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Ao Jiang

Researcher at Wuhan University

Publications -  6
Citations -  1124

Ao Jiang is an academic researcher from Wuhan University. The author has contributed to research in topics: Chemistry & Medicine. The author has an hindex of 3, co-authored 4 publications receiving 718 citations.

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Transcriptomic characteristics of bronchoalveolar lavage fluid and peripheral blood mononuclear cells in COVID-19 patients.

TL;DR: The results reveal distinct host inflammatory cytokine profiles to SARS-CoV-2 infection in patients, and highlight the association between COVID-19 pathogenesis and excessive cytokine release such as CCL2/MCP-1, CXCL10/IP-10, CCL3/MIP-1A, and CCL4/Mip1B.
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METTL3 and N6-Methyladenosine Promote Homologous Recombination-Mediated Repair of DSBs by Modulating DNA-RNA Hybrid Accumulation

TL;DR: In this paper, the RNA methyltransferase METTL3 is activated by ATM-mediated phosphorylation at S43, where it methylates the N6 position of adenosine (m6A) in DNA damage-associated RNAs, which recruits the m6A reader protein YTHDC1 for protection.
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The SARS-CoV-2 subgenome landscape and its novel regulatory features.

TL;DR: In this article, using NGS short-read and Nanopore long-read sequencing to profile poly(A) RNAs in two cell types at multiple time points post-infection of SARS-CoV-2, the authors identified hundreds of template switches and constructed the dynamic landscapes of the subgenomes.
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β-Catenin safeguards the ground state of mousepluripotency by strengthening the robustness of the transcriptional apparatus

TL;DR: It is shown that β-catenin, stabilized by GSK3 inhibition in medium with 2i, supplies transcriptional coregulators at pluripotency loci, which selectively strengthens pluripotent loci and renders them addicted to transcription initiation for productive gene body elongation in detriment to Pol2 pause release.
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Histone methyltransferase Dot1L recruits O-GlcNAc transferase to target chromatin sites to regulate histone O-GlcNAcylation

TL;DR: In this article , the authors search for functional partners of OGT and identified interacting protein Dot1L, a conserved and unique histone methyltransferase known to mediate histone H3 Lys79 methylation, which is required for gene transcription, DNA damage repair, cell proliferation, and embryo development.