Evidence map›Paper›PMID 27233115›Full record

ArticleBiophysical journal2016

Structurally Distinct Cation Channelrhodopsins from Cryptophyte Algae.

Elena G Govorunova, Oleg A Sineshchekov, John L Spudich

Open access · bronzeAbstract readLetter
In one paragraph

Article in Biophysical journal, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.

0numbers the graph read from it
0cells of the map it votes in
30citing papers in PubMed
2.2field-weighted citation impact, top 14% 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

30 citing papers in PubMed, 60 citations in OpenAlex.

  1. Article
  2. Sensing a rainbow of colors: algal photoreceptors.Frontiers in plant science · 2025
    Review
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Potassium-selective channelrhodopsins.Biophysics and physicobiology · 2023
    Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Rhodopsin-Based Optogenetics: Basics and Applications.Methods in molecular biology (Clifton, N.J.) · 2022
    Article
  14. Review
  15. Microbial Rhodopsins.Methods in molecular biology (Clifton, N.J.) · 2022
    Article
  16. Article
  17. Review
  18. History and Perspectives of Ion-Transporting Rhodopsins.Advances in experimental medicine and biology · 2021
    Review
  19. Structure-Function Relationship of Channelrhodopsins.Advances in experimental medicine and biology · 2021
    Review
  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

3 authors at 2 institutions in 1 country.

Elena G GovorunovaCenter for Membrane Biology and Department of Biochemistry and Molecular Biology, University of Texas Health Science Center at Houston, McGovern Medical School, Houston, Texas.
Oleg A SineshchekovCenter for Membrane Biology and Department of Biochemistry and Molecular Biology, University of Texas Health Science Center at Houston, McGovern Medical School, Houston, Texas.
John L SpudichCenter for Membrane Biology and Department of Biochemistry and Molecular Biology, University of Texas Health Science Center at Houston, McGovern Medical School, Houston, Texas. Electronic address: john.l.spudich@uth.tmc.edu.
The University of Texas Health Science Center at Houston · USThe University of Texas Health Science Center · US

Funding

Structure/Function of Microbial Sensory RhodopsinsR01GM027750 · NIGMS · YESHIVA UNIVERSITY · PI SPUDICH, JOHN LEE · 1985 to 2020
$6.6M
Anion channelrhodopsin-based viral tools to manipulate brain networks in behaving animalsU01MH109146 · NIMH · UNIVERSITY OF TEXAS HLTH SCI CTR HOUSTON · PI DRAGOI, VALENTIN, JANZ, ROGER · 2015 to 2017
$3.0M
NIGMS NIH HHS R01 GM027750NIMH NIH HHS U01 MH109146
6 · The paper itself

Abstract

Microbial rhodopsins are remarkable for the diversity of their functional mechanisms based on the same protein scaffold. A class of rhodopsins from cryptophyte algae show close sequence homology with haloarchaeal rhodopsin proton pumps rather than with previously known channelrhodopsins from chlorophyte (green) algae. In particular, both aspartate residues that occupy the positions of the chromophore Schiff base proton acceptor and donor, a hallmark of rhodopsin proton pumps, are conserved in these cryptophyte proteins. We expressed the corresponding polynucleotides in human embryonic kidney (HEK293) cells and studied electrogenic properties of the encoded proteins with whole-cell patch-clamp recording. Despite their lack of residues characteristic of the chlorophyte cation channels, these proteins are cation-conducting channelrhodopsins that carry out light-gated passive transport of Na(+) and H(+). These findings show that channel function in rhodopsins has evolved via multiple routes.

Indexed as

CryptophytaAmino Acid SequenceCations, MonovalentCation Transport ProteinsChlorophytaEvolution, MolecularHEK293 CellsHumansHydrogenHydrogen-Ion ConcentrationLightPatch-Clamp TechniquesPolynucleotidesProtonsSensory RhodopsinsSodiumCations, MonovalentCation Transport ProteinsHydrogenPolynucleotidesProtonsSensory RhodopsinsSodium

Identifiers

PMID27233115
PMCPMC4906376
OpenAlexW2396559509

What OpenQuestion holds

Textmetadata
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.