BIF PhD student in Schulman lab @mpibiochem.bsky.social, interested in structural biology and ubiquitin system
Samuel Maiwald
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The E3 ubiquitin ligase mechanism specifying target-directed microRNA degradation (TDMD) is now published! 🎉🍾 We, @bartellab.bsky.social and Schulman lab, describe how 2-RNA factors control protein degradation by recruiting an E3 ligase. @mpibiochem.bsky.social
www.nature.com/articles/s41...
Formation & function of #MembranelessOrganelles! #CryoET structures of #proteasome storage granules inside cells!
Read our paper @cp-cell.bsky.social!
❕Publication: doi.org/10.1016/j.ce...
❕Press Release: www.biochem.mpg.de/en/pressroom
@uoftmedicine.bsky.social
@erc.europa.eu #UPSmeetMet
LLOMe has long been used to study lysosomal damage, yet how it works has remained a mystery.
Using cryo-electron tomography, we show it forms amyloid structures inside lysosomes that mechanically rupture membranes – revealing a new paradigm for lysosomal failure.
🔗 doi.org/10.64898/202...
#CryoET
New year, new preprint! 🎊
We are excited to share our recent work on #E3 ligase regulation in #metabolism!
www.biorxiv.org/content/10.6...
#ubiquitin #targetedproteindegradation #chemicalbiology
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When RNA Degradation 🤝 meets 🤝 Protein Degradation! tinyurl.com/E3TDMD In a collaboration of @bartellab.bsky.social and Schulman lab, we show that, in target-directed microRNA degradation (TDMD), 2-RNA-factors recruit an E3 ligase and induce the degradation of not only a protein but also RNA (1/5).
New work from the Schulman Dept. shows mechanisms of metabolite-regulated E3 ligase activity.
Read more about it: “Cysteine availability tunes ubiquitin signaling via inverse stability of LRRC58 E3 ligase and its substrate CDO1” in Nature Communications. www.nature.com/articles/s41...
I am incredibly excited to share that I will start my independent lab at the @unidue-zmb.bsky.social at the @unidue.bsky.social as Junior Professor of Cellular Biochemistry. Research in my lab has the goal to decipher the ubiquitin code!
There are multiple open positions!
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Cysteine availability tunes ubiquitin signaling via inverse stability of LRRC58 E3 ligase and its substrate CDO1 https://www.biorxiv.org/content/10.1101/2025.11.14.688510v1
Video
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Cysteine availability tunes ubiquitin signaling via inverse stability of LRRC58 E3 ligase and its substrate CDO1 pubmed.ncbi.nlm.nih.gov/42098103/ #cryoEM
