@misc{oai:repo.qst.go.jp:00085211,
 author = {Kentaro, Fujii and Nobuo, Maita and Masato, Kato and Koichi, Matsuo(Hiroshima Univ.) and Kentaro, Fujii and Nobuo, Maita and Masato, Kato},
 month = {Mar},
 note = {Aggregation of the RNA-binding protein FUS (Fused in Sarcoma) has been implicated in the neurodegenerative diseases such as ALS (amyotrophic lateral sclerosis) and FTD (frontotemporal dementia) [1]. The low-complexity domain of the FUS (FUS-LC) mediated liquid-liquid phase separation (LLPS) [2], but the structural mechanism is not known in detail. To address the revealing the mechanism, several structural analyses such as NMR or x-ray crystallography were examined [2, 3]. Reentry, Murakami and co-authors were performed Raman microscopy to analyze LLPS local structure [4]. They revealed that the FUS LC have extremely high concentrations which could not achieved in vitro experiments. In order to reveal the process to form LLPS such a high concentration, we examined the spectroscopic study using VUV-CD measurement, which can analyze the secondary structure of the proteins., The 26th Hiroshima International Symposium on Synchrotron Radiation},
 title = {Observation of Liquid-Liquid Phase Separation of  FUS-LC using VUV-CD Spectroscopy},
 year = {2022}
}