ArticleScience signaling2016
The second messenger c-di-AMP inhibits the osmolyte uptake system OpuC in Staphylococcus aureus.
Article in Science signaling, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 68 papers.
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.
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.
Who cites it
68 citing papers in PubMed, 111 citations in OpenAlex.
- Mislocalization of PBPs inMicrobiology spectrum · 2026Article
- Cyclic di-AMP signaling and regulation inmSphere · 2026Review
- Article
- Using BONCAT to dissect the proteome ofmSphere · 2025Article
- A Halophilic Bacterium for Bioremediation of Saline-Alkali Land: The Triadic and Synergetic Response Mechanism ofMicroorganisms · 2025Article
- Structurally diverse C-terminal accessory domains in type I ABC importers reveal distinct regulatory mechanisms.Structure (London, England : 1993) · 2025Review
- Resensitizing β-Lactams by Reprogramming Purine Metabolism in Small Colony Variant for Osteomyelitis Treatment.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025Article
- Streptococcus pneumoniae GAPN is a key metabolic player necessary for host infection.Protein science : a publication of the Protein Society · 2025Article
- Article
- Membrane-embedded CdaA is required for efficient synthesis of second messenger cyclic di-AMP.Communications biology · 2024Article
- Biofilm formation byProceedings of the National Academy of Sciences of the United States of America · 2024Article
- Article
- Article
- Bacterial cell volume regulation and the importance of cyclic di-AMP.Microbiology and molecular biology reviews : MMBR · 2024Review
- The substrate-binding domains of the osmoregulatory ABC importer OpuA transiently interact.eLife · 2024Article
- A small step towards an important goal: fragment screen of the c-di-AMP-synthesizing enzyme CdaA.Acta crystallographica. Section D, Structural biology · 2024Article
- mSphere of Influence: Targeting bacterial signaling and metabolism to overcome antimicrobial resistance.mSphere · 2024Article
- Synthesis and degradation of the cyclic dinucleotide messenger c-di-AMP in the hyperthermophilic archaeon Pyrococcus yayanosii.Protein science : a publication of the Protein Society · 2023Article
- All DACs in a Row: Domain Architectures of Bacterial and Archaeal Diadenylate Cyclases.Journal of bacteriology · 2023Review
- Article
8 more citing papers are in PubMed but not listed here.
Corrections and comments
- Commented on by
Authors and funding
7 authors at 1 institution in 1 country.
Funding
Abstract
Staphylococcus aureus is an important opportunistic human pathogen that is highly resistant to osmotic stresses. To survive an increase in osmolarity, bacteria immediately take up potassium ions and small organic compounds known as compatible solutes. The second messenger cyclic diadenosine monophosphate (c-di-AMP) reduces the ability of bacteria to withstand osmotic stress by binding to and inhibiting several proteins that promote potassium uptake. We identified OpuCA, the adenosine triphosphatase (ATPase) component of an uptake system for the compatible solute carnitine, as a c-di-AMP target protein in S aureus and found that the LAC*ΔgdpP strain of S aureus, which overproduces c-di-AMP, showed reduced carnitine uptake. The paired cystathionine-β-synthase (CBS) domains of OpuCA bound to c-di-AMP, and a crystal structure revealed a putative binding pocket for c-di-AMP in the cleft between the two CBS domains. Thus, c-di-AMP inhibits osmoprotection through multiple mechanisms.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
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.