Select Publications
Xiao, R., Hoffmann, F. T., Xie, D., Wiegand, T., Palmieri, A. I., Sternberg, S. H., & Chang, L. (2026). Structural basis of RNA-guided transcription by a dCas12f-σE-RNAP complex. Nature, 653, 288–296.
Hoffmann, F. T., Wiegand, T., Palmieri, A. I., Glass-Klaiber, J., Xiao, R., Tang, S., Le, H. C., Meers, C., Lampe, G. D., Chang, L., & Sternberg, S. H. (2026). Exapted CRISPR–Cas12f homologues drive RNA-guided transcription. Nature, 653, 277–287.
Wang, S., & Chang, L. (2025). Biochemical reconstitution of a type I-B CRISPR-associated transposon. Methods in Enzymology, 712, 55–79.
Kenny, S., Iyer, S., Gabel, C. A., Tegenfeldt, N., DeMarco, A. G., Hall, M. C., Chang, L., Davisson, V. J., Vande Pol, S., & Das, C. (2025). Structure of E6AP in complex with HPV16-E6 and p53 reveals a novel ordered domain important for E3 ligase activation. Structure, 33(3), 504–516.e4.
Wang, S., Siddique, R., Hall, M. C., Rice, P. A., & Chang, L. (2024). Structure of TnsABCD transpososome reveals mechanisms of targeted DNA transposition. Cell, 187(24), 6865–6881.e16.
Höfler, A., Yu, J., Yang, J., Zhang, Z., Chang, L., McLaughlin, S. H., Grime, G. W., Garman, E. F., Boland, A., & Barford, D. (2024). Cryo-EM structures of apo-APC/C and APC/CCDH1:EMI1 complexes provide insights into APC/C regulation. Nature Communications, 15, 10074.
Chang, L. (2023). OAT1 structures reveal insights into drug transport in the kidney. Nature Structural & Molecular Biology, 30(11), 1615–1617.
Wang, S., Gabel, C., Siddique, R., Klose, T., & Chang, L. (2023). Molecular mechanism for Tn7-like transposon recruitment by a type I-B CRISPR effector. Cell, 186(19), 4204–4215.e19.
Gabel, C. A., Li, Z., DeMarco, A. G., Zhang, Z., Yang, J., Hall, M. C., Barford, D., & Chang, L. (2022). Molecular architecture of the augmin complex. Nature Communications, 13(1), 1-13.
Mukherjee, I.A., Gabel, C., Noinaj, N., Bondy-Denomy, J., & Chang, L. (2022) Structural basis of AcrIF24 as an anti-CRISPR protein and transcriptional suppressor. Nat Chem Biol, https://doi.org/10.1038/s41589-022-01137-w
Xiao, R., Wang, S., Han, R., Li, Z., Gabel, C., Mukherjee, I. A., & Chang, L. (2021). Structural basis of target DNA recognition by CRISPR-Cas12k for RNA-guided DNA transposition. Molecular Cell, 81(21), 4457-4466.
Xiao, R., Li, Z., Wang, S., Han, R., & Chang, L. (2021). Structural basis for substrate recognition and cleavage by the dimerization-dependent CRISPR–Cas12f nuclease. Nucleic acids research, 49(7), 4120-4128.
Li, Z., Zhang, H., Xiao, R., Han, R., & L. Chang. Cryo-EM structure of the RNA-guided ribonuclease Cas12g. Nature Chemical Biology, 1-7 (2021), https://doi.org/10.1038/s41589-020-00721-2
Gabel, C., Li, Z., Zhang, H., & Chang, L. (2021). Structural basis for inhibition of the type IF CRISPR–Cas surveillance complex by AcrIF4, AcrIF7 and AcrIF14. Nucleic Acids Research, 49(1), 584-594.
Zhang, H., Li, Z., Xiao, R., and L. Chang. Mechanisms for target recognition and cleavage by the Cas12i RNA-guided endonuclease. Nat Struct Mol Biol 27, 1069–1076 (2020). https://doi.org/10.1038/s41594-020-0499-0
Chang, L., Yang, J., Jo, C.H. et al. Structure of the DOCK2−ELMO1 complex provides insights into regulation of the auto-inhibited state. Nat Commun 11, 3464 (2020). https://doi.org/10.1038/s41467-020-17271-9
Li, Zhuang, Heng Zhang, Renjian Xiao, and Leifu Chang. Cryo-EM structure of a type IF CRISPR RNA guided surveillance complex bound to transposition protein TniQ. Cell Research (2020): 1-3.
Zhang, H. et al. Structural Basis for the Inhibition of CRISPR-Cas12a by Anti-CRISPR Proteins. Cell Host Microbe (2019). doi:https://doi.org/10.1016/j.chom.2019.05.004
C. Alfieri, L. Chang, and D. Barford, Mechanism for remodelling of the cell cycle checkpoint protein MAD2 by the ATPase TRIP13, Nature (2018): 1.
C. Alfieri, L. Chang, Z. Zhang, J. Yang, S. Maslen, M Skehel and D. Barford, Structural basis of APC/C regulation by the spindle assembly checkpoint, Nature, 536 (2016) 431-436.
S. Zhang, L. Chang, C. Alfieri, Z. Zhang, J. Yang, S. Maslen, M Skehel and D. Barford, Molecular mechanism of APC/C activation by mitotic phosphorylation, Nature, 533 (2016) 260-264.
L. Chang, Z. Zhang, J. Yang, S.H. McLaughlin, D. Barford, Atomic structure of the APC/C and its mechanism of protein ubiquitination, Nature, 522 (2015) 450-454.
L. Chang, X. Liu*, Y. Li, C.C. Liu, F. Yang, J. Zhao and S.F. Sui, Structural organisation of an intact phycobilisome and its association with photosystem II, Cell research, 25 (2015) 726-737
L. Chang, D. Barford, Insights into the anaphase-promoting complex: a molecular machine that regulates mitosis, Current opinion in structural biology, 29C (2014) 1-9.
L. Chang, Z. Zhang, J. Yang, S.H. McLaughlin, D. Barford, Molecular architecture and mechanism of the anaphase-promoting complex, Nature, 513 (2014) 388-393.
L.F. Chang, S. Chen, C.C. Liu, X. Pan, J. Jiang, X.C. Bai, X. Xie, H.W. Wang, S.F. Sui, Structural characterization of full-length NSF and 20S particles, Nature structural & molecular biology, 19 (2012) 268-275.