Documents dont l'auteur est "Wei, Guanghong"

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Côté, S., Wei, G., & Mousseau, N. (2014). Atomistic mechanisms of huntingtin N-terminal fragment insertion on a phospholipid bilayer revealed by molecular dynamics simulations. Proteins: Structure, Function, and Bioinformatics, 82(7), 1409-1427. Lien externe

Côté, S., Wei, G., & Mousseau, N. (2012). All-Atom Stability and Oligomerization Simulations of Polyglutamine Nanotubes with and without the 17-Amino-Acid N-Terminal Fragment of the Huntingtin Protein. Journal of Physical Chemistry B, 116(40), 12168-12179. Lien externe

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Derreumaux, P., Wei, G., Santini, S., & Mousseau, N. (2004). Early steps of amyloid-petide oligomerisation explored by simulations. Neurobiology of Aging, 25, S143-S143. Lien externe

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Guo, C., Côté, S., Mousseau, N., & Wei, G. (2015). Distinct Helix Propensities and Membrane Interactions of Human and Rat IAPP1-19 Monomers in Anionic Lipid Bilayers. Journal of Physical Chemistry B, 119(8), 3366-3376. Lien externe

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Laghaei, R., Mousseau, N., & Wei, G. (2011). Structure and Thermodynamics of Amylin Dimer Studied by Hamiltonian-Temperature Replica Exchange Molecular Dynamics Simulations. Journal of Physical Chemistry B, 115(12), 3146-3154. Lien externe

Laghaei, R., Mousseau, N., & Wei, G. (2010). Effect of the Disulfide Bond on the Monomeric Structure of Human Amylin Studied by Combined Hamiltonian and Temperature Replica Exchange Molecular Dynamics Simulations. Journal of Physical Chemistry B, 114(20), 7071-7077. Lien externe

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. Lien externe

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. Lien externe

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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. Lien externe

Santini, S., Wei, G., Mousseau, N., & Derreumaux, P. (avril 2004). Exploring the folding and aggregation mechanisms of amyloid-forming peptides by computer simulations [Communication écrite]. 10th International Symposium on Amyloidosis, Tours, France. Lien externe

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. Lien externe

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. Lien externe

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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. Lien externe

Wei, G., Mousseau, N., & Derreumaux, P. (2007). Computational Simulations of the Early Steps of Protein Aggregation. Prion, 1(1), 3-8. Lien externe

Wei, G., Mousseau, N., & Derreumaux, P. (2004). Complex folding pathways in a simple β-hairpin. Proteins: Structure, Function, and Bioinformatics, 56(3), 464-474. Lien externe

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. Lien externe

Wei, G., Mousseau, N., & Derreumaux, P. (2004). Sampling the self-assembly pathways of KFFE hexamers. Biophysical Journal, 87(6), 3648-3656. Lien externe

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. Lien externe

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. Lien externe