@misc{oai:repo.qst.go.jp:00084330,
 author = {Chan Yao Chong, Maud and Soon Chan, Wai and Kumar, Amarjeet and Shun, Sakuraba and Hidetoshi, Kono and Chan Yao Chong, Maud and Soon Chan, Wai and Kumar, Amarjeet and Shun, Sakuraba and Hidetoshi, Kono},
 month = {Nov},
 note = {In the cell nucleus, liquid-liquid phase separation (LLPS) caused by proteins is thought to be the key mechanism that produces non-membrane compartments which segregate sets of DNA and proteins. 
In some diseases such as amyotrophic lateral sclerosis (ALS) and Alzheimer, it is observed that proteins that separate into LLPS can aggregate and form insoluble fibrils.
In ALS patients, mutations have been found in the low-complexity (LC) regions of the FUS protein. LC domains, do not have a stable conformation, are classified as Intrinsically Disordered Proteins and could self-aggregate and form fibrils.
Using all-atom molecular dynamics simulations, we study the fibril structures of FUS-LC domain and the impact of the mutations to understand the aggregation mechanism., The 59th Annual Meeting of the Biophysical Society of Japan},
 title = {Characterization of the Intrinsically Disordered Region of FUS-LC protein involved in fibril formation with molecular dynamics simulations},
 year = {2021}
}