ArticleJournal of comparative physiology. A, Neuroethology, sensory, neural, and behavioral physiology2005
Vertebrate-like betagamma-crystallins in the ocular lenses of a copepod.
Article in Journal of comparative physiology. A, Neuroethology, sensory, neural, and behavioral physiology, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 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
2 citing papers in PubMed, 8 citations in OpenAlex.
- Cataract induction in an arthropod reveals how lens crystallins contribute to the formation of biological glass.PloS one · 2025Article
- Article
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Authors and funding
6 authors at 4 institutions in 1 country.
Funding
Abstract
The diverse crystallins are water-soluble proteins that are responsible for the optical properties of cellular lenses of animal eyes. While all vertebrate lenses contain physiological stress-related alpha- and betagamma-crystallins, some also contain taxon-specific, often enzyme-related crystallins. To date, the alpha- and betagamma-crystallins have been found only in vertebrate lenses. Here we report lenses from an invertebrate, the pontellid copepod Anomalocera ornata, accumulate betagamma-crystallin family members as judged by immunocytochemistry, western immunoblotting and microsequencing. Our data provide the first example of betagamma-crystallin members in an invertebrate lens, establishing that the use of this protein family as lens crystallins is not confined to vertebrates.
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Registered trials
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