ArticleMolecular microbiology2005
Bacterial metal detectors.
Article in Molecular microbiology, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 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
3 citing papers in PubMed.
- Pore Formation by Pore Forming Proteins in Lipid Membranes: Structural Insights Through Cryo-EM.The Journal of membrane biology · 2025Review
- Comparison ofEpigenomes · 2023Article
- The colicin Ia receptor, Cir, is also the translocator for colicin Ia.Molecular microbiology · 2010Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
1 author.
Funding
Abstract
Gram negative bacteria can detect environmental iron using outer membrane transporters (OMTs), and then regulate certain transport genes to take advantage of a readily available iron source. This process begins with an iron complex being bound by an OMT, and results in a signal being sent across the outer membrane, the periplasmic space, and the inner membrane, to a sigma factor that interacts with RNA polymerase and initiates transcription of relevant genes. Many of the interactions contributing to signalling have been observed by genetic and biochemical studies, but structural studies, which potentially show these interactions in molecular detail, have been limited. In this issue, Garcia-Herrero and Vogel describe an NMR structure of the periplasmic domain of an OMT, which had not been seen in previous X-ray crystal structures. This domain transmits the 'iron availability' signal to the next protein in the signal transduction cascade, which sits in the inner membrane and extends into the periplasm. The new structure extends our knowledge of transporter architecture and suggests how signalling may occur across the outer membrane.
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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.