- postdoctoral associate with Professor Watt Webb at Cornell University (2003-2006)
- postdoctoral associate with Professor Gilad Haran at the Weizmann Institute of Science (2001-2003)
- PhD in Biophysics from the University of Michigan, Ann Arbor (2001)
- B.S. in Physics from Duke University (1994)
Research in the Rhoades lab aims to elucidate the principles that link protein conformational change with structure-function relationships, focusing on understanding structural plasticity in intrinsically disordered proteins (IDPs). IDPs do not form stable structures under physiological conditions; for many, function is dependent upon disorder. This is in striking contrast to the structure-function paradigm that dominates our understanding of globular proteins. Given the large fraction of the eukaryotic proteome predicted to be disordered, the scope of the problem and the need for new insights are enormous.
Much of our effort is directed towards IDPs whose aggregation is central to the pathology of several degenerative diseases: α-synuclein (Parkinson’s disease), tau (Alzheimer’s disease), and IAPP (Type II Diabetes). These three proteins have diverse native functions and binding partners, but share intriguing commonalities of toxic mechanism and the importance of templated selfassembly. Studying systems in parallel allows us to generate protein and disease-specific insights as well as determine principles relevant to general functional and dysfunctional mechanisms of IDPs.
Our primary approaches center on single molecule optical techniques. These approaches enable quantitative and structural assessments of our systems in isolation and in the context of biologically relevant interactions. Single molecule approaches are unique in their ability to characterize systems which exist and function as a dynamic ensemble of states.
- M. Birol, S. Wójcik, A. D. Miranker and E. Rhoades (2019) "Identification of N-linked glycans as specific mediators of neuronal uptake of acetylated α-Synuclein" PLoS Biology, 17: e3000318 doi: doi.org/10.137journal.pbio.3000318
- S. Espinoza Sanchez, L.A. Metskas, S.Z. Chou, E. Rhoades and T.D. Pollard (2018) “Conformational changes in Arp2/3 complex induced by ATP, WASp-VCA and actin filaments” Proceedings of the National Academy of Sciences, 115: E8642-E8651 doi: 10.1073/pnas.1717594115
- M. Birol, S. Kumar, E. Rhoades* and A.D. Miranker* (2018) "Conformational switching within dynamic oligomers underpins toxic gain-of-function by diabetes-associated amyloid" Nature Communications, 9:1312 doi: 10.1038/s41467-018-03651-9
- J.J. Ferrie, C.M. Haney, J. Yoon, B. Pan, Y.C. Lin, Z. Fakhraii, E. Rhoades, A. Nath and E.J. Petersson (2018) "Using a FRET Library with Multiple Probe Pairs to Drive Monte Carlo Simulations" Biophysical Journal, 114: 53-64 doi: 10.1016/j.bpj.2017.11.006
- X-H. Li and E. Rhoades (2017) "Heterogeneous tau-tubulin complexes accelerate microtubule polymerization" Biophysical Journal, 112: 2567-2574 doi: 10.1016/j.bpj.2017.0006
- A.M. Melo, J. Coraor, G. Alpha-Cobb, S. Elbaum-Garfinkle, A. Nath and E. Rhoades (2016) “Conformational Plasticity in the Tau-Tubulin Complex: A Functional Role for Intrinsic Disorder” Proceedings of the National Academy of Sciences, 113:14336-14341 doi: 10.1073/pnas.1610137113
- S. Kumar, M. Birol, D. E. Schlamadinger, E. Rhoades* and A.D. Miranker* (2016) “Foldamer mediated manipulation of a pre-amyloid toxin” Nature Communications, 7: 11412 doi: 10.1038/ncomms11412
- L.A. Metskas and E. Rhoades (2015) “Conformation and Dynamics of the Troponin I C-terminal Domain: Combining Single-Molecule and Computational Approaches for a Disordered Protein Region” Journal of the American Chemical Society, 137: 11962-11969 doi: 10.1021/jacs.5b04471
- X.-H. Li, J. A. Culver and E. Rhoades (2015) “Tau binds to multiple tubulin dimers with helical structure” Journal of the American Chemical Society, 137: 9218-9221 doi: 10.1021/jacs.5b04561.
- D. Jülich, G. Cobb, A.M. Melo, P. McMillen, A. Lawton, S.G.J. Mochrie, E. Rhoades, and S.A. Holley (2015) “Cross-scale Integrin regulation organizes ECM and tissue topology” Developmental Cell, 34: 33-44 doi: 1016/j.devcel.2015.05.005
- D.L.A. Esposito, J.B. Nguyen, D.C. DeWitt, E. Rhoades, and Y. Modis (2015) “Physicochemical requirements and kinetics of membrane fusion of flavivirus-like particles” Journal of General Virology, 96: 1702-1711 doi: 10.1099/vir.0.000113.
- J. LaRochelle, G. Cobb, A. Steinauer, E. Rhoades* and A. Schepartz* (2015) “Fluorescence correlation spectroscopy reveals highly efficient endosomal escape by certain penta-arg proteins and stapled peptides” Journal of the American Chemical Society. 127: 2536-2541 doi: 10.1021/ja510391n
- A.R. Braun, M.M. Lacy, V.C. Ducas, E. Rhoades and J.N. Sachs (2014) “α-Synuclein-induced membrane remodeling is driven by binding affinity, partition depth, and interleaflet order asymmetry” Journal of the American Chemical Society, 136: 9962-9972 doi: 10.1021/ja5016958
- S. Elbaum-Garfinkle, G. Cobb, J. T. Compton, X. Li and E. Rhoades (2014)“Tau mutants bind tubulin heterodimers with enhanced affinity” Proceedings of the National Academy of Sciences U.S.A., 111: 6311-6316 doi: 10.1073/pnas.1315983111.
- J. B. Munro, A. Nath, M. Färber, S.A.K. Datta, A. Rein, E. Rhoades and W. Mothes (2014) “A conformational transition in HIV-1 Gag early during virus assembly”Journal of Virology, 88: 3577-3585 doi: 10.1128/JVI.03353-13
- D. C. DeWitt and E. Rhoades (2013) “α-Synuclein Inhibits SNARE-mediated Vesicle Fusion Through Direct Interactions with Lipid Bilayer” Biochemistry, 52: 2385-2387 doi: 10.1021/bi4002369. *Highlighted on the Biochemistry homepage
- S. Elbaum-Garfinkle and E. Rhoades (2012) “Identification of an aggregation-prone structure of tau” Journal of the American Chemical Society, 134: 16607-16613 doi: 10.1021/ja305206m * Highlighted in C&E News, JACS Spotlights, and ASBMB Today
- A. Nath*, M. Sammalkorpi, D. DeWitt, A.J. Trexler, S. Elbaum-Garfinkle, C.S. O’Hern*and E. Rhoades* (2012) “The Conformational Ensembles of α-Synuclein and Tau: Combining Single-Molecule FRET and Simulations” Biophysical Journal, 103: 1940-1949 doi: 10.1016/j.bpj.2012.09.032
- A.J. Trexler and E. Rhoades (2012) “N-terminal acetylation is critical for forming α-helical oligomer of α-Synuclein” Protein Science, 21:601-605 doi: 10.1002/pro.2056 * Most cited paper in Protein Science 2012
- A.R. Braun, E. Sevcsik, P. Chin, E. Rhoades, S. Tristram-Nagle and J.N. Sachs (2012) “α-Synuclein Induces Both Positive Mean Curvature and Negative Gaussian Curvature in Membranes” Journal of the American Chemical Society, 134: 2613-2620 doi: 10.1021/ja208316h
- E. Sevcsik, A.J. Trexler, J.M. Dunn and E. Rhoades (2011) “Allostery in a disordered protein: Oxidative modifications to α-Synuclein act distally to regulate membrane binding” Journal of the American Chemical Society, 133: 7152-7158 doi: 10.1021/ja2009554
- E. R. Middleton and E. Rhoades (2010) “Effects of vesicle curvature and composition on α-Synuclein binding to lipid vesicles” Biophysical Journal, 99: 2279-2288 doi: 10.1016/j.bpj.2010.07.056
- A.J. Trexler and E. Rhoades (2009) “α-Synuclein binds large unilamellar vesicles as an extended helix” Biochemistry, 48: 2304-2306 doi: 10.1021/bi900114z