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ATRIP Deacetylation by SIRT2 Drives ATR Checkpoint Activation by Promoting Binding to RPA-ssDNA
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文摘

SIRT2 interacts with and deacetylates ATRIP at K32 in vitro and in cells

ATRIP deacetylation by SIRT2 promotes ATR activation and replication stress recovery

ATRIP deacetylation by SIRT2 promotes accumulation to sites of DNA damage

SIRT2 deacetylation of ATRIP at K32 promotes its direct binding to RPA-ssDNA

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