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Northwestern University Feinberg School of Medicine
Ito Lab

Publications

Learn more about the work that we do in the Ito Lab through our recent publications.

  1. Ito F, Li Z, Minakhin L, et al. Structural basis for Polθ-helicase DNA binding and microhomology-mediated end-joining. Nat Commun. 2025;16,3725. https://doi.org/10.1038/s41467-025-58441-x
  2. Ito F, Zhen J, Xie G, Huang H, Silva JC, Wu T, Zhou ZH. Structure of the Kaposi’s sarcoma-associated herpesvirus gB in post-fusion conformation. J Virol. 2025;99:e01533-24. https://doi.org/10.1128/jvi.01533-24
  3. Yang H, Pacheco J, Kim K, et al. Molecular mechanism for regulating APOBEC3G DNA editing function by the non-catalytic domain. Nat Commun. 2024;15,8773. https://doi.org/10.1038/s41467-024-52671-1
  4. Ito F, Li Z, Minakhin L, et al. Structural basis for a Polθ helicase small-molecule inhibitor revealed by cryo-EM. Nat Commun. 2024;15,7003. https://doi.org/10.1038/s41467-024-51351-4
  5. Ito F, Yang H, Zhou ZH, Chen XS. Structural basis for polyuridine tract recognition by SARS-CoV-2 Nsp15. Protein & Cell. 2024;15,7,547–552. https://doi.org/10.1093/procel/pwae009
  6. Ito F, Alvarez-Cabrera AL, Kim, K, et al. Structural basis of HIV-1 Vif-mediated E3 ligase targeting of host APOBEC3H. Nat Commun. 2023;14,5241. https://doi.org/10.1038/s41467-023-40955-x
  7. Ito F, Alvarez-Cabrera AL, Liu S. Structural basis for HIV-1 antagonism of host APOBEC3G via Cullin E3 ligase. Sci Adv. 2023;9,eade3168. doi:10.1126/sciadv.ade3168
  8. Yang H, Ito F, Wolfe AD, et al. Understanding the structural basis of HIV-1 restriction by the full length double-domain APOBEC3G. Nat Commun. 2020;11,632. https://doi.org/10.1038/s41467-020-14377-y
  9. Ito, F., Yang, H., Xiao, X, et al. Understanding the Structure, Multimerization, Subcellular Localization and mC Selectivity of a Genomic Mutator and Anti-HIV Factor APOBEC3H. Sci Rep. 2018;8,3763. https://doi.org/10.1038/s41598-018-21955-0
  10. Ito F, Fu Y, Kao SA, Yang H, Chen XS. Family-Wide Comparative Analysis of Cytidine and Methylcytidine Deamination by Eleven Human APOBEC Proteins. J Mol Biol. 2017;429(12):1787–99. pmid:28479091; PubMed Central PMCID: PMC5530319.
  11. Gu J, Chen Q, Xiao X, Ito F, Wolfe A, Chen XS. Biochemical characterization of APOBEC3H variants: implications for their HIV-1 restriction activity and mC modification. J Mol Biol. 2016;428,4626-4638.
  12. Fu Y, Ito F, Zhang G, Fernandez B, Yang H, Chen XS. DNA cytosine and methylcytosine deamination by APOBEC3B: enhancing methylcytosine deamination by engineering APOBEC3B. Biochem J. 2015;471(1):25–35. doi: https://doi.org/10.1042/BJ20150382