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Ubiquitin-like with PHD and ring finger domains 1 (UHRF1) mRNA encodes a multi-domain protein that plays a critical role in maintaining DNA methylation patterns during cell division (UniProt Q96T88) [1]. UHRF1 acts as a bridge between DNA methylation and histone modifications, specifically by recognizing hemi-methylated DNA and recruiting DNA methyltransferase 1 (DNMT1) to the replication fork (PMID: 27049015) [2]. In many human cancers, UHRF1 is significantly overexpressed, leading to the silencing of tumor suppressor genes through hypermethylation and contributing to genomic instability (PMID: 31110296) [3]. Targeting UHRF1 mRNA using antisense oligonucleotides or RNA interference represents a therapeutic strategy to deplete UHRF1 protein levels, thereby reactivating silenced tumor suppressors and inhibiting cancer cell proliferation (PMID: 23653361) [4]. While primarily studied in the context of oncology, the precise regulation of UHRF1 is essential for normal development, making selective targeting of cancerous cells a key challenge in drug development.
Degradation of target mRNA via RNase H-mediated cleavage or RNA interference (RNAi) to prevent translation of the UHRF1 protein.
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