Patrick A. Eyers

This study identifies TRIB2 as a therapeutic target in AML by demonstrating that its degradation via PROTACs and small molecules can reverse chemoresistance and enhance chemotherapy efficacy.

This paper shows that pervanadate induces oxidation, which activates SRC kinases by disrupting autoinhibition and altering SH2 domain phosphopeptide binding, revealing a redox-dependent mechanism for SRC activation.

This study shows RAF inhibitors activate the integrated stress response via direct GCN2 activation, independent of ERK1/2, leading to ATF4 and CHOP expression.

The paper predicts novel phosphorylation sites across eukaryotes using conservation analysis and evaluates their functional relevance by linking conservation patterns to protein functions and kinase evolution.

The paper identifies allosteric regulation of PSKH1 kinase activity by Ca2+ sensor proteins, showing both activation and suppression by different sensors.

The paper identifies sulfotyrosine (sY) sites in the human phosphoproteome by distinguishing them from phosphorylation using mass error shifts and filters out false positives, finding 31 convincing sY sites.

This study identifies Aurora-A as a CDK12-activating kinase in neuroblastoma, showing its role in transcription termination and tumor growth suppression.

This study identifies PNUTS-PP1 as a regulator of Cdk11 phosphorylation, showing that dephosphorylation by PNUTS-PP1 modulates Cdk11 activity and affects mRNA processing and splicing.

The paper estimates the false discovery rate of phosphosites in public databases and predicts a more realistic count of true phosphosites in the human proteome.

The paper shows that mutations in PKAc cause displacement from AKAP signaling islands, leading to distinct pathogenic signaling pathways in Cushing's syndrome.

The paper identifies EGFR/HER2 inhibitors that destabilize and degrade TRIB2 pseudokinase in cancer cells, suggesting potential for TRIB2-targeted therapies.

This study identifies extensive non-canonical phosphorylation in human cells using a new phosphoproteomics method, revealing over 1000 phospholysine sites and 310 phosphohistidine sites.