ReviewNature chemistry2010
Designing artificial enzymes by intuition and computation.
Review in Nature chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 79 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
79 citing papers in PubMed.
- A magic methyl effect in the active site of a methyltransferase ribozyme.Nature communications · 2026Article
- Moving Beyond Fenton-Based Peroxidase Nanozymes for Analytical Sensing: Perspectives on Nonradical Alternatives from Heterogeneous Catalysis.Analytical chemistry · 2026Review
- Simulation-guided design of peptide-metal coordination interfaces for next-generation metallo-immunotherapy.Nano convergence · 2026Review
- Structure-activity relationships in catalytic amyloids.Journal of inorganic biochemistry · 2026Article
- Exploring the Blueprint of Life: The Innovation in Antibody and Protein Design.Combinatorial chemistry & high throughput screening · 2026Article
- Facile Gram-Scale Production of Cu/CuACS applied materials & interfaces · 2025Article
- An Artificial Metal-Free Peroxidase Designed Using a Ferritin Cage for Bioinspired Catalysis.Angewandte Chemie (International ed. in English) · 2025Article
- De novo design of porphyrin-containing proteins as efficient and stereoselective catalysts.Science (New York, N.Y.) · 2025Article
- Introducing molecular imprinting onto nanozymes: toward selective catalytic analysis.Analytical and bioanalytical chemistry · 2024Review
- Non-Aufbau electronic structure in radical enzymes and control of the highly reactive intermediates.Chemical science · 2024Article
- Co(II) Substitution Enhances the Esterase Activity of a de Novo Designed Zn(II) Carbonic Anhydrase.Chemistry (Weinheim an der Bergstrasse, Germany) · 2024Article
- Targeted Mutation of a Non-catalytic Gating Residue Increases the Rate ofJournal of agricultural and food chemistry · 2023Article
- Structural Analysis of Non-native Peptide-Based Catalysts Using 2D NMR-Guided MD Simulations.The journal of physical chemistry. A · 2023Article
- Incorporation of a molybdenum atom in a Rubredoxin-type Centre of a de novo-designed αJournal of inorganic biochemistry · 2023Article
- Protein Design: From the Aspect of Water Solubility and Stability.Chemical reviews · 2022Review
- Catalysis and Electron Transfer inChemical reviews · 2022Review
- Integration of Adenylate Kinase 1 with Its Peptide Conformational Imprint.International journal of molecular sciences · 2022Article
- Synthesis of Tetrapeptides Containing Dehydroalanine, Dehydrophenylalanine and Oxazole as Building Blocks for Construction of Foldamers and Bioinspired Catalysts.Molecules (Basel, Switzerland) · 2022Article
- A bound iron porphyrin is redox active in hybrid bacterial reaction centers modified to possess a four-helix bundle domain.Photochemical & photobiological sciences : Official journal of the European Photochemistry Association and the European Society for Photobiology · 2022Article
- Engineered Repeat Protein Hybrids: The New Horizon for Biologic Medicines and Diagnostic Tools.Accounts of chemical research · 2021Article
19 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
2 authors.
Funding
Abstract
The rational design of artificial enzymes, either by applying physico-chemical intuition of protein structure and function or with the aid of computational methods, is a promising area of research with the potential to tremendously impact medicine, industrial chemistry and energy production. Designed proteins also provide a powerful platform for dissecting enzyme mechanisms of natural systems. Artificial enzymes have come a long way from simple α-helical peptide catalysts to proteins that facilitate multistep chemical reactions designed by state-of-the-art computational methods. Looking forward, we examine strategies employed by natural enzymes that could be used to improve the speed and selectivity of artificial catalysts.
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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.