ReviewBioMed research international2015
Probing the surface of human carbonic anhydrase for clues towards the design of isoform specific inhibitors.
Review in BioMed research international, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 48 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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
48 citing papers in PubMed, 120 citations in OpenAlex.
- Investigation onPharmaceuticals (Basel, Switzerland) · 2026Article
- Real-Time Binding Kinetics of Small Molecules to CA IX in Live Suspension Cells Using SPR Microscopy.ACS medicinal chemistry letters · 2026Article
- Introduction to Carbonic Anhydrase.Sub-cellular biochemistry · 2026Review
- Off-target binding of the histone deacetylase inhibitor vorinostat to carbonic anhydrase II and IX.Acta crystallographica. Section F, Structural biology communications · 2025Article
- "Several birds with one stone": exploring the potential of AI methods for multi-target drug design.Molecular diversity · 2025Article
- Conformational flexibility of His200 enables catalytic activity in the T200H mutant of carbonic anhydrase II.Molecules and cells · 2025Article
- Repositioning FDA-Approved Sulfonamide-Based Drugs as Potential Carbonic Anhydrase Inhibitors inPharmaceuticals (Basel, Switzerland) · 2025Article
- New benzimidazole derivatives containing hydrazone group as anticancer agents: Inhibition of carbonic anhydrase IX and molecular docking studies.Archiv der Pharmazie · 2025Article
- A series of benzensulfonamide derivatives as new potent carbonic anhydrase IX and XII inhibitors.Future medicinal chemistry · 2025Article
- Machine-Learning-Based Data Analysis Method for Cell-Based Selection of DNA-Encoded Libraries.ACS omega · 2023Article
- MM/GBSA prediction of relative binding affinities of carbonic anhydrase inhibitors: effect of atomic charges and comparison with Autodock4Journal of computer-aided molecular design · 2023Article
- Novel Thiopyrano[2,3-ACS omega · 2023Article
- New Insights into Conformationally Restricted Carbonic Anhydrase Inhibitors.Molecules (Basel, Switzerland) · 2023Article
- Mitochondrial carbonic anhydrase VA and VB: properties and roles in health and disease.The Journal of physiology · 2023Review
- Anti-PD-L1 therapy altered inflammation but not survival in a lethal murine hepatitis virus-1 pneumonia model.Frontiers in immunology · 2023Article
- Targeting carbonic anhydrase IX and XII isoforms with small molecule inhibitors and monoclonal antibodies.Journal of enzyme inhibition and medicinal chemistry · 2022Review
- Beta and Gamma Amino Acid-Substituted Benzenesulfonamides as Inhibitors of Human Carbonic Anhydrases.Pharmaceuticals (Basel, Switzerland) · 2022Article
- Carbonic anhydrase activation profile of indole-based derivatives.Journal of enzyme inhibition and medicinal chemistry · 2021Article
- Article
- Design, Synthesis, Biological Evaluation, and Computational Studies of Novel Tri-Aryl Imidazole-Benzene Sulfonamide Hybrids as Promising Selective Carbonic Anhydrase IX and XII Inhibitors.Molecules (Basel, Switzerland) · 2021Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
The alpha carbonic anhydrases (α-CAs) are a group of structurally related zinc metalloenzymes that catalyze the reversible hydration of CO2 to HCO3(-). Humans have 15 different α-CAs with numerous physiological roles and expression patterns. Of these, 12 are catalytically active, and abnormal expression and activities are linked with various diseases, including glaucoma and cancer. Hence there is a need for CA isoform specific inhibitors to avoid off-target CA inhibition, but due to the high amino acid conservation of the active site and surrounding regions between each enzyme, this has proven difficult. However, residues towards the exit of the active site are variable and can be exploited to design isoform selective inhibitors. Here we discuss and characterize this region of "selective drug targetability" and how these observations can be utilized to develop isoform selective CA inhibitors.
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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.