Zobrazeno 1 - 10
of 45
pro vyhledávání: '"Jun Tamogami"'
Autor:
Masashi Unno, Yuu Hirose, Masaki Mishima, Takashi Kikukawa, Tomotsumi Fujisawa, Tatsuya Iwata, Jun Tamogami
Publikováno v:
Biophysics and Physicobiology, Vol 18 (2021)
Externí odkaz:
https://doaj.org/article/7488bd18ab8749b79a46dfc2640a0be6
Publikováno v:
Biochemistry; 11/5/2024, Vol. 63 Issue 21, p2714-2717, 4p
Autor:
Jun Tamogami
Publikováno v:
YAKUGAKU ZASSHI. 143:111-118
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::ee5c8fdf498e260824fcf68b5fbd826f
https://doi.org/10.1248/yakushi.22-00184
https://doi.org/10.1248/yakushi.22-00184
Publikováno v:
The Journal of Physical Chemistry Letters. 12:9564-9568
Raman optical activity (ROA) spectroscopy was used to study the conformation of the retinal Schiff base chromophore in green-light-absorbing proteorhodopsin, which is a globally distributed light-driven proton pump of aquatic bacteria. The ROA spectr
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ff0ff18f7354316b225d6f434c0f3aa7
https://doi.org/10.1021/acs.jpclett.1c02552
https://doi.org/10.1021/acs.jpclett.1c02552
Autor:
Takashi Kikukawa, Jun Tamogami
Publikováno v:
Epigenetics to Optogenetics-A New Paradigm in the Study of Biology ISBN: 9781838809935
Microbial rhodopsins, which are photoreceptive membrane proteins consisting of seven α-helical structural apoproteins (opsin) and a covalently attached retinal chromophore, are one of the most frequently used optogenetic tools. Since the first succe
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5794c27c11247ba3d4b3c3eb71b2416f
https://doi.org/10.5772/intechopen.97589
https://doi.org/10.5772/intechopen.97589
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
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::367f4d26e85f3a5db6ac372540bcb43a
https://doi.org/10.1016/j.jphotobiol.2018.04.012
https://doi.org/10.1016/j.jphotobiol.2018.04.012
Autor:
Gang Dai, Xiong Geng, Naoki Kamo, Chaoluomeng, Makoto Demura, Takashi Kikukawa, Tatsuo Iwasa, Jun Tamogami
Publikováno v:
Photochemistry and Photobiology. 94:705-714
Aspartic acid 103 (D103) of sensory rhodopsin II from Halobacterium salinarum (HsSRII, or also called phoborhodopsin) corresponds to D115 of bacteriorhodopsin (BR). This amino acid residue is functionally important in BR. This work reveals that a sub
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7466be0264af9c432519107fb0f12a89
https://doi.org/10.1111/php.12917
https://doi.org/10.1111/php.12917
Publikováno v:
The Journal of Biological Chemistry
Many H+-pump rhodopsins conserve "H+ donor" residues in cytoplasmic (CP) half channels to quickly transport H+ from the CP medium to Schiff bases at the center of these proteins. For conventional H+ pumps, the donors are conserved as Asp or Glu but a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c1fefec96d2f77da303f21cb73164411
http://hdl.handle.net/2115/83253
http://hdl.handle.net/2115/83253
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
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::1cfca6ead005ed50362f998dcf35e927
https://doi.org/10.2142/biophysico.14.0_49
https://doi.org/10.2142/biophysico.14.0_49
Publikováno v:
FEBS letters. 592(18)
Proteorhodopsin (PR) is a microbial rhodopsin functioning as a light-driven proton pump in aquatic bacteria. We performed low-temperature Raman measurements of PR to obtain the structure of the primary photoproduct, the K intermediate (PRK ). PRK sho
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3b4686b128209ac609ec16052469760e
https://pubmed.ncbi.nlm.nih.gov/30098005
https://pubmed.ncbi.nlm.nih.gov/30098005