Evidence map›Paper›PMID 39754705›Full record

ArticleBiomolecular NMR assignments2025

Assignment of the N-terminal domain of mouse cGAS.

Hanna Aucharova, Rasmus Linser

Abstract read
In one paragraph

Article in Biomolecular NMR assignments, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it
0cells of the map it votes in
0citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

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.

2 · The registry

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.

3 · Its place in the literature

Who cites it

0 citing papers in PubMed.

No citing paper in PubMed yet.

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

2 authors.

Hanna AucharovaDepartment of Chemistry and Chemical Biology, TU Dortmund University, Dortmund, Germany.
Rasmus LinserDepartment of Chemistry and Chemical Biology, TU Dortmund University, Dortmund, Germany. rasmus.linser@tu-dortmund.de.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Cyclic GMP-AMP synthase (cGAS) is a DNA-sensing enzyme that is a member of the nucleotidyltransferase (NTase) family and functions as a DNA sensor. The protein is comprised of a catalytic NTase core domain and an unstructured hypervariable N-terminal domain (NTD) that was reported to increase protein activity by providing an additional DNA-binding surface. We report nearly complete

Indexed as

Nuclear Magnetic Resonance, BiomolecularNucleotidyltransferasesAnimalsCyclic Guanosine Monophosphate-Adenosine Monophosphate SynthaseMiceProtein DomainscGAS protein, mouseCyclic Guanosine Monophosphate-Adenosine Monophosphate SynthaseNucleotidyltransferasescGASCyclic GMP-AMP synthaseIDPsIntrinsically disordered proteinsNMR spectroscopy

Identifiers

PMID39754705
PMCPMC12116816

What OpenQuestion holds

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Registered trials

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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.