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Cited by 244

The DOI matches its Crossref record; 9 of the 9 references it cites were found in a registry or an index.

Structure of the Cpf1 endonuclease R-loop complex after target DNA cleavage

Stella, Stefano, Alcón, Pablo, Montoya, Guillermo·2017·Nature
DOI 10.1038/nature22398

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Crossref · 10.1038/nature22398

Cites

9 of 9 references verified0 citation errors · 0 not checkable

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  • Cas12 proteins bear some degree of similarity to Cas9, as noted by phylogenetic analysis and the bilobed structure they share in common.

    “These proteins bear some degree of similarity to Cas9, as noted by phylogenetic analysis and the bilobed structure they share in common [18,55,56].”

    From CRISPR-Cas: Converting A Bacterial Defence Mechanism into A State-of-the-Art Genetic Manipulation Tool (2019) · cites this paper as [56]

    The paper’s Abstract (page unavailable) describes Cpf1 as having a “bilobal architecture” with REC and Nuc lobes and calls it a Cas9 “cousin.” It does not say that phylogenetic analysis establishes their similarity or explicitly state that Cas9 shares that bilobal structure. (LLM, conf=0.84)

    Experimental — accuracy not yet measured

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Citations

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Flagged first, then by citations

Research works printed but not linked: 34

  1. Vestergaard, G., Garrett, R. A. & Shah, S. A. CRISPR adaptive immune systems of Archaea. RNA Biol. 11, 156–167 (2014) · DOI
  2. Zetsche, B. et al. Cpf1 is a single RNA-guided endonuclease of a class 2 CRISPR–Cas system. Cell 163, 759–771 (2015) · DOI · Paper page
  3. Dong, D. et al. The crystal structure of Cpf1 in complex with CRISPR RNA. Nature 532, 522–526 (2016) · DOI · Paper page
  4. Marraffini, L. A. CRISPR–Cas immunity in prokaryotes. Nature 526, 55–61 (2015) · DOI
  5. Mohanraju, P. et al. Diverse evolutionary roots and mechanistic variations of the CRISPR–Cas systems. Science 353, aad5147 (2016) · DOI
  6. Mojica, F. J., Díez-Villaseñor, C., García-Martínez, J. & Soria, E. Intervening sequences of regularly spaced prokaryotic repeats derive from foreign genetic elements. J. Mol. Evol. 60, 174–182 (2005) · DOI · Paper page
  7. Makarova, K. S. et al. An updated evolutionary classification of CRISPR–Cas systems. Nat. Rev. Microbiol. 13, 722–736 (2015) · DOI · Paper page
  8. Abudayyeh, O. O. et al. C2c2 is a single-component programmable RNA-guided RNA-targeting CRISPR effector. Science 353, aaf5573 (2016) · DOI · Paper page
  9. Horvath, P. & Barrangou, R. CRISPR/Cas, the immune system of bacteria and archaea. Science 327, 167–170 (2010) · DOI
  10. Makarova, K. S. & Koonin, E. V. Annotation and classification of CRISPR–Cas systems. Methods Mol. Biol. 1311, 47–75 (2015) · DOI
  11. Fonfara, I., Richter, H., Bratovicˇ, M., Le Rhun, A. & Charpentier, E. The CRISPR-associated DNA-cleaving enzyme Cpf1 also processes precursor CRISPR RNA. Nature 532, 517–521 (2016) · DOI · Paper page
  12. Fagerlund, R. D., Staals, R. H. & Fineran, P. C. The Cpf1 CRISPR–Cas protein expands genome-editing tools. Genome Biol. 16, 251 (2015) · DOI
  13. Kim, Y. et al. Generation of knockout mice by Cpf1-mediated gene targeting. Nat. Biotechnol. 34, 808–810 (2016) · DOI
  14. Kleinstiver, B. P. et al. Genome-wide specificities of CRISPR–Cas Cpf1 nucleases in human cells. Nat. Biotechnol. 34, 869–874 (2016) · DOI · Paper page
  15. Endo, A., Masafumi, M., Kaya, H. & Toki, S. Efficient targeted mutagenesis of rice and tobacco genomes using Cpf1 from Francisella novicida. Sci. Rep. 6, 38169 (2016) · DOI
  16. Jiang, F. et al. Structures of a CRISPR–Cas9 R-loop complex primed for DNA cleavage. Science 351, 867–871 (2016) · DOI
  17. Gao, P., Yang, H., Rajashankar, K. R., Huang, Z. & Patel, D. J. Type V CRISPR–Cas Cpf1 endonuclease employs a unique mechanism for crRNA-mediated target DNA recognition. Cell Res. 26, 901–913 (2016) · DOI
  18. Anders, C., Niewoehner, O., Duerst, A. & Jinek, M. Structural basis of PAM-dependent target DNA recognition by the Cas9 endonuclease. Nature 513, 569–573 (2014) · DOI · Paper page
  19. Jiang, F., Zhou, K., Ma, L., Gressel, S. & Doudna, J. A. Structural biology. A Cas9-guide RNA complex preorganized for target DNA recognition. Science 348, 1477–1481 (2015) · DOI
  20. Szczelkun, M. D. et al. Direct observation of R-loop formation by single RNA-guided Cas9 and Cascade effector complexes. Proc. Natl Acad. Sci. USA 111, 9798–9803 (2014) · DOI
  21. Yang, H., Gao, P., Rajashankar, K. R. & Patel, D. J. PAM-dependent target DNA recognition and cleavage by C2c1 CRISPR–Cas endonuclease. Cell 167, 1814–1828 (2016) · DOI
  22. Kim, D. et al. Genome-wide analysis reveals specificities of Cpf1 endonucleases in human cells. Nat. Biotechnol. 34, 863–868 (2016) · DOI · Paper page
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Metadata

Authors
Stella, S., Alcón, P., & Montoya, G.
Venue
Nature
Publisher
Springer Science and Business Media LLC
Published
2017-05-31
Volume
546
Issue
7659
Pages
559-563
ISSN
  • 0028-0836
  • 1476-4687
DOI
10.1038/nature22398
Cited by
244
References
9
Language
en
Update notices
erratum (2017-07-05)
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