@article{27f3c39e5d464243ad9852f3c50429f9,
title = "Elucidating amyloid β-protein folding and assembly: A multidisciplinary approach",
abstract = "Oligomeric, neurotoxic amyloid protein assemblies are thought to be causative agents in Alzheimer's and other neurodegenerative diseases. Development of oligomer-specific therapeutic agents requires a mechanistic understanding of the oligomerization process. This is a daunting task because amyloidogenic protein oligomers often are metastable and comprise structurally heterogeneous populations in equilibrium with monomers and fibrils. A single methodological approach cannot elucidate the entire protein assembly process. An integrated multidisciplinary program is required. We discuss here the synergistic application of in hydro, in vacuo, and in silico methods to the study of the amyloid β-protein, the key pathogenetic agent in Alzheimer's disease.",
author = "Teplow, {David B.} and Lazo, {Noel D.} and Gal Bitan and Summer Bernstein and Thomas Wyttenbach and Bowers, {Michael T.} and Andrij Baumketner and Shea, {Joan Emma} and Brigita Urbanc and Luis Cruz and Jose Borreguero and Stanley, {H. Eugene}",
year = "2006",
month = sep,
doi = "10.1021/ar050063s",
language = "English",
volume = "39",
pages = "635--645",
journal = "Accounts of Chemical Research",
issn = "0001-4842",
publisher = "American Chemical Society",
number = "9",
}