Zobrazeno 1 - 10
of 20
pro vyhledávání: '"Jean-Pierre Duneau"'
Autor:
Axel Magalon, Frédéric Biaso, Julia Rendon, Stéphane Grimaldi, Farida Seduk, Marlon Sidore, Bruno Guigliarelli, Sinan Al-Attar, Jean-Pierre Duneau
Publikováno v:
ACS Catalysis
ACS Catalysis, 2021, 11 (23), pp.14303-14318. ⟨10.1021/acscatal.1c03988⟩
ACS Catalysis, American Chemical Society, 2021, 11 (23), pp.14303-14318. ⟨10.1021/acscatal.1c03988⟩
ACS Catalysis, 2021, 11 (23), pp.14303-14318. ⟨10.1021/acscatal.1c03988⟩
ACS Catalysis, American Chemical Society, 2021, 11 (23), pp.14303-14318. ⟨10.1021/acscatal.1c03988⟩
International audience; The Mo/W-bisPGD enzyme superfamily comprises a vast number of mononuclear molybdenum and tungsten enzymes that catalyze a great diversity of vital reactions in prokaryotes. In the past decades, much attention has been devoted
Publikováno v:
Biophysical Journal. 122:373a
Publikováno v:
Biochimica et Biophysica Acta:Biomembranes
Biochimica et Biophysica Acta:Biomembranes, Elsevier, 2019, 1861 (2), pp.431-440. ⟨10.1016/j.bbamem.2018.10.017⟩
Biochimica et Biophysica Acta:Biomembranes, 2019, 1861 (2), pp.431-440. ⟨10.1016/j.bbamem.2018.10.017⟩
Biochimica et Biophysica Acta:Biomembranes, Elsevier, 2019, 1861 (2), pp.431-440. ⟨10.1016/j.bbamem.2018.10.017⟩
Biochimica et Biophysica Acta:Biomembranes, 2019, 1861 (2), pp.431-440. ⟨10.1016/j.bbamem.2018.10.017⟩
International audience; In this study, we have investigated the lipids surrounding AqpZ, and the effects of a destabilizing mutation W14A (Schmidt and Sturgis, 2017) on lipid protein interactions. In a first approach, we used Styrene Maleic Acid copo
Publikováno v:
Biochimica et Biophysica Acta:Biomembranes
Biochimica et Biophysica Acta:Biomembranes, Elsevier, 2017, 1859 (1), pp.126-134. ⟨10.1016/j.bbamem.2016.10.014⟩
Biochimica et Biophysica Acta:Biomembranes, 2017, 1859 (1), pp.126-134. ⟨10.1016/j.bbamem.2016.10.014⟩
Biochimica et Biophysica Acta:Biomembranes, Elsevier, 2017, 1859 (1), pp.126-134. ⟨10.1016/j.bbamem.2016.10.014⟩
Biochimica et Biophysica Acta:Biomembranes, 2017, 1859 (1), pp.126-134. ⟨10.1016/j.bbamem.2016.10.014⟩
International audience; Understanding how membrane proteins interact with their environment is fundamental to the understanding of their structure, function and interactions. We have performed coarse-grained molecular dynamics simulations on a series
Autor:
Laure Journet, Abdelrahim Zoued, Eric Cascales, Jean-Pierre Duneau, Alexandre P. España, Françoise Guerlesquin, Eric Durand
Publikováno v:
Journal of Molecular Biology
Journal of Molecular Biology, 2018, 430 (7), pp.987-1003. ⟨10.1016/j.jmb.2018.02.008⟩
Journal of Molecular Biology, Elsevier, 2018, 430 (7), pp.987-1003. ⟨10.1016/j.jmb.2018.02.008⟩
Journal of Molecular Biology, 2018, 430 (7), pp.987-1003. ⟨10.1016/j.jmb.2018.02.008⟩
Journal of Molecular Biology, Elsevier, 2018, 430 (7), pp.987-1003. ⟨10.1016/j.jmb.2018.02.008⟩
The type VI secretion system (T6SS) is a multiprotein complex used by bacteria to deliver effectors into target cells. The T6SS comprises a bacteriophage-like contractile tail structure anchored to the cell envelope by a membrane complex constituted
Autor:
Pierre Hubert, James N. Sturgis, Paul Sawma, Jean-Pierre Duneau, Jonathan Khao, Dominique Bagnard, Jélerôme Hénin
Publikováno v:
Cell Adhesion & Migration. 4:313-324
As a whole, integral membrane proteins represent about one third of sequenced genomes, and more than 50% of currently available drugs target membrane proteins, often cell surface receptors. Some membrane protein classes, with a defined number of tran
Publikováno v:
Biochemistry. 46:2010-2019
Bitopic membrane proteins offer an opportunity for studying transmembrane domain interactions without the structural complexity inherent to multitopic integral membrane proteins. To date, only homomeric associations have been extensively studied quan
Autor:
Dominique Bagnard, Cécile Blanchard, Pierre Hubert, Paul Sawma, Lise Roth, Gérard Crémel, Jean-Pierre Duneau, James N. Sturgis, Emmanuelle Bouveret
Publikováno v:
Journal of Molecular Biology
Journal of Molecular Biology, Elsevier, 2014, 426 (24), pp.4099--111. ⟨10.1016/j.jmb.2014.10.007⟩
Journal of Molecular Biology, 2014, 426 (24), pp.4099--111. ⟨10.1016/j.jmb.2014.10.007⟩
Journal of Molecular Biology, Elsevier, 2014, 426 (24), pp.4099--111. ⟨10.1016/j.jmb.2014.10.007⟩
Journal of Molecular Biology, 2014, 426 (24), pp.4099--111. ⟨10.1016/j.jmb.2014.10.007⟩
International audience; Signaling in eukaryotic cells frequently relies on dynamic interactions of single-pass membrane receptors involving their transmembrane (TM) domains. To search for new such interactions, we have developed a bacterial two-hybri
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d5d5f0f5066d52b0fba193ac1bef4f61
https://hal.archives-ouvertes.fr/hal-01458217
https://hal.archives-ouvertes.fr/hal-01458217
Publikováno v:
Journal of Molecular Graphics and Modelling. 23:305-315
Projection of transmembrane helices using a Uniform B-spline Algorithm is a tool for the visualization of interactions between helices in membrane proteins. It allows the user to generate projections of 3D helices, no matter what their deviations fro
Publikováno v:
Biophysical Journal
Biophysical Journal, 2016, 110 (3), pp.252a--253a. ⟨10.1016/j.bpj.2015.11.1389⟩
Biophysical Journal, Biophysical Society, 2016, 110 (3), pp.252a--253a. ⟨10.1016/j.bpj.2015.11.1389⟩
Biophysical Journal, 2016, 110 (3), pp.252a--253a. ⟨10.1016/j.bpj.2015.11.1389⟩
Biophysical Journal, Biophysical Society, 2016, 110 (3), pp.252a--253a. ⟨10.1016/j.bpj.2015.11.1389⟩
Aquaporin Z is a membrane protein of E. coli that is responsible for water transfer across the membrane. The protein normally forms a tetramer in the membrane and the atomic structure has been resolved by X-ray crystallography. The hydrophobic thickn