ArticleScience (New York, N.Y.)2022
Craspase is a CRISPR RNA-guided, RNA-activated protease.
Article in Science (New York, N.Y.), 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 46 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
46 citing papers in PubMed.
- Type IV-C CRISPR-Cas effector complexes recognize double-stranded DNA and switch on collateral cleavage of ssDNA and RNA.Cell reports · 2026Article
- Article
- Craspase Protease Activation Is Sensitive to Oncogenic Single-Nucleotide RNA Mismatches.ACS chemical biology · 2026Article
- Structural mechanism of SAM-AMP and SAM-AMPNature communications · 2026Article
- The antiphage mechanism of a widespread trypsin-MBL defense module.Nature chemical biology · 2026Article
- Enhancement of prime editing by recruiting engineered or evolved components and implementing novel strategies.Biochemistry and biophysics reports · 2026Review
- A synthetic system for RNA-responsive pyroptosis based on type III-E CRISPR nuclease-protease.Nature communications · 2026Article
- Evaluation of AI-Predicted GH11 Xylanase Models Against a Previously Unreported Experimental Structure: Implications for Conformational Accuracy and Ligand Binding.International journal of molecular sciences · 2026Article
- Synthetic Type III-E CRISPR-Cas Effectors for Programmable RNA-targeting.Journal of molecular biology · 2026Article
- Recurrent acquisition of nuclease-protease pairs in antiviral immunity.Science (New York, N.Y.) · 2026Article
- Proteolytic activation of diverse antiviral defense modules in prokaryotes.bioRxiv : the preprint server for biology · 2025Article
- A NanoLock-enabled, Craspase-based strategy for highly sensitive RNA detection.Nucleic acids research · 2025Article
- TIGR-Tas: A family of modular RNA-guided DNA-targeting systems in prokaryotes and their viruses.Science (New York, N.Y.) · 2025Article
- CRISPR RNA binding drives structural ordering that primes Cas7-11 for target cleavage.Nucleic acids research · 2025Article
- Cas7 meets Cas14: a strategic partnership in the type VII CRISPR-Cas.Protein & cell · 2025Article
- Role of CRISPR-Cas systems in periodontal disease pathogenesis and potential for periodontal therapy: A review.Molecular oral microbiology · 2025Review
- Structural basis for regulation of a CBASS-CRISPR-Cas defense island by a transmembrane anti-σ factor and its ECF σ partner.Science advances · 2024Article
- The SAVED domain of the type III CRISPR protease CalpL is a ring nuclease.Nucleic acids research · 2024Article
- Article
- Molecular and structural basis of an ATPase-nuclease dual-enzyme anti-phage defense complex.Cell research · 2024Article
Corrections and comments
- Commented on by
Authors and funding
12 authors.
Funding
Abstract
The CRISPR-Cas type III-E RNA-targeting effector complex gRAMP/Cas7-11 is associated with a caspase-like protein (TPR-CHAT/Csx29) to form Craspase (CRISPR-guided caspase). Here, we use cryo-electron microscopy snapshots of Craspase to explain its target RNA cleavage and protease activation mechanisms. Target-guide pairing extending into the 5' region of the guide RNA displaces a gating loop in gRAMP, which triggers an extensive conformational relay that allosterically aligns the protease catalytic dyad and opens an amino acid side-chain-binding pocket. We further define Csx30 as the endogenous protein substrate that is site-specifically proteolyzed by RNA-activated Craspase. This protease activity is switched off by target RNA cleavage by gRAMP and is not activated by RNA targets containing a matching protospacer flanking sequence. We thus conclude that Craspase is a target RNA-activated protease with self-regulatory capacity.
Indexed as
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.