Ziyuan Jiang

This study uses single-cell transcriptomics to analyze how diverse SHP2 variants affect gene expression and cellular phenotypes in relation to disease.

This study uses proximity-labeling proteomics to analyze how SHP2 mutations alter its interactome and localization, revealing functional consequences of different mutation types.

This study identifies a novel active conformation of SHP2 stabilized by the E139D mutation, which alters phosphoprotein binding preferences compared to canonical hyperactive mutants.

The paper uses deep mutational scanning to analyze SHP2 mutations, revealing diverse regulatory mechanisms and potential pathogenicity of uncharacterized variants.

This study shows that a catalytically inactive Shp2 mutation causes hydrocephalus by altering conformation, which can be rescued by allosteric inhibition.