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Reporters of
protein-protein interaction
Genomic biology has motivated the search for new general techniques for detecting protein-protein interactions in living cells. Existing technologies are either destructive or perturbative, in that they require either cell lysis or fusion of proteins to reporters, which can result in overexpression and/or steric interference with function. We are developing new protein-protein interaction detection methods which will address many of the limitations of existing methods, offering reduced false positive and reduced false negative signals. Our reporter designs are sufficiently general that we envision eventual extension to genome-wide cell-based protein-protein interaction profiling.

Related publications:
Protein-protein interaction detection in vitro and in cells by proximity biotinylation.
Journal of the American Chemical Society 2008, 130, 9251-9253.
M. Fernandez-Suarez, T. S. Chen, and A. Y. Ting
An engineered aryl azide ligase for site-specific mapping of protein-protein interactions through photocrosslinking.
Angewandte Chemie International Edition 2008, 47, 7018-7021.
H. Baruah, S. Puthenveetil, Y.-A. Choi, S. Shah, and A. Y. Ting.Back to research. |