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ALS Publications by Jennifer Doudna

This list is a compilation of all publications with 2020 Chemistry Nobel Laureate Jennifer Doudna as co-author which used the resources of the Advanced Light Source.

Updated October 8, 2020

  1. Knott, G.J., B.F. Cress, J.-J. Liu, B.W. Thornton, R.J. Lew, B. Al-Shayeb, D.J. Rosenberg, M. Hammel, B.A. Adler, M.J. Lobba, M. Xu, A.P. Arkin, C. Fellmann, and J.A. Doudna, “Structural basis for AcrVA4 inhibition of specific CRISPR-Cas12a,” eLife 8, e49110 (2019). (doi:10.7554/eLife.49110) 12.3.1
  2. Knott, G.J., A. East-Seletsky, J.C. Cofsky, J.M. Holton, E. Charles, M.R. O’Connell, and J.A. Doudna, “Guide-bound structures of an RNA-targeting A-cleaving CRISPR–Cas13a enzyme,” Nature Structural & Molecular Biology 24, 825 (2017). (doi:10.1038/nsmb.3466) 8.3.1
  3. Wright, A.V., J.-J. Liu, G.J. Knott, K.W. Doxzen, E. Nogales, and J.A. Doudna, “Structures of the CRISPR genome integration complex,” Science 357, 1113 (2017). (doi:10.1126/science.aao0679) 8.3.1
    Highlight: The CRISPR Target-Recognition Mechanism
  4. Floor, S., K. Condon, D. Sharma, E. Jankowsky, and J.A. Doudna, “Autoinhibitory Interdomain Interactions and Subfamily-Specific Extensions Redefine the Catalytic Core of the Human DEAD-box Protein DDX3,” Journal of Biological Chemistry 291, 2412 (2016). (doi:10.1074/jbc.M115.700625) 8.3.1
  5. Jiang, F., D.W. Taylor, J.S. Chen, J.E. Kornfeld, K.-J. Zhou, A.J. Thompson, E. Nogales, and J.A. Doudna, “Structures of a CRISPR-Cas9 R-loop complex primed for DNA cleavage,” Science 351, 867 (2016). (doi:10.1126/science.aad8282) 8.3.1
  6. Kaya, E., K.W. Doxzen, K.R. Knoll, R.C. Wilson, S. Strutt, P.J. Kranzusch, and J.A. Doudna, “A bacterial Argonaute with noncanonical guide RNA specificity,” Proceedings of the National Academy of Sciences of the United States of America 113, 4057 (2016). (doi:10.1073/pnas.1524385113) 8.3.1
  7. Lee, A.Y., P.J. Kranzusch, J.A. Doudna, and J.H. Cate, “eIF3d is an mRNA cap-binding protein that is required for specialized translation initiation,” Nature 536, 96 (2016). (doi:10.1038/nature18954) 8.3.1
  8. Schulze-Gahmen, U., I. Echeverria, G. Stjepanovic, Y. Bai, H. Lu, D. Schneidman-Duhovny, J.A. Doudna, Q. Zhou, A. Sali, and J.H. Hurley, “Insights into HIV-1 proviral transcription from the structure and dynamics of the Tat:AFF4:P-TEFb:TAR complex,” eLife 5, e15910 (2016). (doi:10.7554/eLife.15910) 8.3.1, 12.3.1
  9. Jiang, F., K.-J. Zhou, L. Ma, S. Gressel, and J.A. Doudna, “A Cas9-guide RNA complex preorganized for target DNA recognition,” Science 348, 1477 (2015). (doi:10.1126/science.aab1452) 8.3.1
  10. Kranzusch, P.J., S.C. Wilson, A.S. Lee, J.M. Berger, J.A. Doudna, and R.E. Vance, “Ancient Origin of cGAS-STING Reveals Mechanism of Universal 20,30 cGAMP Signaling,” Molecular Cell 59, 891 (2015). (doi:10.1016/j.molcel.2015.07.022) 8.3.1
  11. Nunez, J.K., L.B. Harrington, P.J. Kranzusch, A.N. Engelman, and J.A. Doudna, “Foreign DNA capture during CRISPR-Cas adaptive immunity,” Nature 527, 535 (2015). (doi:10.1038/nature15760) 8.3.1
    Brief: Foreign DNA Capture during CRISPR–Cas Adaptive Immunity
  12. Bai, Y., A. Tambe, K.-J. Zhou, and J.A. Doudna, “RNA-guided assembly of Rev-RRE nuclear export complexes,” eLife 3, e03656 (2014). (doi:10.7554/eLife.03656) 12.3.1
  13. Jinek, M., F. Jiang, D.W. Taylor, S.H. Sternberg, E. Kaya, E. Ma, C. Anders, M. Hauer, K.-J. Zhou, S. Lin, M. Kaplan, A.T. Lavarone, E. Charpentier, E. Nogales, and J.A. Doudna, “Structures of Cas9 endonucleases reveal RNA-mediated conformational activation,” Science 343, 1247997 (2014). (doi:10.1126/science.1247997) 8.2.2, 8.3.1
    Highlight: Intriguing DNA Editor Has a Structural Trigger
  14. Kapral, G.J., S. Jain, J. Noeske, J.A. Doudna, D.C. Richardson, and J.S. Richardson, “New tools provide a second look at HDV ribozyme structure, dynamics and cleavage,” Nucleic Acids Research 42, 12833 (2014). (doi:10.1093/nar/gku992) 8.2.1
  15. Kranzusch, P.J., A.Y. Lee, S.C. Wilson, M. Solovykh, R.E. Vance, J.M. Berger, and J.A. Doudna, “Structure-Guided Reprogramming of Human cGAS Dinucleotide Linkage Specificity,” Cell 158, 1011 (2014). (doi:10.1016/j.cell.2014.07.028) 8.3.1
    Brief: A New Link Between Human and Bacterial Signaling Machinery
  16. Niewoehner, O., M. Jinek, and J.A. Doudna, “Evolution of CRISPR RNA recognition and processing by Cas6 endonucleases,” Nucleic Acids Research 42, 1341 (2014). (doi:10.1093/nar/gkt922) 8.2.2
  17. Nunez, J.K., P.J. Kranzusch, J. Noeske, A.V. Wright, C.W. Davies, and J.A. Doudna, “Cas1-Cas2 complex formation mediates spacer acquisition during CRISPR-Cas adaptive immunity,” Nature Structural & Molecular Biology 21, 528 (2014). (doi:10.1038/nsmb.2820) 8.3.1
  18. Kranzusch, P.J., A.Y. Lee, J.M. Berger, and J.A. Doudna, “Structure of Human cGAS Reveals a Conserved Family of Second-Messenger Enzymes in Innate Immunity,” Cell Reports 3, 1362 (2013). (doi:10.1016/j.celrep.2013.05.008) 8.3.1, 8.2.1
  19. Haurwitz, R.E., S.H. Sternberg, and J.A. Doudna, “Csy4 relies on an unusual catalytic dyad to position and cleave CRISPR RNA,” EMBO Journal 31, 2824 (2012). (doi:10.1038/emboj.2012.107) 8.2.1
  20. Ataide, S.F., N. Schmitz, K.A. Shen, A.L. Ke, S.O. Shan, J.A. Doudna, and N.N. Ban, “The crystal structure of the signal recognition particle in complex with its receptor,” Science 331, 881 (2011). (doi:10.1126/science.1196473 ) 8.2.2
  21. Jinek, M., S.M. Coyle, and J.A. Doudna, “Coupled 5′ nucleotide recognition and processivity in Xrn1-mediated mRNA decay.,” Molecular Cell 41, 600 (2011). (doi:10.1016/j.molcel.2011.02.004) 8.2.1
  22. Jore, M.M., M. Lundgren, E. van Duijin, J.B. Bultema, E.R. Westra, S.P. Waghmare, B.A. Wiedenheft, U. Pul, R. Wurm, R. Wagner, M.R. Beijer, A. Barendregt, K.H. Zhou, A.P. Snijders, M.J. Dickman, J.A. Doudna, E.J. Boekema, A.J.R. Heck, J. van der Oost, and S.J.J. Brouns, “Structural Basis for CRISPR RNA-guided DNA Recognition by Cascade,” Nature Structural & Molecular Biology 18, 529 (2011). (doi:10.1038/nsmb.2019) 7.3.3
  23. Sashital, D.G., M. Jinek, and J.A. Doudna, “An RNA-induced conformational change required for CRISPR RNA cleavage by the endoribonuclease Cse3,” Nature Structural & Molecular Biology 18, 680 (2011). (doi:10.1038/nsmb.2043) 8.2.1, 8.3.1
  24. Wiedenheft, B.A., E. van Duijin, J. Bulterna, S. Waghmare, K.H. Zhou, A. Barendregt, W. Westphal, A. Heck, E. Boekema, M. Dickman, and J.A. Doudna, “RNA-guided complex from a bacterial immune system enhances target recognition through seed sequence interactions,” Proceedings of the National Academy of Sciences of the United States of America 108, 10092 (2011). (doi:10.1073/pnas.1102716108) 7.3.3
  25. Haurwitz, R.E., M. Jinek, B.A. Wiedenheft, K.-J. Zhou, and J.A. Doudna, “Sequence- and Structure-Specific RNA Processing by a CRISPR Endonuclease,” Science 329, 1355 (2010). (doi:10.1126/science.1192272) 8.3.1, 8.2.2
  26. Jinek, M., M.R. Fabian, S. Coyle, N. Sonenberg, and J.A. Doudna, “Structural insights into the human GW182-PABC interaction in microRNA-mediated deadenylation,” Nature Structural & Molecular Biology 17, 238 (2010). (doi:10.1038/nsmb.1768) 8.2.1
  27. Weeks, A.M., S.M. Coyles, M. Jinek, J.A. Doudna, and M. Chang, “Structural and biochemical studies of a fluoroacetyl-CoA-specific thioesterase reveal a molecular basis for fluorine selectivity,” Biochemistry 49, 9269 (2010). (doi:10.1021/bi101102u) 8.2.2
  28. Coyle, S., W. Gilbert, and J.A. Doudna, “Direct Link between RACK1 Function and Localization at the Ribosome In Vivo,” Molecular and Cellular Biology 29, 1626 (2009). (doi:10.1128/MCB.01718-08) 8.2.1
  29. Wiedenheft, B.A., K.-J. Zhou, M. Jinek, S.M. Coyle, W. Ma, and J.A. Doudna, “Structural basis for DNase activity of a conserved protein implicated in CRISPR-mediated genome defense.,” Structure 17, 904 (2009). (doi:10.1016/j.str.2009.03.019) 8.2.2
  30. Ke, A., J.D. Batchelor, and J.A. Doudna, “Structural Roles of Monovalent Cations in the HDV Ribozyme,” Structure 15, 281 (2007). (doi:10.1016/j.str.2007.01.017) 8.2.1
  31. MacRae, I., and J.A. Doudna, “An unusual case of pseudo-merohedral twinning in orthorhombic crystals of Dicer,” Acta Crystallographica, Section D: Structural Biology 63, 993 (2007). (doi:10.1107/S0907444907036128) 8.2.1, 8.2.2
  32. MacRae, I., K.-J. Zhou, F. Lei, A. Repic, A.N. Brooks, W.Z. Cande, P.D. Adams, and J.A. Doudna, “Structural Basis for Double-Stranded RNA Processing by Dicer,” Science 311, 195 (2006). (doi:10.1126/science.1121638) 8.2.1, 8.2.2, 8.3.1
    Highlight: First Detailed Look at RNA Dicer
  33. Ke, A., K.-J. Zhou, J.H. Cate, and J.A. Doudna, “A conformational switch controls hepatitis delta virus ribozyme catalysis,” Nature 429, 201 (2004). (doi:10.1038/nature02522) 8.3.1, 8.2.2, 8.2.1
    Highlight: Snapshots of Ribozyme Reaction States Reveal Structural Switch
  34. Batey, R.T., M.B. Sagar, and J.A. Doudna, “Structural and energetic analysis of RNA recognition by a universally conserved protein from the signal recognition particle,” Journal of Molecular Biology 307, 229 (2001). (doi:10.1006/jmbi.2000.4454) 5.0.2
  35. Batey, R.T., R.P. Rambo, L. Lucast, B. Rha, and J.A. Doudna, “Crystal Structure of the Ribonucleoprotein Core of the Signal Recognition Particle,” Science 287, 1232 (2000). (doi:10.1126/science.287.5456.1232) 5.0.2