The DOI matches its Crossref record; 53 of the 53 references it cites were found in a registry or an index.
CRISPR/Cas9 in Genome Editing and Beyond
Abstract
The Cas9 protein (CRISPR-associated protein 9), derived from type II CRISPR (clustered regularly interspaced short palindromic repeats) bacterial immune systems, is emerging as a powerful tool for engineering the genome in diverse organisms. As an RNA-guided DNA endonuclease, Cas9 can be easily programmed to target new sites by altering its guide RNA sequence, and its development as a tool has made sequence-specific gene editing several magnitudes easier. The nuclease-deactivated form of Cas9 further provides a versatile RNA-guided DNA-targeting platform for regulating and imaging the genome, as well as for rewriting the epigenetic status, all in a sequence-specific manner. With all of these advances, we have just begun to explore the possible applications of Cas9 in biomedical research and therapeutics. In this review, we describe the current models of Cas9 function and the structural and biochemical studies that support it. We focus on the applications of Cas9 for genome editing, regulation, and imaging, discuss other possible applications and some technical considerations, and highlight the many advantages that CRISPR/Cas9 technology offers.
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“The CRISPR/Cas9 genome-editing system provides us an unprecedented opportunity to target and modify genomic sequences with high levels of efficacy and specificity [151,152,153,154,155].”
From Cell Immortality: In Vitro Effective Techniques to Achieve and Investigate Its Applications and Challenges (2024) · cites this paper as [154]
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“Although CRISPRi is generally highly efficient in prokaryotes, the dCas9–sgRNA complex alone may not be very efficient at silencing gene expression in mammalian cells (41).”
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Hsu, P. D., Scott, D. A., Weinstein, J. A., Ran, F. A., Konermann, S., Agarwala, V., Li, Y., Fine, E. J., Wu, X., Shalem, O., et al. (2013) · Nature Biotechnology · doi:10.1038/nbt.2647 · Cited by 4,741
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“Alternatively, dCas9 can be fused to a repressor domain such as KRAB to enhance repression (37).”
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Metadata
- Authors
- Wang, H., La Russa, M., & Qi, L. S.
- Affiliations
- Department of Bioengineering, Stanford University, Stanford, California 94305;, ,
- Venue
- Annual Review of Biochemistry
- Publisher
- Annual Reviews
- Published
- 2016-06-02
- Volume
- 85
- Issue
- 1
- Pages
- 227-264
- ISSN
- 0066-4154
- 1545-4509
- PMC
- PMC13384723
- Cited by
- 1,110
- References
- 53
- Language
- en
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