ArticleFrontiers in pharmacology2012
Heme cytotoxicity and the pathogenesis of immune-mediated inflammatory diseases.
Article in Frontiers in pharmacology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 65 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
65 citing papers in PubMed, 107 citations in OpenAlex.
- Conjugates of Heme and Intrinsically Disordered Peptides toward the Development of Synthetic Artificial Oxygen Carriers.Bioconjugate chemistry · 2026Article
- Review
- Cryo-EM provides insight into how thebioRxiv : the preprint server for biology · 2026Article
- Secreted phospholipase PLA2G5 acts as a hemolytic factor in sepsis.The Journal of clinical investigation · 2026Article
- Microbiota-Driven Metabolic Alterations Induced by BPA, TDCPP and PFOA in an Ex Vivo Human Fecal Fermentation Model.Chemical research in toxicology · 2026Article
- The mechanisms by which free heme exacerbates sepsis and the potential therapeutic targets.Frontiers in immunology · 2026Review
- One trigger, two fates: hemolysate shapes neutrophil extracellular traps (NETs) formation in a context-dependent manner.Frontiers in immunology · 2026Article
- Dual-Function Role of Phenolated Albumin in Hemin-Mediated Hydrogel Formation.Gels (Basel, Switzerland) · 2025Article
- Molecular Mechanisms of Iron Metabolism and Overload.Biomedicines · 2025Review
- Fresh autologous blood transfusion reverses erythrocyte damage by reducing oxidative stress via promoting mitochondrial metabolism and M2 macrophage polarization.Archives of medical science : AMS · 2025Article
- Targeting HMGB1 in endothelial cells reverses heme-induced SIRS after radiofrequency ablation of hepatic hemangioma.Frontiers in immunology · 2025Article
- Examining Hemin and its Derivatives: Induction of Heme-Oxygenase-1 Activity and Oxidative Stress in Breast Cancer Cells through Collaborative Experimental Analysis and Molecular Dynamics Simulations.Journal of medicinal chemistry · 2024Article
- Heme (dys)homeostasis and liver disease.Frontiers in physiology · 2024Review
- Free heme and hemopexin in acute kidney injury after cardiopulmonary bypass and transient renal ischemia.Clinical and translational science · 2023Article
- Article
- Proteomic analysis of the effect of hemin in breast cancer.Scientific reports · 2023Article
- Heme Interactions as Regulators of the Alternative Pathway Complement Responses and Implications for Heme-Associated Pathologies.Current issues in molecular biology · 2023Review
- Heme: The Lord of the Iron Ring.Antioxidants (Basel, Switzerland) · 2023Review
- Heme Scavenging and Delivery: The Role of Human Serum Albumin.Biomolecules · 2023Review
- Oxidized hemoglobin triggers polyreactivity and autoreactivity of human IgG via transfer of heme.Communications biology · 2023Article
5 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
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Heme, iron (Fe) protoporphyrin IX, functions as a prosthetic group in a range of hemoproteins essential to support life under aerobic conditions. The Fe contained within the prosthetic heme groups of these hemoproteins can catalyze the production of reactive oxygen species. Presumably for this reason, heme must be sequestered within those hemoproteins, thereby shielding the reactivity of its Fe-heme. However, under pathologic conditions associated with oxidative stress, some hemoproteins can release their prosthetic heme groups. While this heme is not necessarily damaging per se, it becomes highly cytotoxic in the presence of a range of inflammatory mediators such as tumor necrosis factor. This can lead to tissue damage and, as such, exacerbate the pathologic outcome of several immune-mediated inflammatory conditions. Presumably, targeting "free heme" may be used as a therapeutic intervention against these diseases.
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.