Cargando…

Implications for the impairment of the rapid channel closing of Proteomonas sulcata anion channelrhodopsin 1 at high Cl(−) concentrations

Natural anion channelrhodopsins (ACRs) have recently received increased attention because of their effectiveness in optogenetic manipulation for neuronal silencing. In this study, we focused on Proteomonas sulcata ACR1 (PsuACR1), which has rapid channel closing kinetics and a rapid recovery to the i...

Descripción completa

Detalles Bibliográficos
Autores principales:	Tsukamoto, Takashi, Kikuchi, Chihiro, Suzuki, Hiromu, Aizawa, Tomoyasu, Kikukawa, Takashi, Demura, Makoto
Formato:	Online Artículo Texto
Lenguaje:	English
Publicado:	Nature Publishing Group UK 2018
Materias:	Article
Acceso en línea:	https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6128917/ https://www.ncbi.nlm.nih.gov/pubmed/30194401 http://dx.doi.org/10.1038/s41598-018-31742-6

Ejemplares similares

Preference of Proteomonas sulcata anion channelrhodopsin for NO(3)(−) revealed using a pH electrode method
por: Kikuchi, Chihiro, et al.
Publicado: (2021)

The preferential transport of NO(3)(−) by full-length Guillardia theta anion channelrhodopsin 1 is enhanced by its extended cytoplasmic domain
por: Ohki, Yuya, et al.
Publicado: (2023)

An inhibitory role of Arg-84 in anion channelrhodopsin-2 expressed in Escherichia coli
por: Doi, Satoko, et al.
Publicado: (2017)

Mutations conferring SO(4)(2−) pumping ability on the cyanobacterial anion pump rhodopsin and the resultant unique features of the mutant
por: Doi, Yuhei, et al.
Publicado: (2022)

Unique Cl(–) pump rhodopsin with close similarity to H(+) pump rhodopsin
por: Kikukawa, Takashi
Publicado: (2021)

Functional importance of the oligomer formation of the cyanobacterial H(+) pump Gloeobacter rhodopsin
por: Iizuka, Azusa, et al.
Publicado: (2019)

Three-Dimensional Structure of the Antimicrobial Peptide Cecropin P1 in Dodecylphosphocholine Micelles and the Role of the C-Terminal Residues
por: Gu, Hao, et al.
Publicado: (2022)

A new approach to detect small peptides clearly and sensitively by Western blotting using a vacuum-assisted detection method
por: Tomisawa, Satoshi, et al.
Publicado: (2013)

Real-time identification of two substrate-binding intermediates for the light-driven sodium pump rhodopsin
por: Kato, Tomoya, et al.
Publicado: (2021)

Presence of a Haloarchaeal Halorhodopsin-Like Cl(−) Pump in Marine Bacteria
por: Nakajima, Yu, et al.
Publicado: (2018)

Quantitation of the neural silencing activity of anion channelrhodopsins in Caenorhabditis elegans and their applicability for long-term illumination
por: Yamanashi, Taro, et al.
Publicado: (2019)

Anion channelrhodopsins for inhibitory cardiac optogenetics
por: Govorunova, Elena G., et al.
Publicado: (2016)

Role of S-Palmitoylation on IFITM5 for the Interaction with FKBP11 in Osteoblast Cells
por: Tsukamoto, Takashi, et al.
Publicado: (2013)

Proton transfer pathway in anion channelrhodopsin-1
por: Tsujimura, Masaki, et al.
Publicado: (2021)

Optical inhibition of larval zebrafish behaviour with anion channelrhodopsins
por: Mohamed, Gadisti Aisha, et al.
Publicado: (2017)

Cation and Anion Channelrhodopsins: Sequence Motifs and Taxonomic Distribution
por: Govorunova, Elena G., et al.
Publicado: (2021)

Extending the Anion Channelrhodopsin-Based Toolbox for Plant Optogenetics
por: Zhou, Yang, et al.
Publicado: (2021)

The complete mitochondrial genome of Geochelone sulcata
por: Shi, Qiong, et al.
Publicado: (2017)

Extending the Time Domain of Neuronal Silencing with Cryptophyte Anion Channelrhodopsins
por: Govorunova, Elena G., et al.
Publicado: (2018)

Crystal structure of a natural light-gated anion channelrhodopsin
por: Li, Hai, et al.
Publicado: (2019)

High-efficiency optogenetic silencing with soma-targeted anion-conducting channelrhodopsins
por: Mahn, Mathias, et al.
Publicado: (2018)

Crystal structure of the natural anion-conducting channelrhodopsin GtACR1
por: Kim, Yoon Seok, et al.
Publicado: (2018)

In vivo fluorescence correlation spectroscopy analyses of FMBP‐1, a silkworm transcription factor
por: Tsutsumi, Motosuke, et al.
Publicado: (2016)

A blue-shifted anion channelrhodopsin from the Colpodellida alga Vitrella brassicaformis
por: Kojima, Keiichi, et al.
Publicado: (2023)

Anion Permeation in Ca(2+)-Activated Cl(−) Channels
por: Qu, Zhiqiang, et al.
Publicado: (2000)

Overexpression of an antimicrobial peptide derived from C. elegans using an aggregation-prone protein coexpression system
por: Tomisawa, Satoshi, et al.
Publicado: (2013)

A Basic Study of the Effects of Mulberry Leaf Administration to Healthy C57BL/6 Mice on Gut Microbiota and Metabolites
por: Gan, Li, et al.
Publicado: (2023)

Molecular Dynamics of Channelrhodopsin at the Early Stages of Channel Opening
por: Takemoto, Mizuki, et al.
Publicado: (2015)

Anion-conducting channelrhodopsins with tuned spectra and modified kinetics engineered for optogenetic manipulation of behavior
por: Wietek, Jonas, et al.
Publicado: (2017)

Time-resolved spectroscopic and electrophysiological data reveal insights in the gating mechanism of anion channelrhodopsin
por: Dreier, Max-Aylmer, et al.
Publicado: (2021)

Mutational analysis of the conserved carboxylates of anion channelrhodopsin-2 (ACR2) expressed in Escherichia coli and their roles in anion transport
por: Kojima, Keiichi, et al.
Publicado: (2018)

Kinetic Evaluation of Photosensitivity in Bi-Stable Variants of Chimeric Channelrhodopsins
por: Hososhima, Shoko, et al.
Publicado: (2015)

Replaceability of Schiff base proton donors in light-driven proton pump rhodopsins
por: Sasaki, Syogo, et al.
Publicado: (2021)

Kinetic characteristics of chimeric channelrhodopsins implicate the molecular identity involved in desensitization
por: Zamani, Alemeh, et al.
Publicado: (2017)

MerMAIDs: a family of metagenomically discovered marine anion-conducting and intensely desensitizing channelrhodopsins
por: Oppermann, Johannes, et al.
Publicado: (2019)

The Expanding Family of Natural Anion Channelrhodopsins Reveals Large Variations in Kinetics, Conductance, and Spectral Sensitivity
por: Govorunova, Elena G., et al.
Publicado: (2017)

Aion is a bistable anion-conducting channelrhodopsin that provides temporally extended and reversible neuronal silencing
por: Rodriguez-Rozada, Silvia, et al.
Publicado: (2022)

From channelrhodopsins to optogenetics
por: Hegemann, Peter, et al.
Publicado: (2013)

Efficient recombinant production of mouse-derived cryptdin family peptides by a novel facilitation strategy for inclusion body formation
por: Song, Yuchi, et al.
Publicado: (2023)

Author Correction: Anion-conducting channelrhodopsins with tuned spectra and modified kinetics engineered for optogenetic manipulation of behavior
por: Wietek, Jonas, et al.
Publicado: (2018)

Cannot write session to /tmp/vufind_sessions/sess_5pcrfuu92e1r222dcd9vfg6otp