ArticleAdvances in experimental medicine and biology2026
Biological Significance of C-Domain of the Vertebrate CMP-Sialic Acid Synthetases.
Article in Advances in experimental medicine and biology, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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
0 citing papers in PubMed.
No citing paper in PubMed yet.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The CMP-sialic acid synthetase (CSS/CMAS) is essential for the expression of sialic acid (Sia)-containing glycoconjugates on the cell surface and the extracellular space, as it activates free sialic acid (Sia) to CMP-Sia, the sole donor substrate for all kinds of sialytransferases. The vertebrate CSS comprises two domains: the N-terminal domain (N-domain/CSS-N) and the C-terminal domain (C-domain/CSS-C). While CSS-N is highly conserved among most organisms, CSS-C is found only in vertebrates and certain types of bacteria. To investigate the biological significance of CSS-C in vertebrate CSS, its X-ray structure was determined at a resolution of 1.9 Å. CSS-C forms a tetramer and superimposes well with phosphatases of the haloacid dehalogenase superfamily, although it lacks the phosphatase activity due to the blockage of the active-site entrance. Instead, CSS-C functions as a structural platform for the quaternary organization of the CSS. To explore the biological role of CSS-C at the organism level, a medaka mutant strain whose CSS contains a single amino acid substitution, L304Q, was generated. This reverse genetic study revealed that L304 is critical for the CSS stability and that maintaining appropriate levels of soluble CSS expression is essential for animal survival. To obtain further insight into the involvement of CSS-C in regulating enzymatic activity, the effect of CMP-Kdn on the rainbow trout CSS (rtCSS) activity was examined. It was demonstrated that CSS-C regulates Kdn metabolism in rainbow trout, as the activity was inhibited by CMP-Kdn in a C-domain-dependent manner. Taken together, CSS-C not only influences the physicochemical properties but also plays a key role in regulating its enzymatic activity.
Indexed as
Identifiers
41917396What 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.