ArticleNature structural & molecular biology2019
The structure and oxidation of the eye lens chaperone αA-crystallin.
Article in Nature structural & molecular biology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 45 papers.
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.
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.
Who cites it
45 citing papers in PubMed, 70 citations in OpenAlex.
- Reversing the Fold: Polyanionic Macrocycle Dissolves αA66-80 Crystallin Peptide Aggregates.Biomacromolecules · 2026Article
- Review
- Analysis of mouse lens morphological and proteomic abnormalities following deletion of the βB3-crystallin promoter.Experimental eye research · 2025Article
- Small heat shock protein HSPB5 uses disorder to bind zinc with high affinity.bioRxiv : the preprint server for biology · 2025Article
- Cryo-EM structure of amyloid fibrils formed by full-length human αA-crystallin with pathogenic mutation R116C.Communications chemistry · 2025Article
- Article
- MicroRNA-204-5p Attenuates Oxidative Stress, Apoptosis and Inflammation by Targeting TXNIP in Diabetic Cataract.Biochemical genetics · 2025Article
- Mini-αA-crystallin protects a client lens protein from catastrophic aggregation due to heat stress.Protein science : a publication of the Protein Society · 2025Article
- Pharmacological Strategies for Cataract Management: From Molecular Targets to Clinical Translation.International journal of molecular sciences · 2025Review
- Deep Characterization of Isomerization in the Human Eye Lens Proteome by Crystallin-Depleted Data-Independent Acquisition.Aging cell · 2025Article
- Activation mechanism of small heat shock protein HSPB5 revealed by disease-associated mutants.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Capturing the Conformational Heterogeneity of HSPB1 Chaperone Oligomers at Atomic Resolution.Journal of the American Chemical Society · 2025Article
- Mechanism of small heat shock protein client sequestration and induced polydispersity.Nature communications · 2025Article
- Retina-Targeted 17β-Estradiol by the DHED Prodrug Rescues Visual Function and Actuates Neuroprotective Protein Networks After Optic Nerve Crush in a Rat Model of Surgical Menopause.International journal of molecular sciences · 2025Article
- Systemic inflammatory and oxidative stress biomarkers as predictors of pain in sequential bilateral phacoemulsification for age-related cataract.Frontiers in medicine · 2025Article
- Influence of Cataract Causing Mutations on αA-Crystallin: A Computational Approach.The protein journal · 2024Article
- Dynamic fibrillar assembly of αB-crystallin induced by perturbation of the conserved NT-IXI motif resolved by cryo-EM.Nature communications · 2024Article
- Aging of the eye: Lessons from cataracts and age-related macular degeneration.Ageing research reviews · 2024Review
- Review
- The α-crystallin Chaperones Undergo a Quasi-ordered Co-aggregation Process in Response to Saturating Client Interaction.Journal of molecular biology · 2024Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
15 authors at 3 institutions in 2 countries.
Funding
Abstract
The small heat shock protein αA-crystallin is a molecular chaperone important for the optical properties of the vertebrate eye lens. It forms heterogeneous oligomeric ensembles. We determined the structures of human αA-crystallin oligomers by combining cryo-electron microscopy, cross-linking/mass spectrometry, NMR spectroscopy and molecular modeling. The different oligomers can be interconverted by the addition or subtraction of tetramers, leading to mainly 12-, 16- and 20-meric assemblies in which interactions between N-terminal regions are important. Cross-dimer domain-swapping of the C-terminal region is a determinant of αA-crystallin heterogeneity. Human αA-crystallin contains two cysteines, which can form an intramolecular disulfide in vivo. Oxidation in vitro requires conformational changes and oligomer dissociation. The oxidized oligomers, which are larger than reduced αA-crystallin and destabilized against unfolding, are active chaperones and can transfer the disulfide to destabilized substrate proteins. The insight into the structure and function of αA-crystallin provides a basis for understanding its role in the eye lens.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
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.