ABOUT THE RESEARCHER

OVERVIEW

The Hur laboratory studies various protein-nucleic acid interactions involved in the vertebrate immune system. The lab uses a combination of structural biology, biochemistry and cell biology to understand molecule mechanisms of the following proteins.

Innate immune receptors involved in antiviral immune response :

  • pattern recognition receptors
  • antiviral immune response
  • auto-inflammatory disease
  • immuno-oncology application


Transcription factors involved in T cell development of self-tolerance

  • Transcription factors
  • T cell development of self-tolerance
  • Nuclear organization

BACKGROUND

Dr. Hur received her BS in physics from Ewha Women’s University in Korea in 2001, Ph.D. in physical chemistry with Dr. Thomas C. Bruice at the University of California, Santa Barbara in 2003 and did her post-doctoral work in X-ray crystallography with Dr. Robert M. Stroud at the University of California, San Francisco. Dr. Hur joined Harvard Medical School in 2008 as an assistant professor and joined Boston Children's Hospital in 2010. Dr. Hur is a recipient of the 2009 Massachusetts Life Sciences Young Investigator Award, the 2010 Pew Scholar Award, as well as the 2015 Vilcek Prize for Creative Promise in Biomedical Science, the 2015 Burroughs Wellcome Infectious Disease Investigator Award and the 2019 NIH Director's Pioneer award. In 2019, she was promoted to Professor in the department of Biological Chemistry and Molecular Pharmacology and department of Pediatrics at Harvard Medical School.

Selected Publications

  1. 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(5):1187-1200 PMID: 31006531
  2. Ahmad S*, Mu X*, Yang F*, Greenwald E, Park JW, Jacob E, Zhang C-Z and Hur S., Breaching self-tolerance to Alu duplex RNA underlies MDA5-mediated inflammation. Cell, (2018) 172:797-810. PMC5807104
  3. Yao H*, Dittmann M*, Peisley A, Hoffmann H-H, Gilmore RH, Schmidt T, Schmidt-Burgk J, Hornung V, Rice CM, and Hur S, ATP-dependent effector-like functions of RIG-I like receptors. Mol. Cell, (2015), 58:541-8. PMCID: PMC4427555
  4. Peisley A, Wu B, Xu H, Chen ZJ and Hur S., Structural basis for ubiquitin-mediated antiviral signal activation by RIG-I. Nature, (2014), 509:110-4. PMID: 24590070. PMC6136653.
  5. 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 signaling by MDA5. Cell (2013). 152: 276-89. Non-NIH Support.
  6. Peisley A*, Wu B*, Yao H, Walz T and Hur S., RIG-I forms signaling-competent filaments in an ATP-dependent and ubiquitin-independent manner. Mol Cell, (2013), 51, 573-83, PMID: 23993742
  7. Peisley A*, Jo MH*, Lin C, Wu B, Orme-Johnson M, Walz T, Hohng S, Hur S. Kinetic Mechanism for Viral dsRNA Length Discrimination by MDA5 Filament. Proc. Natl. Acad. Sci. U.S.A. (2012), 109(49):E3340-9. PMCID: PMC3523859
  8. Peisley, A., Lin, C., Wu, B., Orme-Johnson, M., Liu, M., Walz, T., Hur S. Cooperative Assembly and Dynamic Disassembly of MDA5 Filaments for Viral dsRNA Recognition. Proc. Natl. Acad. Sci. U.S.A. 2011, 108, 21010-5. PMCID: PMC3248507

PUBLICATIONS

Publications powered by Harvard Catalyst Profiles

  1. Death domain fold proteins in immune signaling and transcriptional regulation. FEBS J. 2021 Apr 27. View abstract
  2. The Role of RNA Editing in the Immune Response. Methods Mol Biol. 2021; 2181:287-307. View abstract
  3. Structural analysis of RIG-I-like receptors reveals ancient rules of engagement between diverse RNA helicases and TRIM ubiquitin ligases. Mol Cell. 2021 02 04; 81(3):599-613.e8. View abstract
  4. Substrate recognition by TRIM and TRIM-like proteins in innate immunity. Semin Cell Dev Biol. 2021 03; 111:76-85. View abstract
  5. Dual functions of Aire CARD multimerization in the transcriptional regulation of T cell tolerance. Nat Commun. 2020 04 02; 11(1):1625. View abstract
  6. Filament-like Assemblies of Intracellular Nucleic Acid Sensors: Commonalities and Differences. Mol Cell. 2019 10 17; 76(2):243-254. View abstract
  7. N6-Methyladenosine Modification Controls Circular RNA Immunity. Mol Cell. 2019 10 03; 76(1):96-109.e9. View abstract
  8. The FDA-Approved Oral Drug Nitazoxanide Amplifies Host Antiviral Responses and Inhibits Ebola Virus. iScience. 2019 Sep 27; 19:1279-1290. View abstract
  9. Ubiquitin-Dependent and -Independent Roles of E3 Ligase RIPLET in Innate Immunity. Cell. 2019 05 16; 177(5):1187-1200.e16. View abstract
  10. Double-Stranded RNA Sensors and Modulators in Innate Immunity. Annu Rev Immunol. 2019 04 26; 37:349-375. View abstract
  11. An origin of the immunogenicity of in vitro transcribed RNA. Nucleic Acids Res. 2018 06 01; 46(10):5239-5249. View abstract
  12. Breaching Self-Tolerance to Alu Duplex RNA Underlies MDA5-Mediated Inflammation. Cell. 2018 02 08; 172(4):797-810.e13. View abstract
  13. Antiviral Immunity and Circular RNA: No End in Sight. Mol Cell. 2017 Jul 20; 67(2):163-164. View abstract
  14. Filament assemblies in foreign nucleic acid sensors. Curr Opin Struct Biol. 2016 Apr; 37:134-44. View abstract
  15. Measuring Monomer-to-Filament Transition of MAVS as an In Vitro Activity Assay for RIG-I-Like Receptors. Methods Mol Biol. 2016; 1390:131-42. View abstract
  16. Helicases in Antiviral Immunity: Dual Properties as Sensors and Effectors. Trends Biochem Sci. 2015 Oct; 40(10):576-585. View abstract
  17. How RIG-I like receptors activate MAVS. Curr Opin Virol. 2015 Jun; 12:91-8. View abstract
  18. ATP-dependent effector-like functions of RIG-I-like receptors. Mol Cell. 2015 May 07; 58(3):541-548. View abstract
  19. MDA5-filament, dynamics and disease. Curr Opin Virol. 2015 Jun; 12:20-5. View abstract
  20. Molecular imprinting as a signal-activation mechanism of the viral RNA sensor RIG-I. Mol Cell. 2014 Aug 21; 55(4):511-23. View abstract
  21. Gain-of-function mutations in IFIH1 cause a spectrum of human disease phenotypes associated with upregulated type I interferon signaling. Nat Genet. 2014 May; 46(5):503-509. View abstract
  22. Structural basis for ubiquitin-mediated antiviral signal activation by RIG-I. Nature. 2014 May 01; 509(7498):110-4. View abstract
  23. RIG-I forms signaling-competent filaments in an ATP-dependent, ubiquitin-independent manner. Mol Cell. 2013 Sep 12; 51(5):573-83. View abstract
  24. Viral counterattack against the host innate immune system. Cell Res. 2013 Jun; 23(6):735-6. View abstract
  25. Structural basis for dsRNA recognition, filament formation, and antiviral signal activation by MDA5. Cell. 2013 Jan 17; 152(1-2):276-89. View abstract
  26. Kinetic mechanism for viral dsRNA length discrimination by MDA5 filaments. Proc Natl Acad Sci U S A. 2012 Dec 04; 109(49):E3340-9. View abstract
  27. Multi-level regulation of cellular recognition of viral dsRNA. Cell Mol Life Sci. 2013 Jun; 70(11):1949-63. View abstract
  28. Cooperative assembly and dynamic disassembly of MDA5 filaments for viral dsRNA recognition. Proc Natl Acad Sci U S A. 2011 Dec 27; 108(52):21010-5. View abstract