Charlotte is a post-doc in the lab. She was a student in the Biochemistry and Molecular Biophysics (BMB) graduate group at Penn from August 2016 to October 2022. She graduated from the University of North Carolina at Chapel Hill in 2016 with a B.S. in biology and minors in both chemistry and physics. In addition to her passion for science, Charlotte enjoys photography, solving crosswords, and exploring Philadelphia. In 2019, Charlotte was awarded a Ruth L. Kirschstein National Research Service Award (NRSA) from the National Institute of Neurological Disorders and Stroke (NINDS). Charlotte defended her Ph.D. thesis 'Engineering Karyopherin-β2 to disaggregate ALS-associated proteins' in October 2022. Charlotte went on to pursue her post-doc with Jeff Rothstein at Johns Hopkins.


Fare, C.M., K. Rhine, A. Lam, S. Myong, and J. Shorter. (2022). A minimal construct of nuclear-import receptor Karyopherin-β2 defines the regions critical for chaperone and disaggregation activity. J. Biol. Chem. 299(2):102806. pdf file link

Shen, H., A. Yanas, M.C. Owens, C. Zhang, C. Fritsch, C.M. Fare, K.E. Copley, J. Shorter, Y.E. Goldman, and K.F. Liu. (2022). Sexually dimorphic RNA helicases DDX3X and DDX3Y differentially regulate RNA metabolism through phase separation. Mol. Cell. 82(14):2588-2603.e9. pdf file link

Kim, H.J.*, P. Mohassel*, S. Donkervoort, L. Guo, K. O’Donovan, M. Coughlin, X. Lornage, N. Foulds, S.R. Hammans, A.R. Foley, C.M. Fare, A.F. Ford, M. Ogasawara, A. Sato, A. Iida, P. Munot, G. Ambegaonkar, R. Phadke, D.G. O’Donovan, R. Buchert, M. Grimmel, A. Töpf, I.T. Zaharieva, L. Brady, Y. Hu, T.E. Lloyd, A. Klein, M. Steinlin, A. Kuster, S. Mercier, P. Marcorelles, Y. Péréon, E. Fleurence, A. Manzur, S. Ennis, R. Upstill-Goddard, L. Bello, C. Bertolin, E. Pegoraro, L. Salviati, C.E. French, A. Shatillo, F.L. Raymond, T. Haack, S. Quijano-Roy, J. Böhm, I. Nelson, T. Stojkovic, T. Evangelista, V. Straub, N.B. Romero, J. Laporte, F. Muntoni, I. Nishino, M.A. Tarnopolsky, J. Shorter, C.G. Bönnemann, and J.P. Taylor. (2021). Heterozygous frameshift variants in hnRNPA2B1 cause early-onset oculopharyngeal muscular dystrophy. Nat. Comm. 13(1):2306. pdf file link (*Co-first author).

Rhine, K., M. Dasovich, J. Yoniles, M. Badiee, S. Skanchy, L. Ganser, Y. Ge, C.M. Fare, J. Shorter, A.K.L. Leung, and S. Myong. (2022). Poly(ADP-Ribose) drives condensation of FUS via a transient interaction. Mol. Cell. 82(5):969-985.e11. pdf file link

Odeh, H.M.*, C.M. Fare*, and J. Shorter. (2021). Nuclear-import receptors counter deleterious phase transitions in neurodegenerative disease. J. Mol. Biol. 434(1):167220. pdf file link cover (*Co-first author).

Beijer, D.*, H.J. Kim*, L. Guo*, K. O’Donovan, I. Mademan, T. Deconinck, K Van Schil, C.M. Fare, L.E. Drake, A.F. Ford, A. Kochański, D. Kabzińska, N. Dubuisson, P. Van den Bergh, N.C. Voermans, R.J.L.F. Lemmers, S.M. van der Maarel, D. Bonner, J.B. Sampson, M.T. Wheeler, A. Mehrabyan, S. Palmer, P. De Jonghe, J. Shorter, J.P. Taylor, and J. Baets. (2021). Characterization of HNRNPA1 mutations defines diversity in pathogenic mechanisms and clinical presentation. JCI Insight. 6(14):e148363.pdf file link (*Co-first author.).

Fare, C.M., A. Villani, L.E. Drake, and J. Shorter. (2021). Higher-order organization of biomolecular condensates. Open Biol. 11(6):210137. pdf file link

Fare, C.M., and J. Shorter. (2021). (Dis)Solving the problem of aberrant protein states. Dis. Mod. Mech. 14(5):dmm048983. pdf file link

Fare, C.M., and J. Shorter. (2021). Open access: a role for p53 in c9ALS/FTD? Trends Genet. 37(5):404-406. pdf file link

Hutten, S., S. Usluer, B. Bourgeois, F. Simonetti, H.M. Odeh, C.M. Fare, M. Czuppa, M. Hruska-Plochan, M. Hofweber, M. Polymenidou, J. Shorter, D. Edbauer, T. Madl, and D. Dormann. (2020). Nuclear import receptors directly bind to arginine-rich dipeptide repeat proteins and suppress their pathological interactions. Cell Rep. 33(12):108538. pdf file link

Rhine, K., M.A. Makurath, J. Liu, S. Skanchy, C. Lopez, K.F. Catalan, Y. Ma, C.M. Fare, J. Shorter, T. Ha, Y.R. Chemla, and S. Myong. (2020). ALS/FTLD-linked mutations in FUS glycine residues cause accelerated gelation and reduced interactions with wild-type FUS. Mol. Cell. 80(4):666-681. pdf file link

Niaki, A.G.*, J. Sarkar*, X. Cai, K. Rhine, V. Vidaurre, B. Guy, M. Hurst, J.C. Lee, H.R. Koh, L. Guo, C.M. Fare, J. Shorter, and S. Myong. (2020). Loss of dynamic RNA interaction and aberrant phase separation induced by two distinct types of ALS/FTD-linked FUS mutations. Mol. Cell. 77(1):82-94. pdf file link (*Co-first author).

Guo, L.*, C.M. Fare*, and J. Shorter. (2019). Therapeutic dissolution of aberrant phases by nuclear-import receptors. Trends. Cell Biol. 29(4):308-322. pdf file link (*Co-first author).

Guo, L.*, H.J. Kim*, H. Wang*, J. Monaghan°, F. Freyermuth°, J.C. Sung°, K. O’Donovan, C.M. Fare, Z. Diaz, N. Singh, Z.C. Zhang, M. Coughlin, E.A. Sweeny, M.E. DeSantis, M.E. Jackrel, C.B. Rodell, J.A. Burdick, O.D. King, A.D. Gitler, C. Lagier-Tourenne, U.B. Pandey, Y.M. Chook, J.P. Taylor, and J. Shorter. (2018). Nuclear-import receptors reverse aberrant phase transitions of RNA-binding proteins with prion-like domains. Cell. 173(3):677-692. pdf file link (*Co-first author. °Co-second author).





Department of Biochemistry & Biophysics
University of Pennsylvania