ArticleScientific reports2023
A de novo evolved domain improves the cadmium detoxification capacity of limpet metallothioneins.
Article in Scientific reports, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
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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
3 citing papers in PubMed, 7 citations in OpenAlex.
- The evolutionary history of chelicerate metallothioneins reveals de novo emergence and metal-binding specialization across the subphylum.Scientific reports · 2026Article
- Myriapod Metallothioneins Conserve the Ancestral Architecture of Arthropods While Displaying Lineage-Specific Adaptations in Metal Binding.Genome biology and evolution · 2026Article
- Experimental recombining of repetitive motifs leads to large functional metallothioneins and demonstrates their modular evolvability potential.Protein science : a publication of the Protein Society · 2025Article
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Authors and funding
7 authors at 3 institutions in 2 countries.
Funding
Abstract
Metallothioneins (MTs) constitute an important family of metal binding proteins. Mollusk MTs, in particular, have been used as model systems to better understand the evolution of their metal binding features and functional adaptation. In the present study two recombinantly produced MTs, LgiMT1 and LgiMT2, and their de novo evolved γ domain, of the marine limpet Lottia gigantea, were analyzed by electronic spectroscopy and mass spectrometry. Both MT proteins, as well as their γ domains, exhibit a strong binding specificity for Cd(II), but not for Zn(II) or Cu(I). The LgiMTs' γ domain renders an M
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