Evidence map›Paper›PMID 37493966›Full record

ArticleJournal of proteome research2023

Absolute Quantification of Photoreceptor Outer Segment Proteins.

Nikolai P Skiba, Tylor R Lewis, William J Spencer, Carson M Castillo, Andrej Shevchenko, Vadim Y Arshavsky

Open access · greenAbstract read
In one paragraph

Article in Journal of proteome research, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
3.2field-weighted citation impact, top 8% 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

17 citing papers in PubMed, 21 citations in OpenAlex.

  1. Article
  2. Article
  3. Absolute quantification of fluorescent protein fusions by mass spectrometry.Protein science : a publication of the Protein Society · 2026
    Article
  4. Article
  5. Article
  6. Design principles of ciliary signaling.Journal of cell science · 2025
    Review
  7. Article
  8. Photopic flicker optoretinography captures the light-driven length modulation of photoreceptors during phototransduction.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  9. In vivo photoreceptor base editing ameliorates rhodopsin-E150K autosomal-recessive retinitis pigmentosa in mice.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  10. Review
  11. Metabolic Phenotyping of Healthy and Diseased Human RPE Cells.Investigative ophthalmology & visual science · 2024
    Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

6 authors at 2 institutions in 2 countries.

Nikolai P SkibaDepartment of Ophthalmology, Duke University School of Medicine, Durham, North Carolina 27710, United States.
Tylor R LewisDepartment of Ophthalmology, Duke University School of Medicine, Durham, North Carolina 27710, United States.ORCID 0000-0001-6832-7972
William J SpencerDepartment of Ophthalmology, Duke University School of Medicine, Durham, North Carolina 27710, United States.
Carson M CastilloDepartment of Ophthalmology, Duke University School of Medicine, Durham, North Carolina 27710, United States.
Andrej ShevchenkoMax Planck Institute of Molecular Cell Biology and Genetics, Dresden 01307, Germany.ORCID 0000-0002-5079-1109
Vadim Y ArshavskyDepartment of Ophthalmology, Duke University School of Medicine, Durham, North Carolina 27710, United States.ORCID 0000-0001-8394-3650
Duke University · USMax Planck Institute of Molecular Cell Biology and Genetics · DE

Funding

VISION RESEARCHP30EY005722 · NEI · DUKE UNIVERSITY · PI Vadim Y Arshavsky · 1985 to 2026
$19.3M
Mechanisms of photoreceptor disc maturationR01EY030451 · NEI · DUKE UNIVERSITY · PI ARSHAVSKY, VADIM Y · 2020 to 2024
$2.4M
The role of ADAM9 in retinal health and diseaseK99EY033763 · NEI · DUKE UNIVERSITY · PI LEWIS, TYLOR ROBERT · 2022 to 2023
$252k
NEI NIH HHS K99 EY033763NEI NIH HHS P30 EY005722NEI NIH HHS R01 EY030451
6 · The paper itself

Abstract

Photoreceptor cells generate neuronal signals in response to capturing light. This process, called phototransduction, takes place in a highly specialized outer segment organelle. There are significant discrepancies in the reported amounts of many proteins supporting this process, particularly those of low abundance, which limits our understanding of their molecular organization and function. In this study, we used quantitative mass spectrometry to simultaneously determine the abundances of 20 key structural and functional proteins residing in mouse rod outer segments. We computed the absolute number of molecules of each protein residing within an individual outer segment and the molar ratio among all 20 proteins. The molar ratios of proteins comprising three well-characterized constitutive complexes in outer segments differed from the established subunit stoichiometries of these complexes by less than 7%, highlighting the exceptional precision of our quantification. Overall, this study resolves multiple existing discrepancies regarding the outer segment abundances of these proteins, thereby advancing our understanding of how the phototransduction pathway functions as a single, well-coordinated molecular ensemble.

Indexed as

ProteinsRod Cell Outer SegmentAnimalsLight Signal TransductionMiceRetinaProteinsabsolute protein quantificationphotoreceptorphototransductionproteomicsretinavision

Identifiers

PMID37493966
PMCPMC10513726
OpenAlexW4385261083

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.