@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 {2019|2072,
	title = {Physics-based oligomeric models of the yeast mitofusin Fzo1 at the molecular scale in the context of membrane docking},
	journal = {Mitochondrion},
	volume = {49},
	year = {2019},
	pages = {234{\textendash}244},
	author = {Brandner, Astrid and De Vecchis, Dario and Marc Baaden and Cohen, Micka{\"e}l M and Antoine Taly}
}
@article {2019|2078,
	title = {Structural dataset from microsecond-long simulations of yeast mitofusin Fzo1 in the context of membrane docking.},
	journal = {Data Brief},
	volume = {26},
	year = {2019},
	month = {2019 Oct},
	pages = {104460},
	abstract = {<p>In this work we present a novel set of possible auto-oligomerisation states of yeast protein Fzo1 in the context of membrane docking. The dataset reports atomistic models and trajectories derived from a molecular dynamics study of the yeast mitofusin Fzo1, residues 101-855. The initial modelling was followed by coarse-grained molecular dynamics simulation to evaluate the stability and the dynamics of each structural model in a solvated membrane environment. Simulations were run for 1\&nbsp;μs and collected with GROMACS v5.0.4 using the martini v2.1 force field. For each structural model, the dataset comprises the production phase under semi-isotropic condition at 1\&nbsp;bar, 310 K and 150 mn NaCl. The integration step is 20 fs and coordinates have been saved every 1 ns. Each trajectory is associated with a ready-available visualization state for the VMD software. These structural detailed informations are a ready-available platform to plan integrative studies on the mitofusin Fzo1 and will aid the community to further elucidate the mitochondrial tethering process during membrane fusion. This dataset is based on the publication \&quot;Physics-based oligomeric models of the yeast mitofusin Fzo1 at the molecular scale in the context of membrane docking.\&quot; (Brandner and De Vecchis et\&nbsp;al., 2019)\&quot;.</p>
},
	issn = {2352-3409},
	doi = {10.1016/j.dib.2019.104460},
	author = {Brandner, Astrid and De Vecchis, Dario 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 = {<p>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.</p>
},
	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}
}
