Evidence map›Paper›PMID 21094180›Full record

ArticleInternational journal of biological macromolecules2011

Light-induced phosphorylation of crystallins in the retinal pigment epithelium.

Hyunju Lee, Hyewon Chung, Sung Haeng Lee, Wan Jin Jahng

Open access · greenAbstract read
In one paragraph

Article in International journal of biological macromolecules, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed, 1 pooled it
0.9field-weighted citation impact, top 27% 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

20 citing papers in PubMed, 1 synthesis or guideline pooled it, 30 citations in OpenAlex.

  1. Pooled it
  2. Article
  3. Article
  4. Article
  5. Review
  6. Article
  7. Article
  8. Zeta-crystallin: a moonlighting player in cancer.Cellular and molecular life sciences : CMLS · 2020
    Review
  9. Article
  10. Article
  11. Article
  12. Interactome Mapping Guided by Tissue-Specific Phosphorylation in Age-Related Macular Degeneration.International journal of scientific and engineering research · 2017
    Article
  13. Disruption of Angiogenesis by Anthocyanin-Rich Extracts ofInternational journal of scientific and engineering research · 2017
    Article
  14. Article
  15. Article
  16. Review
  17. Effects of crystallin-β-b2 on stressed RPE in vitro and in vivo.Graefe's archive for clinical and experimental ophthalmology = Albrecht von Graefes Archiv fur klinische und experimentelle Ophthalmologie · 2013
    Article
  18. 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

4 authors at 3 institutions in 2 countries.

Hyunju LeeDepartment of Ophthalmology, University of South Carolina, Columbia, SC 29208, USA.
Hyewon Chung
Sung Haeng Lee
Wan Jin Jahng
University of South Carolina · USChosun University · KRKonkuk University Medical Center · KR

Funding

SOUTH CAROLINA'S CENTER FOR CLINICAL AND TRANSLATIONAL RESEARCH: PLANNING PHASEP20RR023476 · NCRR · UNIVERSITY OF SOUTH CAROLINA AT COLUMBIA · PI DAVIS, RICHARD M. · 2006 to 2006
$156k
NCRR NIH HHS P20 RR023476
6 · The paper itself

Abstract

Protein phosphorylations have essential regulatory roles in visual signaling. Previously, we found that phosphorylation of several proteins in the retina and retinal pigment epithelium (RPE) is involved in anti-apoptotic signaling under oxidative stress conditions, including light exposure. In this study, we used a phosphoprotein enrichment strategy to evaluate the light-induced phosphoproteome of primary bovine RPE cells. Phosphoprotein-enriched extracts from bovine RPE cells exposed to light or dark conditions for 1h were separated by 2D SDS-PAGE. Serine and tyrosine phosphorylations were visualized by 2D phospho Western blotting and specific phosphorylation sites were analyzed by tandem mass spectrometry. Light induced a marked increase in tyrosine phosphorylation of beta crystallin A3 and A4. The most abundant light-induced up-regulated phosphoproteins were crystallins of 15-25 kDa, including beta crystallin S and zeta crystallin. Phosphorylation of beta crystallin suggests an anti-apoptotic chaperone function of crystallins in the RPE. Other chaperones, cytoskeletal proteins, and proteins involved in energy balance were expressed at higher levels in the dark. A detailed analysis of RPE phosphoproteins provides a molecular basis for understanding of light-induced signal transduction and anti-apoptosis mechanisms. Our data indicates that phosphorylation of crystallins likely represents an important mechanism for RPE shielding from physiological and pathophysiological light-induced oxidative injury.

Indexed as

LightAlkaline PhosphataseAnimalsCattleCrystallinsElectrophoresis, Gel, Two-DimensionalPhosphorylationPhosphoserinePhosphotyrosineProteomeReproducibility of ResultsRetinal Pigment EpitheliumSpectrometry, Mass, Matrix-Assisted Laser Desorption-IonizationAlkaline PhosphataseCrystallinsPhosphoserinePhosphotyrosineProteome

Identifiers

PMID21094180
PMCPMC5294918
OpenAlexW2014978982

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.