Evidence map›Paper›PMID 26358292›Full record

ArticleFEBS letters2015

Misfolded opsin mutants display elevated β-sheet structure.

Lisa M Miller, Megan Gragg, Tae Gyun Kim, Paul S-H Park

Open access · bronzeAbstract read
In one paragraph

Article in FEBS letters, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
1.1field-weighted citation impact, top 26% 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

18 citing papers in PubMed, 26 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. Review
  3. Article
  4. Article
  5. Article
  6. Review
  7. Article
  8. Article
  9. Article
  10. Rhodopsin Oligomerization and Aggregation.The Journal of membrane biology · 2019
    Review
  11. Article
  12. Article
  13. Misfolded rhodopsin mutants display variable aggregation properties.Biochimica et biophysica acta. Molecular basis of disease · 2018
    Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. 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

4 authors at 3 institutions in 1 country.

Lisa M MillerNational Synchrotron Light Source-II, Brookhaven National Laboratory, Upton, NY 11973, USA. Electronic address: lmiller@bnl.gov.
Megan GraggDepartment of Ophthalmology and Visual Sciences, Case Western Reserve University, Cleveland, OH 44106, USA; Department of Molecular Medicine, Cleveland Clinic Lerner College of Medicine, Case Western Reserve University, Cleveland, OH 44195, USA.
Tae Gyun KimDepartment of Ophthalmology and Visual Sciences, Case Western Reserve University, Cleveland, OH 44106, USA.
Paul S-H ParkDepartment of Ophthalmology and Visual Sciences, Case Western Reserve University, Cleveland, OH 44106, USA; Department of Molecular Medicine, Cleveland Clinic Lerner College of Medicine, Case Western Reserve University, Cleveland, OH 44195, USA. Electronic address: paul.park@case.edu.
Case Western Reserve University · USBrookhaven National Laboratory · USCleveland Clinic Lerner College of Medicine · US

Funding

TISSUE CULTURE AND HYBRIDOMA MODULEP30EY011373 · NEI · CASE WESTERN RESERVE UNIVERSITY · PI Irina A Pikuleva · 1997 to 2026
$17.7M
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
Acquisition of a Leica TCS SP5 Confocal Microscope For A Multi-User FacilityS10OD016164 · OD · CASE WESTERN RESERVE UNIVERSITY · PI CONRAD, PATRICIA A · 2013 to 2013
$597k
Synchrotron-Based Infrared Microscope for Chemical Imaging of DiseaseS10RR023782 · NCRR · STATE UNIVERSITY NEW YORK STONY BROOK · PI MILLER, LISA M · 2007 to 2007
$296k
NCRR NIH HHS S10 RR023782NEI NIH HHS P30 EY011373NEI NIH HHS P30EY011373NEI NIH HHS R01 EY021731NEI NIH HHS R01EY021731NEI NIH HHS T32 EY024236NEI NIH HHS T32EY024236NIH HHS S10 OD016164
6 · The paper itself

Abstract

Mutations in rhodopsin can cause misfolding and aggregation of the receptor, which leads to retinitis pigmentosa, a progressive retinal degenerative disease. The structure adopted by misfolded opsin mutants and the associated cell toxicity is poorly understood. Förster resonance energy transfer (FRET) and Fourier transform infrared (FTIR) microspectroscopy were utilized to probe within cells the structures formed by G188R and P23H opsins, which are misfolding mutants that cause autosomal dominant retinitis pigmentosa. Both mutants formed aggregates in the endoplasmic reticulum and exhibited altered secondary structure with elevated β-sheet and reduced α-helical content. The newly formed β-sheet structure may facilitate the aggregation of misfolded opsin mutants. The effects observed for the mutants were unrelated to retention of opsin molecules in the endoplasmic reticulum itself.

Indexed as

MutationProtein FoldingProtein Structure, SecondaryAnimalsEndoplasmic ReticulumFluorescence Resonance Energy TransferHEK293 CellsHumansLuminescent ProteinsMiceMicroscopy, ConfocalOpsinsRetinitis PigmentosaRhodopsinSpectrophotometrySpectroscopy, Fourier Transform InfraredLuminescent ProteinsOpsinsRhodopsinG protein-coupled receptorMembrane proteinProtein aggregationProtein misfoldingRetinal degenerationSecondary structure

Identifiers

PMID26358292
PMCPMC4641566
OpenAlexW1947050232

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.