ArticleActa crystallographica. Section F, Structural biology and crystallization communications2013
Structure of CT584 from Chlamydia trachomatis refined to 3.05 Å resolution.
Article in Acta crystallographica. Section F, Structural biology and crystallization communications, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 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
10 citing papers in PubMed, 13 citations in OpenAlex.
- The prokaryotic origins of the COMMD protein family involved in eukaryotic membrane trafficking.Nature communications · 2026Article
- ThebioRxiv : the preprint server for biology · 2025Article
- CT584 Is Not a Protective Vaccine Antigen against Respiratory Chlamydial Challenge in Mice.Vaccines · 2024Article
- Evaluation in mice of cell-free produced CT584 as a Chlamydia vaccine antigen.bioRxiv : the preprint server for biology · 2024Article
- Type III Secretion inMicrobiology and molecular biology reviews : MMBR · 2023Review
- Review
- Crystal structure of an inorganic pyrophosphatase from Chlamydia trachomatis D/UW-3/Cx.Acta crystallographica. Section F, Structural biology communications · 2022Article
- Article
- Structural insights into the architecture and membrane interactions of the conserved COMMD proteins.eLife · 2018Article
- A working model for the type III secretion mechanism in Chlamydia.Microbes and infection · 2016Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
6 authors at 2 institutions in 1 country.
Funding
Abstract
Chlamydia trachomatis is a major cause of various diseases, including blinding trachoma and pelvic inflammatory disease, and is the leading reported sexually transmitted bacterial infection worldwide. All pathogenic Chlamydiae spp. utilize a supramolecular syringe, or type III secretion system (T3SS), to inject proteins into their obligate host in order to propagate infection. Here, the structure of CT584, a T3SS-associated protein, that has been refined to a resolution of 3.05 Å is reported. The CT584 structure is a hexamer comprised of a trimer of dimers. The structure shares a high degree of similarity to the recently reported structure of an orthologous protein, Cpn0803, from Chlamydia pneumoniae, which highlights the highly conserved nature of this protein across these chlamydial species, despite different tissue tropism and disease pathology.
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.