Ting Ling
Jiangxi Normal University
7 Papers
22 Citations
Ting Ling is an academic researcher from Jiangxi Normal University. The author has contributed to research in topics: Signal transduction & RIG-I. The author has an hindex of 2, co-authored 5 publications.
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Papers
TARBP2 inhibits IRF7 activation by suppressing TRAF6-mediated K63-linked ubiquitination of IRF7.
Ting Ling,Guang-Xiu Weng,Jing Li,Changsheng Li,Weiying Wang,Lingzhen Cao,Hua Rao,Cynthia Ju,Liang-Guo Xu +8 more
TL;DR: The findings further reveal the mechanism by which TARBP2 regulates the antiviral signaling pathways of the innate immune system and inhibit IRF7‐mediated IFN‐&bgr; production triggered by the Sendai virus in 293 T cells.
21
TARBP2 negatively regulates IFN-β production and innate antiviral response by targeting MAVS.
Ting Ling,Sheng-Na Li,Guang-Xiu Weng,Weiying Wang,Changsheng Li,Lingzhen Cao,Hua Rao,Hong-Bing Shu,Liang-Guo Xu +8 more
TL;DR: Transactivation response element RNA‐binding protein (TARBP2), as an inhibitor of the cellular protein kinase PKR, negatively regulates virus ‐induced IFN‐&bgr; production by targets MAVS, and is suggested to be an important non‐redundant virus‐mediated negative regulator of typeI interferon.
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HSPBP1 facilitates cellular RLR-mediated antiviral response by inhibiting the K48-linked ubiquitination of RIG-I.
TL;DR: In this article, the authors demonstrated that Hsp70 binding protein 1 (HSPBP1) promotes RIG-I-mediated signal transduction and showed that HSPBP-1 positively regulates the antiviral signal pathway induced by inhibiting the K48-linked ubiquitination of RIGI.
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Mitochondrial DUT-M potentiates RLR-mediated antiviral signaling by enhancing VISA and TRAF2 association
TL;DR: In this article, a mitochondrial isoform, deoxyuridine triphosphate nucleotidohydrolase (dUTPase), was shown to be a positive regulator in RLR-VISA-mediated antiviral signaling.
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Coupled folding-upon-binding of human tumor suppressor MIG6 to lung cancer EGFR kinase domain and molecular trimming/stapling of MIG6-derived β-hairpins to target the coupling event
TL;DR: It is revealed that the MIG6 fragment 2 is intrinsically disordered in free unbound state, but would fold into a well-structured β-hairpin when binding to EGFR, thus characterized by a so-called coupled folding-upon-binding process, which can be regarded as a compromise between favorable direct readout and unfavorable indirect readout.
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