Zobrazeno 1 - 8
of 8
pro vyhledávání: '"Hideyoshi, Motoki"'
Autor:
Yuji Furutani, Ryuichiro Ishitani, Osamu Nureki, Víctor A. Lórenz-Fonfría, Tetsunari Kimura, Hideyoshi Motoki, Masahiro Higashi, Shintaro Douki
Publikováno v:
The Journal of Physical Chemistry B. 122:9681-9696
Magnesium ions (Mg2+) are crucial for various biological processes. A bacterial Mg2+ channel, MgtE, tightly regulates the intracellular Mg2+ concentration. Previous X-ray crystal structures showed that MgtE forms a dimeric structure composed of a tot
Autor:
Hiroki Watanabe, Koichi Nakajo, Takayuki Uchihashi, Yoshihiro Kubo, Masahiro Higashi, Yuji Furutani, Hisao Tsukamoto, Hideyoshi Motoki, Christian Ganser
Publikováno v:
Journal of Biological Chemistry. 293:6969-6984
Canonical K+ channels are tetrameric and highly K+-selective, whereas two-pore-domain K+ (K2P) channels form dimers, but with a similar pore architecture. A two-pore-domain potassium channel TWIK1 (KCNK1 or K2P1) allows permeation of Na+ and other mo
Publikováno v:
Journal of Computer Chemistry, Japan. 17:8-13
Autor:
Tetsunari, Kimura, Victor A, Lorenz-Fonfria, Shintaro, Douki, Hideyoshi, Motoki, Ryuichiro, Ishitani, Osamu, Nureki, Masahiro, Higashi, Yuji, Furutani
Publikováno v:
The journal of physical chemistry. B. 122(42)
Magnesium ions (Mg
Publikováno v:
The Journal of chemical physics. 148(2)
The structural stability of a cytochrome c domain-swapped dimer compared with that of the monomer was investigated by molecular dynamics (MD) simulations and by three-dimensional reference interaction site model (3D-RISM) theory. The structural fluct
Autor:
Hisao, Tsukamoto, Masahiro, Higashi, Hideyoshi, Motoki, Hiroki, Watanabe, Christian, Ganser, Koichi, Nakajo, Yoshihiro, Kubo, Takayuki, Uchihashi, Yuji, Furutani
Publikováno v:
The Journal of biological chemistry. 293(18)
Canonical K(+) channels are tetrameric and highly K(+)-selective, whereas two-pore–domain K(+) (K2P) channels form dimers, but with a similar pore architecture. A two-pore–domain potassium channel TWIK1 (KCNK1 or K2P1) allows permeation of Na(+)
Structural properties determining low K+ affinity of the selectivity filter in the TWIK1 K+ channel.
Autor:
Hisao Tsukamoto1,2, Masahiro Higashi3, Hideyoshi Motoki3, Hiroki Watanabe4, Ganser, Christian4, Koichi Nakajo5,6, Yoshihiro Kubo5,6, Takayuki Uchihashi4, Yuji Furutani1,2 furutani@ims.ac.jp
Publikováno v:
Journal of Biological Chemistry. 5/4/2018, Vol. 293 Issue 18, p6969-6984. 16p.
Theoretical analysis of the domain-swapped dimerization of cytochrome c: An MD and 3D-RISM approach.
Publikováno v:
Journal of Chemical Physics; 2018, Vol. 148 Issue 2, p1-N.PAG, 7p, 3 Diagrams, 5 Charts, 3 Graphs