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Article

The C-terminal PARP domain of the long ZAP isoform contributes essential effector functions for CpG-directed antiviral activity

2021-06-22

Abstract excerpt

The zinc finger antiviral protein (ZAP) is a broad inhibitor of virus replication. Its best-characterized function is to bind CpG dinucleotides present in viral RNA and, through the recruitment of TRIM25, KHNYN and other cellular RNA degradation machinery, target them for degradation or prevent their translation. ZAP’s activity requires the N-terminal RNA binding domain that selectively binds CpG-containing RNA. H...

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Literature Corpus work
e9e92d3f-94b2-5470-bd06-8267a66912d8
DOI
10.1101/2021.06.22.449398
Open publication

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The C-terminal PARP domain of the long ZAP isoform contributes essential effector functions for CpG-directed antiviral activityDOI 10.1101/2021.06.22.449398
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