The White Lab is interested in identifying novel therapeutic targets for multiple disease states as well as answering some fundamental mechanistic questions in biology. We are particularly involved in quantifying changes in the protein signaling networks using a combination of mass spectrometry based proteomics and computation modeling.
Despite the wealth of computational techniques designed to predict responses from RTK signaling, the data available for these efforts is relatively poor. Major shortcomings include lack of site specificity, relative quantification, and poor temporal resolution. We have developed new mass spectrometry-based methods that improve measurements of signaling dynamics... more >>
Protein phosphorylation plays a vital role in coordinating information flow within the cell and regulating emergent tumor phenotypes ranging from proliferation to invasion and angiogenesis. Quantitative analysis of protein signaling circuits in human tumor specimens can provide insight into intracellular signaling networks underlying tumor behavior while identifying activated kinases and their substrates, signaling components that may represent druggable targets... more >>
Insulin receptor signaling regulates blood glucose homeostasis. Obesity, among other conditions, decreases insulin receptor signaling, resulting in increased blood glucose, increased insulin levels, and a host of adverse health effects... more >>
One of the key challenges of mapping a kinase to particular substrate phosphorylation events is establishing a direct kinase-substrate interaction. Such knowledge would be useful for further understanding signal transduction networks and discovering novel substrates of kinases... more >>
Mass spectrometry-coupled chemical proteomics approaches have been utilized in multiple aspects of small molecule drug research, including identification of drug targets, quantification of drug-to-target interaction affinity, and selectivity profiling... more >>