Evidence map›Paper›PMID 21115004›Full record

ReviewExperimental eye research2011

New focus on alpha-crystallins in retinal neurodegenerative diseases.

Patrice E Fort, Kirsten J Lampi

Abstract readReview
In one paragraph

Review in Experimental eye research, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.

0numbers the graph read from it
0cells of the map it votes in
39citing papers in PubMed
2.4field-weighted citation impact, top 11% 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

39 citing papers in PubMed, 71 citations in OpenAlex.

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  19. Localization of αA-Crystallin in Rat Retinal Müller Glial Cells and Photoreceptors.Microscopy and microanalysis : the official journal of Microscopy Society of America, Microbeam Analysis Society, Microscopical Society of Canada · 2018
    Article
  20. 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

2 authors at 2 institutions in 1 country.

Patrice E FortDepartment of Ophthalmology, 500 University Drive, H166, Hershey, PA 17033, Penn State University, USA. pef11@psu.edu
Kirsten J Lampi
Oregon Health & Science University · USPenn State Milton S. Hershey Medical Center · US

Funding

Role of Deamidation in Human Beta-Crystallin StructureR01EY012239 · NEI · OREGON HEALTH & SCIENCE UNIVERSITY · PI LAMPI, KIRSTEN JEANNE · 2004 to 2012
$2.2M
NEI NIH HHS R01 EY012239
6 · The paper itself

Abstract

The crystallin proteins were initially identified as structural proteins of the ocular lens and have been recently demonstrated to be expressed in normal retina. They are dramatically upregulated by a large range of retinal diseases including diabetic retinopathy, age-related macular degeneration, uveitis, trauma and ischemia. The crystallin family of proteins is composed of alpha-, beta- and gamma-crystallin. Alpha-crystallins, which are small heat shock proteins, have received substantial attention recently. This review summarizes the current knowledge of alpha-crystallins in retinal diseases, their roles in retinal neuron cell survival and retinal inflammation, and the regulation of their expression and activity. Their potential role in the development of new treatments for neurodegenerative diseases is also discussed.

Indexed as

alpha-CrystallinsAnimalsApoptosisCell SurvivalHumansNeurodegenerative DiseasesRetinal DiseasesRetinal NeuronsUp-Regulationalpha-Crystallins

Identifiers

PMID21115004
PMCPMC4454605
OpenAlexW2078251286

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.