Zobrazeno 1 - 3
of 3
pro vyhledávání: '"Naoya Fukui"'
Autor:
Yasushi Yabuki, Yasushi Kawata, Kazuya Matsuo, Naoya Fukui, Kohji Fukunaga, Tomohiro Mizobata, Yuji Owada, Norifumi Shioda, Ichiro Kawahata
Publikováno v:
International Journal of Molecular Sciences, Vol 21, Iss 6, p 2230 (2020)
International Journal of Molecular Sciences
Volume 21
Issue 6
International Journal of Molecular Sciences
Volume 21
Issue 6
Oligomerization and/or aggregation of &alpha
synuclein (&alpha
Syn) triggers &alpha
synucleinopathies such as Parkinson&rsquo
s disease and dementia with Lewy bodies. It is known that &alpha
Syn can spread in the brain like p
synuclein (&alpha
Syn) triggers &alpha
synucleinopathies such as Parkinson&rsquo
s disease and dementia with Lewy bodies. It is known that &alpha
Syn can spread in the brain like p
Autor:
anna yamasaki, Yasushi Kawata, Hanae Yamamoto, Eiichi Saiki, Rio Matsumura, Kunihiro Hongo, Naoya Fukui, Tomohiro Mizobata, Daichi Kuroyanagi, Mayuka Adachi
Publikováno v:
International Journal of Molecular Sciences
Volume 21
Issue 1
Yamamoto Hanae, Fukui Naoya, Adachi Mayuka, et al. Human Molecular Chaperone Hsp60 and Its Apical Domain Suppress Amyloid Fibril Formation of alpha-Synuclein. INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES. 2020. 21(1). doi:10.3390/ijms21010047
Volume 21
Issue 1
Yamamoto Hanae, Fukui Naoya, Adachi Mayuka, et al. Human Molecular Chaperone Hsp60 and Its Apical Domain Suppress Amyloid Fibril Formation of alpha-Synuclein. INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES. 2020. 21(1). doi:10.3390/ijms21010047
Heat shock proteins play roles in assisting other proteins to fold correctly and in preventing the aggregation and accumulation of proteins in misfolded conformations. However, the process of aging significantly degrades this ability to maintain prot
Publikováno v:
Ojha Bimlesh, Fukui Naoya, Hongo Kunihiro, et al. Suppression of amyloid fibrils using the GroEL apical domain. Scientific Reports. 2016. 6. doi:10.1038/srep31041
Scientific Reports
Scientific Reports
In E. coli cells, rescue of non-native proteins and promotion of native state structure is assisted by the chaperonin GroEL. An important key to this activity lies in the structure of the apical domain of GroEL (GroEL-AD) (residue 191–376), which r