Zobrazeno 1 - 10
of 451
pro vyhledávání: '"G. Itoh"'
Autor:
A. Yamazaki, K. Sasa, S. Tomita, S. Ishii, H. Naramoto, M. Sataka, H. Kudo, G. Itoh, M. Ohkubo
Publikováno v:
AIP Advances, Vol 9, Iss 10, Pp 105111-105111-4 (2019)
We have measured microscopic 3-dimensional distribution of plasma-charged hydrogen in polycrystalline Al. The measurements have been carried out nondestructively by using elastic recoil detection analysis under transmission geometry of a collimated 8
Externí odkaz:
https://doaj.org/article/3260a8a088ff415c8c25a08649c5c405
Publikováno v:
Biophysics and Physicobiology, Vol 20 (2023)
Aggregates of amyloid-β (Aβ) peptides are thought to cause Alzheimer’s disease. Polyphenolic compounds are known to inhibit Aβ aggregation. We applied replica permutation with solute tempering (RPST) to the system of Aβ fragments, Aβ(16–22),
Externí odkaz:
https://doaj.org/article/0a591ad00abe416aab2980bdaf2149b1
Autor:
Masayuki X. Mori, Ryo Okada, Reiko Sakaguchi, Hideharu Hase, Yuko Imai, Onur K. Polat, Satoru G. Itoh, Hisashi Okumura, Yasuo Mori, Yasushi Okamura, Ryuji Inoue
Publikováno v:
Scientific Reports, Vol 12, Iss 1, Pp 1-13 (2022)
Abstract Phosphatidylinositol 4,5-bisphosphate (PI(4,5)P2 or PIP2) regulates the activities of numerous membrane proteins, including diacylglycerol(DAG)-activated TRPC3/6/7 channels. Although PIP2 binding is known to support DAG-activated TRP channel
Externí odkaz:
https://doaj.org/article/f7c90b4d91374713a6e8dee08565a3d1
Publikováno v:
PLoS ONE, Vol 18, Iss 9, p e0291093 (2023)
Polyalanine (polyA) disease-causative proteins with an expansion of alanine repeats can be aggregated. Although curative treatments for polyA diseases have not been explored, the dissociation of polyA aggregates likely reduces the cytotoxicity of pol
Externí odkaz:
https://doaj.org/article/1c9cc8c341c848ad9127bd8ad0b83a9a
Publikováno v:
Biophysics and Physicobiology, Vol 19 (2022)
Alzheimer’s disease is thought to be caused by the aggregation of amyloid-β (Aβ) peptides. Their aggregation is accelerated at hydrophilic/hydrophobic interfaces such as the air–water interface and the surface of monosialotetrahexosylgangliosid
Externí odkaz:
https://doaj.org/article/e26e449fc93f4744bb9c4bff7f67b03a
Publikováno v:
Communications Biology, Vol 4, Iss 1, Pp 1-12 (2021)
Thi Hong Dung Nguyen et al. identify which regions within TRP channels TRPV1 and TRPV3 confer their sensitivity to monoterpenes that are major constituents of plant-derived essential oils. This study provides insights into how different TRP channels
Externí odkaz:
https://doaj.org/article/6a7dd3a15c5c4a23879f93e96c0479e4
State-of-the-Art Molecular Dynamics Simulation Studies of RNA-Dependent RNA Polymerase of SARS-CoV-2
Publikováno v:
International Journal of Molecular Sciences, Vol 23, Iss 18, p 10358 (2022)
Molecular dynamics (MD) simulations are powerful theoretical methods that can reveal biomolecular properties, such as structure, fluctuations, and ligand binding, at the level of atomic detail. In this review article, recent MD simulation studies on
Externí odkaz:
https://doaj.org/article/410677bf34264587be4a873b5ef7d7ac
Autor:
Hisashi Okumura, Satoru G. Itoh
Publikováno v:
Molecules, Vol 27, Iss 8, p 2483 (2022)
Alzheimer’s disease is understood to be caused by amyloid fibrils and oligomers formed by aggregated amyloid-β (Aβ) peptides. This review article presents molecular dynamics (MD) simulation studies of Aβ peptides and Aβ fragments on their aggre
Externí odkaz:
https://doaj.org/article/1ef89abbef834657bcdf7567ed0d86f6
Autor:
Kunitoshi Uchida, Tomo Kita, Mitsutoki Hatta, Satoru G. Itoh, Hisashi Okumura, Makoto Tominaga, Jun Yamazaki
Publikováno v:
Heliyon, Vol 7, Iss 1, Pp e06102- (2021)
The transient receptor potential melastatin 5 (TRPM5) channel is a monovalent-permeable cation channel that is activated by intracellular Ca2+. Expression of TRPM5 has been shown in taste cells, pancreas, brainstem and olfactory epithelium, and this
Externí odkaz:
https://doaj.org/article/3090c84e1e064359a34cb27f75a072f4
Autor:
Satoru G. Itoh, Hisashi Okumura
Publikováno v:
International Journal of Molecular Sciences, Vol 22, Iss 4, p 1859 (2021)
Aggregates of amyloid-β (Aβ) peptides are known to be related to Alzheimer’s disease. Their aggregation is enhanced at hydrophilic–hydrophobic interfaces, such as a cell membrane surface and air-water interface, and is inhibited by polyphenols,
Externí odkaz:
https://doaj.org/article/a3743c3eadec4bc194de453868ef74a2