Cited by 1,323

The DOI matches its Crossref record; 18 of the 18 references it cites were found in a registry or an index.

Structural basis of PAM-dependent target DNA recognition by the Cas9 endonuclease

Anders, Carolin, Niewoehner, Ole, Duerst, Alessia, Jinek, Martin·2014·Nature

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Crossref · 10.1038/nature13579

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18 of 18 references verified0 citation errors · 0 not checkable

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  • Once the target is identified, the dsDNA is unwound and crRNA binds to the target ssDNA, leading to an R-loop shape and ultimately to a blunt double-strand break by both catalytic sites of Cas9, RuvC and HNH, 3 nt upstream of the PAM site.

    “Once identified, the dsDNA is unwinded and crRNA binds to the target ssDNA leading to an R-loop shape and ultimately to a blunt double-strand break by both catalytic sites of Cas9, RuvC and HNH, 3 nt upstream of the PAM site [25,53,54].”

    From CRISPR-Cas: Converting A Bacterial Defence Mechanism into A State-of-the-Art Genetic Manipulation Tool (2019) · cites this paper as [25]

    The paper’s model (section labeled Abstract; page unavailable) describes PAM-dependent DNA unwinding and guide RNA–target DNA pairing, and it identifies HNH and RuvC as Cas9’s nuclease domains. Our copy does not state that their cleavage produces a blunt double-strand break three nucleotides upstream of the PAM; the structure described has an inactivated HNH domain and an intact target strand. (LLM, conf=0.84)

    Experimental — accuracy not yet measured
  • gRNA molecules contain both a scaffold sequence that binds to Cas9 and a targeting sequence which directs the system towards the target locus.

    “gRNA molecules contain both a scaffold sequence that binds to Cas9 and a targeting sequence which directs the system towards the target locus [25].”

    From CRISPR-Cas: Converting A Bacterial Defence Mechanism into A State-of-the-Art Genetic Manipulation Tool (2019) · cites this paper as [25]

    The paper’s Abstract (page unavailable) says Cas9 associates with guide RNA and that a 20-nucleotide segment of the guide RNA is complementary to target DNA, supporting the targeting-sequence part of the claim. The passages in our copy do not identify a scaffold sequence or state that it binds Cas9. (LLM, conf=0.82)

    Experimental — accuracy not yet measured
  • In type II systems, Cas9 recognizes the PAM sequence in the double-strand form.

    “As for type II systems, Cas9 recognizes the PAM sequence in the double-strand form [25].”
  • In type I systems, Cas1 binds to the PAM-complementary sequence in its ssDNA form.

    “In type I systems, Cas1 binds to the PAM-complementary sequence in its ssDNA form.”

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Citations

Cites

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Research works printed but not linked: 18

  1. Gasiunas, G., Barrangou, R., Horvath, P. & Siksnys, V. Cas9-crRNA ribonucleoprotein complex mediates specific DNA cleavage for adaptive immunity in bacteria. Proc. Natl Acad. Sci. USA 109, 2579–2586 (2012) · DOI · Paper page
  2. Garneau, J. E. et al. The CRISPR/Cas bacterial immune system cleaves bacteriophage and plasmid DNA. Nature 468, 67–71 (2010) · DOI
  3. Sapranauskas, R. et al. The Streptococcus thermophilus CRISPR/Cas system provides immunity in Escherichia coli . Nucleic Acids Res. 39, 9275–9282 (2011) · DOI
  4. Sternberg, S. H., Redding, S., Jinek, M., Greene, E. C. & Doudna, J. A. DNA interrogation by the CRISPR RNA-guided endonuclease Cas9. Nature 507, 62–67 (2014) · DOI · Paper page
  5. Bassett, A. R., Tibbit, C., Ponting, C. P. & Liu, J.-L. Highly efficient targeted mutagenesis of Drosophila with the CRISPR/Cas9 system. Cell Rep. 4, 220–228 (2013) · DOI
  6. Gratz, S. J. et al. Genome engineering of Drosophila with the CRISPR RNA-guided Cas9 nuclease. Genetics 194, 1029–1035 (2013) · DOI
  7. Bikard, D. et al. Programmable repression and activation of bacterial gene expression using an engineered CRISPR-Cas system. Nucleic Acids Res. 41, 7429–7437 (2013) · DOI · Paper page
  8. Fonfara, I. et al. Phylogeny of Cas9 determines functional exchangeability of dual-RNA and Cas9 among orthologous type II CRISPR-Cas systems. Nucleic Acids Res. 42, 2577–2590 (2013) · DOI · Paper page
  9. Esvelt, K. M. et al. Orthogonal Cas9 proteins for RNA-guided gene regulation and editing. Nature Methods 10, 1116–1121 (2013) · DOI · Paper page
  10. Luscombe, N. M., Laskowski, R. A. & Thornton, J. M. Amino acid-base interactions: a three-dimensional analysis of protein-DNA interactions at an atomic level. Nucleic Acids Res. 29, 2860–2874 (2001) · DOI · Paper page
  11. Briner, A. E. & Barrangou, R. Lactobacillus buchneri genotyping on the basis of clustered regularly interspaced short palindromic repeat (CRISPR) locus diversity. Appl. Environ. Microbiol. 80, 994–1001 (2014) · DOI
  12. Redondo, P. et al. Molecular basis of xeroderma pigmentosum group C DNA recognition by engineered meganucleases. Nature 456, 107–111 (2008) · DOI
  13. Ashworth, J. et al. Computational reprogramming of homing endonuclease specificity at multiple adjacent base pairs. Nucleic Acids Res. 38, 5601–5608 (2010) · DOI
  14. Kabsch, W. XDS. Acta Crystallogr. D 66, 125–132 (2010) · DOI · Paper page
  15. Adams, P. D. et al. PHENIX: a comprehensive Python-based system for macromolecular structure solution. Acta Crystallogr. D 66, 213–221 (2010) · DOI · Paper page
  16. Vonrhein, C., Blanc, E., Roversi, P. & Bricogne, G. Automated structure solution with autoSHARP. Methods Mol. Biol. 364, 215–230 (2007)
  17. Vagin, A. & Teplyakov, A. Molecular replacement with MOLREP. Acta Crystallogr. D 66, 22–25 (2010) · DOI
  18. Katoh, K. & Standley, D. M. MAFFT: iterative refinement and additional methods. Methods Mol. Biol. 1079, 131–146 (2014) · DOI

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Metadata

Authors
Anders, C., Niewoehner, O., Duerst, A., & Jinek, M.
Venue
Nature
Published
2014-07-27
Volume
513
Issue
7519
Pages
569-573
ISSN
  • 0028-0836
  • 1476-4687
Cited by
1,323
References
18
Language
en

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