque, Bernard Hoflack

Publikováno v: Europe PubMed Central

The Quail Neuroretina clone 71 gene (QNR-71) is expressed during the differentiation of retinal pigmented epithelia and the epidermis. It encodes a type I transmembrane glycoprotein that shares significant sequence homologies with several melanosomal

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6ae3145da71cf3fc826fc5572bf6e049
https://doi.org/10.1242/jcs.114.15.2831

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The Ets family member Erg gene is expressed in mesodermal tissues and neural crests at fundamental steps during mouse embryogenesis

Autor: Martine Duterque-Coquillaud, Dominique Stehelin, Xavier Desbiens, Virginie e Vlaeminck-Guillem, Frédérique Dewitte, Séverine Carrère

Publikováno v: Mechanisms of Development. 91:331-335

The Erg gene belongs to the Ets family encoding a class of transcription factors. To gain new insight on the in vivo functional specificity of the Erg gene within the wide Ets family, we used in situ hybridization to determine its expression pattern

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b9f40637c7145563f25e1d3f5d87cb58
https://doi.org/10.1016/s0925-4773(99)00272-5

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Characterization of the human and mouse ETV1/ER81 transcription factor genes: role of the two alternatively spliced isoforms in the human

Autor: Frédérique Dewitte, Kenji Imai, Michel Vidaud, Laurent Pouilly, Jerzy Adamski, Laurent Coutte, Jean-Luc Baert, Didier Monté, Yvan de Launoit

Publikováno v: Oncogene. 18:6278-6286

The Ets transcription factors of the PEA3 group--E1AF/PEA3, ETV1/ER81 and ERM--are almost identical in the ETS DNA-binding and the transcriptional acidic domains. To accelerate our understanding of the molecular basis of putative diseases linked to E

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5721476e03b015a063df6b9a5bdc3d29
https://doi.org/10.1038/sj.onc.1203020

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