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
Research 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 obtained post-doctoral training 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. In her own lab, she investigates immune mechanisms for self vs non-self discrimination. Her research on a family of viral RNA receptors, RIG-I-like receptors (RLRs), has led to the discovery of key mechanistic principles of foreign nucleic acid sensing. She was chosen as a Pew scholar (2010), Burroughs Wellcome Investigator in the Pathogenesis of Infectious Disease (2015), a recipient of the Vilcek Prize for Creative Promise in Biomedical Science (2015), Richard A. and Susan F. Smith President’s Innovation Award (2019) and NIH Director’s Pioneer Award (2019), a finalist for the Blavatnik National Awards in Life Sciences (2020 and 2021) and a winner of the Paul Marks Prize (2022). She was named the Oscar M. Schloss, MD Professor at Harvard University in 2020 and an investigator for Howard Hughes Medical Institute (2021).
Selected Publications
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
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
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
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.
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.
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
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
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
Cutting-Edge Technologies of Meat Analogs: A Review. Food Sci Anim Resour. 2025 Jan; 45(1):223-242. View Abstract
Environmental Impact of Meat Protein Substitutes: A Mini-Review. Food Sci Anim Resour. 2025 Jan; 45(1):62-80. View Abstract
An Investigation of the Status of Commercial Meat Analogs and Their Ingredients: Worldwide and South Korea. Food Sci Anim Resour. 2025 Jan; 45(1):31-61. View Abstract
A review on the characterization of edible scaffolds for cultured meat: Physical, chemical, biocompatibility, and food safety evaluation methods. Food Chem. 2025 Mar 30; 469:142493. View Abstract
Market Status of Meat Analogs and Their Impact on Livestock Industries. Food Sci Anim Resour. 2024 Nov; 44(6):1213-1251. View Abstract
Study on the feasibility of using livestock blood as a fetal bovine serum substitute for cultured meat. J Food Sci. 2024 Nov; 89(11):7143-7156. View Abstract
Comparative study on the bioavailability of peptide extracts from Jeju black pigs and three-way crossbred pigs. J Anim Sci Technol. 2024 Sep; 66(5):1049-1068. View Abstract
Mechanism for controlled assembly of transcriptional condensates by Aire. Nat Immunol. 2024 Sep; 25(9):1580-1592. View Abstract
Analysis of current technology status for the industrialization of cultured meat. Crit Rev Food Sci Nutr. 2024 May 19; 1-32. View Abstract
Study on the Digestion-Induced Changes in the Characteristics and Bioactivity of Korean Native and Overseas Cattle-Derived Peptides. Food Sci Anim Resour. 2024 May; 44(3):551-569. View Abstract
Crusting-fabricated three-dimensional soy-based scaffolds for cultured meat production: A preliminary study. Food Chem. 2024 Sep 15; 452:139511. View Abstract
The Color-Developing Methods for Cultivated Meat and Meat Analogues: A Mini-Review. Food Sci Anim Resour. 2024 Mar; 44(2):356-371. View Abstract
Current Research, Industrialization Status, and Future Perspective of Cultured Meat. Food Sci Anim Resour. 2024 Mar; 44(2):326-355. View Abstract
Preliminary study on comparison of egg extraction methods for development of fetal bovine serum substitutes in cultured meat. Food Chem X. 2024 Mar 30; 21:101202. View Abstract
Current technology and industrialization status of cell-cultivated meat. J Anim Sci Technol. 2024 Jan; 66(1):1-30. View Abstract
Current Technologies and Future Perspective in Meat Analogs Made from Plant, Insect, and Mycoprotein Materials: A Review. Food Sci Anim Resour. 2024 Jan; 44(1):1-18. View Abstract
Study on the current research trends and future agenda in animal products: an Asian perspective. J Anim Sci Technol. 2023 Nov; 65(6):1124-1150. View Abstract
FOXP3 recognizes microsatellites and bridges DNA through multimerization. Nature. 2023 Dec; 624(7991):433-441. View Abstract
Mutations from patients with IPEX ported to mice reveal different patterns of FoxP3 and Treg dysfunction. Cell Rep. 2023 08 29; 42(8):113018. View Abstract
Stress granules are shock absorbers that prevent excessive innate immune responses to dsRNA. Mol Cell. 2023 04 06; 83(7):1180-1196.e8. View Abstract
The roles of growth factors and hormones in the regulation of muscle satellite cells for cultured meat production. J Anim Sci Technol. 2023 Jan; 65(1):16-31. View Abstract
The transcription factor FoxP3 can fold into two dimerization states with divergent implications for regulatory T cell function and immune homeostasis. Immunity. 2022 08 09; 55(8):1354-1369.e8. View Abstract
Death domain fold proteins in immune signaling and transcriptional regulation. FEBS J. 2022 07; 289(14):4082-4097. View Abstract
The Role of RNA Editing in the Immune Response. Methods Mol Biol. 2021; 2181:287-307. View Abstract
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
Substrate recognition by TRIM and TRIM-like proteins in innate immunity. Semin Cell Dev Biol. 2021 03; 111:76-85. View Abstract
Dual functions of Aire CARD multimerization in the transcriptional regulation of T cell tolerance. Nat Commun. 2020 04 02; 11(1):1625. View Abstract
Filament-like Assemblies of Intracellular Nucleic Acid Sensors: Commonalities and Differences. Mol Cell. 2019 10 17; 76(2):243-254. View Abstract
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
Helicases in Antiviral Immunity: Dual Properties as Sensors and Effectors. Trends Biochem Sci. 2015 Oct; 40(10):576-585. View Abstract
How RIG-I like receptors activate MAVS. Curr Opin Virol. 2015 Jun; 12:91-8. View Abstract
ATP-dependent effector-like functions of RIG-I-like receptors. Mol Cell. 2015 May 07; 58(3):541-548. View Abstract
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
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
Structural basis for ubiquitin-mediated antiviral signal activation by RIG-I. Nature. 2014 May 01; 509(7498):110-4. View Abstract
RIG-I forms signaling-competent filaments in an ATP-dependent, ubiquitin-independent manner. Mol Cell. 2013 Sep 12; 51(5):573-83. View Abstract
Viral counterattack against the host innate immune system. Cell Res. 2013 Jun; 23(6):735-6. View Abstract
Structural basis for dsRNA recognition, filament formation, and antiviral signal activation by MDA5. Cell. 2013 Jan 17; 152(1-2):276-89. View Abstract
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
Multi-level regulation of cellular recognition of viral dsRNA. Cell Mol Life Sci. 2013 Jun; 70(11):1949-63. View Abstract
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