Claire E. Eyers

The paper evaluates proteomics platforms for metabolic pathway analysis in biomanufacturing chassis organisms, showing varying proteome coverage across different instruments.

This study develops an integrated mass spectrometry strategy to quantify the proteoform diversity of O-glycoprotein osteopontin, revealing systematic underestimation of glycan sialylation by bottom-up methods.

This paper optimizes haemoglobin depletion in dried blood spots to improve proteomic analysis, increasing protein identifications by ~50% and enabling biomarker discovery in CKD patients.

This study shows that phosphorylation at S345 converts HIF-2α from a transcription factor to an RNA-binding protein, altering its function in hypoxia response.

This study examines proteomic changes in human muscle constructs under microgravity and shows that HSP10 overexpression reduces these changes, suggesting a potential strategy for combating muscle atrophy.

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.

The paper identifies zDHHC23 as a hypoxia-responsive gene associated with metastasis in non-MYCN amplified neuroblastoma, suggesting it as a potential biomarker and therapeutic target.

This study identifies IL-1 and IL-6 as key drivers of neuroinflammation in HSV encephalitis, showing they are not reduced by corticosteroids and are associated with poor outcomes.

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.

This study presents an optimized phosphoproteomics workflow using SP3 beads with improved phosphopeptide identification and detection of multiply phosphorylated peptides in HEK-293T cells.

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.

Cryo-ET of 169 nm β-carboxysomes from low-light Synechococcus elongatus reveals ~639 Rubiscos in concentric layers with CcmM bound at RbcL grooves; QconCAT proteomics yields the complete absolute protein stoichiometry.

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.

This study investigates how redox regulation via cysteine oxidation controls BRSK1/2 kinase activity, revealing conserved mechanisms that modulate catalytic function through disulfide bond formation and salt bridge disruption.

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.