Evidence map›Paper›PMID 37749602›Full record

ReviewCell communication and signaling : CCS2023

Functional diversity of c-di-GMP receptors in prokaryotic and eukaryotic systems.

Fazlurrahman Khan, Geum-Jae Jeong, Nazia Tabassum, Young-Mog Kim

Open access · goldAbstract readVideo-Audio MediaReview
In one paragraph

Review in Cell communication and signaling : CCS, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
6.8field-weighted citation impact, top 2% 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

21 citing papers in PubMed, 37 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Discovery of Novel c-di-GMP-Related Genes inPathogens (Basel, Switzerland) · 2026
    Article
  6. Distinct PlzC mechanisms integrate chemotaxis and c-di-GMP signaling to regulateProceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  7. Article
  8. Article
  9. Article
  10. Review
  11. ComFB, a widespread family of c-di-NMP receptor proteins.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  12. Article
  13. c-di-GMP-Dependent Regulation of Motility bybioRxiv : the preprint server for biology · 2025
    Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Frontiers in immunology · 2025
    Article
  19. Article
  20. ComFB, a new widespread family of c-di-NMP receptor proteins.bioRxiv : the preprint server for biology · 2024
    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

4 authors at 1 institution in 1 country.

Fazlurrahman Khan *Marine Integrated Biomedical Technology Center, The National Key Research Institutes in Universities, Pukyong National University, Busan, 48513, Republic of Korea. fkhan055@pknu.ac.kr.
Geum-Jae Jeong *Department of Food Science and Technology, Pukyong National University, Busan, 48513, Republic of Korea.
Nazia TabassumMarine Integrated Biomedical Technology Center, The National Key Research Institutes in Universities, Pukyong National University, Busan, 48513, Republic of Korea.
Young-Mog KimMarine Integrated Biomedical Technology Center, The National Key Research Institutes in Universities, Pukyong National University, Busan, 48513, Republic of Korea. ymkim@pknu.ac.kr.
Pukyong National University · KR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Cyclic bis-(3', 5')-dimeric guanosine monophosphate (c-di-GMP) is ubiquitous in many bacterial species, where it functions as a nucleotide-based secondary messenger and is a vital regulator of numerous biological processes. Due to its ubiquity, most bacterial species possess a wide range of downstream receptors that has a binding affinity to c-di-GMP and elicit output responses. In eukaryotes, several enzymes and riboswitches operate as receptors that interact with c-di-GMP and transduce cellular or environmental signals. This review examines the functional variety of receptors in prokaryotic and eukaryotic systems that exhibit distinct biological responses after interacting with c-di-GMP. Evolutionary relationships and similarities in distance among the c-di-GMP receptors in various bacterial species were evaluated to understand their specificities. Furthermore, residues of receptors involved in c-di-GMP binding are summarized. This review facilitates the understanding of how distinct receptors from different origins bind c-di-GMP equally well, yet fulfill diverse biological roles at the interspecies, intraspecies, and interkingdom levels. Furthermore, it also highlights c-di-GMP receptors as potential therapeutic targets, particularly those found in pathogenic microorganisms. Video Abstract.

Indexed as

Cyclic GMPEukaryotaPhosphorylationPolymersbis(3',5')-cyclic diguanylic acidCyclic GMPPolymersBacteriaBinding affinityc-di-GMPEukaryotesEvolutionary relatednessInterspeciesReceptor

Identifiers

PMID37749602
PMCPMC10519070
OpenAlexW4387019524

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.