ArticleMolecular cell2019
Structures of Neisseria meningitidis Cas9 Complexes in Catalytically Poised and Anti-CRISPR-Inhibited States.
Article in Molecular cell, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 78 papers.
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Who cites it
78 citing papers in PubMed.
- Article
- Structural basis of AtCas9 recognition of PAM mutants in underwound DNA topology.Nature structural & molecular biology · 2026Article
- Structure basis for single-strand nucleic acid targeting by IscB and variants.Nucleic acids research · 2026Article
- Protocol for enhancing Cas9 efficiency and fidelity through structure-guided phosphate-locking loop engineering.STAR protocols · 2026Article
- Article
- Structural insight into IscB's RNA-lid-based inactivation mechanism.Nature structural & molecular biology · 2026Article
- Structure basis for single-strand nucleic acid targeting by IscB and variants.bioRxiv : the preprint server for biology · 2026Article
- Structural basis for inhibition of SpyCas9 by the anti-CRISPR protein AcrIIA26.The Biochemical journal · 2026Article
- A Computational Model for Nme1Cas9 HNH Activation Driven by Dynamic Interface Engineering at Residues S593 and W596.Biomolecules · 2026Article
- Customizing CRISPR-Cas PAM specificity with protein language models.Nature biotechnology · 2026Article
- Structural visualization of the molecular evolution of CRISPR-Cas9.Nature structural & molecular biology · 2026Article
- The CRISPR/Cas-associated scaRNA modulatesmicroLife · 2026Article
- AcrIIA19 binds to the WED domain and inhibits various Cas9 orthologs at multiple stages.Communications biology · 2025Article
- Loop engineering of AtCas9 for effective and broad genome editing.Cell insight · 2025Article
- Structural and functional insights into internal domain replacement in SpCas9 for protein engineering.Scientific reports · 2025Article
- Functional Characterization of Fp2Cas9, a Cold-Adapted Type II-C CRISPR Nuclease fromInternational journal of molecular sciences · 2025Article
- Article
- And… cut! - how conformational regulation of CRISPR-Cas effectors directs nuclease activity.The Biochemical journal · 2025Review
- Structural basis of a dual-function type II-B CRISPR-Cas9.Nucleic acids research · 2025Article
- Recent advances in therapeutic gene-editing technologies.Molecular therapy : the journal of the American Society of Gene Therapy · 2025Review
18 more citing papers are in PubMed but not listed here.
Corrections and comments
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Authors and funding
17 authors.
Funding
Abstract
High-resolution Cas9 structures have yet to reveal catalytic conformations due to HNH nuclease domain positioning away from the cleavage site. Nme1Cas9 and Nme2Cas9 are compact nucleases for in vivo genome editing. Here, we report structures of meningococcal Cas9 homologs in complex with sgRNA, dsDNA, or the AcrIIC3 anti-CRISPR protein. DNA-bound structures represent an early step of target recognition, a later HNH pre-catalytic state, the HNH catalytic state, and a cleaved-target-DNA-bound state. In the HNH catalytic state of Nme1Cas9, the active site is seen poised at the scissile phosphodiester linkage of the target strand, providing a high-resolution view of the active conformation. The HNH active conformation activates the RuvC domain. Our structures explain how Nme1Cas9 and Nme2Cas9 read distinct PAM sequences and how AcrIIC3 inhibits Nme1Cas9 activity. These structures provide insights into Cas9 domain rearrangements, guide-target engagement, cleavage mechanism, and anti-CRISPR inhibition, facilitating the optimization of these genome-editing platforms.
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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.