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HT-PELSA, a new proteomics tool by EMBL researchers, processes samples 100x faster and works directly with complex crude cell, tissue, and bacterial lysates – developments which could accelerate basic biological research and drug discovery 💊 🔗 https://t.co/gtJZJt9EoR

Happy to see our HT-PELSA paper now published in @NatureSMB 🎊Big thanks for the constructive review process! 📖Read the manuscript here ( https://t.co/Ehen3vkW51...) & check the thread for additional information ⬇️

All data can be interactively explored https://t.co/afxgVAtnt2; This work was led by Kejia Li @KeJia93_Li and Clément Potel, with invaluable contributions from Isabelle Becher, Nico Hüttmann @NicoHuettmann, Martín Garrido-Rodríguez @martingarridorc, and Jennifer Schwarz.

3/3 We extended its application to crude human cell line, bacteria, and tissue and sensitively identify membrane targets! It works extremely well in tissues, which allowed us to identify sunitinib off-targets in mouse heart tissue, and could explain its cardiotoxicity.

2/3 We provide a large collection of ATP-binding proteins in E.coli and give rich information on how they respond to ATP. Our data nicely showed how chaperon protein DnaK binds ATP at ATP-binding site at low ATP concentration and dissociates its substrate protein at high conc.

1/3 We extended the original PELSA to work with 96-well plates and show a 100-fold higher throughput, excellent reproducibility, accurate determination of drug-binding affinities in dose-response experiments as shown by a strong correlation of 0.88 with kinobeads measurements.

1/3 We extended the original PELSA to work with 96-well plates and show a 100-fold higher throughput, excellent reproducibility, accurate determination of drug-binding affinities in dose-response experiments as shown by a strong correlation of 0.88 with kinobeads measurements.

Want to know how the ligands interact with proteins beyond model human cell lines? Interested in membrane targets? Check out our High-Throughput PELSA method which allows you do all these cool screenings for dozens of ligands within 2 hours!

All data can be interactively explored 🖥️ https://t.co/HEeQVq4UIh. This work was led by Clement Potel, @ https://t.co/wy2qddu82V and @ https://t.co/FcbzPZ1k7o . We thank our great collaborators @ https://t.co/qqrvYwuC0h and @ https://t.co/tzWGTkQKQE.

Finally, we once again uncovered site-specific modulation of glycosylation upon perturbation, meaning that only some glycoforms on some glycosites are modulated, even within the same protein, suggesting complex regulatory mechanisms.

We showed remodeling of the mouse brain glycoproteome upon gut microbiome colonization 🐭 The link b/w gut microbiome & brain physiology is long known, but molecular mechanisms remain elusive. We showed that proteins involved in neurotransmission & axon guidance were affected.

We next used our quantitative approach to measure the dynamics of glycosylation changes in human cells treated with a fucosylation inhibitor 🧫 We discovered pervasive site-specific modulation of glycosylation upon perturbation.

Very little is known about glycoform functionality. We developed a functional glycoproteomics approach enabling the proteome-wide characterization of the solubility of different glycosylated proteoforms in the mouse brain 🐭

To understand structural features governing the level of site microheterogeneity, we leveraged our comprehensive dataset in combination with AlphaFold DB 🖥️

It is essential to differentiate surface-exposed glycoforms from intermediate species. To address this, we treated intact living human cells with two enzymes, enabling proteome-wide characterization of mature glycoforms 🧫

Using our quant approach, we discovered that many sites have similar glycosylation patterns across tissues 🐭We identified sites driving tissue-specificity, enriched in domains involved in cell adhesion, signaling & immunity. E.g., only N445 exhibits tissue specificity on INSR.

We are very happy to present our work on N-glycoproteomics!🍬 Our method enables the selective enrichment and precise quantification of intact N-glycopeptides to explore the dynamics of glycosylation microheterogeneity. https://t.co/KrumrYP7m0

Exciting opening at the proteomics core facility at EMBL! Please spread, apply and reach out!

1/11 - With @KMitosch and Clément Potel + colleagues in @savitski_lab @TypasLab @embl, I’m very happy to share our discovery of a hyper-promiscuous phage protein kinase (T7K) which broadly deactivates bacterial defenses! https://t.co/Yjqtwof1um