Sean J. Humphrey

The paper identifies WEE1, CDK1, and PLK1 as regulators of mRNA export during DNA replication stress, showing their role in preventing R-loop associated mRNA from being exported to the cytoplasm.

The paper uses personalized phosphoproteomics to show that mTORC1 regulates exercise-induced insulin sensitization in human skeletal muscle through a feedback pathway involving MKNK2 and eIF4G1.

This study shows that gene therapy with AAV-ALPK3 improves heart function in mouse and human models of cardiomyopathy caused by ALPK3 variants.

The paper identifies a compound that selectively promotes cardiomyocyte proliferation through specific cell cycle mechanisms without affecting other cell types.

This study uses proteomics to identify a cryptic JPH2 loss-of-function in a paediatric DCM patient, revealing a novel mechanism of recessive disease.

This study shows that ageing reduces the phospho-proteomic response to resistance exercise in human skeletal muscle, despite normal mTORC1 activation, suggesting new therapeutic targets for aged muscle.

This study identifies extensive phosphoproteomic remodeling in mouse sperm during maturation and capacitation, revealing key kinases and their roles in fertility.

The paper shows that inhibiting contractile function in cardiomyocytes reactivates the cell cycle, suggesting active contraction maintains differentiation and cell cycle arrest.

This study shows that maturing human cardiac organoids enhances disease modeling and drug discovery by mimicking in vivo development and enabling therapeutic testing for DSP cardiomyopathy.

This study investigates the role of PKD in adipose tissue, revealing sex-dependent effects on metabolism through phosphoproteomics and a mouse model.

The paper develops SnapKin, a deep learning ensemble model for kinase-substrate prediction from phosphoproteomics data, achieving the best performance in this task.

This study uses phosphoproteomics to show how genetic background and diet influence insulin signalling in muscle, revealing key regulators of insulin responsiveness and glycolysis in insulin resistance.

μPhos is a phosphoproteomics platform that enables the identification of 5,000 phosphorylation sites from 5 µg of sample, supporting extensive perturbation experiments.

This study uses phosphoproteomics to show that insulin resistance involves rewired signaling networks and widespread dysregulation of GSK3 activity.

The paper compares proteomics profiles of subcutaneous and visceral adipose tissue in mice to identify depot-specific differences and responses to diet.

PhosR provides tools for processing and analyzing phosphoproteomic data, enabling data imputation, normalization, and functional analysis of kinase activity and signaling pathways.

The paper maps multi-omic changes during mouse pluripotency transition, showing phosphoproteome dynamics precede epigenome and transcriptome changes.

The paper uses phosphoproteomics to identify signaling changes in diabetic islets, revealing GSK3's role in PDX1 and insulin secretion.