The preferential transport of NO3− by full-length Guillardia theta anion channelrhodopsin 1 is enhanced by its extended cytoplasmic domain-Reference-Cited by-同舟云学术

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The preferential transport of NO3− by full-length Guillardia theta anion channelrhodopsin 1 is enhanced by its extended cytoplasmic domain

Published:2023-11 Issue:11 Volume:299 Page:105305
ISSN:0021-9258
Container-title:Journal of Biological Chemistry
language:en
Short-container-title:Journal of Biological Chemistry

Author:

Ohki Yuya,Shinone Tsukasa,Inoko Sayo,Sudo Miu,Demura Makoto^ORCID,Kikukawa Takashi^ORCID,Tsukamoto Takashi^ORCID

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry

Reference64 articles.

1. Microbial rhodopsins: the last two decades;Rozenberg;Annu. Rev. Microbiol.,2021

2. Enzymerhodopsins: novel photoregulated catalysts for optogenetics;Mukherjee;Curr. Opin. Struct. Biol.,2019

3. Biophysics of channelrhodopsin;Schneider;Annu. Rev. Biophys.,2015

4. Channelrhodopsin-1: a light-gated proton channel in green algae;Nagel;Science,2002

5. Two rhodopsins mediate phototaxis to low- and high-intensity light in Chlamydomonas reinhardtii;Sineshchekov;Proc. Natl. Acad. Sci. U. S. A.,2002

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