ArticleNature communications2020
Elucidating the role of metal ions in carbonic anhydrase catalysis.
Article in Nature communications, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 57 papers.
What it found
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Who cites it
57 citing papers in PubMed, 166 citations in OpenAlex.
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- Carbonic anhydrase under the computational lens: a review of advances, challenges, and future directions.Journal of molecular modeling · 2026Review
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- Native mass spectrometry enabled by infrared matrix-assisted laser desorption electrospray ionization for rapid measurement of protein-ligand biophysical parameters.Analytical and bioanalytical chemistry · 2026Article
- Elucidating copper ion interactions with carbonic anhydrase: insights from fluorescence quenching and thermodynamic analysis.Photosynthetica · 2026Article
- Substitution of ZnACS omega · 2025Article
- Structural characterization and inhibition of carbonic anhydrase fromJournal of structural biology: X · 2025Article
- Metallo-coiled Coil Stabilization via Chemical Cross-Linking: Implications for Gd(III)-Based MRI Contrast Agents.Journal of the American Chemical Society · 2025Article
- Targeting metalloptosis in tumor therapy: from molecular mechanisms to application of metal nanoparticles.Molecular cancer · 2025Review
- Supramolecular networks with high shear stiffening enabled by metal ion-mediated hydrogen bonding enhancement strategy.Nature communications · 2025Article
- Phenylalanine-Based DNA-Encoded Chemical Libraries for the Discovery of Potent and Selective Small Organic Ligands Against Markers of Cancer and Immune Cells.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025Article
- Coordination Geometry Tuning in a Single-Atom Nanozyme to Mimic Metalloenzymes with Nonplanar Active Site.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025Article
- Assembled peptoid crystalline nanomaterials as carbonic anhydrase mimics for promoted hydration and sequestration of CONature communications · 2025Article
- Conformational flexibility of His200 enables catalytic activity in the T200H mutant of carbonic anhydrase II.Molecules and cells · 2025Article
Corrections and comments
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Authors and funding
8 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Why metalloenzymes often show dramatic changes in their catalytic activity when subjected to chemically similar but non-native metal substitutions is a long-standing puzzle. Here, we report on the catalytic roles of metal ions in a model metalloenzyme system, human carbonic anhydrase II (CA II). Through a comparative study on the intermediate states of the zinc-bound native CA II and non-native metal-substituted CA IIs, we demonstrate that the characteristic metal ion coordination geometries (tetrahedral for Zn
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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.