@article {2019|2068, title = {Molecular modelling as the spark for active learning approaches for interdisciplinary biology teaching}, journal = {Interface focus}, volume = {9}, year = {2019}, pages = {20180065}, author = {Antoine Taly and Nitti, Francesco and Marc Baaden and Pasquali, S} } @article {2019|2073, title = {A molecular perspective on mitochondrial membrane fusion: from the key players to oligomerization and tethering of mitofusin}, journal = {The Journal of membrane biology}, volume = {252}, year = {2019}, pages = {293{\textendash}306}, author = {De Vecchis, Dario and Brandner, Astrid and Marc Baaden and Cohen, Micka{\"e}l M and Antoine Taly} } @article {2017|2021, title = {A membrane-inserted structural model of the yeast mitofusin Fzo1}, journal = {Sci Rep}, volume = {7}, year = {2017}, month = {2017 Aug 31}, pages = {10217}, type = {Research Article}, abstract = {

Mitofusins are large transmembrane GTPases of the dynamin-related protein family, and are required for the tethering and fusion of mitochondrial outer membranes. Their full-length structures remain unknown, which is a limiting factor in the study of outer membrane fusion. We investigated the structure and dynamics of the yeast mitofusin Fzo1 through a hybrid computational and experimental approach, combining molecular modelling and all-atom molecular dynamics simulations in a lipid bilayer with site-directed mutagenesis and in vivo functional assays. The predicted architecture of Fzo1 improves upon the current domain annotation, with a precise description of the helical spans linked by flexible hinges, which are likely of functional significance. In vivo site-directed mutagenesis validates salient aspects of this model, notably, the long-distance contacts and residues participating in hinges. GDP is predicted to interact with Fzo1 through the G1 and G4 motifs of the GTPase domain. The model reveals structural determinants critical for protein function, including regions that may be involved in GTPase domain-dependent rearrangements.

}, issn = {2045-2322}, doi = {10.1038/s41598-017-10687-2}, author = {De Vecchis, Dario and Cavellini, Laetitia and Marc Baaden and J{\'e}r{\^o}me H{\'e}nin and Cohen, Micka{\"e}l M and Antoine Taly} } @article {2013|1998, title = {{M}oving through the gate in {A}{T}{P}-activated {P}2{X} receptors}, journal = {Trends Biochem. Sci.}, volume = {38}, number = {1}, year = {2013}, month = {jan}, pages = {20{\textendash}29}, author = {Jiang, R. and Antoine Taly and Grutter, T.} } @article {2013|1770, title = {Moving through the gate in ATP-activated P2X receptors}, journal = {Trends Biochem. Sci.}, volume = {38}, number = {1}, year = {2013}, pages = {20{\textendash}29}, publisher = {Elsevier Current Trends}, author = {Jiang, Ruotian and Antoine Taly and Grutter, Thomas} } @article {2005|2011, title = {{M}olecular tuning of fast gating in pentameric ligand-gated ion channels}, journal = {Proc. Natl. Acad. Sci. U.s.a.}, volume = {102}, number = {50}, year = {2005}, month = {dec}, pages = {18207{\textendash}18212}, publisher = {National Acad Sciences}, author = {Grutter, T. and de Carvalho, L. P. and Dufresne, V. and Antoine Taly and Edelstein, S. J. and Jean-Pierre Changeux} }