Malte Gersch
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maltegersch.bsky.social
Malte Gersch
@maltegersch.bsky.social
Chemical Biologist & Research Groupleader at Max Planck & TU Dortmund. Interested in DUBs, proteases, ubiquitin, the outdoors and more. Views are my own. cgc.mpg.de/gersch
Reposted by Malte Gersch
We call these mechanism based sirtuin inhibitors SirTraps that trap the enzyme via this ADP ribose adduct onlinelibrary.wiley.com/doi/10.1002/... 2/
From Pharmacophore to Warhead: NAD+‐Targeting Triazoles as Mechanism‐Based Sirtuin Inhibitors
We report “Sirtuin Trapping Ligands” (SirTraps), mechanism-based 1,2,3-triazole inhibitors that hijack sirtuin (SIRT) catalysis to form covalent triazolium– or triazole–ADP-ribose (ADPR) adducts from...
onlinelibrary.wiley.com
November 2, 2025 at 1:20 PM
Reposted by Malte Gersch
Also enjoyed reading the News & Views from @maltegersch.bsky.social, which beautifully summarizes the recent advancements in studying MARUbylation as a novel hybrid PTM.
www.nature.com/articles/s41...
ADPr gets a ubiquitin upgrade - Nature Chemical Biology
MARUbylation is a hybrid post-translational protein modification in which mono-ADP-ribosylation acts as a scaffold for sequential mono- and polyubiquitylation. Recent studies illuminate its substrates...
www.nature.com
October 30, 2025 at 3:41 PM
This looks very useful (as does the preprint from the Hummer lab). I‘d be curios in how many of those examples one would expect a precisely positioned Ub based on nearby UBDs?
October 16, 2025 at 12:02 PM