ArticleACS catalysis2021
Rigidifying a
Article in ACS catalysis, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 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
15 citing papers in PubMed.
- Modulating thermal folded stability and catalytic activity of aRSC advances · 2026Article
- Less is more: miniaturized heme enzymes with broad reactivity.Chemical science · 2026Review
- Buttressing ligand-binding pockets in de novo designed NTF2-like domains.Protein science : a publication of the Protein Society · 2025Article
- Article
- An Artificial Metal-Free Peroxidase Designed Using a Ferritin Cage for Bioinspired Catalysis.Angewandte Chemie (International ed. in English) · 2025Article
- Recent advances in de novo designed metallopeptides as tailored enzyme mimics.Current opinion in chemical biology · 2025Review
- Molecular Stiffening by Macrocycle Clustering.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
- A Bioengineered Stable Protein 1-Hemin Complex with Enhanced Peroxidase-Like Catalytic Properties.Small science · 2024Article
- Cooperative Conformational Transitions Underpin the Activation Heat Capacity in the Temperature Dependence of Enzyme Catalysis.ACS catalysis · 2024Article
- An expandable, modular de novo protein platform for precision redox engineering.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Glycosylation increases active site rigidity leading to improved enzyme stability and turnover.The FEBS journal · 2023Article
- Selective Oxidation of Halophenols Catalyzed by an Artificial Miniaturized Peroxidase.International journal of molecular sciences · 2023Article
- Oxidative dehalogenation of trichlorophenol catalyzed by a promiscuous artificial heme-enzyme.RSC advances · 2022Article
- A Thermodynamic Model for Interpreting Tryptophan Excitation-Energy-Dependent Fluorescence Spectra Provides Insight Into Protein Conformational Sampling and Stability.Frontiers in molecular biosciences · 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
9 authors.
Funding
Abstract
Conformational sampling profoundly impacts the overall activity and temperature dependence of enzymes. Peroxidases have emerged as versatile platforms for high-value biocatalysis owing to their broad palette of potential biotransformations. Here, we explore the role of conformational sampling in mediating activity in the
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.