S
Sung-il Yoon
Researcher at Kangwon National University
Publications - 77
Citations - 2394
Sung-il Yoon is an academic researcher from Kangwon National University. The author has contributed to research in topics: Flagellin & Medicine. The author has an hindex of 20, co-authored 63 publications receiving 1797 citations. Previous affiliations of Sung-il Yoon include Scripps Research Institute & University of Alabama at Birmingham.
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Journal ArticleDOI
Precisely printable and biocompatible silk fibroin bioink for digital light processing 3D printing
Soon Hee Kim,Yeung Kyu Yeon,Jung Min Lee,Janet Ren Chao,Young Jin Lee,Ye Been Seo,Md. Tipu Sultan,Ok Joo Lee,Ji Seung Lee,Sung-il Yoon,In-Sun Hong,Gilson Khang,Sang Jin Lee,James J. Yoo,Chan Hum Park +14 more
TL;DR: Sil-MA bioink created from silk fibroin (SF) for digital light processing (DLP) 3D bioprinting in tissue engineering applications allowed us to build highly complex organ structures with excellent structural stability and reliable biocompatibility.
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Structural Basis of TLR5-Flagellin Recognition and Signaling
Sung-il Yoon,Oleg V. Kurnasov,Venkatesh Natarajan,Minsun Hong,Andrei V. Gudkov,Andrei L. Osterman,Ian A. Wilson +6 more
TL;DR: The crystal structure of zebrafish TLR5 (as a variable lymphocyte receptor hybrid protein) in complex with the D1/D2/D3 fragment of Salmonella flagellin, FliC, is determined at 2.47 angstrom resolution.
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Antibody Recognition of the Pandemic H1N1 Influenza Virus Hemagglutinin Receptor Binding Site
Minsun Hong,Peter Lee,Ryan M. B. Hoffman,Xueyong Zhu,Jens C. Krause,Nick S. Laursen,Sung-il Yoon,Langzhou Song,Lynda Tussey,James E. Crowe,Andrew B. Ward,Ian A. Wilson +11 more
TL;DR: The crystal structure of 5J8 Fab in complex with a bacterially expressed and refolded globular head domain from the hemagglutinin (HA) of the A/California/07/2009 (H1N1) pandemic virus is presented and consistent with previous studies, the bacterially expression H1 HA properly refolds, retaining its antigenic structure, and presents a low-cost and rapid alternative for engineering and manufacturing candidate flu vaccines.
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Conformational changes mediate interleukin-10 receptor 2 (IL-10R2) binding to IL-10 and assembly of the signaling complex.
TL;DR: Interestingly, IL-10R2 binding residues located in the N-terminal end of helix A exhibit large structural differences between unbound cil-10 and cIL-10·IL- 10R1 crystal structures, which suggests IL-9R1-induced conformational changes regulate IL-11R2binding and assembly of the ternary IL- 10·IL -10R1·ILR2 complex.
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A conserved TLR5 binding and activation hot spot on flagellin
TL;DR: This work provides a conserved structural mechanism by which flagellins from Gram-negative γ-proteobacteria and Gram-positive Firmicutes bacteria bind and activate Toll-like receptor 5 (TLR5) and establishes the groundwork for the future design of flageLLin-based therapeutics.