A true tour-de-force study by the group of Bernhard Küster posted as bioRxiv preprint. They profiled 133 kinase inhibitors in 5 cell lines at 11 doses using #phosphoproteomics with #decryptM to identify 5,318 confident kinase::substrate relationships for 96 human #kinases. https://www.biorxiv.org/content/10.1101/2025.11.18.689017v1

#Chemistry #ChemBio #Proteomics #DrugDiscovery #Signalling

A tour-de-force study by the group of Bernhard Küster (@kusterlab.bsky.social@bsky.brid.gy). They profiled 133 kinase inhibitors in 5 cell lines at 11 doses using #phosphoproteomics to identify 5,318 confident kinase::substrate relationships for 96 human #kinases www.biorxiv.org/content/10.1... #ChemSky #ChemBio

biorxiv.org/content/10.110...

Our new preprint, presenting PulsPhos, a novel method for proteome-wide measurement of the dynamics of protein phosphorylation at specific sites in living cells, is now out!

This required inventing an elegant strategy for measuring the pool of available phosphates in, which allows us to account for the complex biotransformations of phosphates that occur in intact cells.

https://www.biorxiv.org/content/10.1101/2024.07.23.604744v1

#proteomics #phosphoproteomics #massspec
#bioinformatics

The #phosphoproteomics data also supports the importance of the large exon missing from the 1251 aa exoform.

#Phosphoproteomics reveal pervasive rewiring of #Cdk1 and Polo kinase phosphorylations during yeast #meiosis, ensuring the occurrence of two successive divisions without intervening S-phase

Lori Koch, Adele Marston et al

https://www.embopress.org/doi/full/10.1038/s44318-024-00059-8

Global phosphoproteomics reveal the diverse roles of casein kinase 1 in plant development

Protein phosphorylation is a major posttranslational modification carried out by protein kinases that constitute an integral part of complex signaling networks in eukaryotes. Casein kinase 1 (CK1) is a conserved serine/threonine protein kinase in eukaryotes and plays pivotal roles in both plants and mammals through phosphorylating various substrates.

Phys.org

Discovering the dynamic world of the EGFR-MAPK phosphoproteome. 🌐🔎

Feng, Sanford and colleagues #EMSLscience developed a multiplexed deep phosphoproteome profiling workflow unveiling 4500 protein sites exhibiting increased phosphorylation upon EGF stimulation.

Another great #preLight by Benjamin Maier 👉 https://prelights.biologists.com/highlights/a-phosphoproteomics-data-resource-for-systems-level-modeling-of-kinase-signaling-networks-v2/

#preprint # modelling #phosphoproteomics #signalling #bioinformatics #SystemsBiology

A Phosphoproteomics Data Resource for Systems-level Modeling of Kinase Signaling Networks - preLights

Discovering the dynamic world of the EGFR-MAPK phosphoproteome: Feng, Sanford and colleagues developed a multiplexed deep phosphoproteome profiling workflow unveiling 4500 protein sites exhibiting increased phosphorylation upon EGF stimulation.

preLights
Estimation of activity changes for >500 kinases & transcription factors in >1,000 cancer samples & cell lines identifies drivers of signalling dysregulation & patient survival ➡️ https://www.embopress.org/doi/full/10.15252/msb.202110631
@pedrobeltrao IMSB ETH
@saezlab UniHeidelberg
@Epetsalaki EMBL-EBI
#CancerGenomics #Genomics #Phosphoproteomics #SystemsBiology