ArticleMolecules (Basel, Switzerland)2019
Mechanism of Action of Non-Synonymous Single Nucleotide Variations Associated with
Article in Molecules (Basel, Switzerland), 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 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
16 citing papers in PubMed, 24 citations in OpenAlex.
- Engineering of a Carbonic Anhydrase fromInternational journal of molecular sciences · 2026Article
- Rational engineering of a highly active and resilient α-carbonic anhydrase from the hydrothermal vent species Persephonella hydrogeniphila.The FEBS journal · 2025Article
- Alpha Carbonic Anhydrase fromInternational journal of molecular sciences · 2024Article
- Deciphering Isoniazid Drug Resistance Mechanisms on DimericACS omega · 2022Article
- Dissecting mutational allosteric effects in alkaline phosphatases associated with different Hypophosphatasia phenotypes: An integrative computational investigation.PLoS computational biology · 2022Article
- Slipknot or Crystallographic Error: A Computational Analysis of theInternational journal of molecular sciences · 2022Article
- Exploring the dynamic mechanism of allosteric drug SHP099 inhibiting SHP2Molecular diversity · 2021Article
- In Silico Investigation of Potential Applications of Gamma Carbonic Anhydrases as Catalysts of COInternational journal of molecular sciences · 2021Article
- Novel dynamic residue network analysis approaches to study allosteric modulation: SARS-CoV-2 MComputational and structural biotechnology journal · 2021Article
- MDM-TASK-web: MD-TASK and MODE-TASK web server for analyzing protein dynamics.Computational and structural biotechnology journal · 2021Article
- Allosteric pockets and dynamic residue network hubs of falcipain 2 in mutations including those linked to artemisinin resistance.Computational and structural biotechnology journal · 2021Article
- Alpha-Carbonic Anhydrases from Hydrothermal Vent Sources as Potential Carbon Dioxide Sequestration Agents:International journal of molecular sciences · 2020Article
- Computational SNP Analysis and Molecular Simulation Revealed the Most Deleterious Missense Variants in the NBD1 Domain of Human ABCA1 Transporter.International journal of molecular sciences · 2020Article
- Structural Characterization of Carbonic Anhydrase VIII and Effects of Missense Single Nucleotide Variations to Protein Structure and Function.International journal of molecular sciences · 2020Article
- Understanding the Pyrimethamine Drug Resistance Mechanism via Combined Molecular Dynamics and Dynamic Residue Network Analysis.Molecules (Basel, Switzerland) · 2020Article
- Integrated Computational Approaches and Tools forAllosteric Drug Discovery.International journal of molecular sciences · 2020Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors at 1 institution in 2 countries.
Funding
Abstract
Human carbonic anhydrase II (CA-II) is a Zinc (Zn 2 + ) metalloenzyme responsible for maintenance of acid-base balance within the body through the reversible hydration of CO 2 to produce protons (H + ) and bicarbonate (BCT). Due to its importance, alterations to the amino acid sequence of the protein as a result of single nucleotide variations (nsSNVs) have detrimental effects on homeostasis. Six pathogenic CA-II nsSNVs, K18E, K18Q, H107Y, P236H, P236R and N252D were identified, and variant protein models calculated using homology modeling. The effect of each nsSNV was analyzed using motif analysis, molecular dynamics (MD) simulations, principal component (PCA) and dynamic residue network (DRN) analysis. Motif analysis identified 11 functionally important motifs in CA-II. RMSD data indicated subtle SNV effects, while PCA analysis revealed that the presence of BCT results in greater conformational sampling and free energy in proteins. DRN analysis showed variant allosteric effects, and the average
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.