ArticleMetallomics : integrated biometal science2017
Human calprotectin affects the redox speciation of iron.
Article in Metallomics : integrated biometal science, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 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
24 citing papers in PubMed, 30 citations in OpenAlex.
- The Abundance Paradox of S100A8/A9 in Neutrophils: Functional Logic of Calprotectin Dominance in the Cytosolic Proteome.International journal of molecular sciences · 2026Review
- Exploring Metalloproteome Remodeling in Calprotectin-StressedACS chemical biology · 2025Article
- Article
- Exploring metalloproteome remodeling in calprotectin-stressedbioRxiv : the preprint server for biology · 2025Article
- Targeting bacterial nickel transport with aspergillomarasmine A suppresses virulence-associated Ni-dependent enzymes.Nature communications · 2024Article
- Spectroscopic and computational investigations of Cobalt(II) binding to the innate immune protein human calprotectin.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2024Article
- Post-translational modifications on the metal-sequestering protein calprotectin.Biometals : an international journal on the role of metal ions in biology, biochemistry, and medicine · 2023Review
- Key players in the regulation of iron homeostasis at the host-pathogen interface.Frontiers in immunology · 2023Review
- Metal sequestration by S100 proteins in chemically diverse environments.Trends in microbiology · 2022Review
- Review
- Bacterial Responses to Iron Withholding by Calprotectin.Biochemistry · 2021Review
- Article
- Emerging role of ferrous iron in bacterial growth and host-pathogen interaction: New tools for chemical (micro)biology and antibacterial therapy.Current opinion in chemical biology · 2021Review
- Iron Acquisition by Bacterial Pathogens: Beyond Tris-Catecholate Complexes.Chembiochem : a European journal of chemical biology · 2020Review
- Metal Sequestration and Antimicrobial Activity of Human Calprotectin Are pH-Dependent.Biochemistry · 2020Article
- Multi-metal nutrient restriction and crosstalk in metallostasis systems in microbial pathogens.Current opinion in microbiology · 2020Review
- Exploring Iron Withholding by the Innate Immune Protein Human Calprotectin.Accounts of chemical research · 2019Article
- An efficient, step-economical strategy for the design of functional metalloproteins.Nature chemistry · 2019Article
- The human innate immune protein calprotectin induces iron starvation responses inThe Journal of biological chemistry · 2019Article
- Preparation and Iron Redox Speciation Study of the Fe(II)-Binding Antimicrobial Protein Calprotectin.Methods in molecular biology (Clifton, N.J.) · 2019Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
We report that the metal-sequestering human host-defense protein calprotectin (CP, S100A8/S100A9 oligomer) affects the redox speciation of iron (Fe) in bacterial growth media and buffered aqueous solution. Under aerobic conditions and in the absence of an exogenous reducing agent, CP-Ser (S100A8(C42S)/S100A9(C3S) oligomer) depletes Fe from three different bacterial growth media preparations over a 48 h timeframe (T = 30 °C). The presence of the reducing agent β-mercaptoethanol accelerates this process and allows CP-Ser to deplete Fe over a ≈1 h timeframe. Fe-depletion assays performed with metal-binding-site variants of CP-Ser show that the hexahistidine (His
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.