Evidence map›Paper›PMID 19463898›Full record

ReviewBiochimica et biophysica acta2009

Lens aging: effects of crystallins.

K Krishna Sharma, Puttur Santhoshkumar

Open access · greenAbstract readReview
In one paragraph

Review in Biochimica et biophysica acta, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 155 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
155citing papers in PubMed, 1 pooled it
5.9field-weighted citation impact, top 3% 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

155 citing papers in PubMed, 1 synthesis or guideline pooled it, 328 citations in OpenAlex.

  1. Pooled it
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  13. Ocular changes as potential biomarkers for early diagnosis of Alzheimer's disease.Alzheimer's & dementia : the journal of the Alzheimer's Association · 2025
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95 more citing papers are in PubMed but not listed here.

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.

K Krishna SharmaDepartment of Ophthalmology, University of Missouri-Columbia, 1 Hospital Drive, Columbia, MO 65212, USA. sharmak@health.missouri.edu
Puttur Santhoshkumar
University of Missouri · USUniversity of Missouri Hospital · US

Funding

FUNCTIONAL ELEMENTS IN ALPHA CRYSTALLIN CHAPERONER01EY011981 · NEI · UNIVERSITY OF MISSOURI-COLUMBIA · PI SHARMA, KRISHNA K · 1998 to 2010
$2.8M
AMINOPEPTIDASES IN NORMAL AND CATARACT LENSESR01EY009855 · NEI · UNIVERSITY OF MISSOURI-COLUMBIA · PI SHARMA, KRISHNA K · 1999 to 2009
$1.7M
PROTEIN AND HISTOLOGY MINICORE GRANT FOR VISION RESEARCHR24EY014795 · NEI · UNIVERSITY OF MISSOURI-COLUMBIA · PI SHARMA, KRISHNA K · 2003 to 2007
$855k
NEI NIH HHS R01 EY009855NEI NIH HHS R01 EY011981NEI NIH HHS R24 EY014795
6 · The paper itself

Abstract

The primary function of the eye lens is to focus light on the retina. The major proteins in the lens--alpha, beta, and gamma-crystallins--are constantly subjected to age-related changes such as oxidation, deamidation, truncation, glycation, and methylation. Such age-related modifications are cumulative and affect crystallin structure and function. With time, the modified crystallins aggregate, causing the lens to increasingly scatter light on the retina instead of focusing light on it and causing the lens to lose its transparency gradually and become opaque. Age-related lens opacity, or cataract, is the major cause of blindness worldwide. We review deamidation, and glycation that occur in the lenses during aging keeping in mind the structural and functional changes that these modifications bring about in the proteins. In addition, we review proteolysis and discuss recent observations on how crystallin fragments generated in vivo, through their anti-chaperone activity may cause crystallin aggregation in aging lenses. We also review hyperbaric oxygen treatment induced guinea pig and 'humanized' ascorbate transporting mouse models as suitable options for studies on age-related changes in lens proteins.

Indexed as

AgingAnimalsCataractCrystallinsGlycosylationHumansLens, CrystallineModels, BiologicalOxidation-ReductionPhosphorylationCrystallins

Identifiers

PMID19463898
PMCPMC2743770
OpenAlexW2017203664

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.