Photo of Sun Hur,  PhD

Sun Hur, PhD

Boston Children's Hospital

Boston Children's Hospital
Phone: (617) 713-8250
Fax: (617) 713-8260


Sun.Hur@crystal.harvard.edu

Sun Hur, PhD

Boston Children's Hospital

EDUCATIONAL TITLES

  • Professor, Biological Chemistry and Molecular Pharmacology, Harvard Medical School

DF/HCC PROGRAM AFFILIATION

Research Abstract

My lab studies structural and biochemical mechanisms of antiviral immunity. Over the last several years, we defined the molecular mechanisms of the RIG-I-like receptors, which are conserved viral RNA sensors in the vertebrate innate immune system. They are cytosolic receptors responsible for detecting viral RNAs during infection and activating the type I interferon (IFN) response. While their functions are best characterized in the context of antiviral immunity, more recent studies showed that these receptors and the downstream IFN pathways are activated during conventional cancer therapies (such as chemotherapy, and radiation therapy) and their activities play important roles in effective cancer immunotherapies. Our current interest includes defining the mechanism by which chemo- and radiation therapies activate these receptors and developing small molecules that can specifically modulate their signaling functions for therapeutic application.

Publications from Harvard Catalyst Profiles

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  • Huoh YS, Hur S. Death domain fold proteins in immune signaling and transcriptional regulation. FEBS J 2021. PubMed
  • Wang HT, Hur S. Substrate recognition by TRIM and TRIM-like proteins in innate immunity. Semin Cell Dev Biol 2021; 111:76-85. PubMed
  • Ahmad S, Mu X, Hur S. The Role of RNA Editing in the Immune Response. Methods Mol Biol 2021; 2181:287-307. PubMed
  • Kato K, Ahmad S, Zhu Z, Young JM, Mu X, Park S, Malik HS, Hur S. Structural analysis of RIG-I-like receptors reveals ancient rules of engagement between diverse RNA helicases and TRIM ubiquitin ligases. Mol Cell 2021; 81:599-613.e8. PubMed
  • Huoh YS, Wu B, Park S, Yang D, Bansal K, Greenwald E, Wong WP, Mathis D, Hur S. Dual functions of Aire CARD multimerization in the transcriptional regulation of T cell tolerance. Nat Commun 2020; 11:1625. PubMed
  • Ablasser A, Hur S. Regulation of cGAS- and RLR-mediated immunity to nucleic acids. Nat Immunol 2020; 21:17-29. PubMed
  • Cadena C, Hur S. Filament-like Assemblies of Intracellular Nucleic Acid Sensors: Commonalities and Differences. Mol Cell 2019; 76:243-254. PubMed
  • Chen YG, Chen R, Ahmad S, Verma R, Kasturi SP, Amaya L, Broughton JP, Kim J, Cadena C, Pulendran B, Hur S, Chang HY. N6-Methyladenosine Modification Controls Circular RNA Immunity. Mol Cell 2019. PubMed
  • Cadena C, Ahmad S, Xavier A, Willemsen J, Park S, Park JW, Oh SW, Fujita T, Hou F, Binder M, Hur S. Ubiquitin-Dependent and -Independent Roles of E3 Ligase RIPLET in Innate Immunity. Cell 2019; 177:1187-1200.e16. PubMed
  • Hur S. Double-Stranded RNA Sensors and Modulators in Innate Immunity. Annu Rev Immunol 2019. PubMed
  • Mu X, Greenwald E, Ahmad S, Hur S. An origin of the immunogenicity of in vitro transcribed RNA. Nucleic Acids Res 2018; 46:5239-5249. PubMed
  • Ahmad S, Mu X, Yang F, Greenwald E, Park JW, Jacob E, Zhang CZ, Hur S. Breaching Self-Tolerance to Alu Duplex RNA Underlies MDA5-Mediated Inflammation. Cell 2018; 172:797-810.e13. PubMed
  • Abbott JK, Huoh YS, Reynolds PR, Yu L, Rewers M, Reddy M, Anderson MS, Hur S, Gelfand EW. Dominant-negative loss of function arises from a second, more frequent variant within the SAND domain of autoimmune regulator (AIRE). J Autoimmun 2018; 88:114-120. PubMed
  • Peisley A, Wu B, Xu H, Chen ZJ, Hur S. Structural basis for ubiquitin-mediated antiviral signal activation by RIG-I. Nature 2014; 509:110-4. PubMed
  • Wu B, Peisley A, Richards C, Yao H, Zeng X, Lin C, Chu F, Walz T, Hur S. Structural basis for dsRNA recognition, filament formation, and antiviral signal activation by MDA5. Cell 2013; 152:276-89. PubMed
  • 28. Cadena C, Ahmad S, Xavier A, Willemsen J, Park JW, Oh SW, Fujita T, Hou F, Binder M, and Hur S. Ubiquitin-dependent and –independent roles of E3 ligase RIPLET in innate immunity Cell .
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