ArticleChemical science2017
Tuning SpyTag-SpyCatcher mutant pairs toward orthogonal reactivity encryption.
Article in Chemical science, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 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
8 citing papers in PubMed.
- Engineering Protein-Peptide Interfaces via Combinatorial Mutagenesis and Mass Photometric Screening.Biomolecules · 2025Article
- Surface Engineering of the Encapsulin Nanocompartment ofACS omega · 2025Article
- In situ characterization of amine-forming enzymes shows altered oligomeric state.Protein science : a publication of the Protein Society · 2025Article
- Therapeutic Potential of Engineered Virus-like Particles of Parvovirus B19.Pathogens (Basel, Switzerland) · 2023Review
- Protein-protein interactions enhance the thermal resilience of SpyRing-cyclized enzymes: A molecular dynamic simulation study.PloS one · 2022Article
- Directed co-evolution of interacting protein-peptide pairs by compartmentalized two-hybrid replication (C2HR).Nucleic acids research · 2020Article
- Enhanced stability of a rumen-derived xylanase using SpyTag/SpyCatcher cyclization.World journal of microbiology & biotechnology · 2020Article
- Achieving Controlled Biomolecule-Biomaterial Conjugation.Chemical reviews · 2018Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
6 authors.
Funding
Abstract
Genetically encoded covalent peptide tagging technology, such as the SpyTag-SpyCatcher reaction, has emerged as a unique way to do chemistry with proteins. Herein, we report the reactivity engineering of SpyTag-SpyCatcher mutant pairs and show that distinct reactivity can be encrypted for the same reaction based on protein sequences of high similarity. Valuable features, including high selectivity, inverse temperature dependence and (nearly) orthogonal reactivity, could be achieved based on as few as three mutations. This demonstrates the robustness of the SpyTag-SpyCatcher reaction and the plasticity of its sequence specificity, pointing to a family of engineered protein chemistry tools.
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.