Zobrazeno 1 - 6
of 6
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
Autor:
Yuxi Lin, Naoya Fukui, Mayu S. Terakawa, Toshihiko Sugiki, Yuji Goto, Young-Ho Lee, Yasushi Kawata, Misaki Kinoshita, Tatsuya Ikenoue
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Biomembranes. 1860:757-766
Amyloid fibrillation causes serious neurodegenerative diseases and amyloidosis; however, the detailed mechanisms by which the structural states of precursor proteins in a lipid membrane-associated environment contribute to amyloidogenesis still remai
Autor:
Yasuharu Shinoda, Yasushi Yabuki, Yuki Aoyama, Naoya Fukui, Hanae Yamamoto, Kohji Fukunaga, Tomohiro Mizobata, Ichiro Kawahata, Yasushi Kawata, Kunihiro Hongo, Moe Miyabe
Publikováno v:
The Journal of Biological Chemistry
Fukui, Naoya. Yamamoto, Hanae. Miyabe, Moe. et al. An α-synuclein decoy peptide prevents cytotoxic α-synuclein aggregation caused by fatty acid binding protein 3. Journal of Biological Chemistry. 296, 100663. 2021-04-20.
Fukui, Naoya. Yamamoto, Hanae. Miyabe, Moe. et al. An α-synuclein decoy peptide prevents cytotoxic α-synuclein aggregation caused by fatty acid binding protein 3. Journal of Biological Chemistry. 296, 100663. 2021-04-20.
α-synuclein (αSyn) is a protein known to form intracellular aggregates during the manifestation of Parkinson’s disease. Previously, it was shown that αSyn aggregation was strongly suppressed in the midbrain region of mice that did not possess th
Publikováno v:
The Journal of biological chemistry. 291(48)
The isolated apical domain of the Escherichia coli GroEL subunit displays the ability to suppress the irreversible fibrillation of numerous amyloid-forming polypeptides. In previous experiments, we have shown that mutating Gly-192 (located at hinge I
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