Evidence map›Paper›PMID 22577956›Full record

ArticleBiochemistry2012

Enhancement of the long-wavelength sensitivity of optogenetic microbial rhodopsins by 3,4-dehydroretinal.

Oleg A Sineshchekov, Elena G Govorunova, Jihong Wang, John L Spudich

Abstract read
In one paragraph

Article in Biochemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
1.2field-weighted citation impact, top 25% of its field
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

20 citing papers in PubMed, 51 citations in OpenAlex.

  1. Enzymatic vitamin APflugers Archiv : European journal of physiology · 2023
    Article
  2. Article
  3. Review
  4. Review
  5. Review
  6. Imaging Voltage with Microbial Rhodopsins.Frontiers in molecular biosciences · 2021
    Review
  7. Article
  8. RubyACRs, nonalgal anion channelrhodopsins with highly red-shifted absorption.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Retinal-Based Proton Pumping in the Near Infrared.Journal of the American Chemical Society · 2017
    Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

4 authors at 1 institution in 1 country.

Oleg A SineshchekovCenter for Membrane Biology, Department of Biochemistry and Molecular Biology, University of Texas Medical School, Houston, Texas 77030, United States. oleg.a.sineshchekov@uth.tmc.edu
Elena G Govorunova
Jihong Wang
John L Spudich
The University of Texas at Austin · US

Funding

Structure/Function of Microbial Sensory RhodopsinsR37GM027750 · NIGMS · UNIVERSITY OF TEXAS HLTH SCI CTR HOUSTON · PI SPUDICH, JOHN LEE · 2003 to 2012
$6.0M
Advanced Naturally Designed Channelrhodopsins for Photocontrol of Neural ActivityRC1AG035779 · NIA · UNIVERSITY OF TEXAS HLTH SCI CTR HOUSTON · PI SINESHCHEKOV, OLEG A, SPUDICH, JOHN LEE · 2009 to 2010
$900k
NIA NIH HHS RC1 AG035779NIA NIH HHS RC1AG035779NIGMS NIH HHS R37 GM027750NIGMS NIH HHS R37GM027750
6 · The paper itself

Abstract

Electrogenic microbial rhodopsins (ion pumps and channelrhodopsins) are widely used to control the activity of neurons and other cells by light (optogenetics). Long-wavelength absorption by optogenetic tools is desirable for increasing the penetration depth of the stimulus light by minimizing tissue scattering and absorption by hemoglobin. A2 retinal (3,4-dehydroretinal) is a natural retinoid that serves as the chromophore in red-shifted visual pigments of several lower aquatic animals. Here we show that A2 retinal reconstitutes a fully functional archaerhodopsin-3 (AR-3) proton pump and four channelrhodopsin variants (CrChR1, CrChR2, CaChR1, and MvChR1). Substitution of A1 with A2 retinal significantly shifted the spectral sensitivity of all tested rhodopsins to longer wavelengths without altering other aspects of their function. The spectral shift upon substitution of A1 with A2 in AR-3 was close to that measured in other archaeal rhodopsins. Notably, the shifts in channelrhodopsins were larger than those measured in archaeal rhodopsins and close to those in animal visual pigments with similar absorption maxima of their A1-bound forms. Our results show that chromophore substitution provides a complementary strategy for improving the efficiency of optogenetic tools.

Indexed as

ChlamydomonasCloning, MolecularEscherichia coliGene ExpressionHalorubrumHEK293 CellsHumansPatch-Clamp TechniquesPichiaRetinaldehydeRhodopsins, MicrobialSpectrophotometrydehydroretinalRetinaldehydeRhodopsins, Microbial

Identifiers

PMID22577956
PMCPMC3437234
OpenAlexW1968303064

What OpenQuestion holds

Textmetadata
LicenceTDM
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.