ArticleAdvanced science (Weinheim, Baden-Wurttemberg, Germany)2025
Replicating PET Hydrolytic Activity by Positioning Active Sites with Smaller Synthetic Protein Scaffolds.
Article in Advanced science (Weinheim, Baden-Wurttemberg, Germany), 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 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
5 citing papers in PubMed.
- Sequence redesign of glycosyltransferases for enhanced heterologous expression and glycosylation efficiency in Escherichia coli.Nature communications · 2026Article
- Rethinking plastic waste: innovations in enzymatic breakdown of oil-based polyesters and bioplastics.FEBS open bio · 2026Review
- Enzyme miniaturization: Revolutionizing future biocatalysts.Biotechnology advances · 2025Review
- Standardization guidelines and future trends for PET hydrolase research.Nature communications · 2025Review
- Replicating PET Hydrolytic Activity by Positioning Active Sites with Smaller Synthetic Protein Scaffolds.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
5 authors.
Funding
Abstract
Evolutionary constraints significantly limit the diversity of naturally occurring enzymes, thereby reducing the sequence repertoire available for enzyme discovery and engineering. Recent breakthroughs in protein structure prediction and de novo design, powered by artificial intelligence, now enable to create enzymes with desired functions without solely relying on traditional genome mining. Here, a computational strategy is demonstrated for creating new-to-nature polyethylene terephthalate hydrolases (PET hydrolases) by leveraging the known catalytic mechanisms and implementing multiple deep learning algorithms and molecular computations. This strategy includes the extraction of functional motifs from a template enzyme (here leaf-branch compost cutinase, LCC, is used), regeneration of new protein sequences, computational screening, experimental validation, and sequence refinement. PET hydrolytic activity is successfully replicated with designer enzymes that are at least 30% shorter in sequence length than LCC. Among them, RsPETase1 stands out due to its robust expressibility. It exhibits comparable catalytic efficiency (k
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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.