ArticleMethods in enzymology2019
Directed evolution studies of a thermophilic Type II-C Cas9.
Article in Methods in enzymology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
What it found
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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.
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Who cites it
9 citing papers in PubMed, 15 citations in OpenAlex.
- Article
- Customizing CRISPR-Cas PAM specificity with protein language models.Nature biotechnology · 2026Article
- CRISPR-driven diagnostics: Molecular mechanisms, clinical efficacy and translational challenges.Clinical and translational medicine · 2025Review
- Engineering of CRISPR-Cas PAM recognition using deep learning of vast evolutionary data.bioRxiv : the preprint server for biology · 2025Article
- Expression and Functional Analysis of the Compact ThermophilicInternational journal of molecular sciences · 2023Article
- Coupled catalytic states and the role of metal coordination in Cas9.Nature catalysis · 2023Article
- Engineering highly thermostable Cas12b via de novo structural analyses for one-pot detection of nucleic acids.Cell reports. Medicine · 2023Article
- Catalytically Enhanced Cas9 through Directed Protein Evolution.The CRISPR journal · 2021Article
- The molecular basis for recognition of 5'-NNNCC-3' PAM and its methylation state by Acidothermus cellulolyticus Cas9.Nature communications · 2020Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Though making up nearly half of the known CRISPR-Cas9 family of enzymes, the Type II-C CRISPR-Cas9 has been underexplored for their molecular mechanisms and potential in safe gene editing applications. In comparison with the more popular Type II-A CRISPR-Cas9, the Type II-C enzymes are generally smaller in size and utilize longer base pairing in identification of their DNA substrates. These characteristics suggest easier portability and potentially less off-targets for Type II-C in gene editing applications. We describe identification and biochemical characterization of a thermophilic Type II-C CRISPR-Cas from Acidothermus cellulolyticus (AceCas9). We describe several library-based methods that enabled us to identify the PAM sequence and elements critical to protospacer mismatch surveillance of AceCas9.
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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.