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Andreas Kolvenbach

@aklvnbch.bsky.social
60 followers 173 following 4 posts

Interested in mass spectrometry and the crosstalk of ADP-ribosylation and ubiquitylation during the DNA damage response.

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Reposted by Andreas Kolvenbach
The Matić Lab @maticlab.bsky.social · 08/04/2026
The paper describing our sensitive poly-ADPr antibodies and a few other things is now out in Nature Communications. Congrats to all the authors!! www.nature.com/articles/s41...
nature.com
Versatile and sensitive detection of mono- and poly(ADP-ribosyl)ation reveals XRCC1-dependent remodelling of PARP1 signalling - Nature Communications
ADP-ribosylation regulates DNA repair, but its distinct forms have been difficult to distinguish. Here, the authors develop sensitive, modular antibodies to precisely detect mono- and poly-ADP-ribosyl...
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Reposted by Andreas Kolvenbach
The Matić Lab @maticlab.bsky.social · 18/09/2025
Superb News&Views on our recent paper reporting identification of ADP-ribosyl-linked serine ubiquitylation www.nature.com/articles/s41...
nature.com
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...
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Reposted by Andreas Kolvenbach
The Matić Lab @maticlab.bsky.social · 11/07/2025
At its core, it’s a technological paper—necessary to overcome some of the many challenges of working with ADPrUb. But beyond the technical details, below are the main highlights:
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Reposted by Andreas Kolvenbach
Nature Chemical Biology @natchembio.nature.com · 10/07/2025
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...
nature.com
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...
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Reposted by Andreas Kolvenbach
Maria Dilia Palumbieri @mariapalumbieri.bsky.social · 10/07/2025
Thrilled to share my first first-author postdoc publication — a team effort with @aklvnbch.bsky.social. We present the first MS-based evidence of ADP-ribosylation–linked ubiquitin (ADPrUb) in cells after DNA damage. Grateful for all I’ve learned and looking forward to uncovering more about ADPrUb
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Andreas Kolvenbach @aklvnbch.bsky.social · 09/07/2025
Really happy that our paper is finally released. We show that PARP1 and histones are targets of ADP-ribosyl-linked ubiquitylation during DNA damage and describe how to detect the dual modification. Great teamwork with @mariapalumbieri.bsky.social & thanks to everyone involved @maticlab.bsky.social !
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Reposted by Andreas Kolvenbach
Maria Dilia Palumbieri @mariapalumbieri.bsky.social · 19/05/2025
Thrilled to have presented our latest work at FEBS PARP 2025! A fantastic joint effort with @aklvnbch.bsky.social . I really enjoyed sharing our results and discussing with experts in the field—looking forward to what’s next! Many thanks to the organizers for making this great meeting possible!
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Reposted by Andreas Kolvenbach
The Matić Lab @maticlab.bsky.social · 09/02/2025
We’ve uploaded a bioRxiv preprint on new antibodies specific for poly-ADP-ribosylation (PARylation). These modular tools were developed and validated through novel applications of our Serine ADP-ribosylation-based technology. www.biorxiv.org/content/10.1...
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