Evidence map›Paper›PMID 32633874›Full record

ArticleChembiochem : a European journal of chemical biology2020

Catalytic Promiscuity of cGAS: A Facile Enzymatic Synthesis of 2'-3'-Linked Cyclic Dinucleotides.

Katrin Rosenthal, Martin Becker, Jascha Rolf, Regine Siedentop, Michael Hillen, Markus Nett, Stephan Lütz

Open access · hybridAbstract read
In one paragraph

Article in Chembiochem : a European journal of chemical biology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
1.3field-weighted citation impact, top 20% of its field
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

12 citing papers in PubMed, 20 citations in OpenAlex.

  1. Review
  2. Reaction Engineering of In Vitro Natural Product Biosynthesis: Challenges and Strategies.Chembiochem : a European journal of chemical biology · 2025
    Review
  3. Article
  4. Article
  5. 10th anniversary of discovering cGAMP: synthesis and beyond.Organic chemistry frontiers : an international journal of organic chemistry · 2023
    Article
  6. Article
  7. Review
  8. Review
  9. Article
  10. Article
  11. Article
  12. Article
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

7 authors at 1 institution in 1 country.

Katrin RosenthalDepartment of Biochemical and Chemical Engineering, Chair for Bioprocess Engineering, TU Dortmund University E, mil-Figge-Strasse 66, 44227, Dortmund, Germany.ORCID 0000-0002-6176-6224
Martin BeckerDepartment of Biochemical and Chemical Engineering, Chair for Bioprocess Engineering, TU Dortmund University E, mil-Figge-Strasse 66, 44227, Dortmund, Germany.
Jascha RolfDepartment of Biochemical and Chemical Engineering, Chair for Bioprocess Engineering, TU Dortmund University E, mil-Figge-Strasse 66, 44227, Dortmund, Germany.ORCID 0000-0002-8394-6795
Regine SiedentopDepartment of Biochemical and Chemical Engineering, Chair for Bioprocess Engineering, TU Dortmund University E, mil-Figge-Strasse 66, 44227, Dortmund, Germany.
Michael HillenDepartment of Biochemical and Chemical Engineering, Chair for Bioprocess Engineering, TU Dortmund University E, mil-Figge-Strasse 66, 44227, Dortmund, Germany.
Markus NettDepartment of Biochemical and Chemical Engineering, Laboratory of Technical Biology, TU Dortmund University, Emil-Figge-Strasse 66, 44227, Dortmund, Germany.ORCID 0000-0003-0847-086X
Stephan LützDepartment of Biochemical and Chemical Engineering, Chair for Bioprocess Engineering, TU Dortmund University E, mil-Figge-Strasse 66, 44227, Dortmund, Germany.ORCID 0000-0001-8534-0554
TU Dortmund University · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Cyclic GMP-AMP synthase (cGAS) is a cytosolic DNA sensor that catalyzes the synthesis of the cyclic GMP-AMP dinucleotide 2'3'-cGAMP. 2'3'-cGAMP functions as inducer for the production of type I interferons. Derivatives of this important second messenger are highly valuable for pharmaceutical applications. However, the production of these analogues requires complex, multistep syntheses. Herein, human cGAS is shown to react with a series of unnatural nucleotides, thus leading to novel cyclic dinucleotides. Most substrate derivatives with modifications at the nucleobase, ribose, and the α-thio phosphate were accepted. These results demonstrate the catalytic promiscuity of human cGAS and its utility for the biocatalytic synthesis of cyclic dinucleotide derivatives.

Indexed as

BiocatalysisCyclic Guanosine Monophosphate-Adenosine Monophosphate SynthaseHumansNucleic Acid ConformationNucleotides, CyclicNucleotidyltransferasescGAS protein, humanCyclic Guanosine Monophosphate-Adenosine Monophosphate SynthaseNucleotides, CyclicNucleotidyltransferasesbiocatalysiscatalytic promiscuitycGAScyclic dinucleotidesenzymes

Identifiers

PMID32633874
PMCPMC7754487
OpenAlexW3040942816

What OpenQuestion holds

Textmetadata
LicenceCC BY
Read underepoch 390

Registered trials

None linked

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.