ArticleScientific reports2020
A disulfide constrains the ToxR periplasmic domain structure, altering its interactions with ToxS and bile-salts.
Article in Scientific reports, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 9 papers.
What it found
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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
9 citing papers in PubMed, 15 citations in OpenAlex.
- Bile-mediated ToxS homodimerization provides a model for ToxRS periplasmic interactions.bioRxiv : the preprint server for biology · 2026Article
- RND-mediated efflux couples antimicrobial resistance and hypervirulence in contemporary Vibrio cholerae.PLoS pathogens · 2026Article
- Article
- Article
- ToxR activates theProceedings of the National Academy of Sciences of the United States of America · 2023Article
- Structural Insights into Regulation of Vibrio Virulence Gene Networks.Advances in experimental medicine and biology · 2023Article
- Co-component signal transduction systems: Fast-evolving virulence regulation cassettes discovered in enteric bacteria.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- PsaF Is a Membrane-Localized pH Sensor That RegulatesJournal of bacteriology · 2021Article
- The periplasmic domains of Vibriocholerae ToxR and ToxS are forming a strong heterodimeric complex independent on the redox state of ToxR cysteines.Molecular microbiology · 2021Article
Corrections and comments
- Erratum issued
Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
ToxR is a transmembrane transcription factor that, together with its integral membrane periplasmic binding partner ToxS, is conserved across the Vibrionaceae family. In some pathogenic Vibrios, including V. parahaemolyticus and V. cholerae, ToxR is required for bile resistance and virulence, and ToxR is fully activated and protected from degradation by ToxS. ToxS achieves this in part by ensuring formation of an intra-chain disulfide bond in the C-terminal periplasmic domain of ToxR (dbToxRp). In this study, biochemical analysis showed dbToxRp to have a higher affinity for the ToxS periplasmic domain than the non-disulfide bonded conformation. Analysis of our dbToxRp crystal structure showed this is due to disulfide bond stabilization. Furthermore, dbToxRp is structurally homologous to the V. parahaemolyticus VtrA periplasmic domain. These results highlight the critical structural role of disulfide bond in ToxR and along with VtrA define a domain fold involved in environmental sensing conserved across the Vibrionaceae family.
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.