@misc{oai:repo.qst.go.jp:00086338,
 author = {Chan Yao Chong, Maud and Soon Chan, Wai and Hidetoshi, Kono and Chan Yao Chong, Maud and Soon Chan, Wai and Hidetoshi, Kono},
 month = {May},
 note = {Amyloid fibrils formations are involved in many neurodegenerative diseases such as Alzheimer’s disease, Parkinson disease, Amyotrophic Lateral Sclerosis (ALS) and others. The proteins associated with the formation of amyloid fibrils are Intrinsically Disordered Proteins (IDP) in the native state. These IDPs can self- aggregate and form cross-β amyloid fibrils structures at physiological condition. 
The FUS Low-complexity (LC) domain (FUS-LC domain) is such an IDP. This domain is of interest because in ALS patients, mutants in this domain enhance amyloid fibrils and increase stability. Unfortunately, not all the force fields (FF) used in molecular dynamics simulation well describe the behavior of IDPs.  To study the mechanism of FUC-LC fibril formation, we first benchmarked 12 all-atom molecular mechanics force fields to evaluate if they can sample both random coil (IDP) and cross-β amyloid fibrils structures of the wild-type FUS-LC domain. We report how well the FFs reproduce the structures of the FUS-LC domain., 量子生命科学会 第4回大会},
 title = {Benchmark of force fields to characterize the intrinsically disordered region of FUS-LC domain},
 year = {2022}
}