Zobrazeno 1 - 10
of 77
pro vyhledávání: '"Andrés D, Maturana"'
Autor:
Tatsuya Hagino, Takafumi Kato, Go Kasuya, Kan Kobayashi, Tsukasa Kusakizako, Shin Hamamoto, Tomoaki Sobajima, Yuichiro Fujiwara, Keitaro Yamashita, Hisashi Kawasaki, Andrés D. Maturana, Tomohiro Nishizawa, Osamu Nureki
Publikováno v:
Nature Communications, Vol 13, Iss 1, Pp 1-10 (2022)
VCCN1 is a plant homolog of bestrophin channels and tunes photoreaction as a voltage-gated anion channel at thylakoids. Here, authors report the cryo-EM structures and functional features of apple VCCN1, with insights into its activation mechanism.
Externí odkaz:
https://doaj.org/article/8eb76456739540798060b72b508dd7d4
Autor:
Fei Jin, Minxuan Sun, Takashi Fujii, Yurika Yamada, Jin Wang, Andrés D Maturana, Miki Wada, Shichen Su, Jinbiao Ma, Hironori Takeda, Tsukasa Kusakizako, Atsuhiro Tomita, Yoshiko Nakada-Nakura, Kehong Liu, Tomoko Uemura, Yayoi Nomura, Norimichi Nomura, Koichi Ito, Osamu Nureki, Keiichi Namba, So Iwata, Ye Yu, Motoyuki Hattori
Publikováno v:
PLoS Biology, Vol 19, Iss 4, p e3001231 (2021)
MgtE is a Mg2+ channel conserved in organisms ranging from prokaryotes to eukaryotes, including humans, and plays an important role in Mg2+ homeostasis. The previously determined MgtE structures in the Mg2+-bound, closed-state, and structure-based fu
Externí odkaz:
https://doaj.org/article/1ea7be941cf6441f841a041603748098
Autor:
Kazumasa Oda, Takashi Nomura, Takanori Nakane, Keitaro Yamashita, Keiichi Inoue, Shota Ito, Johannes Vierock, Kunio Hirata, Andrés D Maturana, Kota Katayama, Tatsuya Ikuta, Itsuki Ishigami, Tamaki Izume, Rie Umeda, Ryuun Eguma, Satomi Oishi, Go Kasuya, Takafumi Kato, Tsukasa Kusakizako, Wataru Shihoya, Hiroto Shimada, Tomoyuki Takatsuji, Mizuki Takemoto, Reiya Taniguchi, Atsuhiro Tomita, Ryoki Nakamura, Masahiro Fukuda, Hirotake Miyauchi, Yongchan Lee, Eriko Nango, Rie Tanaka, Tomoyuki Tanaka, Michihiro Sugahara, Tetsunari Kimura, Tatsuro Shimamura, Takaaki Fujiwara, Yasuaki Yamanaka, Shigeki Owada, Yasumasa Joti, Kensuke Tono, Ryuichiro Ishitani, Shigehiko Hayashi, Hideki Kandori, Peter Hegemann, So Iwata, Minoru Kubo, Tomohiro Nishizawa, Osamu Nureki
Publikováno v:
eLife, Vol 10 (2021)
Channelrhodopsins (ChRs) are microbial light-gated ion channels utilized in optogenetics to control neural activity with light . Light absorption causes retinal chromophore isomerization and subsequent protein conformational changes visualized as opt
Externí odkaz:
https://doaj.org/article/bceebbada3ce47869ff14a50376a93f1
Publikováno v:
The Scientific World Journal, Vol 10, Pp 1646-1654 (2010)
Fasciculation and elongation protein zeta-1 (FEZ1) is a mammalian ortholog of the Caenorhabditis elegans UNC-76 protein that possesses four coiled-coil domains and a nuclear localization signal. It is mainly expressed in the brain. Suppression of FEZ
Externí odkaz:
https://doaj.org/article/25f2a2eb5e364ea08f17f2da2f8f8af9
Autor:
Mizuki Takemoto, Hideaki E Kato, Michio Koyama, Jumpei Ito, Motoshi Kamiya, Shigehiko Hayashi, Andrés D Maturana, Karl Deisseroth, Ryuichiro Ishitani, Osamu Nureki
Publikováno v:
PLoS ONE, Vol 10, Iss 6, p e0131094 (2015)
Channelrhodopsin (ChR) is a light-gated cation channel that responds to blue light. Since ChR can be readily expressed in specific neurons to precisely control their activities by light, it has become a powerful tool in neuroscience. Although the rec
Externí odkaz:
https://doaj.org/article/16dfdbad64584a98bd07efc67fc88013
Publikováno v:
Journal of Molecular Biology. 434:167777
Since neural epidermal growth factor-like-like (NELL) 2 was identified as a novel ligand for the roundabout (Robo) 3 receptor, research on NELL-Robo signaling has become increasingly important. We have previously reported that Robo2 can bind to NELL1
Autor:
Tatsuya Hagino, Takafumi Kato, Go Kasuya, Kan Kobayashi, Tsukasa Kusakizako, Shin Hamamoto, Tomoaki Sobajima, Yuichiro Fujiwara, Keitaro Yamashita, Hisashi Kawasaki, Andrés D. Maturana, Tomohiro Nishizawa, Osamu Nureki
Publikováno v:
Nature communications. 13(1)
In the light reaction of plant photosynthesis, modulation of electron transport chain reactions is important to maintain the efficiency of photosynthesis under a broad range of light intensities. VCCN1 was recently identified as a voltage-gated chlor
Autor:
Tomoyuki Takatsuji, Tomoyuki Tanaka, Yasumasa Joti, Tomohiro Nishizawa, Satomi Oishi, Rie Umeda, Hiroto Shimada, Shigehiko Hayashi, Wataru Shihoya, Osamu Nureki, Rie Tanaka, Atsuhiro Tomita, Tetsunari Kimura, Peter Hegemann, Tatsuya Ikuta, Kunio Hirata, Takafumi Kato, Andrés D. Maturana, Kazumasa Oda, Yongchan Lee, Tamaki Izume, Reiya Taniguchi, Hideki Kandori, Masahiro Fukuda, Hirotake Miyauchi, Takashi Nomura, Kota Katayama, Keiichi Inoue, Minoru Kubo, Ryuun Eguma, So Iwata, Ryuichiro Ishitani, Keitaro Yamashita, Kensuke Tono, Eriko Nango, Takanori Nakane, Yasuaki Yamanaka, Ryoki Nakamura, Go Kasuya, Shota Ito, Shigeki Owada, Mizuki Takemoto, Tatsuro Shimamura, Tsukasa Kusakizako, Johannes Vierock, Michihiro Sugahara, Takaaki Fujiwara, Itsuki Ishigami
Publikováno v:
eLife, Vol 10 (2021)
eLife
eLife
Channelrhodopsins (ChRs) are microbial light-gated ion channels utilized in optogenetics to control neural activity with light . Light absorption causes retinal chromophore isomerization and subsequent protein conformational changes visualized as opt
Autor:
Takashi Fujii, Miki Wada, Jun-Song Wang, Yayoi Nomura, Andrés D. Maturana, Tsukasa Kusakizako, Yurika Yamada, So Iwata, Osamu Nureki, Yoshiko Nakada-Nakura, Atsuhiro Tomita, Motoyuki Hattori, Jie Ma, Keiichi Namba, Kei K. Ito, Minxuan Sun, H. Takeda, Fei Jin, Tomoko Uemura, Shichen Su, Norimichi Nomura, Ye Yu, Kehong Liu
MgtE is a Mg2+ channel conserved in organisms ranging from prokaryotes to eukaryotes, including humans, and plays an important role in Mg2+ homeostasis. The previously determined MgtE structures in the Mg2+-bound, closed state and structure-based fun
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::cee246f6a6872896253039229e7be2e3
https://doi.org/10.1101/2020.08.27.270991
https://doi.org/10.1101/2020.08.27.270991
Publikováno v:
International Journal of Molecular Sciences
The CACNA1C gene encodes for the CaV1.2 protein, which is the pore subunit of cardiac l-type voltage-gated calcium (Ca2+) channels (l-channels). Through alternative splicing, CACNA1C encodes for various CaV1.2 isoforms with different electrophysiolog