Evidence map›Paper›PMID 33929105›Full record

ArticleZoological research2021

Cataract-causing allele in CRYAA (Y118D) proceeds through endoplasmic reticulum stress in mouse model.

Zhe-Kun Jia, Chen-Xi Fu, Ai-Ling Wang, Ke Yao, Xiang-Jun Chen

Open access · diamondAbstract read
In one paragraph

Article in Zoological research, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
1.0field-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

11 citing papers in PubMed, 14 citations in OpenAlex.

  1. Human Crystallin Variation and Cataract.Investigative ophthalmology & visual science · 2026
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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 1 institution in 1 country.

Zhe-Kun JiaEye Center of the Second Affiliated Hospital, Zhejiang University School of Medicine, Hangzhou, Zhejiang 310009, China.
Chen-Xi FuEye Center of the Second Affiliated Hospital, Zhejiang University School of Medicine, Hangzhou, Zhejiang 310009, China.
Ai-Ling WangInstitute of Translational Medicine, Zhejiang University School of Medicine, Hangzhou, Zhejiang 310020, China.
Ke YaoEye Center of the Second Affiliated Hospital, Zhejiang University School of Medicine, Hangzhou, Zhejiang 310009, China. E-mail:xlren@zju.du.cn.
Xiang-Jun ChenEye Center of the Second Affiliated Hospital, Zhejiang University School of Medicine, Hangzhou, Zhejiang 310009, China.
Second Affiliated Hospital of Zhejiang University · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

As small heat shock proteins, α-crystallins function as molecular chaperones and inhibit the misfolding and aggregation of β/γ-crystallins. Genetic mutations of

Indexed as

Disease Models, AnimalAllelesalpha-Crystallin A ChainAnimalsCataractEndoplasmic Reticulum StressMiceMutationalpha-Crystallin A ChainCryaa protein, mouseCataractEndoplasmic reticulum stressUnfolded protein responseαA-crystallin

Identifiers

PMID33929105
PMCPMC8175955
OpenAlexW3159842978

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.