Tianyi Wang
Los Alamos National Laboratory
4 Papers
95 Citations
Tianyi Wang is an academic researcher from Los Alamos National Laboratory. The author has contributed to research in topics: Innate immune system & Proteome. The author has an hindex of 4, co-authored 4 publications. Previous affiliations of Tianyi Wang include University of North Carolina at Chapel Hill & University of California, Los Angeles.
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Papers
The Dynamic Alterations of H2AX Complex during DNA Repair Detected by a Proteomic Approach Reveal the Critical Roles of Ca2+/Calmodulin in the Ionizing Radiation-induced Cell Cycle Arrest
Yu Chun Du,Sheng Gu,Jianhong Zhou,Tianyi Wang,Hong Cai,Mark A. MacInnes,E. Morton Bradbury,Xian Chen +7 more
TL;DR: The results suggest that the H2AX complex undergoes dynamic changes upon induction of DNA damage and during DNA repair, and indicates that Ca2+/CaM plays important roles in regulating IR-induced cell cycle arrest, possibly through mediating chromatin structure.
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Flightless I homolog negatively modulates the TLR pathway.
Tianyi Wang,Tsung Hsien Chuang,Tapani Ronni,Sheng Gu,Yu Chun Du,Hong Cai,Hui Qiao Sun,Helen L. Yin,Xian Chen +8 more
TL;DR: Results from immunoprecipitation and a two-hybrid assay indicated that Fliih directly interfered with the formation of the TLR4-MyD88 signaling complex, suggesting a new basis for the regulation of theTLR pathway by FliiH.
Quantitative proteomic analysis of LPS‐induced differential immune response associated with TLR4 Polymorphisms by multiplex amino acid coded mass tagging
TL;DR: The LPS‐induced differential protein expression in TLR4‐deficient and wild‐type proteomes were obtained by comparing the intensities of isotopically encoded peptides and can be readily extended to other comparative proteomic quantitation of different cell populations.
In vivo dual-tagging proteomic approach in studying signaling pathways in immune response.
TL;DR: An in vivo dual-tagging quantitative approach that allows single affinity purification of the natural complexes formed at real-time, and amino acid-coded mass tagging that assists mass spectrometry-based quantitative measurement to identify the specific components of a signaling complex formed in macrophage cells upon lipopolysaccharide (LPS) stimulation is designed.