Research Interest: Mutations in other matrix proteins such as elastin and collagen been instrumental in understanding how these proteins function, are processed by the cell, and their significance in normal physiology and pathology. In contrast, mutations to aid the study of FN are historically non-existent. The recent discovery of a point mutation in a FN self-association domain represents a powerful opportunity to study how the FN matrix is assembled and how reductions in matrix affect cellular behavior.

Research Interest: Fibronectin is necessary for a collagen matrix to be present, but fibronectin's role in collagen matrix assembly has yet to be established. I am investigating how the fibronectin matrix as well as its associated proteins influence collagen matrix assembly.

Research Interest: The role of the fibronectin matrix in collagen processing and nascent fibrillogenesis is largely unknown. My work focuses on understanding how the fibronectin matrix and its associated proteins are involved in these initial processes that lead to collagen matrix formation.