English (United Kingdom)

https://curated-unify.zendy.io/wp-json/zendy-region/v1/featured_content/oa?rat=en

https://curated-unify.zendy.io/wp-json/zendy-region/v1/highlighted_journal/

Global: Zendy Plus annual

Presents the access of premium content as premium feature

Premium Content

Presents the keyphrase highlighting as premium feature

Keyphrase Highlighting

Presents the summarisation as premium feature

Summarisation

Insights

Presents the pdf analysis as premium feature

PDF Analysis

Presents the zaia usage as premium feature

ZAIA

Global: Zendy Tools annual

Global: Zendy Free Plan

Global: Zendy Tools monthly

Global: Zendy Plus monthly

Significance Cas12a is a type V CRISPR-Cas endonuclease that relies on a programmable guide RNA to bind specific DNA sequences, and like most CRISPR-Cas systems, it suffers from spurious off-target binding. Improving the specificity of Cas12a is an important step toward its broader use as a tool for biomedical research, but a fundamental understanding of the biophysical determinants of nonspecific Cas12a binding is still lacking. Here, we developed a massively parallel CRISPR interference assay to reveal the thermodynamic factors involved in Cas12a off-target binding. Since our approach uses a parameter-free thermodynamic model that is broadly applicable to any RNA-guided endonucleases, our work should enhance our understanding of on- and off-target binding when applied to other CRISPR-Cas systems.

Massively parallel CRISPRi assays reveal concealed thermodynamic determinants of dCas12a binding