Evidence map›Paper›PMID 30616829›Full record

ArticleMethods in cell biology2019

Detection of misfolded rhodopsin aggregates in cells by Förster resonance energy transfer.

Megan Gragg, Paul S-H Park

Open access · greenAbstract read
In one paragraph

Article in Methods in cell biology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.

0numbers the graph read from it
0cells of the map it votes in
9citing papers in PubMed
2.8field-weighted citation impact, top 10% 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

9 citing papers in PubMed, 13 citations in OpenAlex.

  1. Aggregation of the Constitutively Active K296E Rhodopsin Mutant Contributes to Retinal Degeneration.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2025
    Article
  2. Article
  3. Article
  4. Article
  5. Supramolecular organization of rhodopsin in rod photoreceptor cell membranes.Pflugers Archiv : European journal of physiology · 2021
    Review
  6. Structural aspects of rod opsin and their implication in genetic diseases.Pflugers Archiv : European journal of physiology · 2021
    Review
  7. Article
  8. Review
  9. Rhodopsin Oligomerization and Aggregation.The Journal of membrane biology · 2019
    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 at 1 institution in 1 country.

Megan GraggDepartment of Ophthalmology and Visual Sciences, Case Western Reserve University, Cleveland, OH, United States.
Paul S-H ParkDepartment of Ophthalmology and Visual Sciences, Case Western Reserve University, Cleveland, OH, United States. Electronic address: paul.park@case.edu.
Case Western Reserve University · US

Funding

PHOTOTRANSDUCTION IN HEALTH AND DISEASE - Administrative SupplementR01EY021731 · NEI · CASE WESTERN RESERVE UNIVERSITY · PI Paul S Park · 2011 to 2026
$6.5M
Cole Eye Institute Vision Science Training ProgramT32EY024236 · NEI · CLEVELAND CLINIC LERNER COM-CWRU · PI ANAND-APTE, BELA · 2015 to 2025
$1.0M
NEI NIH HHS R01 EY021731NEI NIH HHS T32 EY024236
6 · The paper itself

Abstract

Rhodopsin is the light receptor in rod photoreceptor cells of the retina that plays a central role in phototransduction and rod photoreceptor cell health. Rhodopsin mutations are the leading known cause of autosomal dominant retinitis pigmentosa, a retinal degenerative disease. A majority of rhodopsin mutations cause misfolding and aggregation of the apoprotein opsin. The nature of aggregates formed by misfolded rhodopsin mutants and the associated cell toxicity is poorly understood. Misfolding rhodopsin mutants have been characterized biochemically, and categorized as either partial or complete misfolding mutants. This classification is incomplete and does not provide sufficient information to fully understand rhodopsin aggregation, disease pathogenesis, and evaluate therapeutic strategies. To better understand the aggregation of misfolded rhodopsin mutants, a Förster resonance energy transfer assay has been developed to monitor the aggregation of fluorescently tagged mutant rhodopsins expressed in live cells.

Indexed as

Protein AggregatesProtein FoldingFluorescence Resonance Energy TransferHEK293 CellsHumansMutationRhodopsinProtein AggregatesRhodopsinFörster resonance energy transferPhototransductionProtein aggregationProtein misfoldingRetinal degenerationRetinitis pigmentosa

Identifiers

PMID30616829
PMCPMC6941733
OpenAlexW2892378277

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.