Evidence map›Paper›PMID 24183695›Full record

ReviewBiochimica et biophysica acta2014

Fluorescence spectroscopy of rhodopsins: insights and approaches.

Ulrike Alexiev, David L Farrens

Abstract readReview
In one paragraph

Review in Biochimica et biophysica acta, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.

0numbers the graph read from it
0cells of the map it votes in
33citing 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

33 citing papers in PubMed.

  1. Article
  2. Structure of human green cone opsin yields insights into mechanisms underlying the rapid decay of its active, signaling state.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  3. Article
  4. Article
  5. Article
  6. Outstanding women scientists who have broadened the knowledge on biological photoreceptors-II.Photochemical & photobiological sciences : Official journal of the European Photochemistry Association and the European Society for Photobiology · 2024
    Article
  7. Visualization of Nanocarriers and Drugs in Cells and Tissue.Handbook of experimental pharmacology · 2024
    Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Molecular Biology of Microbial Rhodopsins.Methods in molecular biology (Clifton, N.J.) · 2022
    Review
  14. Review
  15. Article
  16. Article
  17. Article
  18. Stereospecific modulation of dimeric rhodopsin.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2019
    Article
  19. Article
  20. Review
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

2 authors.

Ulrike AlexievPhysics Department, Freie Universität Berlin, Berlin, Germany. Electronic address: alexiev@physik.fu-berlin.de.
David L FarrensDepartments of Biochemistry and Molecular Biology, Oregon Health Sciences University, USA.

Funding

Structural Dynamics of Retinal Binding and ReleaseR01EY015436 · NEI · OREGON HEALTH & SCIENCE UNIVERSITY · PI FARRENS, DAVID L · 2006 to 2014
$2.6M
NEI NIH HHS R01 EY015436
6 · The paper itself

Abstract

Fluorescence spectroscopy has become an established tool at the interface of biology, chemistry and physics because of its exquisite sensitivity and recent technical advancements. However, rhodopsin proteins present the fluorescence spectroscopist with a unique set of challenges and opportunities due to the presence of the light-sensitive retinal chromophore. This review briefly summarizes some approaches that have successfully met these challenges and the novel insights they have yielded about rhodopsin structure and function. We start with a brief overview of fluorescence fundamentals and experimental methodologies, followed by more specific discussions of technical challenges rhodopsin proteins present to fluorescence studies. Finally, we end by discussing some of the unique insights that have been gained specifically about visual rhodopsin and its interactions with affiliate proteins through the use of fluorescence spectroscopy. This article is part of a Special Issue entitled: Retinal Proteins - You can teach an old dog new tricks.

Indexed as

Models, MolecularPhotonsAmino Acid SequenceAnimalsCattleFluorescence PolarizationFluorescent DyesHumansMolecular Sequence DataProtein Structure, SecondaryProtein Structure, TertiaryRetinaldehydeRhodopsinSpectrometry, FluorescenceFluorescent DyesRetinaldehydeRhodopsinFluorescence spectroscopyRetinal proteinSite-directed fluorescence labelingVisual rhodopsin

Identifiers

PMID24183695
PMCPMC3965647

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.