Evidence map›Paper›PMID 11171989›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2001

Electrophysiological characterization of specific interactions between bacterial sensory rhodopsins and their transducers.

G Schmies, M Engelhard, P G Wood, G Nagel, E Bamberg

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
3.1field-weighted citation impact, top 7% 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

24 citing papers in PubMed, 73 citations in OpenAlex.

  1. Review
  2. Article
  3. Mechanism divergence in microbial rhodopsins.Biochimica et biophysica acta · 2014
    Review
  4. From channelrhodopsins to optogenetics.EMBO molecular medicine · 2013
    Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Review
  11. Article
  12. A Schiff base connectivity switch in sensory rhodopsin signaling.Proceedings of the National Academy of Sciences of the United States of America · 2008
    Article
  13. Resolving voltage-dependent structural changes of a membrane photoreceptor by surface-enhanced IR difference spectroscopy.Proceedings of the National Academy of Sciences of the United States of America · 2008
    Article
  14. Article
  15. Three strategically placed hydrogen-bonding residues convert a proton pump into a sensory receptor.Proceedings of the National Academy of Sciences of the United States of America · 2006
    Article
  16. Article
  17. Channelrhodopsin-2, a directly light-gated cation-selective membrane channel.Proceedings of the National Academy of Sciences of the United States of America · 2003
    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

5 authors at 2 institutions in 1 country.

G SchmiesMax-Planck-Institut für Molekulare Physiologie, Otto-Hahn-Strasse 11, 44227 Dortmund, Germany.
M Engelhard
P G Wood
G Nagel
E Bamberg
Max Planck Institute of Molecular Physiology · DEMax Planck Institute of Biophysics · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The halobacterial phototaxis receptors sensory rhodopsin I and II (SRI, SRII) enable the bacteria to seek optimal light conditions for ion pumping by bacteriorhodopsin and/or halorhodopsin. The incoming signal is transferred across the plasma membrane by means of receptor-specific transducer proteins that bind tightly to their corresponding photoreceptors. To investigate the receptor/transducer interaction, advantage is taken of the observation that both SRI and SRII can function as proton pumps. SRI from Halobacterium salinarum, which triggers the positive phototaxis, the photophobic receptor SRII from Natronobacterium pharaonis (pSRII), as well as the mutant pSRII-F86D were expressed in Xenopus oocytes. Voltage-clamp studies confirm that SRI and pSRII function as light-driven, outwardly directed proton pumps with a much stronger voltage dependence than the ion pumps bacteriorhodopsin and halorhodopsin. Coexpression of SRI and pSRII-F86D with their corresponding transducers suppresses the proton transport, revealing a tight binding and specific interaction of the two proteins. These latter results may be exploited to further analyze the binding interaction of the photoreceptors with their downstream effectors.

Indexed as

Archaeal ProteinsAnimalsBacterial ProteinsElectrophysiologyGene ExpressionHalobacterium salinarumMembrane ProteinsNatronobacteriumProton PumpsRhodopsinXenopus laevisArchaeal ProteinsBacterial ProteinsHtrII protein, Halobacterium salinariumhtrI protein, Halobacterium salinariumMembrane ProteinsProton PumpsRhodopsin

Identifiers

PMID11171989
PMCPMC29295
OpenAlexW2041701790

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.