@article {2017|2030,
	title = {Why Is Research on Amyloid-β Failing to Give New Drugs for Alzheimer{\textquoteright}s Disease?},
	journal = {ACS Chem Neurosci},
	volume = {8},
	year = {2017},
	month = {2017 Jul 19},
	pages = {1435-1437},
	abstract = {<p>The two hallmarks of Alzheimer\&$\#$39;s disease (AD) are the presence of neurofibrillary tangles (NFT) made of aggregates of the hyperphosphorylated tau protein and of amyloid plaques composed of amyloid-β (Aβ) peptides, primarily Aβ1-40 and Aβ1-42. Targeting the production, aggregation, and toxicity of Aβ with small molecule drugs or antibodies is an active area of AD research due to the general acceptance of the amyloid cascade hypothesis, but thus far all drugs targeting Aβ have failed. From a review of the recent literature and our own experience based on in vitro, in silico, and in vivo studies, we present some reasons to explain this repetitive failure.</p>
},
	keywords = {Alzheimer Disease, Amyloid beta-Peptides, Animals, Drug Discovery, Humans, Neuroprotective Agents},
	issn = {1948-7193},
	doi = {10.1021/acschemneuro.7b00188},
	author = {Doig, Andrew J and Del Castillo-Frias, Maria P and Berthoumieu, Olivia and Tarus, Bogdan and Nasica-Labouze, Jessica and Sterpone, Fabio and Phuong Hoang Nguyen and Hooper, Nigel M and Faller, Peter and Philippe Derreumaux}
}
@article {2016|1578,
	title = {Impact of the A2V Mutation on the Heterozygous and Homozygous A beta 1-40 Dimer Structures from Atomistic Simulations},
	journal = {Acs Chem. Neurosci.},
	volume = {7},
	number = {6},
	year = {2016},
	month = {jun},
	pages = {823{\textendash}832},
	abstract = {The A2V mutation was reported to protect from Alzheimer{\textquoteright}s disease in its heterozygous form and cause an early Alzheimer{\textquoteright}s disease type dementia in its homozygous form. Experiments showed that the aggregation rate follows the order A2V > WT (wild-type) > A2V-WT. To understand the impact of this mutation, we carried out replica exchange molecular dynamics simulations of A beta 1-40 WT-A2V and A2V-A2V dimers and compared to the WT dimer. Our atomistic simulations reveal that the mean secondary structure remains constant, but there are substantial differences in the intramolecular and intermolecular conformations upon single and double A2V mutation. Upon single mutation, the intrinsic disorder is reduced, the intermolecular potential energies are reduced, the population of intramolecular three-stranded beta-sheets is increased, and the number of all a dimer topologies is decreased. Taken together, these results offer an explanation for the reduced aggregation rate of the A beta 1-40 A2V-WT peptides and the protective effect of A2V in heterozygotes.},
	issn = {1948-7193},
	doi = {10.1021/acschemneuro.6b00053},
	author = {Phuong Hoang Nguyen and Fabio Sterpone and Campanera, Josep M. and Nasica-Labouze, Jessica and Philippe Derreumaux}
}
@article {2015|1634,
	title = {Amyloid beta Protein and Alzheimer{\textquoteright}s Disease: When Computer Simulations Complement Experimental Studies},
	journal = {Chem. Rev.},
	volume = {115},
	number = {9},
	year = {2015},
	month = {may},
	pages = {3518{\textendash}3563},
	doi = {10.1021/cr500638n},
	author = {Nasica-Labouze, Jessica and Phuong Hoang Nguyen and Fabio Sterpone and Berthoumieu, Olivia and Buchete, Nicolae-Viorel and Cote, Sebastien and De Simone, Alfonso and Doig, Andrew J. and Faller, Peter and Garcia, Angel and Laio, Alessandro and Li, Mai Suan and Melchionna, Simone and Mousseau, Normand and Mu, Yuguang and Paravastu, Anant and Pasquali, Samuela and Rosenman, David J. and Strodel, Birgit and Tarus, Bogdan and Viles, John H. and Zhang, Tong and Wang, Chunyu and Philippe Derreumaux}
}
@article {2015|1635,
	title = {Combined Experimental and Simulation Studies Suggest a Revised Mode of Action of the Anti-Alzheimer Disease Drug NQ-Trp},
	journal = {Chemistry-a European Journal},
	volume = {21},
	number = {36},
	year = {2015},
	pages = {12657{\textendash}12666},
	doi = {10.1002/chem.201500888},
	author = {Berthoumieu, Olivia and Phuong Hoang Nguyen and del Castillo-Frias, Maria P. and Ferre, Sabrina and Tarus, Bogdan and Nasica-Labouze, Jessica and Noel, Sabrina and Saurel, Olivier and Rampon, Claire and Doig, Andrew J. and Philippe Derreumaux and Faller, Peter}
}
@article {2015|1713,
	title = {Folding Atomistic Proteins in Explicit Solvent Using Simulated Tempering},
	journal = {J. Phys. Chem. B},
	volume = {119},
	number = {23},
	year = {2015},
	month = {jun},
	pages = {6941{\textendash}6951},
	author = {Zhang, Tong and Phuong Hoang Nguyen and Nasica-Labouze, Jessica and Mu, Yuguang 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}
}
@conference {2015|1609,
	title = {What Computational Methods can Teach us about the Alzheimer-Protective Nature of A2V-and A2T-Mutant Amyloid-Beta Oligomers},
	booktitle = {Biophys. J.},
	volume = {108},
	number = {2},
	year = {2015},
	pages = {204A-204A},
	author = {Nasica-Labouze, Jessica and Tarus, Bogdan and Phuong Hoang Nguyen and Philippe Derreumaux}
}
@conference {2011|1611,
	title = {Characterization of the Aggregation Pathway for a 20-mer of GNNQQNY using Coarse-Grained and All-Atom Representations},
	booktitle = {Biophys. J.},
	volume = {100},
	number = {3},
	year = {2011},
	month = {feb},
	pages = {Biophys Soc},
	author = {Nasica-Labouze, Jessica and Meli, Massimiliano and Philippe Derreumaux and Colombo, Giorgio and Mousseau, Normand}
}
@article {2011|1962,
	title = {A Multiscale Approach to Characterize the Early Aggregation Steps of the Amyloid-Forming Peptide GNNQQNY from the Yeast Prion Sup-35},
	journal = {Plos Comput. Biol.},
	volume = {7},
	number = {5},
	year = {2011},
	month = {may},
	pages = {e1002051},
	doi = {10.1371/journal.pcbi.1002051},
	author = {Nasica-Labouze, Jessica and Meli, Massimiliano and Philippe Derreumaux and Colombo, Giorgio and Mousseau, Normand}
}
