Hupp Lab
Research
How is p53 converted from a restrained protein into an active tumour suppressor?
The laboratory investigates biochemical mechanisms that activate and stabilise p53, including phosphorylation, ubiquitination and conformational control.
Mechanistic protein chemistry and cellular assays identify regulatory sites and interaction surfaces that may be exploited in cancers retaining a recoverable p53 pathway.
Which dominant oncogenic signals disable p53 without mutating TP53?
Many tumours retain wild-type p53 but neutralise its activity through altered binding partners and signalling networks.
The group maps dominant oncogenic interactions and uses functional perturbation and high-content phenotyping to find pathway nodes that reactivate tumour suppression.
How can tumour sequence variation be translated into actionable protein information?
The laboratory integrates genomic variation with protein expression, structure and immune recognition to prioritise alterations that are translated and biologically exposed in cancer cells.
Computational and experimental pipelines nominate tumour-associated antigens, classify variant effects and develop detection strategies.
Can mechanistic target knowledge be converted into selective biologics and small molecules?
The group develops affinity reagents and screening strategies against cancer-associated proteins, building from mechanistic assays to candidate biologics and small molecules.
Projects connect epitope definition, antibody engineering, nanosensing and phenotypic validation to establish target engagement and selectivity.
