Ranaghan MJ, Durney MA, Mesleh MF, et al. The autophagy-related beclin-1 protein requires both the coiled-coil and BARA domains to form a homodimer with sub-micromolar Affinity. Biochemistry 2017;56(51):6639–6651.
Tsai M-F, Phillips C, Ranaghan MJ, et al. Dual functions of a small regulatory subunit in the mitochondrial calcium uniporter complex. eLife, 2016;15545.
Ranaghan MJ, Schwall C, Alder NN, Birge RR. Green proteorhodopsin reconstituted into nanoscale phospholipid bilayers (nanodiscs) as photoactive monomers. J Am Chem Soc. 2011;133(45):18318–18327.
Matthew Ranaghan, Ph.D.
Matthew Ranaghan is a research scientist II in the Center for the Development of Therapeutics (CDoT) at the Broad Institute of MIT and Harvard under the direction of Colin Garvie. His areas of expertise include molecular biology, protein purification, biochemistry, and biophysics. Ranaghan currently works on discovering therapeutic tools to modulate and on developing in vitro methods to monitor protein-protein interactions.
Prior to joining the Broad Institute in May 2015, Ranaghan did his postdoctoral research in the laboratory of Daniel Oprian at Brandeis University, where he studied the calcium-dependent signal termination mechanism of rhodopsin, a visual G protein-coupled receptor. Ranaghan also collaborated with the laboratory of Christopher Miller (Brandeis) to study the structure-function relationship of proteins in the mitochondrial calcium uniporter complex.
Ranaghan holds a Ph.D. in biochemistry from the laboratory of Robert Birge at the University of Connecticut, where he worked to enhance microbial rhodopsins for application in biophotonic (e.g., photovoltaics, 3D volumetric memories) and biomimetic (e.g., artificial retina) devices. Part of his thesis work was contributed to a patent that helped start LambdaVision, Inc., which seeks to develop protein-based prosthetics to treat visual disorders. He also holds a B.S. in chemistry from Roger Williams University.
Contact Matthew Ranaghan via email at firstname.lastname@example.org.