{"id":155,"date":"2023-08-03T19:05:05","date_gmt":"2023-08-04T02:05:05","guid":{"rendered":"https:\/\/live-usc-dornsife.pantheonsite.io\/xj-chen-lab\/?page_id=155"},"modified":"2023-10-27T11:08:45","modified_gmt":"2023-10-27T18:08:45","slug":"publications","status":"publish","type":"page","link":"https:\/\/dornsife.usc.edu\/xiaojiang_chen-lab\/publications\/","title":{"rendered":"Featured Publications"},"content":{"rendered":"\n\n \n \n\n\n\n\n\n\n\n
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  1. Ito F, Alvarez A, Liu S, Zhou H, Chen XS. Structural basis of HIV-1 Vif mediated E3 ligase targeting of host APOBEC3H.\u00a0 Nature Comm<\/em><\/strong>.<\/em> 14(1):5241. PMCID: PMC10462622. DOI: 10.1038\/s41467-023-40955-x.<\/li>\n
  2. Ito F, Alvarez A, Liu S, Yang H, Shiriaeva A, Zhou H, Chen XS. Structural basis for HIV-1 antagonism of host APOBEC3G via Cullin E3 ligase. Science Adv<\/em><\/strong> 2023, Vol\u00a09 (1) 1-12 doi: 10.1126\/sciadv.ade316<\/li>\n
  3. Kim K, Calabrese P, Wang S, Qin C, Rao Y, Feng P, Chen XS. The roles of APOBEC-mediated RNA editing in SARS-CoV-2 mutations, replication, and fitness. Scientific Reports<\/em><\/strong> 2022 Sep 13;12(1):14972. doi: 10.1038\/s41598-022-19067-x. PMID: 36100631; PMCID: PMC9470679.<\/li>\n
  4. Yang H, Kim K, Li S, Pacheco J, Chen XS. Structural basis of sequence-specific RNA recognition by the antiviral factor APOBEC3G. Nature Comm.<\/em> <\/strong>2022, 13, 7498. doi.org\/10.1038\/s41467-022-35201-9<\/li>\n
  5. Chandramouly G, Zhao J, McDevitt S, Rusanov T, Hoang T, Borisonnik N, Treddinick T, Lopezcolorado FW, Kent T, Siddique LA, Mallon J, Huhn J, Shoda Z, Kashkina E, Brambati A, Stark JM,\u00a0Chen XS,\u00a0Pomerantz RT. Pol\u03b8 reverse transcribes RNA and promotes RNA-templated DNA repair. Science Adv<\/em><\/strong>. 2021 Jun 11;7(24):eabf1771. doi: 10.1126\/sciadv.abf1771.<\/li>\n
  6. Yang, H., Ito, F., Wolfe, A., Li, S., Love, R.P., Yan, M., Gaba, A., Chelico, L. and Chen, X.S. Structural Basis of Domain Organization, Dimerization, RNA binding, and HIV-1 Restriction of Full Length APOBEC3G. Nature Comm.<\/em><\/strong> 11(1):632. (2020). PMID: 32005813. PMCID: PMC6994475, DOI: 10.1038\/s41467-020-14377-y<\/li>\n
  7. Wolfe, A., Goedderz, C. and Chen, X.S. The structure of APOBEC1 and insights into RNA and DNA substrate selectivity. NAR Cancer<\/em><\/strong>, 2020 Dec;2(4):zcaa027. doi: 10.1093\/narcan\/zcaa027.<\/li>\n
  8. Schlierf M, Wang G, Chen XS, Ha T. Hexameric helicase G40P unwinds DNA in single base pair steps. Elife<\/em><\/strong>. 2019 Jan 28;8. pii: e42001. doi: 10.7554\/eLife.42001. PubMed PMID: 30688211; PubMed Central PMCID: PMC6370340<\/li>\n
  9. Xiao, X., Yang, H., Li., S, Chen, X. S. \u00a0Structure\/Function of N-Terminal Domain of a Primate APOBEC3G: Interplay of DNA Binding, Oligomerization and HIV Targeting of APOBEC3G.\u00a0 Nature Commun.<\/em><\/strong> 2016 Aug 2;7:12193.<\/li>\n
  10. Fu Y, Ito F, Zhang G, Fernandez B, Yang H, Chen X. DNA cytosine and methylcytosine deamination by APOBEC3B: enhancing methylcytosine deamination by engineering APOBEC3B.\u00a0 Biochem J.<\/em><\/strong> 2015 Oct 1;471(1):25-35.<\/li>\n
  11. Yu, J., et al., Mechanism of Subunit Coordination of An AAA+ Hexameric Molecular Nanomachine. Nanomedicine<\/em><\/strong>. 2015 Apr;11(3):531-41. doi: 10.1016\/j.nano.2014.11.005.<\/li>\n
  12. Chang Y, Xu M, Machado C, Yu X, Rohs R, Chen XS Origin DNA Recognition by the SV40 Large Tumor Antigen: Insights into the Mechanism of Initiator Assembly Cell Reports<\/em><\/strong>\u00a0 2013, 3(4):1117-27<\/li>\n
  13. Liu H, Shi Y, Chen X,\u00a0 Warshel A.\u00a0\u00a0 Simulating the electrostatic guidance of the vectorial translocations in hexameric helicases and translocases.\u00a0 PNAS<\/em><\/strong>. (2009) 106(18):7449-54.<\/li>\n
  14. Shi Y, Liu H, Gai D, Ma JP, Chen X A Computational Analysis of ATP Binding of SV40 Large Tumor Antigen Helicase Motor\u00a0\u00a0 PloS Computational Biol<\/em><\/strong>, 2009, 5 (9) 1-13<\/li>\n
  15. Holden L, Prochnow C, Chang YP, Bransteitter R, Stevens R, Goodman M, Chen X.\u00a0 Structure of the Anti-Viral APOBEC3G Catalytic Domain and Functional Implications,\u00a0\u00a0\u00a0 NATURE<\/em><\/strong>,\u00a0 (2008), 6;456(7218):121-4.<\/li>\n
  16. Brewster A, Wang G, Yu X, Greenleaf W, Carazo JM, Tjajadi M, Klein M, Chen X. Crystal structure of a near-full-length archaeal MCM: functional insights for an AAA+ hexameric helicase. PNAS<\/em><\/strong>\u00a0 (2008), 105(51):20191-6.<\/li>\n
  17. Wang G, Klein MG, Tokonzaba E, Zhang Y, Holden LG, Chen X. The structure of a DnaB-family replicative helicase and its interactions with primase.\u00a0 NATURE\u00a0 STUCT MOL. BIOL.<\/em><\/strong> (2008)\u00a0 15:94-100.<\/li>\n
  18. Prochnow C, Bransteitter R, Klein M, Goodman M, Chen X. The APOBEC-2 crystal structure and functional implications for the deaminase AID. NATURE<\/em><\/strong>. (2007) 25;445(7126):447-51<\/li>\n
  19. Lilyestrom W, Klein M, Zhang R, Joachimiak A, Chen X. Crystal structure of SV40 large T-antigen bound to p53: interplay between a viral oncoprotein and a cellular tumor suppressor. GENES & DEV<\/em><\/strong>. (2006) 20(17):2373-82.<\/li>\n
  20. Szakonyi G, Klein M, Hannan J, Young K, Ma R, Asokan R, Holers M, Chen X. Structure of The Epstein Barr Virus Major Envelope Glycoprotein NATURE STUCT MOL. BIOL<\/em><\/strong>.<\/em> (2006) 13:996-1001<\/li>\n
  21. Gai, D. Zhao, R. Li, D. Finkielstein,C.V. and Chen, X.\u00a0\u00a0\u00a0 \u00a0\u00a0The Mechanisms of Conformational Change for A Replicative Hexameric Helicase of SV40 Large T Antigen.\u00a0\u00a0 CELL<\/em><\/strong>\u00a0\u00a0 (2004) 119:47-60<\/li>\n
  22. Sclafani, Robert. Fletcher, C. Ryan.\u00a0 and\u00a0 Chen, X.\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0\u00a0 Two Heads Are Better Than One: Regulation of DNA replication by double-hexameric replicative helicases\u00a0\u00a0\u00a0\u00a0 GENES & DEV.<\/em><\/strong>\u00a0 (2004) 18:2039-2045.<\/li>\n
  23. Li, D. Zhao,R. Lilyestrom,W. Gai,D. Zhang,R. Fanning,E. Szakonyi,G and Chen, X.\u00a0\u00a0\u00a0 The Structure of the Hexameri Replicative Helicase of SV40 Large Tumor antigen.\u00a0\u00a0\u00a0\u00a0 NATURE<\/em><\/strong>.\u00a0 (2003) 423, 512-518<\/li>\n
  24. Fletcher R. J, Bishop B. E, Leon R. P, Sclafani R. A, Ogata C. M, Chen X.\u00a0\u00a0\u00a0\u00a0\u00a0 The structure and function of the MCM complex from archaeal M. Thermoautotrophicum.\u00a0 NATURE\u00a0\u00a0 BIOL. <\/em><\/strong>\u00a0(2003)\u00a0 10,160-167<\/li>\n
  25. Boackle S, Holers M, Chen X,\u00a0 <\/strong>Szakonyi G, Karp D, Wakeland E and Morel L.\u00a0\u00a0 Cr2, a gene in the NZM2410 Sle1c lupus susceptibility locus, encodes a dysfunctional protein.\u00a0 IMMUNITY<\/em><\/strong>,\u00a0 (2001) 15, 729-738.<\/li>\n
  26. Szakonyi G., Guthridge J., Li D., Young J. K., Holers M., Chen X.\u00a0\u00a0\u00a0\u00a0 Structure of Complement Receptor Type 2 (CR2\/CD21) in Complex with Its Cellular\u00a0 Ligand C3d.\u00a0\u00a0\u00a0 SCIENCE<\/em><\/strong>\u00a0\u00a0 (2001)\u00a0 292,\u00a0\u00a0 1725-1728<\/li>\n<\/ol>\n\n\n\n<\/div>\n\n\n <\/div><\/div>\n","protected":false},"excerpt":{"rendered":"","protected":false},"author":9,"featured_media":0,"parent":0,"menu_order":0,"comment_status":"closed","ping_status":"closed","template":"page-content-detail.php","meta":{"_acf_changed":false,"footnotes":""},"class_list":["post-155","page","type-page","status-publish","hentry"],"acf":[],"yoast_head":"\nFeatured Publications - Xiaojiang Chen lab<\/title>\n<meta name=\"robots\" content=\"index, follow, max-snippet:-1, max-image-preview:large, max-video-preview:-1\" \/>\n<link rel=\"canonical\" href=\"https:\/\/dornsife.usc.edu\/xiaojiang_chen-lab\/publications\/\" \/>\n<meta property=\"og:locale\" content=\"en_US\" \/>\n<meta property=\"og:type\" content=\"article\" \/>\n<meta property=\"og:title\" content=\"Featured Publications - 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