ReviewAntioxidants & redox signaling2010
Heme degradation and vascular injury.
Review in Antioxidants & redox signaling, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 138 papers, 1 of them a synthesis that pooled it.
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
138 citing papers in PubMed, 1 synthesis or guideline pooled it, 241 citations in OpenAlex.
- Pooled it
- Haemoglobin mass and running time trial performance after recombinant human erythropoietin administration in trained men.PloS one · 2013Trial
- Review
- Sex determines cardiac and renal Vulnerability to chronic hemoglobin toxicity.Biomedicine & pharmacotherapy = Biomedecine & pharmacotherapie · 2026Article
- Poly(3-hydroxybutyrate)-Based Biomimetic Materials Encapsulated with Amide Derivatives of Chlorin-e6 for Advanced Photodynamic Therapy.Nanomaterials (Basel, Switzerland) · 2026Article
- Apohemoglobin-haptoglobin complex is a therapeutic against vaso-occlusive crisis: scavenging of hemoglobin and heme.Blood advances · 2026Article
- Review
- Loss of energy homeostasis contributes to hepatic damage development in sickle cell disease.Molecular metabolism · 2026Article
- Extracellular heme:DNA complexes promote oxidative stress and inflammation during lupus-associated hemolysis.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Acellular Hemoglobin Impairs Cardiomyocyte Excitation-Contraction Coupling.ASAIO journal (American Society for Artificial Internal Organs : 1992) · 2026Article
- Plasma heme pool compartmentalization is linked to pathophysiology in Sickle Cell Disease.PloS one · 2026Article
- Redox signaling in chronic airway diseases: pathogenic mechanisms and therapeutic implications.Frontiers in physiology · 2026Review
- Synthesis of nanoparticles of cobalt protoporphyrin IX (Co(iii)PPIX NPs). Antiradical, cytotoxicity and antibacterial properties.RSC advances · 2025Article
- Iron: More than Meets the Eye.Nutrients · 2025Review
- Podocyte dysfunction driven by heme in sickle-cell nephropathy.Scientific reports · 2025Article
- Mechanisms of heme transport in the mitochondria.Biochemical Society transactions · 2025Review
- Biomarkers of postoperative cardiac surgery-associated acute kidney injury: Narrowing the field.JTCVS open · 2025Article
- Deciphering the Role of Ferroptosis in the Pathogenesis of Peripheral Artery Disease Myopathy.Biology · 2025Article
- Small-molecule inhibitor screen to identify mechanisms of sickle hemoglobin clearance by liver endothelium.Blood vessels, thrombosis & hemostasis · 2025Article
- Red blood cell extracellular vesicles: new frontiers in hematological biomarker discovery.Frontiers in medicine · 2025Review
78 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
5 authors at 1 institution in 1 country.
Funding
Abstract
Heme is an essential molecule in aerobic organisms. Heme consists of protoporphyrin IX and a ferrous (Fe(2+)) iron atom, which has high affinity for oxygen (O(2)). Hemoglobin, the major oxygen-carrying protein in blood, is the most abundant heme-protein in animals and humans. Hemoglobin consists of four globin subunits (alpha(2)beta(2)), with each subunit carrying a heme group. Ferrous (Fe(2+)) hemoglobin is easily oxidized in circulation to ferric (Fe(3+)) hemoglobin, which readily releases free hemin. Hemin is hydrophobic and intercalates into cell membranes. Hydrogen peroxide can split the heme ring and release "free" redox-active iron, which catalytically amplifies the production of reactive oxygen species. These oxidants can oxidize lipids, proteins, and DNA; activate cell-signaling pathways and oxidant-sensitive, proinflammatory transcription factors; alter protein expression; perturb membrane channels; and induce apoptosis and cell death. Heme-derived oxidants induce recruitment of leukocytes, platelets, and red blood cells to the vessel wall; oxidize low-density lipoproteins; and consume nitric oxide. Heme metabolism, extracellular and intracellular defenses against heme, and cellular cytoprotective adaptations are emphasized. Sickle cell disease, an archetypal example of hemolysis, heme-induced oxidative stress, and cytoprotective adaptation, is reviewed.
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.