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RSS FeedsPutting phage to work in deubiquitinase ligand discovery [Protein Structure and Folding] (Journal of Biological Chemistry)

 
 

11 january 2019 13:00:17

 
Putting phage to work in deubiquitinase ligand discovery [Protein Structure and Folding] (Journal of Biological Chemistry)
 




Inhibiting deubiquitinase (DUB) function is a promising strategy for the treatment of cancers and other human diseases. Of the hundreds of human DUBs, USP11 has emerged as an ideal therapeutic target, as it regulates DNA double-strand break repair by homologous recombination (HR) and other functions central to eukaryotic cell survival. A new study by Spiliotopoulos et al. cleverly uses next-generation phage display (NGPD) to identify peptide ligands that bind USP11 in a unique pocket that impacts HR. The study provides an important step toward novel DUB inhibitors that may reduce the resistance of some cancers to current treatment options.


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19 viewsCategory: Biochemistry
 
Discovery of peptide ligands targeting a specific ubiquitin-like domain-binding site in the deubiquitinase USP11 [Methods and Resources] (Journal of Biological Chemistry)
The inflammasome adapter ASC assembles into filaments with integral participation of its two Death Domains, PYD and CARD [Molecular Bases of Disease] (Journal of Biological Chemistry)
 
 
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