ArticleMolecular cell2013
Same same but different: new structural insight into CRISPR-Cas complexes.
Article in Molecular cell, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 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
6 citing papers in PubMed.
- Functional Identification of theFrontiers in microbiology · 2021Article
- Efficient programmable gene silencing by Cascade.Nucleic acids research · 2015Article
- Structure Principles of CRISPR-Cas Surveillance and Effector Complexes.Annual review of biophysics · 2015Review
- Structural biology. Crystal structure of a CRISPR RNA-guided surveillance complex bound to a ssDNA target.Science (New York, N.Y.) · 2014Article
- Unravelling the structural and mechanistic basis of CRISPR-Cas systems.Nature reviews. Microbiology · 2014Review
- CRISPR-Cas systems: new players in gene regulation and bacterial physiology.Frontiers in cellular and infection microbiology · 2014Review
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Authors and funding
2 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Three papers in this issue of Molecular Cell report on the structure and functional activity of type III CRISPR-Cas effector complexes, revealing novel and conserved features of the ribonucleoprotein particles that underlie prokaryotic genome defense. The new structures suggest that type I and type III complexes follow the same architectural principles and are most likely descendants of a common ancestor, the differences in RNA and protein sequences and structure of individual components notwithstanding.
Indexed as
Identifiers
24119398What 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.