ArticleNature communications2017
Construction and in vivo assembly of a catalytically proficient and hyperthermostable de novo enzyme.
Article in Nature communications, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 44 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
44 citing papers in PubMed, 113 citations in OpenAlex.
- Modulating thermal folded stability and catalytic activity of aRSC advances · 2026Article
- Artificial metalloenzymes in complex biological environments.Nature chemical biology · 2026Review
- Less is more: miniaturized heme enzymes with broad reactivity.Chemical science · 2026Review
- Computational redesign and directed evolution of a lanthanide-dependent photoredox enzyme for enantioselective diol cleavage.Chemical science · 2026Article
- Unlocking Enzyme Discovery: Leveraging Multi-Omics, Machine Learning, and De Novo Design.Methods in molecular biology (Clifton, N.J.) · 2026Article
- A Minimalist Iron Porphyrin Which Can Catalyze Both Peroxidation and Oxygen Reduction Reaction.JACS Au · 2025Article
- 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
- De Novo design of α-helical heme binding proteins capable of versatile cofactor ligation.Methods in enzymology · 2025Article
- De novo design of four-helix bundle proteins to bind metalloporphyrin cofactors.Methods in enzymology · 2025Article
- Delineating redox cooperativity in water-soluble and membrane multiheme cytochromes through protein design.Protein science : a publication of the Protein Society · 2024Article
- A Bioengineered Stable Protein 1-Hemin Complex with Enhanced Peroxidase-Like Catalytic Properties.Small science · 2024Article
- Acid-resistant enzymes: the acquisition strategies and applications.Applied microbiology and biotechnology · 2023Review
- 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
- Atomically Accurate Design of Metalloproteins with Predefined Coordination Geometries.Journal of the American Chemical Society · 2023Article
- Design of Heme Enzymes with a Tunable Substrate Binding Pocket Adjacent to an Open Metal Coordination Site.Journal of the American Chemical Society · 2023Article
- Review
- Structures of the CcmABCD heme release complex at multiple states.Nature communications · 2022Article
- Tailorable Tetrahelical Bundles as a Toolkit for Redox Studies.The journal of physical chemistry. B · 2022Article
- From peptides to proteins: coiled-coil tetramers to single-chain 4-helix bundles.Chemical science · 2022Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
16 authors at 2 institutions in 1 country.
Funding
Abstract
Although catalytic mechanisms in natural enzymes are well understood, achieving the diverse palette of reaction chemistries in re-engineered native proteins has proved challenging. Wholesale modification of natural enzymes is potentially compromised by their intrinsic complexity, which often obscures the underlying principles governing biocatalytic efficiency. The maquette approach can circumvent this complexity by combining a robust de novo designed chassis with a design process that avoids atomistic mimicry of natural proteins. Here, we apply this method to the construction of a highly efficient, promiscuous, and thermostable artificial enzyme that catalyzes a diverse array of substrate oxidations coupled to the reduction of H
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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.