Samuel N. Young

This study identifies dysregulated epithelial cell death signaling in inflammatory bowel disease, showing it persists during remission despite therapy.

This study compares three RIPK3 kinase-dead variants to show that their scaffolding functions differ based on kinase domain conformation, not just kinase activity, and highlights implications for inhibitor development.

The paper identifies an unconventional mechanism where Ca2+-CaM binds CHK2 kinase to inhibit its activity, contrasting with its typical role in promoting kinase activity.

This study shows that partial reduction of BECLIN1 in intestinal epithelial cells leads to intestinal defects and increased susceptibility to inflammation, suggesting its importance in maintaining gut health.

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

The paper develops automated immunohistochemistry protocols to detect necroptotic pathway proteins in mouse and human tissues, revealing heterogeneity and disease-related changes in expression.

This study demonstrates that MLKL ubiquitylation, triggered by oligomerization, regulates necroptosis by modulating MLKL activity and turnover.

This study identifies a missense mutation in MLKL causing lethal neonatal inflammation in mice and links it to increased frequency in human autoinflammatory disease.