@conference {2016|1606,
	title = {Alzheimer{\textquoteright}s Disease: Insights into Amyloid Fibril Formation from Lattice Monte Carlo Simulations},
	booktitle = {Biophys. J.},
	volume = {110},
	number = {3, 1},
	year = {2016},
	note = {60th Annual Meeting of the Biophysical-Society, Los Angeles, CA, FEB 27-MAR 02, 2016},
	month = {feb},
	pages = {219A},
	publisher = {Biophys Soc},
	organization = {Biophys Soc},
	issn = {0006-3495},
	author = {Thanh-Thuy Tran and Phuong Hoang Nguyen and Philippe Derreumaux}
}
@article {2016|1656,
	title = {Coarse-grained and All-atom Simulations towards the Early and Late Steps of Amyloid Fibril Formation},
	journal = {Isr. J. Chem.},
	volume = {DOI: 10.1002/ijch.201600048.},
	year = {2016},
	author = {M. Chiricotto and Thanh-Thuy Tran and Phuong Hoang Nguyen and S. Melchionna and Fabio Sterpone and Philippe Derreumaux}
}
@article {2016|1703,
	title = {Lattice model for amyloid peptides: OPEP force field parametrization and applications to the nucleus size of Alzheimer{\textquoteright}s peptides},
	journal = {J. Chem. Phys.},
	volume = {144},
	number = {20},
	year = {2016},
	month = {may},
	abstract = {Coarse-grained protein lattice models approximate atomistic details and keep the essential interactions. They are, therefore, suitable for capturing generic features of protein folding and amyloid formation at low computational cost. As our aim is to study the critical nucleus sizes of two experimentally well-characterized peptide fragments A beta(16-22) and A beta(37-42) of the full length A beta(1-42) Alzheimer{\textquoteright}s peptide, it is important that simulations with the lattice model reproduce all-atom simulations. In this study, we present a comprehensive force field parameterization based on the OPEP (Optimized Potential for Efficient protein structure Prediction) force field for an on-lattice protein model, which incorporates explicitly the formation of hydrogen bonds and directions of side-chains. Our bottom-up approach starts with the determination of the best lattice force parameters for the A beta(16-22) dimer by fitting its equilibrium parallel and anti-parallel beta-sheet populations to all-atom simulation results. Surprisingly, the calibrated force field is transferable to the trimer of A beta(16-22) and the dimer and trimer of A beta(37-42). Encouraged by this finding, we characterized the free energy landscapes of the two decamers. The dominant structure of the A beta(16-22) decamer matches the microcrystal structure. Pushing the simulations for aggregates between 4-mer and 12-mer suggests a nucleus size for fibril formation of 10 chains. In contrast, the A beta(37-42) decamer is largely disordered with mixed by parallel and antiparallel chains, suggesting that the nucleus size is >10 peptides. Our refined force field coupled to this on-lattice model should provide useful insights into the critical nucleation number associated with neurodegenerative diseases. Published by AIP Publishing.},
	issn = {0021-9606},
	doi = {10.1063/1.4951739},
	author = {Thanh-Thuy Tran and Phuong Hoang Nguyen and Philippe Derreumaux}
}
@article {2015|1714,
	title = {Structures of the Alzheimer{\textquoteright}s Wild-Type A beta 1-40 Dimer from Atomistic Simulations},
	journal = {J. Phys. Chem. B},
	volume = {119},
	number = {33},
	year = {2015},
	pages = {10478{\textendash}10487},
	doi = {10.1021/acs.jpcb.5b05593},
	author = {Tarus, Bogdan and Thanh-Thuy Tran and Nasica-Labouze, Jessica and Fabio Sterpone and Phuong Hoang Nguyen and Philippe Derreumaux}
}
