Hokkaido University Collection of Scholarly and Academic Papers
(53,958 recursos)
HUSCAP (Hokkaido University Collection of Scholarly and Academic Papers) contains peer-reviewed journal articles, proceedings, educational resources and any kind of scholarly works of Hokkaido University.
84.
Luteophanol D, New Polyhydroxyl Metabolite from Marine Dinoflagellate Amphidinium sp. - Kubota, Takaaki; Takahashi, Ayako; Tsuda, Masashi; Kobayashi, Jun'ichi
Luteophanol D (1), a new polyhydroxyl linear carbon-chain metabolite,
has been isolated from the cultured marine dinoflagellate Amphidinium sp., which
was isolated from Okinawan marine acoel flatworm Pseudaphanostoma luteocoloris.
85.
Role of Arg-72 of pharaonis Phoborhodopsin (sensory rhodopsin II) on its photochemistry. - Ikeura, Yukako; Shimono, Kazumi; Iwamoto, Masayuki; Sudo, Yuki; Kamo, Naoki
Using various Arg-72 ppR mutants, we obtained the following results: 1), Arg-72ppR together possibly with Asp-193 influenced the pKa of the counterion of the protonated Schiff base.
86.
Role of Asp193 in chromophore-protein interaction of pharaonis phoborhodopsin (sensory rhodopsin II). - Iwamoto, Masayuki; Furutani, Yuji; Sudo, Yuki; Shimono, Kazumi; Kandori, Hideki; Kamo, Naoki
The pKa of the Schiff base (SBH+) of D193N was ~10.1-10.0 (at XH+) and ~11.4-11.6 (at X) depending on the protonation state of a certain residue (designated by X) and independent of Cl, whereas those of the wild type and D193E were >12.
91.
Importance of specific hydrogen bonds of archaeal rhodopsins for the binding to the transducer protein† - Sudo, Yuki; Yamabi, Masaki; Kato, Shinnosuke; Hasegawa, Chisa; Iwamoto, Masayuki; Shimono, Kazumi; Kamo, Naoki; ??, ??
sR and pR work as a photo-sensor of phototaxis, and form signaling complexes in membranes with their respective cognate transducer proteins HtrI (with sR) and HtrII (with pR), through which light signals are transmitted to cytoplasm.
96.
Identification and Herc5-mediated ISGylation of novel target proteins - Takeuchi, Tomoharu; Inoue, Satoshi; Yokosawa, Hideyoshi
ISG15, a protein containing two ubiquitin-like domains, is an interferon-stimulated gene product that functions in antiviral response and is conjugated to various cellular proteins (ISGylation) upon interferon stimulation.