ArticleBiomolecules2026
Distinct Domains Contribute to the Subcellular Localization of Human cGAS in Yeast.
Article in Biomolecules, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.
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.
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
1 citing paper in PubMed.
- The Significance of cGAS-STING Signaling in Response to Oncogenic Viruses.Cell biochemistry and function · 2026Review
Corrections and comments
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Authors and funding
5 authors.
Funding
Abstract
Cyclic GMP-AMP synthase (cGAS) functions as a DNA sensor in the cytoplasm, triggering immune responses, but it is also translocated to the nucleus, where it is kept catalytically inactive. It consists of an unstructured N-terminal domain of around 160 amino acids, and a larger C-terminal fold comprising the catalytic and DNA-binding domains. Subcellular localization of cGAS is thought to play a key role in its regulation. Here, we make use of heterologous expression in the eukaryotic model
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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.