Xin Mu
Harvard University
7 Papers
Xin Mu is an academic researcher from Harvard University. The author has contributed to research in topics: RNA & MDA5. The author has an hindex of 4, co-authored 7 publications. Previous affiliations of Xin Mu include Tianjin University & Boston Children's Hospital.
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Papers
Breaching Self-Tolerance to Alu Duplex RNA Underlies MDA5-Mediated Inflammation.
Sadeem Ahmad,Xin Mu,Xin Mu,Fei Yang,Fei Yang,Emily Greenwald,Ji Woo Park,Etai Jacob,Cheng-Zhong Zhang,Sun Hur,Sun Hur +10 more
TL;DR: It is demonstrated here that constitutive activation of MDA5 in AGS results from the loss of tolerance to cellular dsRNAs formed by Alu retroelements, and implicates a unique role of Alu-dsRNAs as virus-like elements that shape the primate immune system.
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An origin of the immunogenicity of in vitro transcribed RNA.
TL;DR: It is shown that the immune-stimulatory activity of T7 transcript is contributed by its aberrant activity to initiate transcription from a promoter-less DNA end, and this activity results in the production of an antisense RNA that is fully complementary to the intended sense RNA product.
159
An origin of the immunogenicity of in vitro transcribed RNA
TL;DR: It is shown that the immune-stimulatory activity of T7 transcript is contributed by its aberrant activity to initiate transcription from a promoter-less DNA end, which results in the production of an antisense RNA that is fully complementary to the intended sense RNA product.
97
Immunogenicity of In Vitro -Transcribed RNA.
TL;DR: In this article, the authors investigated the mechanisms by which the innate immune system discriminates between "self" and "nonself" RNA, with the focus on the cytoplasmic dsRNA receptors retinoic acid-inducible gene I (RIG-I) and melanoma differentiation-associated 5 (MDA5).
68
Structural analysis of RIG-I-like receptors reveals ancient rules of engagement between diverse RNA helicases and TRIM ubiquitin ligases
Kazuki Kato,Kazuki Kato,Sadeem Ahmad,Sadeem Ahmad,Zixiang Zhu,Janet M. Young,Xin Mu,Xin Mu,Xin Mu,Sehoon Park,Harmit S. Malik,Sun Hur,Sun Hur +12 more
TL;DR: Cryo-electron microscopy and biochemistry show that RIG-I-like receptors, viral RNA receptors with helicase domains, interact with their cognate TRIM/TRIM-like E3 ligases through similar epitopes in the helicase domain, thereby linking ubiquitin and RNA biology throughout animal evolution.