ArticleJournal of the Royal Society, Interface2013
Structural insights into human heme oxygenase-1 inhibition by potent and selective azole-based compounds.
Article in Journal of the Royal Society, Interface, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers, 1 of them a synthesis that pooled it.
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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
18 citing papers in PubMed, 1 synthesis or guideline pooled it, 41 citations in OpenAlex.
- The Impairment in Kidney Function in the Oral Anticoagulation Era. A Pathophysiological Insight.Cardiovascular drugs and therapy · 2021Pooled it
- Article
- Thai rice instant granules containing turmeric extract andFrontiers in toxicology · 2025Article
- A Potential Role of Keratinocyte-Derived Bilirubin in Human Skin Yellowness and Its Amelioration by Sucrose Laurate/Dilaurate.International journal of molecular sciences · 2022Article
- Heme Oxygenase Modulation Drives Ferroptosis in TNBC Cells.International journal of molecular sciences · 2022Article
- Novel Tyrosine Kinase Inhibitors to Target Chronic Myeloid Leukemia.Molecules (Basel, Switzerland) · 2022Article
- Non-canonical vs. Canonical Functions of Heme Oxygenase-1 in Cancer.Journal of cancer prevention · 2022Review
- Discovery of Novel Acetamide-Based Heme Oxygenase-1 Inhibitors with PotentJournal of medicinal chemistry · 2021Article
- Heme Oxygenase-1 Signaling and Redox Homeostasis in Physiopathological Conditions.Biomolecules · 2021Review
- New Arylethanolimidazole Derivatives as HO-1 Inhibitors with Cytotoxicity against MCF-7 Breast Cancer Cells.International journal of molecular sciences · 2020Article
- Recent Advances in the Understanding of the Reaction Chemistries of the Heme Catabolizing Enzymes HO and BVR Based on High Resolution Protein Structures.Current medicinal chemistry · 2020Review
- Fourfold Filtered Statistical/Computational Approach for the Identification of Imidazole Compounds as HO-1 Inhibitors from Natural Products.Marine drugs · 2019Article
- Regulatory role of heme oxygenase-1 in silica-induced lung injury.Respiratory research · 2018Article
- Novel Structural Insight into Inhibitors of Heme Oxygenase-1 (HO-1) by New Imidazole-Based Compounds: Biochemical and In Vitro Anticancer Activity Evaluation.Molecules (Basel, Switzerland) · 2018Article
- Identification of danthron as an isoform-specific inhibitor of HEME OXYGENASE-1/cytochrome P450 reductase interaction with anti-tumor activity.Journal of biomedical science · 2018Article
- Targeting heme oxygenase-1 and carbon monoxide for therapeutic modulation of inflammation.Translational research : the journal of laboratory and clinical medicine · 2016Review
- A review on hemeoxygenase-2: focus on cellular protection and oxygen response.Oxidative medicine and cellular longevity · 2014Review
- Drug-enhanced carbon monoxide production from heme by cytochrome P450 reductase.Medical gas researchArticle
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
6 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The development of heme oxygenase (HO) inhibitors, especially those that are isozyme-selective, promises powerful pharmacological tools to elucidate the regulatory characteristics of the HO system. It is already known that HO has cytoprotective properties and may play a role in several disease states, making it an enticing therapeutic target. Traditionally, the metalloporphyrins have been used as competitive HO inhibitors owing to their structural similarity with the substrate, heme. However, given heme's important role in several other proteins (e.g. cytochromes P450, nitric oxide synthase), non-selectivity is an unfortunate side-effect. Reports that azalanstat and other non-porphyrin molecules inhibited HO led to a multi-faceted effort to develop novel compounds as potent, selective inhibitors of HO. This resulted in the creation of non-competitive inhibitors with selectivity for HO, including a subset with isozyme selectivity for HO-1. Using X-ray crystallography, the structures of several complexes of HO-1 with novel inhibitors have been elucidated, which provided insightful information regarding the salient features required for inhibitor binding. This included the structural basis for non-competitive inhibition, flexibility and adaptability of the inhibitor binding pocket, and multiple, potential interaction subsites, all of which can be exploited in future drug-design strategies.
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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.