ArticleThe Journal of biological chemistry2012
Structural characterization of human cytochrome P450 2C19: active site differences between P450s 2C8, 2C9, and 2C19.
Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 47 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
47 citing papers in PubMed, 133 citations in OpenAlex.
- Metabolic Stability of Fluorinated Small Molecules: A Physical Organic Chemistry Perspective.Journal of medicinal chemistry · 2026Review
- Binding Site Vectors Enable Mapping of Cytochrome P450 Functional Landscapes.Journal of chemical information and modeling · 2026Article
- Design and Development of Sulfonamide-Chalcones as Antiepileptic Candidates: Computational and Zebrafish-Based Validation Approaches.ACS omega · 2025Article
- Review
- Proof of principle concept for the analysis and functional prediction of rare genetic variants in the CYP2C19 and CYP2D6 genes.Human genomics · 2025Article
- Decoding the selective chemical modulation of CYP3A4.Nature communications · 2025Article
- Investigating the potential mechanism of bisphenols on neurodegeneration through network toxicology and molecular docking.NAM journal · 2025Article
- Article
- Investigation ofComputational and structural biotechnology journal · 2024Review
- Deep mutational scanning of CYP2C19 in human cells reveals a substrate specificity-abundance tradeoff.Genetics · 2024Article
- Computational Binding Study Hints at Ecdysone 20-Mono-Oxygenase as the Hitherto Unknown Target for Ring C-Seco Limonoid-Type Insecticides.Molecules (Basel, Switzerland) · 2024Article
- Melatonin Activation by Human Cytochrome P450 Enzymes: A Comparison between Different Isozymes.Molecules (Basel, Switzerland) · 2023Article
- The Effect of Plastic-Related Compounds on Transcriptome-Wide Gene Expression on CYP2C19-Overexpressing HepG2 Cells.Molecules (Basel, Switzerland) · 2023Article
- A Robust Machine Learning Framework Built Upon Molecular Representations Predicts CYP450 Inhibition: Toward Precision in Drug Repurposing.Omics : a journal of integrative biology · 2023Article
- Article
- ComprehensiveFrontiers in pharmacology · 2023Article
- Methyl Effect on the Metabolism, Chemical Stability, and Permeability Profile of BioactiveACS omega · 2022Article
- Assessment of the Effects of Triticonazole on Soil and Human Health.Molecules (Basel, Switzerland) · 2022Article
- In Silico Design and SAR Study of Dibenzyl Trisulfide Analogues for Improved CYP1A1 Inhibition.ChemistryOpen · 2022Article
- CYP2C9 and 3A4 play opposing roles in bioactivation and detoxification of diphenylamine NSAIDs.Biochemical pharmacology · 2021Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
To identify the structural features underlying the distinct substrate and inhibitor profiles of P450 2C19 relative to the closely related human enzymes, P450s 2C8 and 2C9, the atomic structure (Protein Data Bank code 4GQS) of cytochrome P450 2C19 complexed with the inhibitor (2-methyl-1-benzofuran-3-yl)-(4-hydroxy-3,5-dimethylphenyl)methanone (Protein Data Bank chemical component 0XV) was determined to 2.87 Å resolution by x-ray crystallography. The conformation of the peptide backbone of P450 2C19 is most similar to that of P450 2C8, but the substrate-binding cavity of P450 2C8 is much larger than that of P450 2C19 due to differences in the amino acid residues that form the substrate-binding cavities of the two enzymes. In contrast, the substrate-binding cavity of P450 2C19 is much more similar in size to that of the structure of the P450 2C9 flurbiprofen complex than to that of a modified P450 2C9 or that of P450 2C8. The cavities of the P450 2C19 0XV complex and the P450 2C9 flurbiprofen complex differ, however, because the helix B-C loops of the two enzymes are dissimilar. These conformational differences reflect the effects of adjacent structural elements that interact with the B-C loops and that differ between the two enzymes. The availability of a structure for 2C19 will facilitate computational approaches for predictions of substrate and inhibitor binding to this enzyme.
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.