Evidence map›Paper›PMID 41738955›Full record

ReviewChembiochem : a European journal of chemical biology2026

Biochemical Engineering Perspective on cGAS: From Enzyme Discovery to Potential Industrial Application.

Makram Fataeri, Katrin Rosenthal

Abstract readReview
In one paragraph

Review in Chembiochem : a European journal of chemical 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.

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.

Makram FataeriFaculty of Technology, Bioprocess Engineering, Bielefeld University, Bielefeld, Germany.ORCID https://orcid.org/0009-0004-0268-4917
Katrin RosenthalFaculty of Technology, Bioprocess Engineering, Bielefeld University, Bielefeld, Germany.ORCID https://orcid.org/0000-0002-6176-6224

Funding

Bundesministerium für Wirtschaft und Klimaschutz KK5681701AJ4
6 · The paper itself

Abstract

Since its discovery as a pivotal enzyme in innate immunity, cyclic GMP-AMP synthase (cGAS) has been extensively studied for its immunological significance and catalytic mechanism. However, its potential as a biocatalyst for the efficient synthesis of the second messenger 2'3'-cyclic GMP-AMP (2'3'-cGAMP) remains underexplored. This review provides a comprehensive biotechnological perspective on cGAS, highlighting its enzymatic and structural features, substrate promiscuity, homologs, and engineered variants. We examined the expression systems reported in previous studies and assessed their suitability for scalable cGAS production. Furthermore, we explored reaction engineering strategies for 2'3'-cGAMP synthesis by comparing published production and purification methods. This review aims to bridge the gap between fundamental enzymology and applied bioprocessing by positioning cGAS as a promising biocatalyst for the pharmaceutical industry, with potential applications in immunotherapy, vaccine adjuvants, and beyond.

Indexed as

Nucleotides, CyclicNucleotidyltransferasesProtein EngineeringAnimalsBiocatalysisCyclic Guanosine Monophosphate-Adenosine Monophosphate SynthaseHumanscGAS protein, humancyclic guanosine monophosphate-adenosine monophosphateCyclic Guanosine Monophosphate-Adenosine Monophosphate SynthaseNucleotides, CyclicNucleotidyltransferasesbiocatalysisbioprocesscGAMPcGAScyclic dinucleotides

Identifiers

PMID41738955
PMCPMC12934549

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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.