ArticleJournal of molecular biology2011
The molecular refractive function of lens γ-Crystallins.
Article in Journal of molecular biology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 42 papers.
What it found
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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.
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Who cites it
42 citing papers in PubMed, 84 citations in OpenAlex.
- Functionally Graded Surfaces and Materials: From Fabrication to Biomedical Applications.Chemical reviews · 2026Review
- On the self-assembly of αB-crystallin.Soft matter · 2025Article
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- Cataract-prone variants of γD-crystallin populate a conformation with a partially unfolded N-terminal domain under native conditions.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Aging of the eye: Lessons from cataracts and age-related macular degeneration.Ageing research reviews · 2024Review
- Review
- On the Cranial Nerves.NeuroSci · 2024Review
- Design and Characterization of Model Systems that Promote and Disrupt Transparency of Vertebrate Crystallins In Vitro.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2023Article
- Age-Dependent Changes in the Water Content and Optical Power of the In Vivo Mouse Lens Revealed by Multi-Parametric MRI and Optical Modeling.Investigative ophthalmology & visual science · 2023Article
- Role of Oxidative Stress in Ocular Diseases: A Balancing Act.Metabolites · 2023Review
- Transcriptomic evidence for visual adaptation during the aquatic to terrestrial metamorphosis in leopard frogs.BMC biology · 2022Article
- Redox chemistry of lens crystallins: A system of cysteines.Experimental eye research · 2021Review
- Assessing the Structures and Interactions of γD-Crystallin Deamidation Variants.Structure (London, England : 1993) · 2021Article
- Genetic Adaptations in Mudskipper and Tetrapod Give Insights into Their Convergent Water-to-Land Transition.Animals : an open access journal from MDPI · 2021Article
- Spatiotemporal changes in the human lens proteome: Critical insights into long-lived proteins.Progress in retinal and eye research · 2020Review
- MALDI imaging mass spectrometry of β- and γ-crystallins in the ocular lens.Journal of mass spectrometry : JMS · 2020Article
- Ultrafast Dynamics of Water-Protein Coupled Motions around the Surface of Eye Crystallin.Journal of the American Chemical Society · 2020Article
- Transcriptional profiling of single fiber cells in a transgenic paradigm of an inherited childhood cataract reveals absence of molecular heterogeneity.The Journal of biological chemistry · 2019Article
- Kinetic Stability of Long-Lived Human Lens γ-Crystallins and Their Isolated Double Greek Key Domains.Biophysical journal · 2019Article
- Measuring Ultra-Weak Protein Self-Association by Non-ideal Sedimentation Velocity.Journal of the American Chemical Society · 2019Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
γ-Crystallins constitute the major protein component in the nucleus of the vertebrate eye lens. Present at very high concentrations, they exhibit extreme solubility and thermodynamic stability to prevent scattering of light and formation of cataracts. However, functions beyond this structural role have remained mostly unclear. Here, we calculate molecular refractive index increments of crystallins. We show that all lens γ-crystallins have evolved a significantly elevated molecular refractive index increment, which is far above those of most proteins, including nonlens members of the βγ-crystallin family from different species. The same trait has evolved in parallel in crystallins of different phyla, including S-crystallins of cephalopods. A high refractive index increment can lower the crystallin concentration required to achieve a suitable refractive power of the lens and thereby reduce their propensity to aggregate and form cataracts. To produce a significant increase in the refractive index increment, a substantial global shift in amino acid composition is required, which can naturally explain the highly unusual amino acid composition of γ-crystallins and their functional homologues. This function provides a new perspective for interpreting their molecular structure.
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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.