Evidence map›Paper›PMID 30158697›Full record

ArticleNature2018

Structural mechanisms of selectivity and gating in anion channelrhodopsins.

Hideaki E Kato, Yoon Seok Kim, Joseph M Paggi, Kathryn E Evans, William E Allen, Claire Richardson, Keiichi Inoue, Shota Ito, Charu Ramakrishnan, Lief E Fenno and 9 more

Abstract read
In one paragraph

Article in Nature, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 45 papers.

0numbers the graph read from it
0cells of the map it votes in
45citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

45 citing papers in PubMed.

  1. Article
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  11. Article
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  15. Article
  16. Article
  17. Microbial Rhodopsins.Methods in molecular biology (Clifton, N.J.) · 2022
    Article
  18. Rhodopsin-Based Optogenetics: Basics and Applications.Methods in molecular biology (Clifton, N.J.) · 2022
    Article
  19. Article
  20. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

19 authors.

Hideaki E KatoDepartment of Molecular and Cellular Physiology, Stanford University School of Medicine, Stanford, CA, USA. hekato@stanford.edu.
Yoon Seok KimDepartment of Bioengineering, Stanford University, Stanford, CA, USA.
Joseph M PaggiDepartment of Computer Science, Stanford University, Stanford, CA, USA.
Kathryn E EvansDepartment of Bioengineering, Stanford University, Stanford, CA, USA.
William E AllenDepartment of Bioengineering, Stanford University, Stanford, CA, USA.
Claire RichardsonDepartment of Computer Science, Stanford University, Stanford, CA, USA.
Keiichi InouePRESTO, Japan Science and Technology Agency, Kawaguchi, Japan.
Shota ItoDepartment of Life Science and Applied Chemistry, Nagoya Institute of Technology, Nagoya, Japan.
Charu RamakrishnanDepartment of Bioengineering, Stanford University, Stanford, CA, USA.
Lief E FennoDepartment of Bioengineering, Stanford University, Stanford, CA, USA.
Keitaro YamashitaRIKEN SPring-8 Center, Hyogo, Japan.
Daniel HilgerDepartment of Molecular and Cellular Physiology, Stanford University School of Medicine, Stanford, CA, USA.
Soo Yeun LeeDepartment of Bioengineering, Stanford University, Stanford, CA, USA.
Andre BerndtDepartment of Bioengineering, Stanford University, Stanford, CA, USA.
Kang ShenDepartment of Biology, Stanford University, Stanford, CA, USA.
Hideki KandoriDepartment of Life Science and Applied Chemistry, Nagoya Institute of Technology, Nagoya, Japan.
Ron O DrorDepartment of Computer Science, Stanford University, Stanford, CA, USA.
Brian K KobilkaDepartment of Molecular and Cellular Physiology, Stanford University School of Medicine, Stanford, CA, USA.
Karl DeisserothDepartment of Bioengineering, Stanford University, Stanford, CA, USA. deissero@stanford.edu.

Funding

Channel Structure-Based Tools for Precise Interrogation of Circuitry and BehaviorR37MH075957 · NIMH · STANFORD UNIVERSITY · PI DEISSEROTH, KARL A. · 2013 to 2022
$7.3M
Technology development for fast optical interrogation of living neural circuitryR01MH075957 · NIMH · STANFORD UNIVERSITY · PI DEISSEROTH, KARL A. · 2008 to 2012
$2.6M
Howard Hughes Medical InstituteNIMH NIH HHS R01 MH075957NIMH NIH HHS R37 MH075957
6 · The paper itself

Abstract

Both designed and natural anion-conducting channelrhodopsins (dACRs and nACRs, respectively) have been widely applied in optogenetics (enabling selective inhibition of target-cell activity during animal behaviour studies), but each class exhibits performance limitations, underscoring trade-offs in channel structure-function relationships. Therefore, molecular and structural insights into dACRs and nACRs will be critical not only for understanding the fundamental mechanisms of these light-gated anion channels, but also to create next-generation optogenetic tools. Here we report crystal structures of the dACR iC++, along with spectroscopic, electrophysiological and computational analyses that provide unexpected insights into pH dependence, substrate recognition, channel gating and ion selectivity of both dACRs and nACRs. These results enabled us to create an anion-conducting channelrhodopsin integrating the key features of large photocurrent and fast kinetics alongside exclusive anion selectivity.

Indexed as

Ion Channel GatingAnimalsAnionsCaenorhabditis elegansCells, CulturedChannelrhodopsinsCrystallography, X-RayElectrophysiologyFemaleHEK293 CellsHippocampusHumansHydrogen-Ion ConcentrationIon TransportKineticsMaleAnionsChannelrhodopsins

Identifiers

PMID30158697
PMCPMC6317992

What OpenQuestion holds

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Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.