selected recent PUBLICATIONS

  1. Alam, S. K., Zhang, Y., Wang, L., & Zhu, Z. et al. (2022). DARPP-32 promotes ERBB3-mediated resistance to molecular targeted therapy in EGFR-mutated lung adenocarcinoma. Oncogene, 41(1), 83-98. https://doi.org/10.1038/s41388-021-02028-5
  2. Banales, J. M., Marin, J. J. G., Lamarca, A., & Rodrigues, P. M. et al. (2020). Cholangiocarcinoma 2020: the next horizon in mechanisms and management. Nature Reviews Gastroenterology and Hepatology, 17(9), 557-588. https://doi.org/10.1038/s41575-020-0310-z
  3. Bhatt, V., Shi, K., Salamango, D. J., & Moeller, N. H. et al. (2020). Structural basis of host protein hijacking in human T-cell leukemia virus integration. Nature Communications, 11(1), Article 3121. https://doi.org/10.1038/s41467-020-16963-6
  4. Caballero-Camino, F. J., Rivilla, I., Herraez, E., & Briz, O. et al. (2020). Synthetic Conjugates of Ursodeoxycholic Acid Inhibit Cystogenesis in Experimental Models of Polycystic Liver Disease. Hepatology, 73(1), 186-203. https://doi.org/10.1002/hep.31216
  5. CCA Model Consortium (2023). Criteria for preclinical models of cholangiocarcinoma: scientific and medical relevance. Nature Reviews Gastroenterology and Hepatology, 20(7), 462-480. https://doi.org/10.1038/s41575-022-00739-y
  6. Che, M., Chaturvedi, A., Munro, S. A., & Pitzen, S. P. et al. (2021). Opposing transcriptional programs of KLF5 and AR emerge during therapy for advanced prostate cancer. Nature Communications, 12(1), Article 6377. https://doi.org/10.1038/s41467-021-26612-1
  7. Dou, L., Yan, F., Pang, J., & Zheng, D. et al. (2019). Protein lysine 43 methylation by EZH1 promotes AML1-ETO transcriptional repression in leukemia. Nature Communications, 10(1), Article 5051. https://doi.org/10.1038/s41467-019-12960-6
  8. Du, Y., Han, M., Cao, K., & Li, Q. et al. (2021). Gold Nanorods Exhibit Intrinsic Therapeutic Activity via Controlling N6-Methyladenosine-Based Epitranscriptomics in Acute Myeloid Leukemia. ACS Nano, 15(11), 17689- 17704. https://doi.org/10.1021/acsnano.1c05547
  9. Fan, M., Xia, P., Clarke, R. R., & Wang, Y. et al. (2020). Radiogenomic signatures reveal multiscale intratumour heterogeneity associated with biological functions and survival in breast cancer. Nature Communications, 11(1), Article 4861. https://doi.org/10.1038/s41467-020-18703-2
  10. Ferrari, M. G., Jimenez-Uribe, A. P., Wang, L., & Hoeppner, L. H. et al. (2024). Myeloid differentiation factor-2/LY96, a potential predictive biomarker of metastasis and poor outcomes in prostate cancer: clinical implications as a potential therapeutic target. Oncogene, 43(7), 484-494. https://doi.org/10.1038/s41388-023-02925-x
  11. Heltemes-Harris, L. M., Hubbard, G. K., LaRue, R. S., & Munro, S. A. et al. (2021). Identification of mutations that cooperate with defects in B cell transcription factors to initiate leukemia. Oncogene, 40(43), 6166-6179. https://doi.org/10.1038/s41388-021-02012-z
  12. Hu, Y., & Liu, B. (2022). Roles of zinc-binding domain of bacterial RNA polymerase in transcription. Trends in Biochemical Sciences, 47(8), 710-724. https://doi.org/10.1016/j.tibs.2022.03.007
  13. Karri, S., Yang, Y., Zhou, J., & Dickinson, Q. et al. (2024). Defective transfer of parental histone decreases frequency of homologous recombination by increasing free histone pools in budding yeast. Nucleic Acids Research, 52(9), 5138-5151. https://doi.org/10.1093/nar/gkae205
  14. Kim-Holzapfel, D. M., Dey, R., Richardson, B. C., & Arachchige, D. et al. (2023). Human uridine 5′-monophosphate synthase stores metabolic potential in inactive biomolecular condensates. Journal of Biological Chemistry, 299(3), Article 102949. https://doi.org/10.1016/j.jbc.2023.102949
  15. Klionsky, D. J., Abdel-Aziz, A. K., Abdelfatah, S., & Abdellatif, M. et al. (2021). Guidelines for the use and interpretation of assays for monitoring autophagy (4th edition). Autophagy, 17(1), 1-382 (several HI authors contributed). https://doi.org/10.1080/15548627.2020.1797280
  16. Kompaniiets, D., He, L., Wang, D., & Zhou, W. et al. (2024). Structural basis for transcription activation by the nitrate-responsive regulator NarL. Nucleic Acids Research, 52(3), 1471-1482. https://doi.org/10.1093/nar/gkad1231
  17. Korangath, P., Jin, L., Yang, C. T., & Healy, S. et al. (2024). Iron Oxide Nanoparticles Inhibit Tumor Progression and Suppress Lung Metastases in Mouse Models of Breast Cancer. ACS Nano, 18(15), 10509-10526. https://doi.org/10.1021/acsnano.3c12064
  18. Kwak, G., Gololobova, O., Sharma, N., & Caine, C. et al. (2023). Extracellular vesicles enhance pulmonary transduction of stably associated adenoassociated virus following intratracheal administration. Journal of Extracellular Vesicles, 12(6), Article 12324. https://doi.org/10.1002/jev2.12324
  19. Le, L. T. M., Thompson, J. R., Dehghani-Ghahnaviyeh, S., & Pant, S. et al. (2023). Cryo-EM structures of human ABCA7 provide insights into its phospholipid translocation mechanisms. EMBO Journal, 42(3), Article e111065. https://doi.org/10.15252/embj.2022111065
  20. Li, Y., Yang, R., Henzler, C. M., & Ho, Y. et al. (2020). Diverse AR gene rearrangements mediate resistance to androgen receptor inhibitors in metastatic prostate cancer. Clinical Cancer Research, 26(8), 1965-1976. https://doi.org/10.1158/1078-0432.CCR-19-3023
  21. Liu, C., Shi, W., Becker, S. T., & Schatz, D. G. et al. (2021). Structural basis of mismatch recognition by a SARS-CoV-2 proofreading enzyme. Science, 373(6559), 1142-1146. https://doi.org/10.1126/science.abi9310
  22. Nelson, A. C., Turbyville, T. J., Dharmaiah, S., & Rigby, M. et al. (2020). RAS internal tandem duplication disrupts GTPase-activating protein (GAP) binding to activate oncogenic signaling. Journal of Biological Chemistry, 295(28), 9335-9348. https://doi.org/10.1074/jbc.RA119.011080
  23. Nosol, K., Romane, K., Irobalieva, R. N., & Alam, A. et al. (2020). Cryo-EM structures reveal distinct mechanisms of inhibition of the human multidrug transporter ABCB1. Proceedings of the National Academy of Sciences of the United States of America, 117(42), 26245-26253. https://doi.org/10.1073/pnas.2010264117
  24. Olsen, J. A., Alam, A., Kowal, J., & Stieger, B. et al. (2020). Structure of the human lipid exporter ABCB4 in a lipid environment. Nature Structural and Molecular Biology, 27(1), 62-70. https://doi.org/10.1038/s41594-019-0354-3
  25. O'Sullivan, C. C., Clarke, R., Goetz, M. P., & Robertson, J. (2023). Cyclin- Dependent Kinase 4/6 Inhibitors for Treatment of Hormone Receptor-Positive, ERBB2-Negative Breast Cancer: A Review. JAMA Oncology, 9(9), 1273-1282. https://doi.org/10.1001/jamaoncol.2023.2000
  26. Pant, K., Peixoto, E., Richard, S., & Biswas, A. S. et al. (2021). Histone Deacetylase SIRT1 promotes loss of primary cilia in Cholangiocarcinoma. Hepatology, 74(6), 3235-3248. https://doi.org/10.1002/hep.32080
  27. Paul, S., Kaplan, M. H., Khanna, D., & McCourt, P. M. et al. (2022). Centromere defects, chromosome instability, and cGAS-STING activation in systemic sclerosis. Nature Communications, 13(1), Article 7074.https://doi.org/10.1038/s41467-022-34775-8
  28. Gao, J., Wei, B., Liu, M., & Hirsova, P. et al. (2021). Portal Hypertension and Hepatic Fibrosis Through C-C Motif Chemokine Ligand 2–Mediated Angiocrine Signaling. Hepatology, 73(6), 2468-2483. https://doi.org/10.1002/hep.31617
  29. Saha, A. K., Contreras-Galindo, R., Niknafs, Y. S., & Iyer, M. et al. (2020). The role of the histone H3 variant CENPA in prostate cancer. Journal of Biological Chemistry, 295(25), 8537-8549. https://doi.org/10.1074/jbc.RA119.010080
  30. Serra-Cardona, A., Yu, C., Zhang, X., & Hua, X. et al. (2021). A mechanism for Rad53 to couple leading- And lagging-strand DNA synthesis under replication stress in budding yeast. Proceedings of the National Academy of Sciences of the United States of America, 118(38), Article e2109334118. https://doi.org/10.1073/pnas.2109334118
  31. Shi, W., Zhou, W., Chen, M., & Yang, Y. et al. (2021). Structural basis for activation of Swi2/Snf2 ATPase RapA by RNA polymerase. Nucleic Acids Research, 49(18), 10707-10716. https://doi.org/10.1093/nar/gkab744
  32. Shi, W., Zhou, W., Zhang, B., & Huang, S. et al. (2020). Structural basis of bacterial σ28-mediated transcription reveals roles of the RNA polymerase zinc binding domain. EMBO Journal, 39(14), Article e104389. https://doi.org/10.15252/embj.2020104389
  33. Sperger, J. M., Helzer, K. T., Stahlfeld, C. N., & Jiang, D. et al. (2023). Expression and Therapeutic Targeting of TROP-2 in Treatment-Resistant Prostate Cancer. Clinical Cancer Research, 29(12), 2324-2335. https://doi.org/10.1158/1078-0432.CCR-22-1305
  34. Tian, C., Zhang, Q., Jia, J., & Zhou, J. et al. (2024). DNA polymerase delta governs parental histone transfer to DNA replication lagging strand. Proceedings of the National Academy of Sciences of the United States of America, 121(20), Article e2400610121. https://doi.org/10.1073/pnas.2400610121
  35. Tian, C., Zhou, J., Li, X., & Gao, Y. et al. (2023). Impaired histone inheritance promotes tumor progression. Nature Communications, 14(1), Article 3429. https://doi.org/10.1038/s41467-023-39185-y
  36. Wang, Q., Morris, R. J., Bode, A. M., & Zhang, T. (2022). Prostaglandin Pathways: Opportunities for Cancer Prevention and Therapy. Cancer Research, 82(6), 949-965. https://doi.org/10.1158/0008-5472.CAN-21-2297
  37. Wang, T. Y., Liu, Q., Ren, Y., & Alam, S. K. et al. (2021). A pan-cancer transcriptome analysis of exitron splicing identifies novel cancer driver genes and neoepitopes. Molecular Cell, 81(10), 2246-2260.e12. https://doi.org/10.1016/j.molcel.2021.03.028
  38. Wang, Y., Hoeppner, L. H., Angom, R. S., & Wang, E. et al. (2019). Protein kinase D up-regulates transcription of VEGF receptor-2 in endothelial cells by suppressing nuclear localization of the transcription factor AP2β. Journal of Biological Chemistry, 294(43), 15759-15767. https://doi.org/10.1074/jbc.RA119.010152
  39. Wang, Y., Tu, K., Liu, D., & Guo, L. et al. (2019). p300 Acetyltransferase Is a Cytoplasm-to-Nucleus Shuttle for SMAD2/3 and TAZ Nuclear Transport in Transforming Growth Factor β–Stimulated Hepatic Stellate Cells. Hepatology, 70(4), 1409-1423. https://doi.org/10.1002/hep.30668
  40. Yang, F., Hilakivi-Clarke, L., Shaha, A., & Wang, Y. et al. (2023). Metabolic reprogramming and its clinical implication for liver cancer. Hepatology, 78(5), 1602-1624. https://doi.org/10.1097/HEP.0000000000000005
  41. Yang, Y., Liu, C., Zhou, W., & Shi, W. et al. (2021). Structural visualization of transcription activated by a multidrug-sensing MerR family regulator. Nature Communications, 12(1), Article 2702. https://doi.org/10.1038/s41467-021-22990-8
  42. Ye, G., Liu, B., & Li, F. (2022). Cryo-EM structure of a SARS-CoV-2 omicron spike protein ectodomain. Nature Communications, 13(1), 1214. Article 1214. https://doi.org/10.1038/s41467-022-28882-9
  43. Ye, J., Chen, H., Wang, K., & Wang, Y. et al. (2024). Structural insights into vesicular monoamine storage and drug interactions. Nature, 629(8010), 235- 243. https://doi.org/10.1038/s41586-024-07290-7
  44. Zhang, L., Nesvick, C. L., Day, C. A., & Choi, J. et al. (2022). STAT3 is a biologically relevant therapeutic target in H3K27M-mutant diffuse midline glioma. Neuro-Oncology, 24(10), 1700-1711. https://doi.org/10.1093/neuonc/noac093
  45. Zhao, S. G., Chen, W. S., Li, H., & Foye, A. et al. (2020). The DNA methylation landscape of advanced prostate cancer. Nature Genetics, 52(8), 778-789. https://doi.org/10.1038/s41588-020-0648-8