Happy to share our latest article on SirT6 😊 In this paper, we demonstrate that SirT6 can efficiently ADP-ribosylate proteins on both histidine and tyrosine residues. Check it out here: royalsocietypublishing.org/rsob/article...
Histidine and tyrosine residues are targets for SIRT6 ADP-ribosylation activity
Abstract. SIRT6, a highly conserved member of the sirtuin family, plays a critical role in diverse cellular processes, including gene regulation, DNA damag
royalsocietypublishing.org
New research from #OpenBiology: Histidine and tyrosine residues are targets for SIRT6 ADP-ribosylation activity royalsocietypublishing.org/rsob/article... | #Biochemistry
In this paper, we demonstrate that the sirtuin SIRT6 can efficiently ADP-ribosylate histidine and tyrosine residues in proteins. royalsocietypublishing.org/rsob/article...
Histidine and tyrosine residues are targets for SIRT6 ADP-ribosylation activity
Abstract. SIRT6, a highly conserved member of the sirtuin family, plays a critical role in diverse cellular processes, including gene regulation, DNA damag
royalsocietypublishing.org
Excited to share our lab’s new article in Biochemical Pharmacology on PARG as a key regulator opposing PARP functions and its emerging therapeutic potential in cancer. Overview of current PARG inhibitors included. www.sciencedirect.com/science/arti...
The PARG frontier: mechanisms of PAR turnover and opportunities in precision oncology
ADP-ribosylation is a versatile post-translational modification that governs fundamental processes, including DNA repair, transcription, and stress ad…
sciencedirect.com
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...
Redirecting
doi.org
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...
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...
nature.com