Select Publications

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, 

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),

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).

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).

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:

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.

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