Deubiquitylating enzymes (DUBs) maintain relative homeostasis of the cellular ubiquitome
by removing the post‐translational modification ubiquitin moiety from substrates. Numerous …

Ubiquitination represents a post-translational modification (PTM) essential for the
maintenance of cellular homeostasis. Ubiquitination is involved in the regulation of protein …

How chromatin dynamics is regulated to ensure efficient DNA repair remains to be
understood. Here, we report that the ubiquitin-specific protease USP11 acts as a histone …

Cross-talk between distinct protein post-translational modifications is critical for an effective
DNA damage response. Arginine methylation plays an important role in maintaining …

Emerging evidence indicates the deubiquitinase USP22 regulates transcriptional activation
and modification of target substrates to promote pro-oncogenic phenotypes. Here, in vivo …

Deubiquitylating enzymes (DUBs) are proteases that remove the ubiquitin moiety from
ubiquitylated substrates to antagonize the modification mediated by E3 ubiquitin ligases …

USP11 is a member of the ubiquitin-specific protease family and plays a crucial role in tumor
progression in various cancers. However, the precise mechanism by which USP11 …

The ubiquitin specific protease, USP7, regulates multiple cellular pathways relevant for
cancer through its ability to bind and sometimes stabilize specific target proteins through …

Global genome nucleotide excision repair (GG-NER) eliminates a broad spectrum of DNA
lesions from genomic DNA. Genomic DNA is tightly wrapped around histones creating a …

Ubiquitination is a critical biological process in post-translational modification of proteins
and involves multiple signaling pathways in protein metabolism, apoptosis, DNA damage …