- Previous Affiliation: Assistant Professor, Ben May Department for Cancer Research
- Current Affiliation: Vice President, VMRD, Inc, Pullman, WA
900 East 57th Street, KCBD 10118
Chicago, IL 60637
The University of Chicago
Phone: (773) 702-2185
Fax: (773) 834-2877
In order for a metazoan to develop from a fertilized egg and become an adult organism, it must utilize a complex set of autocrine, paracrine, and endocrine molecular networks. While large-scale gene expression analyses of cell, tissue, and whole organisms have uncovered some of these biological systems, complete analysis of all dynamic protein signaling networks have proven to be a challenge. Our lab is focused on this problem by using protein micro-array, mass spectrometric, and cell biological tools to study protein-protein interactions, protein abundance dynamics, post-translational modifications, and interaction pathway activities. The overall goal is to better understand the roles of signaling system molecules within critical spatial-temporal contexts to regulate cell growth, migration, differentiation, and apoptosis. These processes lie at the heart of cancer biology. An understanding of these network-based mechanisms will foster the development of new diagnostic tools and therapeutic agents for human diseases. Lab projects are focused on:
1. Analysis of mechanisms of receptor tyrosine kinase signaling in cancers.
2. Large-scale analysis of the SH2-protein recruitment capacity of receptor tyrosine kinases.
3. Large-scale analysis of receptor tyrosine kinase network connectivity.
4. Large-scale analysis of the relationship of human genetic variation, mRNA expression, protein expression, and variation
in response to chemotherapeutic agents.
- Systems analysis of EGF receptor signaling dynamics with microwestern arrays
- Relating human genetic variation to variation in drug responses.
- Innate immune and chemically triggered oxidative stress modifies translational fidelity.
- Comprehensive Binary Interaction Mapping of SH2 Domains via Fluorescence Polarization Reveals Novel
- Cholestane-3?, 5?, 6?-triol Suppresses Proliferation, Migration, and Invasion of Human Prostate
- Caffeic acid phenethyl ester suppresses the proliferation of human prostate cancer cells
- A potent and highly specific FN3 monobody inhibitor of the Abl SH2 domain