aklvnbch.bsky.social
Andreas Kolvenbach
@aklvnbch.bsky.social
26 followers 110 following 2 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
cga-age.bsky.social
Cologne Graduate School of Ageing Research @cga-age.bsky.social · Aug 12
Apply now for a fully funded #PhD position at the Cologne Graduate School of Ageing Research and become part of our vibrant #AgingResearch commmuny.
🗓️ Deadline: November 3, 2025.
ℹ️ More info: www.ageing-grad-school.de
📣 Spread the news!
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Reposted by Andreas Kolvenbach
maticlab.bsky.social
The Matić Lab @maticlab.bsky.social · 20d
Superb News&Views on our recent paper reporting identification of ADP-ribosyl-linked serine ubiquitylation
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
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Reposted by Andreas Kolvenbach
maticlab.bsky.social
The Matić Lab @maticlab.bsky.social · Jul 11
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:
maticlab.bsky.social
The Matić Lab @maticlab.bsky.social · Jul 9
Our latest study on ADP-ribosyl-linked serine ubiquitylation in the context of PARP1 signaling and the DNA damage response is out today in Nature Chemical Biology 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
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Reposted by Andreas Kolvenbach
natchembio.nature.com
Nature Chemical Biology @natchembio.nature.com · Jul 10
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
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Reposted by Andreas Kolvenbach
mariapalumbieri.bsky.social
Maria Dilia Palumbieri @mariapalumbieri.bsky.social · Jul 10
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
maticlab.bsky.social
The Matić Lab @maticlab.bsky.social · Jul 9
Our latest study on ADP-ribosyl-linked serine ubiquitylation in the context of PARP1 signaling and the DNA damage response is out today in Nature Chemical Biology 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
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aklvnbch.bsky.social
Andreas Kolvenbach @aklvnbch.bsky.social · Jul 9
Also take a look at the related paper, showing the specificity of RNF114 for ADP-ribosyl-linked ubiquitylation. Congratulations to all the authors! www.nature.com/articles/s41...
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
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aklvnbch.bsky.social
Andreas Kolvenbach @aklvnbch.bsky.social · Jul 9
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 !
maticlab.bsky.social
The Matić Lab @maticlab.bsky.social · Jul 9
Our latest study on ADP-ribosyl-linked serine ubiquitylation in the context of PARP1 signaling and the DNA damage response is out today in Nature Chemical Biology 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
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Reposted by Andreas Kolvenbach
mariapalumbieri.bsky.social
Maria Dilia Palumbieri @mariapalumbieri.bsky.social · May 19
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
maticlab.bsky.social
The Matić Lab @maticlab.bsky.social · Feb 9
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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