Faculty RankAssistant Professor
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- Function of the neuropilin family as essential pleiotropic cell surface receptors. Parker MW, Guo H-F, Li X, Linkugel AD and Vander Kooi CW. Biochemistry 51:9437-46, 2012.
- Mechanism of selective VEGF-a binding by neuropilin-1 reveals a basis for specific ligand inhibition. Parker MW, Xu P, Guo H-F and Vander Kooi CW. PLoS ONE 7: e49188, 2012.
- Structural basis for VEGF-a isoform specific binding to neuropilin. Parker MW, Li X, Gou H-F, Xu P and Vander Kooi CW. J. Biol Chem 287:11082-9, 2012.
- Furin processing of semaphorin 3F determines its anti-angiogenic activity by regulating direct binding and competition for neuropilin. Parker MW, Hellman LM, Xu P, Fried MG and Vander Kooi CW. Biochemistry 49:4068-75, 2010.
- Structural basis for ligand and heparin binding to neuropilin B domains. Vander Kooi CW, Jusino MA, Perman B, Neau DB, Bellamy HD and Leahy DJ. Proc Natl Acad Sci USA 104:6152-7, 2007.
Cancer Center Member
Our lab focuses on understanding the basic mechanisms by which secreted growth factors regulate and coordinate cell signaling in complex multicellular organisms. Our specific interest centers on the essential human cell surface receptor neuropilin. Neuropilin is a conserved bi-functional mammalian cell surface receptor. Neuropilin has fundamental biomedical importance since it is essential to two distinct biological processes, angiogenesis and axon guidance. In additions to its normal roles, neuropilin also functions in tumor angiogenesis. Neuropilin expression is observed in tumor vasculature, and overexpression promotes tumorigenesis in vivo for a variety of solid tumors including those of the pituitary, prostate, breast, and colon. Strategies to inhibit neuropilin activity are being developed as potential antitumor therapies. Our lab seeks to define and improve mechanisms of inhibiting the neuropilin signaling pathway.