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Shanshan Wang

Researcher at Chinese Academy of Sciences

Publications -  11
Citations -  468

Shanshan Wang is an academic researcher from Chinese Academy of Sciences. The author has contributed to research in topics: Virus & Influenza A virus. The author has an hindex of 9, co-authored 11 publications receiving 388 citations. Previous affiliations of Shanshan Wang include Dalian Jiaotong University & University of Texas at Austin.

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SYNTHESIS; CHARACTERIZATION AND THERMAL ANALYSIS OF POLYANILINE (PANI)/Co3O4 COMPOSITES

TL;DR: In this paper, the authors synthesized polyaniline/Cobaltosic oxide composites by in situ deposition technique in the presence of hydrochloric acid (HCl) as a dopant by adding the fine grade powder (an average particle size of approximately 80 nm) of Co3O4 into the polymerization reaction mixture of aniline.
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Influenza B virus non-structural protein 1 counteracts ISG15 antiviral activity by sequestering ISGylated viral proteins

TL;DR: It is shown that Influenza B virus encodes non-structural protein 1 (NS1B) that binds human ISG15 and provides an appropriate model for determining how ISGylation affects virus replication in human cells and is largely responsible for inhibition of viral RNA synthesis by generating recombinant viruses that lack known ISgylation sites in NP.
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Cyclophilin A-regulated ubiquitination is critical for RIG-I-mediated antiviral immune responses

TL;DR: It is found that cyclophilin A (CypA), a peptidyl-prolyl cis/trans isomerase, functioned as a critical positive regulator of RIG-I-mediated antiviral immune responses and inhibited TRIM25-induced K48-linked ubiquitination of MAVS.
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Tyrosine 132 Phosphorylation of Influenza A Virus M1 Protein Is Crucial for Virus Replication by Controlling the Nuclear Import of M1

TL;DR: A pivotal role is revealed of this tyrosine phosphorylation in the intracellular transportation of M1, which controls the process of viral replication.
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Phosphorylation controls the nuclear-cytoplasmic shuttling of influenza A virus nucleoprotein

TL;DR: It is demonstrated that the phosphorylation status of these sites on NP can mediate its nuclear-cytoplasmic shuttling, which drives the trafficking of vRNP complexes in infected cells.