Noah Holzleitner
PhD Student at Grünewald Lab (TUM)
🧬Protein Design for CRISPR proteins🧑🏽💻👨🏽🎨
- Reposted by Noah Holzleitner🧬🌉Online @science.org Programmable genome editing in human cells using RNA-guided bridge recombinases | Science www.science.org/doi/10.1126/...
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- Reposted by Noah HolzleitnerDoes the noncoding genome actually carry more genetic information than coding seqs? Motivated by this question we mutated every bp in the 10kb MYC locus. Results are even more exciting: Decoding the MYC locus reveals a druggable ultraconserved RNA element www.biorxiv.org/content/10.6...
- Reposted by Noah HolzleitnerFoldMason is out now in @science.org. It generates accurate multiple structure alignments for thousands of protein structures in seconds. Great work by Cameron L. M. Gilchrist and @milot.bsky.social. 📄 www.science.org/doi/10.1126/... 🌐 search.foldseek.com/foldmason 💾 github.com/steineggerla...
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- Reposted by Noah HolzleitnerEDEN: a family of genomic language models trained on up to 9.7 trillion nucleotides from @basecamp-research.bsky.social's BaseData can design large serine recombinases, bridge recombinases, and antimicrobial peptides. www.biorxiv.org/content/10.6... Happy to have played a small part in this!
- Reposted by Noah HolzleitnerCan we design mutations that bias proteins towards desired conformational states? Today in @science.org, we introduce Conformational Biasing (CB), a simple and scalable computational method that uses contrastive scoring by inverse folding models to identify conformation-biasing mutations.
- Reposted by Noah Holzleitner1/ Check out our newest paper where we ask: How fast can we experimentally discover binders from scratch? And we mean scratch: a blinded study. TLDR: 26 days. And the binders work…and led to new cancer biology. We’re coming for you AI…. chemrxiv.org/engage/chemr...
- Reposted by Noah Holzleitner✨New preprint! 🧵1/4 Excited to share our work on AI-guided design of minimal RNA-guided nucleases. Amazing work by @petrskopintsev.bsky.social @isabelesain.bsky.social @evandeturk.bsky.social et al! Multi-lab collaboration @banfieldlab.bsky.social @jhdcate.bsky.social @jacobsenucla.bsky.social🧬 🔗👇
- Reposted by Noah HolzleitnerCheck out our newest work! This is a story on how to get selectivity in binders - both isoform and site selectivity. Read the paper or enjoy this brief Skytorial of what we did! www.biorxiv.org/content/10.1... 1/n
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- Reposted by Noah HolzleitnerNew preprint from @gocastelobranco.bsky.social lab!! We use MPRA & scCRISPRi/a to interrogate possible functions of GWAS-identified Multiple sclerosis risk SNPs in iPSC-derived oligodendrocytes. www.biorxiv.org/content/10.1...
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- Super interesting! Love the “Turning an Art into Science” aspect 🧬
- Our latest work seeks to answer a longstanding question: why is discovering new protein binders seemingly unpredictable – and can we better quantify and understand the de novo binder discover process? 1/12 www.biorxiv.org/content/10.1...
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- Reposted by Noah HolzleitnerTwo group leader positions available in the broader areas of RNA science, RNA technologies, and RNA medicine. Attractive packages and a great environment. Come and join us at Helmholtz RNA Würzburg, Bavaria.
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- Reposted by Noah HolzleitnerThe team is already working to expand the platform’s abilities, including testing in clinically relevant immune and stem cells, and engineering future versions of the system that can rearrange sequences beyond one megabase. Learn more in the full paper: www.science.org/doi/10.1126/...
- Looks very nice!
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- Reposted by Noah Holzleitnervery cool work and a milestone in synthetic biology. how impressive are the new phage genomes? with generative bioML, i'm always looking at how similar the generated sequences are to known sequences. let's take a look
- Reposted by Noah HolzleitnerOptimization of a bespoke base editor to treat a severe pediatric vascular disease! 🫀🧬 Our manuscript describes: 1️⃣ Engineering a target-specific BE🧬 2⃣ A *must avoid* bystander edit that occurs with WT SpCas9 BEs! 🙅♂️ 3⃣ Extension of lifespan after in vivo editing! 🐁✅ www.nature.com/articles/s41...
- Reposted by Noah HolzleitnerLooking for a new approach to studying or eliminating phages? Check out our study introducing anti-phage ASOs (antisense oligos) out in @Nature today. nature.com/articles/s4158…
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- Reposted by Noah HolzleitnerExciting to see our protein binder design pipeline BindCraft published in its final form in @Nature ! This has been an amazing collaborative effort with Lennart, Christian, @sokrypton.org, Bruno and many other amazing lab members and collaborators. www.nature.com/articles/s41...
- Reposted by Noah HolzleitnerRFdiffusion2 is now live! github.com/RosettaCommo... You can now design proteins, and in particular enzymes from just partially defined amino acid side chains, and without defining their sequence position or order!
- Reposted by Noah HolzleitnerIf you use Boltz1/2, BioEmu, Chai1, or other MSA-dependent models, you’re likely using our ColabFold server. Please be considerate! Avoid large submissions across many IPs instead generate the MSA locally. Our server is an old-timer from 2014 and can’t handle that load.
- Reposted by Noah Holzleitner(1/7) Training biomolecular foundation models shouldn't be so hard. And open-source structure prediction is important. So today we're releasing two software packages: AtomWorks and RosettaFold3 (RF3) [https://www.biorxiv.org/content/10.1101/2025.08.14.670328v2](www.biorxiv.org/content/10.1...)
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- Reposted by Noah HolzleitnerThis preprint from Helen Sakharova is one of the coolest things to come out of my lab: “Protein language models reveal evolutionary constraints on synonymous codon choice.” Codon choice is a big puzzle in how information is encoded in genomes, and we have a new angle. www.biorxiv.org/content/10.1...
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- This looks pretty cool to advance protein testing!
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- Reposted by Noah HolzleitnerUnexpectedly, @jurgjn.bsky.social found that running Alphafold3 predictions for protein interactions can yield ipTM scores that are more predictive of true interactions when run in pools of proteins instead of pairwise predictions. Presumably, this reflects some sort of "competition effect".
- Reposted by Noah HolzleitnerYou designed binders for your favourite protein and wish there was a way to experimentally screen them within 24h w/ only a set of pipettes and a plate reader? Check out our Cell-Free 2-Hybrid approach (CF2H) Full post: tinyurl.com/48cz5nb6 Preprint: www.biorxiv.org/cgi/content/...
- Reposted by Noah HolzleitnerStructural motif search across the protein-universe with Folddisco biorxiv.org/content/10.1101/202…
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- Reposted by Noah HolzleitnerPresenting RISoTTo, a molecular context-aware model for RNA sequence design, building on our work with PeSTo (for protein binding interface prediction) and CARBonAra (for protein design). 📄 Preprint: www.biorxiv.org/content/10.1... 💻 Code & more coming soon! #RNAdesign #RNAbiology #AI4Science
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- Reposted by Noah HolzleitnerExcited to unveil Boltz-2, our new model capable not only of predicting structures but also binding affinities! Boltz-2 is the first AI model to approach the performance of FEP simulations while being more than 1000x faster! All open-sourced under MIT license! A thread… 🤗🚀
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- Reposted by Noah Holzleitner1/10 Today in @science.org in collaboration with the Liu group we report the development of a laboratory-evolved CRISPR-associated transposase (evoCAST) that supports therapeutically relevant levels of RNA-programmable gene insertion in human cells. drive.google.com/file/d/1I-Ub...
- Reposted by Noah HolzleitnerGenomes encode biological complexity, which is determined by combinations of DNA mutations across millions of bases In new work @arcinstitute.org, we report the discovery and engineering of the first programmable DNA recombinases capable of megabase-scale human genome rearrangement
