Luca Palazzo lab
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Luca Palazzo lab
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Reposted by Luca Palazzo lab
ahellab.bsky.social
Our review article 'PARPs and ADP-ribosyl hydrolases in cancer therapy: from drug targets to biomarkers' is now available online.
doi.org/10.1016/j.dn...
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June 29, 2025 at 7:57 PM
Reposted by Luca Palazzo lab
ahellab.bsky.social
A few years back we discovered a dual hybrid protein modification composed of ADP-ribose dinucleotide and ubiquitin (ADPr-Ub). Now we reveal that ADPr-Ub can be further ubiquitinated by the E3 ubiquitin ligase RNF114!
www.nature.com/articles/s41...

www.science.org/doi/10.1126/...
Identification of RNF114 as ADPr-Ub reader through non-hydrolysable ubiquitinated ADP-ribose - Nature Communications
Deltex E3s modify ADP-ribosylated targets with ubiquitin, creating a hybrid modification whose readers remains unknown. Here, the authors synthesise a non-hydrolysable probe that mimics the modificati...
www.nature.com
July 10, 2025 at 6:11 AM
Reposted by Luca Palazzo lab
natchembio.nature.com
RNF114 is an E3 ligase that can recognize ADP-ribose (ADPr) and ubiquitin with separate domains. A proteomics approach is developed using these domains to map ADP-ribosyl-ubiquitylation sites

www.nature.com/articles/s41...
Serine ADPr on histones and PARP1 is a cellular target of ester-linked ubiquitylation - Nature Chemical Biology
RNF114 is an E3 ligase that can recognize ADP-ribose (ADPr) and ubiquitin with separate domains. Using these domains, Kolvenbach and Palumbieri et al. developed a proteomics approach to map ADP-ribosy...
www.nature.com
July 10, 2025 at 4:56 PM