Zobrazeno 1 - 10
of 48
pro vyhledávání: '"Toshifumi Nara"'
Autor:
Seiji Miyauchi, Mikako Shirouzu, Tomomi Kimura-Someya, Noboru Ohsawa, Takashi Kikukawa, Shigeyuki Yokoyama, Keisuke Ohkawa, Makoto Demura, Naoki Kamo, Kazumi Shimono, Toshifumi Nara, Jun Tamogami
Publikováno v:
Journal of Photochemistry and Photobiology B: Biology. 183:35-45
Acetabularia rhodopsin II (ARII or Ace2), an outward light-driven algal proton pump found in the giant unicellular marine alga Acetabularia acetabulum, has a unique property in the cytoplasmic (CP) side of its channel. The X-ray crystal structure of
Autor:
Kazumi Shimono, Tomomi Kimura-Someya, Shigeyuki Yokoyama, Makoto Demura, Mikako Shirouzu, Seiji Miyauchi, Naoki Kamo, Takashi Kikukawa, Toshifumi Nara, Jun Tamogami
Publikováno v:
Biophysics and Physicobiology. 14:49-55
Conflicts of Interest All authors declare that they have no conflict of interest. Author Contributions J. T., T. K., K. S., and N. K. directed the research. J. T. and N. K. co-wrote the manuscript. K. S. prepared ARII samples. T. K. performed flash p
Autor:
Takashi Kikukawa, Atsushi Matsuyama, Makoto Demura, Jun Tamogami, Toshifumi Nara, Katsunori Iwano, Naoki Kamo
Publikováno v:
Journal of Photochemistry and Photobiology B: Biology. 141:192-201
Whether Cl(-) binds to the sensory rhodopsin II from Natronomonas pharaonis (NpSRII) that acts as a negative phototaxis receptor remains controversial. Two previous photoelectrochemical studies using SnO2 transparent electrodes and ATR-FTIR demonstra
Autor:
Kazumi Shimono, Tastuya Ikehara, Hiroko Osanai, Seiji Miyauchi, Naoki Kamo, Jun Tamogami, Toshifumi Nara
Publikováno v:
Journal of Biophysical Chemistry. :11-21
Isothermal titration calorimetry (ITC) was applied to investigate the interaction of drugs with liposomes. Two types of titration are possible. One type is when the liposome suspension in the cell is titrated by aliquots of drug solution, and the oth
Autor:
Toshifumi Nara, Takashi Kikukawa, Jun Tamogami, Makoto Demura, Sukuna Kurokawa, Eiro Muneyuki, Seiji Miyauchi, Naoki Kamo, Keitaro Sato, Takumi Yamada
Publikováno v:
Biochemistry. 55(7)
Proteorhodopsin (PR) is an outward light-driven proton pump observed in marine eubacteria. Despite many structural and functional similarities to bacteriorhodopsin (BR) in archaea, which also acts as an outward proton pump, the mechanism of the photo
Publikováno v:
Biochemistry. 51:9290-9301
Proteorhodopsin (PR) is one of the microbial rhodopsins that are found in marine eubacteria and likely functions as an outward light-driven proton pump. Previously, we [Tamogami, J., et al. (2009) Photochem. Photobiol.85, 578-589] reported the occurr
Publikováno v:
Journal of Photochemistry and Photobiology B: Biology. 106:87-94
Sensory rhodopsin II from Halobacterium salinarum (HsSRII) is a retinal protein in which retinal binds to a specific lysine residue through a Schiff base. Here, we investigated the photobleaching of HsSRII in the presence of hydroxylamine. For identi
Publikováno v:
Journal of Biochemistry. 142:621-625
EmrE in Escherichia coli belongs to the small multidrug resistance (SMR) transporter family. It functions as a homo-dimer, but the orientation of the two monomers in the membrane (membrane topology) is under debate. We expressed various single-cystei
Publikováno v:
Biochemical and Biophysical Research Communications. 358(4):1071-1075
EbrAB is a multidrug-resistance transporter in Bacillus subtilis that belongs to the small multidrug resistance, and requires two polypeptides of both EbrA and EbrB, implying that it functions in the hetero-dimeric state. In this study, we investigat
Autor:
Toshifumi Nara, Takashi Kikukawa
Publikováno v:
Seibutsu Butsuri. 47:264-267