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Nasica-Labouze, J., Nguyen, P. H., Sterpone, F., Berthoumieu, O., Buchete, N.-V., Coté, S., De Simone, A., Doig, A. J., Faller, P., Garcia, A., Laio, A., Li, M. S., Melchionna, S., Mousseau, N., Mu, Y., Paravastu, A., Pasquali, S., Rosenman, D. J., Strodel, B., ... Derreumaux, P. (2015). Amyloid β Protein and Alzheimer's Disease: When Computer Simulations Complement Experimental Studies. Chemical Reviews, 115(9), 3518-3563. External link
Sterpone, F., Melchionna, S., Tuffery, P., Pasquali, S., Mousseau, N., Cragnolini, T., Chebaro, Y., St-Pierre, J.-F., Kalimeri, M., Barducci, A., Laurin, Y., Tek, A., Baaden, M., Nguyen, P. H., & Derreumaux, P. (2014). The OPEP protein model: from single molecules, amyloid formation, crowding and hydrodynamics to DNA/RNA systems. Chemical Society Reviews, 43(13), 4871-4893. External link
Côté, S., Laghaei, R., Derreumaux, P., & Mousseau, N. (2012). Distinct Dimerization for Various Alloforms of the Amyloid-Beta Protein: Aβ1-40, Aβ1-42, and Aβ1-40(D23N). Journal of Physical Chemistry B, 116(13), 4043-4055. External link
Chebaro, Y., Jiang, P., Zang, T., Mu, Y., Nguyen, P. H., Mousseau, N., & Derreumaux, P. (2012). Structures of Aβ17-42 Trimers in Isolation and with Five Small-Molecule Drugs Using a Hierarchical Computational Procedure. Journal of Physical Chemistry B, 116(29), 8412-8422. External link
Côté, S., Derreumaux, P., & Mousseau, N. (2011). Distinct Morphologies for Amyloid Beta Protein Monomer: Aβ1-40, Aβ1-42, and Aβ1-40(D23N). Journal of Chemical Theory and Computation, 7(8), 2584-2592. External link
Nasica-Labouze, J., Meli, M., Derreumaux, P., Colombo, G., & Mousseau, N. (2011). A multiscale approach to characterize the early aggregation steps of the amyloid-forming peptide GNNQQNY from the yeast prion sup-35. PLOS Computational Biology, 7(5), e1002051 (18 pages). Available
Chebaro, Y., Dong, X., Laghaei, R., Derreumaux, P., & Mousseau, N. (2009). Replica Exchange Molecular Dynamics Simulations of Coarse-grained Proteins in Implicit Solvent. Journal of Physical Chemistry B, 113(1), 267-274. External link
Chebaro, Y., Mousseau, N., & Derreumaux, P. (2009). Structures and Thermodynamics of Alzheimer's Amyloid-β Aβ(16−35) Monomer and Dimer by Replica Exchange Molecular Dynamics Simulations: Implication for Full-Length Aβ Fibrillation. Journal of Physical Chemistry B, 113(21), 7668-7675. External link
Lu, Y., Derreumaux, P., Guo, Z., Mousseau, N., & Wei, G. (2009). Thermodynamics and dynamics of amyloid peptide oligomerization are sequence dependent. Proteins: Structure, Function, and Bioinformatics, 75(4), 954-963. External link
Liang, C., Derreumaux, P., Mousseau, N., & Wei, G. (2008). The β-Strand-Loop-β-Strand Conformation Is Marginally Populated in β2-Microglobulin (20-41) Peptide in Solution as Revealed by Replica Exchange Molecular Dynamics Simulations. Biophysical Journal, 95(2), 510-517. External link
St-Pierre, J.-F., Mousseau, N., & Derreumaux, P. (2008). The complex folding pathways of protein A suggest a multiple-funnelled energy landscape. Journal of Chemical Physics, 128(4), 045101 (8 pages). External link
Dong, X., Chen, W., Mousseau, N., & Derreumaux, P. (2008). Energy landscapes of the monomer and dimer of the Alzheimer's peptide Aβ(1-28). Journal of Chemical Physics, 128(12), 125108. External link
Mousseau, N., & Derreumaux, P. (2008). Exploring energy landscapes of protein folding and aggregation. Frontiers in Bioscience-Landmark, 13, 4495-4516. External link
Melquiond, A., Dong, X., Mousseau, N., & Derreumaux, P. (2008). Role of the Region 23-28 in Aβ Fibril Formation: Insights from Simulations of the Monomers and Dimers of Alzheimers Peptides Aβ40 and Aβ42. Current Alzheimer Research, 5(3), 244-250. External link
Wei, G., Song, W., Derreumaux, P., & Mousseau, N. (2008). Self-assembly of amyloid-forming peptides by molecular dynamics simulations. Frontiers in Bioscience, 13, 5681-5692. External link
Song, W., Wei, G., Mousseau, N., & Derreumaux, P. (2008). Self-Assembly of the β2-Microglobulin NHVTLSQ Peptide Using a Coarse-Grained Protein Model Reveals a β-Barrel Species. Journal of Physical Chemistry B, 112(14), 4410-4418. External link
Derreumaux, P., & Mousseau, N. (2007). Coarse-grained protein molecular dynamics simulations. Journal of Chemical Physics, 126(2), 025101 (6 pages). External link
Wei, G., Mousseau, N., & Derreumaux, P. (2007). Computational Simulations of the Early Steps of Protein Aggregation. Prion, 1(1), 3-8. External link
Melquiond, A., Gelly, J.-C., Mousseau, N., & Derreumaux, P. (2007). Probing amyloid fibril formation of the NFGAIL peptide by computer simulations. Journal of Chemical Physics, 126(6), 065101 (7 pages). External link
Boucher, G., Mousseau, N., & Derreumaux, P. (2006). Aggregating the amyloid Aβ11-25 peptide into a four-stranded β-sheet structure. Proteins: Structure, Function, and Bioinformatics, 65(4), 877-888. External link
Chen, W., Mousseau, N., & Derreumaux, P. (2006). The conformations of the amyloid-β (21-30) fragment can be described by three families in solution. Journal of Chemical Physics, 125(8), 084911. External link
Melquiond, A., Mousseau, N., & Derreumaux, P. (2006). Structures of soluble amyloid oligomers from computer simulations. Proteins: Structure, Function, and Bioinformatics, 65(1), 180-191. External link
Mousseau, N., & Derreumaux, P. (2005). Exploring the early steps of amyloid peptide aggregation by computers. Accounts of Chemical Research, 38(11), 885-891. External link
Melquiond, A., Boucher, G., Mousseau, N., & Derreumaux, P. (2005). Following the aggregation of amyloid-forming peptides by computer simulations. Journal of Chemical Physics, 122(17), 174904 (8 pages). External link
Wei, G., Mousseau, N., & Derreumaux, P. (2004). Complex folding pathways in a simple β-hairpin. Proteins: Structure, Function, and Bioinformatics, 56(3), 464-474. External link
Derreumaux, P., Wei, G., Santini, S., & Mousseau, N. (2004). Early steps of amyloid-petide oligomerisation explored by simulations. Neurobiology of Aging, 25, S143-S143. External link
Wei, G., Mousseau, N., & Derreumaux, P. (2004). Exploring the early steps of aggregation of amyloid-forming peptide KFFE. Journal of Physics: Condensed Matter, 16(44), S5047-S5054. External link
Santini, S., Mousseau, N., & Derreumaux, P. (2004). In Silico Assembly of Alzheimer's Aβ16-22 Peptide into β-Sheets. Journal of the American Chemical Society, 126(37), 11509-11516. External link
Santini, S., Wei, G., Mousseau, N., & Derreumaux, P. (2004). Pathway Complexity of Alzheimer's β-Amyloid Aβ16-22 Peptide Assembly. Structure, 12(7), 1245-1255. External link
Wei, G., Mousseau, N., & Derreumaux, P. (2004). Sampling the self-assembly pathways of KFFE hexamers. Biophysical Journal, 87(6), 3648-3656. External link
Santini, S., Wei, G., Mousseau, N., & Derreumaux, P. (2003). Exploring the Folding Pathways of Proteins through Energy Landscape Sampling: Application to Alzheimer's β-Amyloid Peptide. Internet Electronic Journal of Molecular Design, 2, 564-577. External link
Wei, G., Derreumaux, P., & Mousseau, N. (2003). Sampling the complex energy landscape of a simple β-hairpin. Journal of Chemical Physics, 119(13), 6403-6406. External link
Wei, G., Mousseau, N., & Derreumaux, P. (2002). Exploring the energy landscape of proteins: A characterization of the activation-relaxation technique. Journal of Chemical Physics, 117(24), 11379-11387. External link
Mousseau, N., & Derreumaux, P. (2002). Sampling methods for protein folding. Trends in Chemical Physics, 10, 235-240. External link
Mousseau, N., Derreumaux, P., Barkema, G. T., & Malek, R. (2001). Sampling activated mechanisms in proteins with the activation-relaxation technique. Journal of Molecular Graphics and Modelling, 19(1), 78-86. External link
Santini, S., Wei, G., Mousseau, N., & Derreumaux, P. (2004, April). Exploring the folding and aggregation mechanisms of amyloid-forming peptides by computer simulations [Paper]. 10th International Symposium on Amyloidosis, Tours, France. External link
Nasica-Labouze, J., & Mousseau, N. (2013). Kinetics of Amyloid Growth. In Derreumaux, P. (ed.), Alzheimer's Disease : Insights into Low Molecular Weight and Cytotoxic Aggregates from In Vitro and Computer Experiments (Vol. 7, pp. 209-237). External link
