ArticleNature2012
Structural basis for iron piracy by pathogenic Neisseria.
Article in Nature, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 140 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.
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Who cites it
140 citing papers in PubMed, 265 citations in OpenAlex.
- Emergence of short-lived meningococci causing focal epidemics can be associated with gene transfer from carriage-associatedbioRxiv : the preprint server for biology · 2026Article
- Urate as a COAntioxidants (Basel, Switzerland) · 2026Article
- Structural insights into the mechanism underpinning iron piracy in pathogenicScience advances · 2026Article
- A new family of TonB-dependent copper transporters linked to respiratory oxidase function.The Journal of biological chemistry · 2026Article
- Structural insights into zinc piracy by Neisseria gonorrhoeae to overcome nutritional immunity.Structure (London, England : 1993) · 2026Article
- Unraveling the binding mechanism of olanzapine with human serum transferrin: a multispectroscopic and computational investigation.Molecular diversity · 2026Article
- Unveiling the Bio-Interface via Spectroscopic and Computational Studies of (Propyl-3-ol/butyl-4-ol)triphenyltin(IV) Compound Binding to Human Serum Transferrin.Materials (Basel, Switzerland) · 2026Article
- Porphyrin pathways as targets for combating antimicrobial resistance: virulence and therapeutic opportunities.Frontiers in cellular and infection microbiology · 2026Review
- Review
- Exploring the binding of cinchonine with human transferrin: combined experimental and computational approaches.Scientific reports · 2025Article
- Structural insights into outer membrane protein biogenesis in pathogenic Neisseria.Structure (London, England : 1993) · 2025Article
- Iron Metabolism Disorders Associated With the Severity of Pyogenic Liver Abscess.Food science & nutrition · 2025Article
- Structure of a distinct β-barrel assembly machinery complex in the Bacteroidota.Nature microbiology · 2025Article
- Surface protein machineries in Gram-negative bacteria.Journal of cell science · 2025Review
- Iron-depleting nutritional immunity controls extracellular bacterial replication in Legionella pneumophila infections.Nature communications · 2024Article
- Prevalence of Slam-dependent hemophilins in Gram-negative bacteria.Journal of bacteriology · 2024Article
- Tag-free protein modification by lipoate ligase A: exploring substrate tolerance.Analytical sciences : the international journal of the Japan Society for Analytical Chemistry · 2024Article
- Implication of Caffeic Acid for the Prevention and Treatment of Alzheimer's Disease: Understanding the Binding with Human Transferrin Using In Silico and In Vitro Approaches.Molecular neurobiology · 2024Article
- Lactoferrins in Their Interactions with Molecular Targets: A Structure-Based Overview.Pharmaceuticals (Basel, Switzerland) · 2024Review
- Comprehensive spectroscopic and computational insight into the binding of vanillin with human transferrin: targeting neuroinflammation in Alzheimer's disease therapeutics.Frontiers in pharmacology · 2024Article
80 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
15 authors at 7 institutions in 2 countries.
Funding
Abstract
Neisseria are obligate human pathogens causing bacterial meningitis, septicaemia and gonorrhoea. Neisseria require iron for survival and can extract it directly from human transferrin for transport across the outer membrane. The transport system consists of TbpA, an integral outer membrane protein, and TbpB, a co-receptor attached to the cell surface; both proteins are potentially important vaccine and therapeutic targets. Two key questions driving Neisseria research are how human transferrin is specifically targeted, and how the bacteria liberate iron from transferrin at neutral pH. To address these questions, we solved crystal structures of the TbpA-transferrin complex and of the corresponding co-receptor TbpB. We characterized the TbpB-transferrin complex by small-angle X-ray scattering and the TbpA-TbpB-transferrin complex by electron microscopy. Our studies provide a rational basis for the specificity of TbpA for human transferrin, show how TbpA promotes iron release from transferrin, and elucidate how TbpB facilitates this process.
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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.