ArticleNature2016
The crystal structure of Cpf1 in complex with CRISPR RNA.
Article in Nature, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 207 papers, 1 of them a synthesis that pooled it.
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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.
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Who cites it
207 citing papers in PubMed, 1 synthesis or guideline pooled it, 411 citations in OpenAlex.
- CRISPR/Cas-Based Modifications for Therapeutic Applications: A Review.Molecular biotechnology · 2022Pooled it
- Advances in CRISPR multiplex gene editing to map and modify stress-responsive transcription factor networks for crop improvement.Plant cell reports · 2026Review
- Review
- Suboptimal PAM Enables One-Pot RPA-CRISPR/Cas12a Detection ofCurrent issues in molecular biology · 2026Article
- Molecular mechanisms and biotechnology applications of CRISPR-Cas12a.Nature reviews. Molecular cell biology · 2026Review
- Indiscriminate Trans-Cleavage Activity of CRISPR/SuCas12a2 Enables Sensitive Detection of SARS-CoV-2.ACS sensors · 2026Article
- Structural mining and engineering of metagenome-derived Cas12a orthologs expands the CRISPR genome editing and multiplex diagnostics toolkit.Molecular therapy : the journal of the American Society of Gene Therapy · 2026Article
- Molecular engineering of CRISPR/Cas12a: from activity enhancement to exponential signal amplification.Chemical science · 2026Review
- Ratiometric transcriptional activation by protein degradation.bioRxiv : the preprint server for biology · 2026Article
- Activation mechanism and integrated one-pot assay of chiral-like cRNA-enhanced CRISPR/Cas12a systems.Nature communications · 2026Article
- Kinetic Modeling of Target-Amplification-Free CRISPR-Cas-Based Autocatalysis Reactions.bioRxiv : the preprint server for biology · 2026Article
- crRNA scaffold remodeling controls CRISPR-Cas12a activity for enhanced performance.Nucleic acids research · 2026Article
- Bridge helix of Cas12a is an allosteric regulator of R-loop formation and RuvC activation.Nature communications · 2026Article
- Functions and applications of enzymes in nucleic acid nanotechnology.Journal of nanobiotechnology · 2025Review
- Conformational changes induced by K949A mutation in the CRISPR-Cas12a complex drives an effective target-binding mechanism.Current research in structural biology · 2025Article
- Tailoring Cas12a functionality with a user-friendly and versatile crRNA variant toolbox.Nature communications · 2025Article
- And… cut! - how conformational regulation of CRISPR-Cas effectors directs nuclease activity.The Biochemical journal · 2025Review
- CRISPR-Cas12a REC2-Nuc interactions drive target-strand cleavage and constrain trans cleavage.Nucleic acids research · 2025Article
- AsCas12a tolerates insertions in target DNA.Nucleic acids research · 2025Article
- Discovery of CRISPR-Cas12a clades using a large language model.Nature communications · 2025Article
147 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
18 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The CRISPR-Cas systems, as exemplified by CRISPR-Cas9, are RNA-guided adaptive immune systems used by bacteria and archaea to defend against viral infection. The CRISPR-Cpf1 system, a new class 2 CRISPR-Cas system, mediates robust DNA interference in human cells. Although functionally conserved, Cpf1 and Cas9 differ in many aspects including their guide RNAs and substrate specificity. Here we report the 2.38 Å crystal structure of the CRISPR RNA (crRNA)-bound Lachnospiraceae bacterium ND2006 Cpf1 (LbCpf1). LbCpf1 has a triangle-shaped architecture with a large positively charged channel at the centre. Recognized by the oligonucleotide-binding domain of LbCpf1, the crRNA adopts a highly distorted conformation stabilized by extensive intramolecular interactions and the (Mg(H2O)6)(2+) ion. The oligonucleotide-binding domain also harbours a looped-out helical domain that is important for LbCpf1 substrate binding. Binding of crRNA or crRNA lacking the guide sequence induces marked conformational changes but no oligomerization of LbCpf1. Our study reveals the crRNA recognition mechanism and provides insight into crRNA-guided substrate binding of LbCpf1, establishing a framework for engineering LbCpf1 to improve its efficiency and specificity for genome editing.
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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.