Evidence map›Paper›PMID 34096886›Full record

ArticleAging2021

Racemization in cataractous lens from diabetic and aging individuals: analysis of Asp 58 residue in αA-crystallin.

Xiang-Jia Zhu, Ke-Ke Zhang, Wen-Wen He, Jiao Qi, Yi Lu

Open access · hybridAbstract read
In one paragraph

Article in Aging, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
0.2field-weighted citation impact, top 51% 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

3 citing papers in PubMed, 6 citations in OpenAlex.

  1. Article
  2. Review
  3. 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

5 authors at 3 institutions in 1 country.

Xiang-Jia ZhuEye Institute and Department of Ophthalmology, Eye & ENT Hospital, Fudan University, Shanghai 200031, People's Republic of China.
Ke-Ke ZhangEye Institute and Department of Ophthalmology, Eye & ENT Hospital, Fudan University, Shanghai 200031, People's Republic of China.
Wen-Wen HeEye Institute and Department of Ophthalmology, Eye & ENT Hospital, Fudan University, Shanghai 200031, People's Republic of China.
Jiao QiEye Institute and Department of Ophthalmology, Eye & ENT Hospital, Fudan University, Shanghai 200031, People's Republic of China.
Yi LuEye Institute and Department of Ophthalmology, Eye & ENT Hospital, Fudan University, Shanghai 200031, People's Republic of China.
Chinese Academy of Medical Sciences & Peking Union Medical College · CNFudan University · CNEye & ENT Hospital of Fudan University · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Cataract is the leading cause of visual impairment globally. Racemization of lens proteins may contribute to cataract formation in aging individuals. As a special type of age-related cataract (ARC), diabetic cataract (DC) is characterized by the early onset of cortical opacification and finally developed into a mixed type of cortical and nuclear opacification. We compared racemization of Asp 58 residue, a hotspot position in αA-crystallin, from the cortex and nucleus of diabetic and age-matched senile cataractous lenses, by identifying L-Asp/L-isoAsp/D-Asp/D-isoAsp by mass spectrometry. Compared to nondiabetic cataractous lenses, DC lenses showed a significantly increased cortex/nucleus ratio of D-Asp 58, which originated primarily from an increased percentage of D-Asp 58 in the lens cortex of DC. Moreover, patients diagnosed with diabetes for over 10 years showed a lower cortex/nucleus ratio of D-isoAsp 58 in the lens compared with those who had a shorter duration of diabetes, which originated mainly from an increased percentage of D-isoAsp 58 in the lens nucleus of DC with increasing time of hyperglycemia. Further analysis confirmed decreased protein solubility in diabetic cataractous lenses. The different racemization pattern in DC may be distinguished from ARC and influence its phenotype over the protracted duration of diabetes.

Indexed as

AgedAgingAspartic AcidCataractCell NucleusCrystallinsFemaleHumansIsomerismLens, CrystallineMaleSolubilityAspartic AcidCRYAA protein, humanCrystallinsagingaspartyl residuecataractcrystallindiabeteslensracemization

Identifiers

PMID34096886
PMCPMC8221327
OpenAlexW3170472292

What OpenQuestion holds

Textmetadata
LicenceCC BY
Read underepoch 390

Registered trials

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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.