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Mauriz Lichtenstein

@mlichtenstein.bsky.social
193 followers 220 following 12 posts

PhD student Winter lab @ AITHYRA/ CeMM Vienna | interested in using structural and synthetic biology to engineer cellular decision making | previously Baker lab @ IPD and Taylor lab @ mpiib-berlin

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Reposted by Mauriz Lichtenstein
CeMM @cemm.oeaw.ac.at · 08/10/2025
1️⃣ @mmbronstein.bsky.social (@aithyra.bsky.social Scientific Director of AI) spoke with @mlichtenstein.bsky.social (@georgwinter.bsky.social's group) about the value of taking on ambitious projects & the key role of collaboration in science.
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Reposted by Mauriz Lichtenstein
Magnus Bauer @kinasekid.bsky.social · 30/09/2025
Phosphorylation on tyrosines control key pathways in immunity, cancer, and metabolism. For the first time, we can now design proteins that specifically recognize individual phosphotyrosines, even in disordered regions. (1/8) Preprint: www.biorxiv.org/content/10.1...
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Reposted by Mauriz Lichtenstein
Arvind Pillai @arvindspillai.bsky.social · 15/05/2025
I'm thrilled to join the Stowers Institute to explore how molecular complexity arises during evolution and how it can be designed! If you are a young scientist interested in questions related to protein design and evolution, feel free to e-mail me to learn more about opportunities!
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Mauriz Lichtenstein @mlichtenstein.bsky.social · 25/04/2025
Excited to share our paper out now in @science.org . We (@mpiib-berlin.mpg.de ) engineered single-component signalosomes to dissect the biophysical properties required for signaling. Read on for a cool story on using #synthetic-biology to study #signaling. 1/10 www.science.org/doi/10.1126/...
science.org
Bottom-up reconstruction of functional death fold signalosomes reveals a requirement for polymer stability and avidity
Protein polymer scaffolds composed of death fold (DF) proteins are critical to the formation of signalosomes in immune signaling. The biophysical properties that these polymeric scaffolds require for ...
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Reposted by Mauriz Lichtenstein
estella newcombe @estellaan.bsky.social · 27/11/2024
We did this crazy project where we tried to see if proteins could interact with their mirror image ligand. Seems impossible when proteins need to form 3D structures to interact. But what about if the interaction remains disordered??? www.nature.com/articles/s41...
nature.com
Stereochemistry in the disorder–order continuum of protein interactions - Nature
Studies on protein–protein interactions using proteins containing d- or l-amino acids show that stereoselectivity of binding varies with the degree of disorder within the complex.
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Reposted by Mauriz Lichtenstein
Adam Broerman @adambroerman.bsky.social · 20/11/2024
@mlichtenstein.bsky.social and I also used facilitated dissociation to make biosensors which are just as modular as those built previously with our LOCKR platform, but which respond 70 times faster.
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Reposted by Mauriz Lichtenstein
Adam Broerman @adambroerman.bsky.social · 20/11/2024
Also, if you have ideas for how these switchable cytokines can modulate biological systems in new ways, we would love to discuss/collaborate! We envision these tools could open up a whole new way to explore the biology of transient cytokine signaling.
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Mauriz Lichtenstein @mlichtenstein.bsky.social · 20/11/2024
Check out this great work by @adambroerman.bsky.social. We describe a general way to control and sense ppi with fast kinetics using #proteindesign. Congrats! www.biorxiv.org/content/10.1...
biorxiv.org
Design of facilitated dissociation enables control over cytokine signaling duration
Protein design has focused primarily on the design of ground states, ensuring they are sufficiently low energy to be highly populated[1][1]. Designing the kinetics and dynamics of a system requires, i...
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