Evidence map›Paper›PMID 19756011›Full record

ReviewNature reviews. Microbiology2009

Structural and mechanistic determinants of c-di-GMP signalling.

Tilman Schirmer, Urs Jenal

Abstract readReview
PubMed Publisher
In one paragraph

Review in Nature reviews. Microbiology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 265 papers.

0numbers the graph read from it
0cells of the map it votes in
265citing papers in PubMed
24.6field-weighted citation impact, top 1% 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

265 citing papers in PubMed, 472 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Article
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  7. Article
  8. Article
  9. Article
  10. Discovery of Novel c-di-GMP-Related Genes inPathogens (Basel, Switzerland) · 2026
    Article
  11. Quorum sensing in theApplied and environmental microbiology · 2026
    Review
  12. 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
  13. Review
  14. Article
  15. Review
  16. Article
  17. Article
  18. Review
  19. Signaling inComputational and structural biotechnology journal · 2025
    Review
  20. Article

205 more citing papers are in PubMed but not listed here.

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 at 1 institution in 1 country.

Tilman SchirmerBiozentrum, University of Basel, Klingelbergstrasse 50, CH-4056 Basel, Switzerland. tilman.schirmer@unibas.ch
Urs Jenal
University of Basel · CH

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Bis-(3'-5')-cyclic dimeric GMP (c-di-GMP) is a ubiquitous second messenger that regulates cell surface-associated traits in bacteria. Components of this regulatory network include GGDEF and EAL domain-containing proteins that determine the cellular concentrations of c-di-GMP by mediating its synthesis and degradation, respectively. Crystal structure analyses in combination with functional studies have revealed the catalytic mechanisms and regulatory principles involved. Downstream, c-di-GMP is recognized by PilZ domain-containing receptors that can undergo large-scale domain rearrangements on ligand binding. Here, we review recent data on the structure and functional properties of the protein families that are involved in c-di-GMP signalling and discuss the mechanistic implications.

Indexed as

Signal TransductionBacteriaBacterial ProteinsCyclic GMPPhosphoric Diester HydrolasesProtein BindingBacterial Proteinsbis(3',5')-cyclic diguanylic acidCyclic GMPPhosphoric Diester Hydrolases

Identifiers

PMID19756011
OpenAlexW1997450290

What OpenQuestion holds

Textmetadata
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.