ArticleScientific reports2021
A point-mutation in the C-domain of CMP-sialic acid synthetase leads to lethality of medaka due to protein insolubility.
Article in Scientific reports, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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Who cites it
5 citing papers in PubMed, 7 citations in OpenAlex.
- Biosynthetic and genetic pathways related to sialic acid metabolism.The Journal of biological chemistry · 2026Review
- Identification and Evaluation of CMP-Sialic Acids.Methods in molecular biology (Clifton, N.J.) · 2026Article
- Biological Significance of C-Domain of the Vertebrate CMP-Sialic Acid Synthetases.Advances in experimental medicine and biology · 2026Article
- Nature-Inspired Intelligent Computing: A Comprehensive Survey.Research (Washington, D.C.) · 2024Review
- Sulfation of sialic acid is ubiquitous and essential for vertebrate development.Scientific reports · 2022Article
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Authors and funding
9 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Vertebrate CMP-sialic acid synthetase (CSS), which catalyzes the synthesis of CMP-sialic acid (CMP-Sia), consists of a 28 kDa-N-domain and a 20 kDa-C-domain. The N-domain is known to be a catalytic domain; however, the significance of the C-domain still remains unknown. To elucidate the function of the C-domain at the organism level, we screened the medaka TILLING library and obtained medaka with non-synonymous mutations (t911a), or single amino acid substitutions of CSS, L304Q, in the C-domain. Prominently, most L304Q medaka was lethal within 19 days post-fertilization (dpf). L304Q young fry displayed free Sia accumulation, and impairment of sialylation, up to 8 dpf. At 8 dpf, a marked abnormality in ventricular contraction and skeletal myogenesis was observed. To gain insight into the mechanism of L304Q-induced abnormalities, L304Q was biochemically characterized. Although bacterially expressed soluble L304Q and WT showed the similar V
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