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Ling E. Cheung

Researcher at Johns Hopkins University School of Medicine

Publications -  7
Citations -  883

Ling E. Cheung is an academic researcher from Johns Hopkins University School of Medicine. The author has contributed to research in topics: Retrotransposon & Ribonucleoprotein. The author has an hindex of 7, co-authored 7 publications receiving 766 citations. Previous affiliations of Ling E. Cheung include Johns Hopkins University.

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MOV10 RNA helicase is a potent inhibitor of retrotransposition in cells.

TL;DR: MOV10 protein, a putative RNA helicase and component of the RNA–induced silencing complex (RISC), inhibits retrovirus replication and shows that MOV10 also severely restricts human LINE1, Alu, and SVA retrotransposons.
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Modulation of LINE-1 and Alu/SVA retrotransposition by Aicardi-Goutières syndrome-related SAMHD1.

TL;DR: It is demonstrated that the Aicardi-Goutières syndrome gene product SAMHD1, recently revealed to be an inhibitor of HIV/simian immunodeficiency virus (SIV) infectivity and neutralized by the viral Vpx protein, is also a potent regulator of LINE-1 and Line-1-mediated Alu/SVA retrotransposition.
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Retrotransposition of marked SVA elements by human L1s in cultured cells

TL;DR: This assay demonstrates that SVA elements are indeed mobilized in trans by L1, and previously intractable questions regarding SVA biology can now be addressed.
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Mapping the LINE1 ORF1 protein interactome reveals associated inhibitors of human retrotransposition

TL;DR: Co-immunoprecipitation of tagged L1 constructs and mass spectrometry suggests candidate cofactors that interact with the L1 to modulate its activity and increases the understanding of the means by which the cell coexists with these genomic ‘parasites’.
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The Broad-Spectrum Antiviral Protein ZAP Restricts Human Retrotransposition.

TL;DR: ZAP, a zinc-finger protein that targets viruses of several families, is focused on, and it is shown that ZAP expression also strongly restricts retrotransposition in cell culture through loss of L1 RNA and ribonucleoprotein particle integrity.