ReviewBiology of metals1991
Transport of iron across the outer membrane.
Review in Biology of metals, 1991. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 53 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.
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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
53 citing papers in PubMed, 124 citations in OpenAlex.
- Fungal siderophore metabolism with a focus on Aspergillus fumigatus: impact on biotic interactions and potential translational applications.Essays in biochemistry · 2023Article
- Broad and Efficient Control of Klebsiella Pathogens by Peptidoglycan-Degrading and Pore-Forming Bacteriocins Klebicins.Scientific reports · 2019Article
- OmpR-Mediated Transcriptional Regulation and Function of Two Heme Receptor Proteins ofFrontiers in cellular and infection microbiology · 2018Article
- A Natural ChimericmBio · 2017Article
- Pangenome and immuno-proteomics analysis of Acinetobacter baumannii strains revealed the core peptide vaccine targets.BMC genomics · 2016Article
- Multiplicity and specificity of siderophore uptake in the cyanobacterium Anabaena sp. PCC 7120.Plant molecular biology · 2016Article
- Novel colicin Fy of Yersinia frederiksenii inhibits pathogenic Yersinia strains via YiuR-mediated reception, TonB import, and cell membrane pore formation.Journal of bacteriology · 2012Article
- Staphylococcus lugdunensis IsdG liberates iron from host heme.Journal of bacteriology · 2011Article
- Legionella pneumophila LbtU acts as a novel, TonB-independent receptor for the legiobactin siderophore.Journal of bacteriology · 2011Article
- Complete genome and comparative analysis of the chemolithoautotrophic bacterium Oligotropha carboxidovorans OM5.BMC genomics · 2010Article
- Heme uptake across the outer membrane as revealed by crystal structures of the receptor-hemophore complex.Proceedings of the National Academy of Sciences of the United States of America · 2009Article
- Staphylococcus aureus haem oxygenases are differentially regulated by iron and haem.Molecular microbiology · 2008Article
- Deletion and substitution analysis of the Escherichia coli TonB Q160 region.Journal of bacteriology · 2007Article
- Cloning, sequencing, and characterization of the Azospirillum brasilense fhuE gene.Current microbiology · 2006Article
- Role of the regulatory gene rirA in the transcriptional response of Sinorhizobium meliloti to iron limitation.Applied and environmental microbiology · 2005Article
- Recognition of ferric catecholates by FepA.Journal of bacteriology · 2004Article
- The iron- and temperature-regulated cjrBC genes of Shigella and enteroinvasive Escherichia coli strains code for colicin Js uptake.Journal of bacteriology · 2001Article
- Antigenic and sequence diversity in gonococcal transferrin-binding protein A.Infection and immunity · 2000Article
- Identification by genetic suppression of Escherichia coli TolB residues important for TolB-Pal interaction.Journal of bacteriology · 2000Article
- Role of ornibactin biosynthesis in the virulence of Burkholderia cepacia: characterization of pvdA, the gene encoding L-ornithine N(5)-oxygenase.Infection and immunity · 1999Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The TonB protein is involved in energ-coupled receptor-dependent transport processes across the outer membrane. The TonB protein is anchored in the cytoplasmic membrane but exposed to the periplasmic space. To fulfill its function, it has to couple the energy-providing metabolism in the cytoplasmic membrane with regulation of outer membrane receptor activity. Ferrichrome and albomycin transport, uptake of colicin M, and infection by the phages T1 and phi 80 occur via the same receptor, the FhuA protein in the outer membrane. Therefore, this receptor is particularly suitable for the study of energy-coupled TonB-dependent transport across the outer membrane. Ferrichrome, albomycin and colicin M bind to the FhuA receptor but are not released into the periplasmic space of unenergized cells, or tonB mutants. In vivo interaction between FhuA and TonB is suggested by the restoration of activity of inactive FhuA proteins, bearing amino acid replacements in the TonB box, by TonB derivatives with single amino acid substitutions. Point mutations in the fhuA gene are suppressed by point mutations in the tonB gene. In addition, naturally occurring degradation of the TonB protein and its derivatives is preferentially prevented in vivo by FhuA and FhuA derivatives where functional interaction takes place. It is proposed that in the energized state, TonB induces a conformation in FhuA which leads to the release of the FhuA-bound compounds into the periplasmic space. Activation of FhuA by TonB depends on the ExbBD proteins in the cytoplasmic membrane. They can be partially replaced by the TolQR proteins which show strong sequence similarity to the ExbBD proteins.(ABSTRACT TRUNCATED AT 250 WORDS)
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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.