192. Lin, J., P.J. Carman, C.W. Gambogi, N.M. Kendsersky, E. Chuang, S.N. Gates, A.L. Yokom, A.N. Rizo, D.R. Southworth, and J. Shorter^. (2024). Design principles to tailor Hsp104 therapeutics. bioRxiv. doi:

191. The Atomwise Aims Program. (2024). AI is a viable alternative to high throughput screening: a 318-target study. Sci. Rep. 14, 7526. pdf file link

190. Sweeney, K.M., S. Chantarawong, E.M. Barbieri, G. Cajka, M. Liu, L. Spruce, H. Fazelinia, B. Portz, K. Copley, T. Lapidot, L. Duhamel, P. Greenwald, N. Saida, R. Shalgi, J. Shorter, and O. Shalem. (2024). CRISPR screen for protein inclusion formation uncovers a role for SRRD in the regulation of intermediate filament dynamics and aggresome assembly. PLoS Genet. 20(2):e1011138. pdf file link

189. Khalil, B.*, M. Linsenmeier*, C.L. Smith, J. Shorter^, and W. Rossoll^. (2024). Nuclear-import receptors as gatekeepers of pathological phase transitions in ALS/FTD. Mol. Neurodegen. 19(8). doi: 10.1186/s13024-023-00698-1 pdf file link (*Co-first author. ^Co-corresponding author).

188. Cupo, R.R., and J. Shorter^. (2024). Decoding Skd3 (human CLPB): a mitochondrial protein disaggregase critical for human health. Isr. J. Chem. doi: 10.1002/ijch.202300153. pdf file link (^Corresponding author).

187. Miller, L., and J. Shorter^. (2024). Mo' m1A, mo' problems. Cell Chem. Biol. 31(1):14-16. pdf file link (^Corresponding author).

186. Chuang, E., R.R. Cupo, J.R. Bevan, M.L. Rice, S. Mao, E.L. Gorenberg, K.L. Mack, D.M. Huryn, P. Wipf, J.L. Brodsky, and J. Shorter^. (2024). Defining a small-molecule stimulator of the human Hsp70-disaggregase system with selectivity for DnaJB proteins. bioRxiv. doi: 10.1101/2024.01.11.575109. pdf file link (^Corresponding author).


185. Guo, L.*^, J.R. Mann*, J.C. Mauna°, K.E. Copley°, H. Wang°, J.D. Rubien°, H.M. Odeh, J. Lin, B.L. Lee, L. Ganser, E. Robinson, K.M. Kim, A.C. Murthy, T. Paul, B. Portz, A.M. Gleixner, Z. Diaz, J.L. Carey, A. Smirnov, G. Padilla, E. Lavorando, C. Espy, Y. Shang, E.J. Huang, A. Chesi, N.L. Fawzi, S. Myong, C.J. Donnelly^, and J. Shorter^. (2023). Defining RNA oligonucleotides that reverse deleterious phase transitions of RNA-binding proteins with prion-like domains. bioRxiv. doi:10.1101/2023.09.04.555754. pdf file link (*Co-first author. °Co-second author. ^Co-corresponding author).

184. Mack, K.L.*, H. Kim*, E.M. Barbieri, J. Lin, S. Braganza, M.E. Jackrel, J.E. DeNizio, X. Yan, E. Chuang, A. Tariq, R.R. Cupo, L.M. Castellano, K.A. Caldwell, G.A. Caldwell^, and J. Shorter^. (2023). Tuning Hsp104 specificity to selectively detoxify α-synuclein. Mol. Cell. 83(18):3314-3332.e9. pdf file link (*Co-first author. ^Co-corresponding author).

183. Myong, S.^, and J. Shorter^. (2023). Introduction: Phase Separation. Chem. Rev. 123(14):8943-8944. pdf file link (^Co-corresponding author).

182. Sharma, K., S. Banerjee, D. Savran, C. Rajes, S. Wiese, A. Girdhar, N. Schwierz, C. Lee, J. Shorter, M. Schmidt, L. Guo, and M. Fändrich. (2023). Cryo-EM structure of the full-length hnRNPA1 amyloid fibril. J. Mol. Biol. 435(18):168211. pdf file link

181. Balendra, R., I. Ruiz de los Mozos, H.M. Odeh, I. Glaria, C. Milioto, K.M. Wilson, A.M. Ule, M. Hallegger, L. Masino, S. Martin, R. Patani, J. Shorter, J. Ule, and A.M. Isaacs. (2023). Genome-wide RNA binding analysis of C9orf72 poly(PR) dipeptides. Life Sci. Alliance. 6(9):e202201824. pdf file link

180. Rhine, K., H.M. Odeh, J. Shorter, and S. Myong. (2023). Regulation of biomolecular condensates by poly(ADP-ribose). Chem. Rev. 123(14):9065-9093. pdf file link

179. Ervilha Pereira, P., N. Schuermans, A. Meylemans, P. LeBlanc, L. Versluys, K.E. Copley, J.D. Rubien, C. Altheimer, M. Peetermans, E. Debackere, O. Vanakker, S. Janssens, J. Baets, K. Verhoeven, M. Lammens, S. Symoens, B. De Paepe, S.J. Barmada, J. Shorter, J.L. De Bleecker, E. Bogaert, and B. Dermaut. (2023). C-terminal frameshift variant of TDP-43 with pronounced aggregation-propensity causes rimmed vacuole myopathy but not ALS/FTD. Acta Neuropathol.145(6):793-814. pdf file link

178. Copley, K.E., and J. Shorter^. (2023). Repetitive elements in aging and neurodegeneration. Trends Genet. 39(5):381-400. pdf file link (^Corresponding author).

177. Boeynaems, S.*, S. Chong*, J. Gsponer*, L. Holt*, D. Milovanovic*, D.M. Mitrea* O. Mueller-Cajar*, B. Portz*, J.F. Reilly*, C.D. Reinkemeier*, B.R. Sabari*, S. Sanulli*, J. Shorter*, E. Sontag*, L. Strader*, J. Stachowiak*, S.C. Weber*, M. White*, H. Zhang*, M. Zweckstetter*, S. Elbaum-Garfinkle^, and R. Kriwacki^. (2023). Phase separation in biology and disease; current perspectives and open questions. J. Mol. Biol. 435(5):167971. pdf file link (*Co-first author. ^Co-corresponding author).

176. Fare, C.M., K. Rhine, A. Lam, S. Myong, and J. Shorter^. (2023). 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 (^Corresponding author).


175. Khalil, B., D. Chhangani, M.C. Wren, C.L.Smith, J.H. Lee, X. Li, C. Puttinger, C.W. Tsai, G. Fortin, D. Morderer, J. Gao, F. Liu, C.K. Lim, J. Chen, C.C. Chou, C.L. Croft, A.M. Gleixner, C.J. Donnelly, T.E. Golde, L. Petrucelli, B. Oskarsson, D.W. Dickson, K. Zhang, J. Shorter, S.H. Yoshimura, S.J. Barmada, D.E. Rincon-Limas, and W. Rossoll. (2022). Nuclear import receptors are recruited by FG-nucleoporins to rescue hallmarks of TDP-43 proteinopathy. Mol. Neurodegener. 17(1):80. pdf file link

174. Cupo, R.R.*, A. Rizo*, G.A. Braun, E. Tse, E. Chuang, K. Gupta, D.R. Southworth^, and J. Shorter^. (2022). Unique structural features govern the activity of a human mitochondrial AAA+ disaggregase, Skd3. Cell Rep. 40(13): 111408. pdf file link (*Co-first author. ^Corresponding author).

173. Weil, T., A. Kirupakaran, M-H. Le, P. Rebmann, J. Mieres-Perez, L. Issmail, C. Conzelmann, J.A. Müller, L. Rauch, A. Gilg, L. Wettstein, R. Groß, C. Read, T. Bergner, S. Axberg Pålsson, N. Uhlig, V. Eberlein, H. Wöll, F-G. Klärner, S. Stenger, B.M. Kümmerer, H. Streeck, G. Fois, M. Frick, P. Braubach, A-L. Spetz, T. Grunwald, J. Shorter, E. Sanchez-Garcia, T. Schrader, and J. Münch. (2022). Advanced molecular tweezers with lipid anchors against SARS-CoV-2 and other respiratory viruses. JACS Au. 2(9):2187–2202. pdf file link

172. 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

171. François-Moutal, L., D.D. Scott, A.J. Ambrose, C.J. Zerio, M. Rodriguez-Sanchez, K. Dissanayake, D.G. May, J.M. Carlson, E. Barbieri, A. Moutal, K.J. Roux, J. Shorter, R. Khanna, S.J. Barmada, L. McGurk, and M. Khanna. (2022). Heat shock protein Grp78/BiP/HspA5 binds directly to TDP-43 and mitigates toxicity associated with neurodegenerative disease pathology. Sci. Rep. 12(1):8140. pdf file link

170. Peinado, J.R., K. Chaplot, T.S. Jarvela, E. Barbieri, J. Shorter, and I. Lindberg. (2022). Sequestration of TDP-43(216-414) aggregates by cytoplasmic expression of the proSAAS chaperone. ACS Chem. Neurosci. 13(11):1651-1665. pdf file link cover

169. 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. (2022). Heterozygous frameshift variants in hnRNPA2B1 cause early-onset oculopharyngeal muscular dystrophy. Nat. Comm. 13(1):2306. pdf file link (*Co-first author).

168. Copley, K.E., and J. Shorter^. (2022). Flying under the radar: TMEM106B(120-254) fibrils break out in diverse neurodegenerative disorders. Cell. 185(8):1290-1292. pdf file link (^Corresponding author).

167. Lin, J.^, J. Shorter^, and A.L. Lucius^. (2022). AAA+ proteins: one motor, multiple ways to work. Biochem. Soc. Trans. 50(2):895-906. pdf file link (^Co-corresponding author).

166. Ma, X.R., M. Prudencio, Y. Koike, S.C. Vatsavayai, G. Kim, F. Harbinski, A. Briner, C.M. Rodriguez, C. Guo, T. Akiyama, H.B. Schmidt, B.B. Cummings, D.W. Wyatt, K. Kurylo, G. Miller, S. Mekhoubad, N. Sallee, G. Mekonnen, L. Ganser, J.D. Rubien, K. Jansen-West, C.N. Cook, S. Pickles, B. Oskarsson, N.R. Graff-Radford, B.F. Boeve, D.S. Knopman, R.C. Petersen, D.W. Dickson, J. Shorter, S. Myong, E.M. Green, W.W. Seeley, L. Petrucelli, and A.D. Gitler. (2022). TDP-43 represses cryptic exon inclusion in the FTD–ALS gene UNC13A. Nature. 603(7899):124-130. pdf file link

165. 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

164. Warren, J.T., R.R. Cupo, P. Wattanasirakul, D. Spencer, A.E. Locke, V. Makaryan, A.A. Bolyard, M.L. Kelley, N.L. Kingston, J. Shorter, C. Bellanné-Chantelot, J. Donadieu, D.C. Dale, and D.C. Link. (2022). Heterozygous variants of CLPB are a cause of severe congenital neutropenia. Blood. 139(5):779-791. pdf file link

163. Odeh, H.M., and J. Shorter^. (2022). Aggregates of TDP-43 protein spiral into view. Nature. 601(7891):29-30. pdf file link (^Corresponding author).

162. Odeh, H.M.*, C.M. Fare*, and J. Shorter^. (2022). Nuclear-import receptors counter deleterious phase transitions in neurodegenerative disease. J. Mol. Biol. 43(1):167220. pdf file link cover (*Co-first author. ^Corresponding author).


161. Gottlieb, L., L. Guo, J. Shorter, and R. Marmorstein. (2021). N-alpha-acetylation of Huntingtin protein increases its propensity to aggregate. J. Biol. Chem. 297(6):101363. pdf file link

160. Huang, L., T. Agrawal, G. Zhu, S. Yu, L. Tao, J. Lin, R. Marmorstein, J. Shorter, and X. Yang. (2021). DAXX represents a new type of protein-folding enabler. Nature. 597(7874):132-37. pdf file link

159. Hallegger, M.*, A.M. Chakrabarti*, F.C.Y. Lee*, B.L. Lee, A.G. Amalietti, H.M. Odeh, K.E. Copley, J.D. Rubien, B. Portz, K. Kuret, I. Huppertz, F. Rau, R. Patani, N.L. Fawzi, J. Shorter, N.M. Luscombe, and J. Ule. (2021). TDP-43 condensation properties specify its RNA-binding and regulatory repertoire. Cell. 184(18):4680-4696.e22. pdf file link (*Co-first author).

158. Aikio, M., H.J. Wobst, H.M. Odeh, B.L. Lee, B. Class, T.A. Ollerhead, K.L. Mack, A.F. Ford, E.M. Barbieri, R.R. Cupo, L.E. Drake, N. Castello, A. Baral, J. Dunlop, A.D. Gitler, A. Javaherian, S. Finkbeiner, D.G. Brown, S.J. Moss^, N.J. Brandon^, and J. Shorter^. (2021). Opposing roles of p38α-mediated phosphorylation and arginine methylation in driving TDP-43 proteinopathy. bioRxiv. doi:pdf file link (^Co-corresponding author).

157. 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. ^Co-corresponding author).

156. 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 (^Corresponding author).

155. Portz, B., and J. Shorter^. (2021). Biochemical timekeeping via reentrant phase transitions. J. Mol. Biol. 433(12):166794. pdf file link (^Corresponding author).

154. Gorenberg, E.L., and J. Shorter^. (2021). Tau heckles speckles: a pathogenic mechanism in tauopathy? Neuron. 109(10):1585-1587. pdf file link (^Corresponding author).

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

152. Darling, A.L., and J. Shorter^. (2021). Combating deleterious phase transitions in neurodegenerative disease. Biochimica et Biophysica Acta. 1868(5):118984. pdf file link (^Corresponding author).

151. 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 (^Corresponding author).

150. Portz, B., B.L. Lee, and J. Shorter^. (2021). FUS and TDP-43 phases in health and disease. Trends Biochem. Sci. 46(7):550-563. pdf file link (^Corresponding author).


149. 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

148. March, Z.M., K. Sweeney°, H. Kim°, X. Yan°, L.M. Castellano, M.E. Jackrel, J. Lin, E. Chuang, E. Gomes, C. W. Willicott, K. Michalska, R. Jedrzejczak, A. Joachimiak, K.A. Caldwell, G.A. Caldwell, O. Shalem, and J. Shorter^. (2020). Therapeutic genetic variation revealed in diverse Hsp104 homologs. eLife. 9:e57457. pdf file link (°Co-second author. ^Corresponding author).

147. Cupo, R.R., and J. Shorter^. (2020). Expression and purification of recombinant Skd3 (human ClpB) protein and tobacco etch virus (TEV) protease from Escherichia coli. Bio Protoc. 10(23):e3858. pdf file link (^Corresponding author).

146. Zhu, G.*, D.S. Harischandra*, S. Ghaisas, P. Zhang, W. Prall, L. Huang, C. Maghames, L. Guo, E. Luna, K.L. Mack, M.P. Torrente, K.C. Luk, J. Shorter, and X. Yang. (2020). TRIM11 prevents and reverses protein aggregation and rescues a mouse model of Parkinson’s disease. Cell Rep. 33(9):108418. pdf file link (*Co-first author).

145. 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

144. Weil, T.*, R. Groß*, A. Röcker*, K. Bravo-Rodriguez*, C. Heid, A. Sowislok, M-H. Le, N. Erwin, M. Dwivedi, S. Bart, P. Bates, L. Wettstein, J. Müller, M. Harms, K. Sparrer, Y.B. Ruiz-Blanco, C. Stuerzel, J. von Einem, S. Lippold, C. Read, P. Walther, M. Hebel, F. Kreppel, F-G. Klärner, G. Bitan, M. Ehrmann, T. Weil, R. Winter, T. Schrader^, J. Shorter^, E. Sanchez-Garcia^, and J. Münch^. (2020). Supramolecular mechanism of viral envelope disruption by molecular tweezers. J. Am. Chem. Soc. 142(40):17024–17038. pdf file link (*Co-first author. ^Co-corresponding author).

143. Cook, C.N.*, Y. Wu*, H.M. Odeh*, T.F. Gendron, K. Jansen-West, G. del Rosso, M. Yue, P. Jiang, E. Gomes, J. Tong, L.M. Daughrity, N.M. Avendano, M. Castanedes-Casey, W. Shao, B. Oskarsson, G.S. Tomassy, A. McCampbell, F. Rigo, D.W. Dickson, J. Shorter^, Y-J. Zhang^, and L. Petrucelli^. (2020). C9orf72 poly(GR) aggregation induces TDP-43 proteinopathy. Sci. Transl. Med. 12(559):eabb3774. pdf file link (*Co-first author. ^Co-corresponding author).

142. Robinson, E., J. Shorter, and L. Guo. (2020). Karyopherin-β2 inhibits and reverses aggregation and liquid-liquid phase separation of the ALS/FTD-associated protein FUS. Bio Protoc. 10(16):e3725. pdf file link

141. Darling, A.L., and J. Shorter^. (2020). Atomic structures of amyloid-β oligomers illuminate a neurotoxic mechanism. Trends Neurosci. 43(10):740-743. pdf file link (^Corresponding author).

140. Odeh, H.M., and J. Shorter^. (2020). Arginine-rich dipeptide-repeat proteins as phase disruptors in C9-ALS/FTD. Emerg. Top. Life Sci. 4(3):293–305. pdf file link cover (^Corresponding author).

139. Cupo, R.R., and J. Shorter^. (2020). Skd3 (human ClpB) is a potent mitochondrial protein disaggregase that is inactivated by 3-methylglutaconic aciduria-linked mutations. eLife. 9:e55279. pdf file link (^Corresponding author).

138. Lopez, K.E.*, A.N. Rizo*, E. Tse, J. Lin, N.W. Skull, A.C. Thwin, A.L. Lucius, J. Shorter, and D.R. Southworth. (2020). Conformational plasticity of the ClpAP AAA+ protease couples protein unfolding and proteolysis. Nat. Struct. Mol. Biol. 27(5):406-416. (*Co-first author). pdf file link

137. Gitler, A.D.^, J. Shorter^, T. Ha^, and S. Myong^. (2020). Just took a DNA test, turns out 100% not that phase. Mol. Cell. 78(2):193-194. pdf file link (^Co-corresponding author).

136. Ye, X., J. Lin, L. Mayne, J. Shorter, and S.W. Englander. (2020). Structural and kinetic basis for the regulation and potentiation of Hsp104 function. Proc. Natl. Acad. Sci. U.S.A. 117(17):9384-9392. pdf file link

135. Odeh, H.M., and J. Shorter^. (2020). The sense of targeting nonsense-mediated decay in C9-ALS/FTD. Neuron. 106(1):6-9. pdf file link (^Corresponding author).

134. Wobst, H.J.^, K.L. Mack, D.G. Brown, N.J. Brandon, and J. Shorter^. (2020). The clinical trial landscape in amyotrophic lateral sclerosis – past, present and future. Med. Res. Rev. 40(4):1352-1384. pdf file link (^Co-corresponding author).

133. Brown, D.G., J. Shorter, and H.J. Wobst. (2020). Emerging small-molecule therapeutic approaches for amyotrophic lateral sclerosis and frontotemporal dementia. Bioorg. Med. Chem. Lett. 30(4):126942. pdf file link

132. Sweeny, E.A.^, A. Tariq, E. Gurpinar, M.S. Go, M.A. Sochor, Z.Y. Kan, L. Mayne, S.W. Englander, and J. Shorter^. (2020). Structural and mechanistic insights into Hsp104 function revealed by synchrotron x-ray footprinting. J. Biol. Chem. 295(6):1517–1538. pdf file link (^Co-corresponding author).

131. Jones, R.D., C. Enam, R. Ibarra, H.R. Borror, K.E. Mostoller, E.K. Fredrickson, J. Lin, E. Chuang, Z. March, J. Shorter, T. Ravid, G. Kleiger, and R.G. Gardner. (2020). The extent of Ssa1/Ssa2 Hsp70 chaperone involvement in nuclear protein quality control degradation varies with the substrate. Mol. Biol. Cell. 31(3):221-233. pdf file link

130. 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).

129. Portz, B., and J. Shorter^. (2020). Switching condensates: the CTD code goes liquid. Trends. Biochem. Sci. 45(1):1-3. pdf file link (^Corresponding author).


128. Cheng, W.*, S. Wang*, Z. Zhang, D.W. Morgens, L.R. Hayes, S. Lee, B. Portz, Y. Xie, B.V. Nguyen, M.S. Haney, S. Yan, D. Dong, A.N. Coyne, J. Yang, F. Xian, D.W. Cleveland, Z. Qiu, J.D. Rothstein, J. Shorter, F-B. Gao, M.C. Bassik, and S. Sun. (2019). CRISPR-Cas9 screens identify the RNA helicase DDX3X as a repressor of C9ORF72 (GGGGCC)n repeat-associated non-AUG translation. Neuron. 104(5):885–898. pdf file link (*Co-first author).

127. Tariq, A.*, J. Lin*, M.E. Jackrel*, C.D. Hesketh, P.J. Carman, K.L. Mack, R. Weitzman, C. Gambogi, O.A. Hernandez Murillo, E.A. Sweeny, E. Gurpinar, A.L. Yokom, S.N. Gates, K. Yee, S. Sudesh, J. Stillman, A.N. Rizo, D.R. Southworth, and J. Shorter^. (2019). Mining disaggregase sequence space to safely counter TDP-43, FUS, and alpha-synuclein proteotoxicity. Cell Rep. 28(8):2080–2095. pdf file link (*Co-first author, ^Corresponding author).

126. Ryan, J.J., M.L. Sprunger, K. Holthaus, J. Shorter^, and M.E. Jackrel^. (2019). Engineered protein disaggregases mitigate toxicity of aberrant prion-like fusion proteins underlying sarcoma. J. Biol. Chem. 294(29):11286–11296. pdf file link (^Co-corresponding author).

125. Rizo, A.N., J. Lin, S.N. Gates, E. Tse, S.M. Bart, L.M. Castellano, F. DiMaio, J. Shorter, and D.R. Southworth. (2019). Structural basis for substrate gripping and translocation by the ClpB AAA+ disaggregase. Nat. Comm. 10:2393. pdf file link

124. Durie, C.L., J. Lin, N.W. Scull, K.L. Mack, M.E. Jackrel, E.A. Sweeny, L.M. Castellano, J. Shorter, and A.L. Lucius. (2019). Hsp104 and potentiated variants can operate as distinct non-processive translocases. Biophys. J. 116(10):1856-1872. pdf file link

123. Gomes, E. and J. Shorter^. (2019). The molecular language of membraneless organelles. J. Biol. Chem. 294(18):7115–7127. pdf file link (^Corresponding author).

122. Shorter, J^. (2019). Phase separation of RNA-binding proteins in physiology and disease: An introduction to the JBC Reviews thematic series. J. Biol. Chem. 294(18):7113–7114. pdf file link (^Corresponding author).

121. Ye, X., J. Lin, L. Mayne, J. Shorter, and S.W. Englander. (2019). Hydrogen exchange reveals Hsp104 architecture, structural dynamics, and energetics in physiological solution. Proc. Natl. Acad. Sci. U.S.A. 116(15):7333-7342. pdf file link

120. March, Z.M.*, K.L. Mack*, and J. Shorter^. (2019). AAA+ protein-based technologies to counter neurodegenerative disease. Biophys. J. 116(8):1380-1385. pdf file link (*Co-first author. ^Corresponding author).

119. Gasset-Rosa, F., S. Lu, H. Yu, C. Chen, Z. Melamed, L. Guo, J. Shorter, S. Da Cruz, and D.W. Cleveland. (2019). Cytoplasmic TDP-43 de-mixing independent of stress granules drives inhibition of nuclear import, loss of nuclear TDP-43, and cell death. Neuron. 102(2):339-357. pdf file link cover

118. Michalska, K.*, K. Zhang*, Z.M. March*, C. Hatzos-Skintges, G. Pintilie, L. Bigelow, L.M. Castellano, L.J. Miles, M.E. Jackrel, E. Chuang, R. Jedrzejczak, J. Shorter^, W. Chiu^, and A. Joachimiak^. (2019). Structure of Calcarisporiella thermophila Hsp104 disaggregase that antagonizes diverse proteotoxic misfolding events. Structure. 27(3):449-463. pdf file link (*Co-first author. ^Co-corresponding author).

117. Mann, J.R., A.M. Gleixner, J.C. Mauna, E. Gomes, M.R. DeChellis-Marks, P.G. Needham, K.E. Copley, B. Hurtle, B. Portz, N.J. Pyles, L. Guo, C.B. Calder, Z.P. Wills, U.B. Pandey, J.K. Kofler, J.L. Brodsky, A. Thathiah, J. Shorter, and C.J. Donnelly. (2019). RNA binding antagonizes neurotoxic phase transitions of TDP-43. Neuron. 102(2):321-338. pdf file link

116. Zhang, Y-J., L. Guo, P.K. Gonzales, T.F. Gendron, Y. Wu, K. Jansen-West, A.D. O’Raw, S.R. Pickles, M. Prudencio, Y. Carlomagno, M.A. Gachechiladze, C. Ludwig, R. Tian, J. Chew, M. DeTure, W-L. Lin, J. Tong, L.M. Daughrity, M. Yue, Y. Song, J.W. Andersen, M. Castanedes-Casey, A. Kurti, A. Datta, G. Antognetti, A. McCampbell, R. Rademakers, B. Oskarsson, D.W. Dickson, M. Kampmann, M.E. Ward, J.D. Fryer, C.D. Link, J. Shorter, and L. Petrucelli. (2019). Heterochromatin anomalies and double-stranded RNA accumulation underlie C9orf72 poly(PR) toxicity. Science. 363(6428):eaav2606. pdf file link

115. Shorter, J.^, and D.R. Southworth^. (2019). Spiraling in control: structures and mechanisms of the Hsp104 disaggregase. Cold Spring Harb. Perspect. Biol. 11:a034033. pdf file link cover (^Co-corresponding author).

114. 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. ^Corresponding author).

113. Barbieri, E.M., and J. Shorter^. (2019). TDP-43 shapeshifts to encipher FTD severity. Nat. Neurosci. 22(1):3-5. pdf file link (^Corresponding author).


112. McGurk, L.*, E. Gomes*, L. Guo*, J. Shorter^, and N.M. Bonini^. (2018). Poly(ADP-ribose) engages the TDP-43 nuclear-localization sequence to regulate granulo-filamentous aggregation. Biochemistry. 57(51):6923−6926. pdf file link (*Co-first author. ^Co-corresponding author).

111. Portz, B., and J. Shorter^. (2018). 3' UTRs in the eye of the tiger. Dev. Cell. 47(5):544-546. pdf file link

110. Vogler, T.O., J.R. Wheeler, E.D. Nguyen, M.P. Hughes, K.A. Britson, E. Lester, B. Rao, N. Dalla Betta, O.N. Whitney, T.E. Ewachiw, E. Gomes, J. Shorter, T.E. Lloyd, D.S. Eisenberg, J.P. Taylor, A.M. Johnson, B.B. Olwin, and R. Parker. (2018). TDP-43 and RNA form amyloid-like myo-granules in regenerating muscle. Nature. 563(7732):508-513. pdf file link

109. Shorter, J.^, and W.A. Houry^. (2018). Editorial: The role of AAA+ proteins in protein repair and degradation. Front. Mol. Biosci. 5:85. pdf file link (^Co-corresponding author).

108. McGurk L., L. Mojsilovic-Petrovic, V. Van Deerlin, J. Shorter, R.G. Kalb, V.M. Lee, J.Q. Trojanowksi, E.B. Lee, and N.M. Bonini. (2018). Nuclear poly(ADP-ribose) activity is a therapeutic target in amyotrophic lateral sclerosis. Acta Neuropathol. Commun. 6:84. pdf file link

107. McGurk L., E. Gomes, L. Guo, J. Mojsilovic-Petrovic, V. Tran, R.G. Kalb, J. Shorter^, and N.M. Bonini^. (2018). Poly(ADP-ribose) prevents aberrant phase separation of TDP-43 by promoting liquid demixing and stress-granule localization. Mol. Cell. 71(5):703-717. pdf file link (^Co-corresponding author).

106. Bogaert, E., S. Boeynaems, M. Kato, L. Guo, T.R. Caulfield, J. Steyaert, W. Scheveneels, N. Wilmans, W. Haeck, N. Hersmus, J. Schymkowitz, F. Rousseau, J. Shorter, P. Callaerts, W. Robberecht, P. Van Damme, and L. Van Den Bosch. (2018). Molecular dissection of FUS points at synergistic effect of low-complexity domains in toxicity. Cell Rep. 24(3):529-537 pdf file link cover

105. Bart, S.M., C. Cohen, J.M. Dye, J. Shorter, and P. Bates. (2018). Enhancement of Ebola virus infection by seminal amyloid fibrils. Proc. Natl. Acad. Sci. U.S.A. 115(28):7410-7415. pdf file link

104. 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. ^Co-corresponding author).

103. Chuang, E.*, A.M. Hori*, C.D. Hesketh*, and J. Shorter^. (2018). Amyloid assembly and disassembly. J. Cell. Sci. 131(8): jcs189928. pdf file link (*Co-first author. ^Corresponding author).

102. Tariq, A.*, J. Lin*, M.M. Noll*, M.P. Torrente, K.L. Mack, O. Hernandez Murillo, M.E. Jackrel, and J. Shorter^. (2018). Potentiating Hsp104 activity via phosphomimetic mutations in the middle domain. FEMS Yeast Res. 18(5) doi:10.1093/femsyr/foy042. pdf file link (*Co-first author. ^Corresponding author).

101. Boeynaems, S., S. Alberti, N.L. Fawzi, T. Mittag, M. Polymenidou, F. Rousseau, J. Schymkowitz, J. Shorter, B. Wolozin, L. Van Den Bosch, P. Tompa, and M. Fuxreiter. (2018). Protein phase separation: a new phase in cell biology. Trends Cell Biol. 28(6):420-435. pdf file link cover

100. Subudhi, I., and J. Shorter^. (2018). Ubiquilin 2: shuttling clients out of phase? Mol. Cell. 69(6):919-921. pdf file link (^Corresponding author).

99. Zhang, T.*, Y-C. Wu*, P. Mullane, Y.J. Ji, H. Liu, L. He, A. Arora, H-Y. Hwang, A.F. Alessi, A.G. Niaki, G. Periz, L. Guo, H. Wang, E. Elkayam, L. Joshua-Tor, S. Myong, J.K. Kim, J. Shorter, S-E. Ong, A.K.L. Leung, and J. Wang. (2018). FUS regulates activity of microRNA-mediated gene silencing. Mol. Cell. 69(5):787-801. pdf file link (*Co-first author).


98. Shorter, J^. (2017). Liquidizing FUS via prion-like domain phosphorylation. EMBO J. e201798078. pdf file link (^Corresponding author).

97. Shorter, J^. (2017). Prion-like domains program Ewing's sarcoma. Cell. 171(1):30-31. pdf file link (^Corresponding author).

96. Gates, S.N*., A.L. Yokom*, J. Lin, M.E. Jackrel, A.N. Rizo, N.M. Kendsersky, C.E. Buell, E.A. Sweeny, K.L. Mack, E. Chuang, M.P. Torrente, M. Su, J. Shorter, and D.R. Southworth. (2017). Ratchet-like polypeptide translocation mechanism of the AAA+ disaggregase Hsp104. Science. 357(6348):273-279. pdf file link (*Co-first author).

95. Gitler, A.D.^, P. Dillon, and J. Shorter^. (2017). Neurodegenerative disease: models, mechanisms, and a new hope. Dis. Model Mech. 10: 499-502. pdf file link (^Co-corresponding author).

94. Harrison, A.F., and J. Shorter^. (2017). RNA-binding proteins with prion-like domains in health and disease. Biochem. J. 474(8):1417-1438. pdf file link cover (^Corresponding author).

93. Weaver, C.L., E.C. Duran, K.L. Mack, J. Lin, M.E. Jackrel, E.A. Sweeny, J. Shorter, and A.L. Lucius. (2017). Avidity for polypeptide binding by nucleotide-bound Hsp104 structures. Biochemistry. 56(15):2071–2075. pdf file link

92. Yasuda, K., S.F. Clatterbuck-Soper, M.E. Jackrel, J. Shorter, and S. Mili. (2017). Cytoplasmic FUS inclusions disrupt Kinesin-­1 leading to loss of detyrosinated microtubules and RNA mislocalization. J. Cell Biol. 216(4):1015-1034. pdf file link

91. Jackrel, M.E.^, and J. Shorter^. (2017). Protein-remodeling factors as potential therapeutics for neurodegenerative disease. Front. Neurosci. 11:99. pdf file link (^Co-corresponding author).

90. Shorter, J^. (2017). Designer protein disaggregases to counter neurodegenerative disease. Curr. Opin. Genet. Dev. 44:1-8. pdf file link (^Corresponding author).

89. Shorter, J^. (2017). In Memoriam: Susan Lee Lindquist (1949-2016). Trends Biochem. Sci. 42(3):169-170. pdf file link (^Corresponding author).

88. Guo, L., and J. Shorter^. (2017). Biology and pathobiology of TDP-43 and emergent therapeutic strategies. Cold Spring Harb Perspect Med. 7(9). pii: a024554. pdf file link (^Corresponding author).


87. Shorter, J^., and A.D. Gitler^. (2016). Susan Lee Lindquist (1949-2016). Nature. 540(7631):40. (^Co-corresponding author). pdf file link

86. Yokom, A.L., S.N. Gates, M.E. Jackrel, K.L. Mack, M. Su, J. Shorter, and D.R. Southworth. (2016). Spiral architecture of the Hsp104 disaggregase reveals the basis for polypeptide translocation. Nat. Struct. Mol. Biol. 23(9):830-7. pdf file link pdb emd

85. Shorter, J^. (2016). Membraneless organelles: Phasing in and out. Nat. Chem. 8(6):528-530. pdf file link (^Corresponding author).

84. Shorter, J^. (2016). Engineering therapeutic protein disaggregases. Mol. Biol. Cell. 27(10):1556-1560. pdf file link (^Corresponding author).

83. March, Z. M., O.D. King^, and J. Shorter^. (2016). Prion-like domains as epigenetic regulators, scaffolds for subcellular organization, and drivers of neurodegenerative disease. Brain Res. 1647:9-18. pdf file link (^Co-corresponding author).

82. Mack, K.L., and J. Shorter^. (2016). Engineering and evolution of molecular chaperones and protein disaggregases with enhanced activity. Front. Mol. Biosci. 3:8. pdf file link (^Corresponding author).

81. Torrente, M.P., E. Chuang, M.M. Noll, M.E. Jackrel, M.S. Go, and J. Shorter^. (2016). Mechanistic insights into Hsp104 potentiation. J. Biol. Chem. 291(10):5101-5115. pdf file link (^Corresponding author).

80. Sweeny, E.A., and J. Shorter^. (2016). Mechanistic and structural insights into the prion-disaggregase activity of Hsp104. J. Mol. Biol. 428(9):1870-1885. pdf file link (^Corresponding author).


79. Guo, L., and J. Shorter^. (2015). It's raining liquids: RNA tunes viscoelasticity and dynamics of membraneless organelles. Mol. Cell. 60(2):189-192. pdf file link (^Corresponding author).

78. Lindberg, I., J. Shorter, R.L. Wiseman, F. Chiti, C.A. Dickey, and P.J. McLean. (2015). Chaperones in neurodegeneration. J. Neurosci. 35(41): 13853-13859. pdf file link

77. Ford, A.F., and J. Shorter^. (2015). Fleeting amyloid-like forms of Rim4 ensure meiotic fidelity. Cell. 163(2):275-276. pdf file link (^Corresponding author).

76. Jackrel, M.E., K. Yee, A. Tariq, A.I. Chen, and J. Shorter^. (2015). Disparate mutations confer therapeutic gain of Hsp104 function. ACS Chem. Biol. 10(12):2672-2679. pdf file link (^Corresponding author).

75. Castellano, L.M., R.M. Hammond, V.M. Holmes, D. Weissman, and J. Shorter^. (2015). Epigallocatechin-3-gallate rapidly remodels PAP85-120, SEM1(45-107), and SEM2(49-107) seminal amyloid fibrils. Biol. Open. 4:1206-1212. pdf file link (^Corresponding author).

74. Lump, E.*, L.M. Castellano*, C. Meier, J. Seeliger, N. Erwin, B. Sperlich, C.M. Stürzel, S. Usmani, R.M. Hammond, J. von Einem, G. Gerold, F. Kreppel, K. Bravo-Rodriguez, T. Pietschmann, V.M. Holmes, D. Palesch, O. Zirafi, D. Weissman, A. Sowislok, B. Wettig, C. Heid, F. Kirchhoff, T. Weil, F.G. Klärner, T. Schrader, G. Bitan, E. Sanchez-Garcia, R. Winter, J. Shorter^, and J. Münch^. (2015). A molecular tweezer antagonizes seminal amyloids and HIV infection. eLife. 4:e05397. pdf file link (*Co-first author. ^Co-corresponding author).

73. Castellano, L.M., S.M. Bart, V.M. Holmes, D. Weissman, and J. Shorter^. (2015). Repurposing Hsp104 to antagonize seminal amyloid and counter HIV infection. Chem. Biol. 22(8):1074-1086. pdf file link (^Corresponding author).

72. Zirafi, O.*, K. Kyeong-Ae*, S. Ludger*, K.B. Mohr, D. Sauter, A. Heigele, S.F. Kluge, E. Wiercinska, D. Chudziak, R. Richter, B. Moepps, P. Gierschik, V. Vas, H. Geiger, M. Lamla, T. Weil, T. Burster, A. Zgraja, F. Daubeuf, N. Frossard, M. Hachet-Haas, F. Heunisch, C. Reichetzeder, J.L. Galzi, J. Pérez-Castells, A. Canales-Mayordomo, J. Jiménez-Barbero, G. Giménez-Gallego, M. Schneider, J. Shorter, A. Telenti, B. Hocher, W.G. Forssmann, H. Bönig, F. Kirchhoff, and J. Münch. (2015). Discovery and characterization of an endogenous CXCR4 antagonist. Cell Rep. 11(5):737-747. pdf file link (*Co-first author).

71. Jackrel, M.E., and J. Shorter^. (2015). Engineering enhanced protein disaggregases for neurodegenerative disease. Prion. 9(2):90-109. pdf file link (^Corresponding author).

70. Sweeny, E.A., M.E. Jackrel, M.S. Go, M.A. Sochor, B.M. Razzo, M.E. DeSantis, K. Gupta, and J. Shorter^. (2015). The Hsp104 N-terminal domain enables disaggregase plasticity and potentiation. Mol. Cell. 57(5):836-849. pdf file link (^Corresponding author).


69. Jackrel, M.E., A. Tariq, K. Yee, R. Weitzman, and J. Shorter^. (2014). Isolating potentiated Hsp104 variants using yeast proteinopathy models. J. Vis. Exp. 93:e52089 doi:10.3791/52089. pdf file link (^Corresponding author).

68. Torrente, M.P., L.M. Castellano, and J. Shorter^. (2014). Suramin inhibits Hsp104 ATPase and disaggregase activity. PLoS ONE. 9(10): e110115. pdf file link (^Corresponding author).

67. Seither, K.M., H.A. McMahon, N. Singh, H. Wang, M. Cushman-Nick, G.L. Montalvo, W.F. DeGrado, and J. Shorter^. (2014). Specific aromatic foldamers potently inhibit spontaneous and seeded Aβ42 and Aβ43 fibril assembly. Biochem. J. 464:85-98. pdf file link (^Corresponding author).

66. Jackrel, M.E., and J. Shorter^. (2014). Potentiated Hsp104 variants suppress toxicity of diverse neurodegenerative disease-linked proteins. Dis. Model Mech. 7(10):1175-1184. pdf file link (^Corresponding author).

65. Guo, L. B.I. Giasson, A. Glavis-Bloom, M.D. Brewer, J. Shorter, A.D. Gitler, and X. Yang. (2014). A cellular system that degrades misfolded proteins through sequential sumoylation and ubiquitination. Mol. Cell. 55(1):15-30. pdf file link cover

64. Jackrel, M.E., and J. Shorter^. (2014). Reversing deleterious protein aggregation with re-engineered protein disaggregases. Cell Cycle. 13(9):1379-1383. pdf file link (^Corresponding author).

63. Qiu, H., S. Lee, Y. Shang, W.Y. Wang, K.F. Au, S. Kamiya, S. J. Barmada, S. Finkbeiner, H. Lui, C.E. Carlton, A.A. Tang, M.C. Oldham, H. Wang, J. Shorter, A.J. Filiano, E.D. Roberson, W.G. Tourtellotte, B. Chen, L.H. Tsai, and E.J. Huang. (2014). ALS-associated mutation FUS-R521C causes DNA damage and RNA splicing defects. J. Clin. Invest. 124(3):981–999. pdf file link

62. Jackrel, M.E., M.E. DeSantis, B.A. Martinez, L.M. Castellano, R.M. Stewart, K.A. Caldwell, G.A. Caldwell, and J. Shorter^. (2014). Potentiated Hsp104 variants antagonize diverse proteotoxic misfolding events. Cell. 156(1-2):170–182. pdf file link (^Corresponding author).

61. DeSantis, M.E., E.A. Sweeny, D. Snead, E.H. Leung, M.S. Go, K. Gupta, P. Wendler, and J. Shorter^. (2014). Conserved distal loop residues in the Hsp104 and ClpB middle domain contact nucleotide-binding domain 2 and enable Hsp70-dependent protein disaggregation. J. Biol. Chem. 289(2):848-867. pdf file link (^Corresponding author).


60. Torrente, M.P., and J. Shorter^. (2013). The metazoan protein disaggregase and amyloid depolymerase system: Hsp110, Hsp70, Hsp40, and small heat shock proteins. Prion. 7(6):457-463. pdf file link (^Corresponding author).

59. Coelho, M., A. Dereli, A. Haese, S. Kühn, L. Malinovska, M.E. DeSantis, J. Shorter, S. Alberti, T. Gross, and I.M. Tolić-Nørrelykke. (2013). Fission yeast does not age under favorable conditions, but does so after stress. Curr. Biol. 23(19): 1844-1852. pdf file link

58. Cushman-Nick, M., N.M. Bonini^, and J. Shorter^. (2013). Hsp104 suppresses polyglutamine-induced degeneration post onset in a Drosophila MJD/SCA3 model. PLoS Genetics. 9(9): e1003781. pdf file link (^Co-corresponding author).

57. Shorter, J.^, and J.P. Taylor^. (2013). Disease mutations in the prion-like domains of hnRNPA1 and hnRNPA2B1 introduce potent steric zippers that drive excess RNP granule assembly. Rare Diseases. 1(2):e25200. pdf file link (^Co-corresponding author).

56. Li, Y.R.^, O.D. King, J. Shorter^, and A.D. Gitler^. (2013). Stress granules as crucibles of ALS pathogenesis. J. Cell Biol. 201(3):361-372. pdf file link (^Co-corresponding author).

55. Kim*, H.J., N.C.Kim*, Y.D. Wang*, E.A. Scarborough*, J. Moore*, Z. Diaz*, K.S. MacLea, B. Freibaum, S. Li, A. Molliex, A.P. Kanagaraj, R. Carter, K.B. Boylan, A.M. Wojtas, R. Rademakers, J.L. Pinkus, S.A. Greenberg, J.Q. Trojanowski, B.J. Traynor, B.N. Smith, S. Topp, A.S. Gkazi, J. Miller, C.E. Shaw, M. Kottlors, J. Kirschner, A. Pestronk, Y.R. Li, A.F. Ford, A.D. Gitler, M. Benatar, O.D. King, V.E. Kimonis, E.D. Ross, C.C. Weihl, J. Shorter^, and J.P. Taylor^. (2013). Mutations in prion-like domains in hnRNPA2B1 and hnRNPA1 cause multisystem proteinopathy and ALS. Nature. 495(7442):467–473. pdf file link (*Co-first author. ^Co-corresponding author).


54. DeSantis, M.E., and J. Shorter^. (2012). Hsp104 drives ''protein-only'' positive selection of Sup35 prion strains encoding strong [PSI+]. Chem. Biol. 19(11):1400-1410. pdf file link (^Corresponding author).

53. DeSantis, M.E., E.H. Leung, E.A. Sweeny, M.E. Jackrel, M. Cushman-Nick, A. Neuhaus-Follini, S. Vashist, M.A. Sochor, M.N. Knight, and J. Shorter^. (2012). Operational plasticity enables Hsp104 to disaggregate diverse amyloid and nonamyloid clients. Cell. 151(4):778-793. pdf file link (^Corresponding author).

52. Armakola, M., M.J. Higgins, M.D. Figley, S.J. Barmada, E.A. Scarborough, Z. Diaz, , X. Fang, J. Shorter, N.J. Krogan, S. Finkbeiner, R.V. Farese Jr., and A.D. Gitler. (2012). Inhibition of RNA lariat debranching enzyme suppresses TDP-43 toxicity in ALS disease models. Nat. Genet. 44(12):1302–1309. pdf file link

51. Duennwald, M.L., A.L. Echeverria, and J. Shorter^. (2012). Small heat shock proteins potentiate amyloid dissolution by protein disaggregases from yeast and humans. PLoS Biol. 9(6):e1001346. pdf file link (^Corresponding author).

50. Castellano, L.M., and J. Shorter^. (2012). The surprising role of amyloid fibrils in HIV infection. Biology. 1(1):58-80. pdf file link (^Corresponding author).

49. Couthouis, J., M.P. Hart, R. Erion, Z. Diaz, T. Nakaya, F. Ibrahim, H.J. Kim, J. Mojsilovic-Petrovic, D. Clay-Falcone, L. Elman, L. McCluskey, R. Greene, R.G. Kalb, V.M. Lee, J.Q. Trojanowski, G.A. Nicholson, I.P. Blair, O.D. King, N.M. Bonini, V.M. Van Deerlin, Z. Mourelatos, J. Shorter, and A.D. Gitler. (2012). Evaluating the role of the FUS/TLS-related gene EWSR1 in amyotrophic lateral sclerosis. Hum. Mol. Genet. 21(13):2899-911. pdf file link

48. Ugras, S.E., and J. Shorter^. (2012). RNA-binding proteins in amyotrophic lateral sclerosis and neurodegeneration. Neurol. Res. Int. doi:10.1155/2012/432780. pdf file link (^Corresponding author).

47. King, O.D.^, A.D. Gitler^, and J. Shorter^. (2012). The tip of the iceberg: RNA-binding proteins with prion-like domains in neurodegenerative disease. Brain Res. 1462:61-80. pdf file link (^Co-corresponding authors).

46. DeSantis, M.E., and J. Shorter^. (2012). The elusive middle domain of Hsp104 and ClpB: location and function. Biochimica et Biophysica Acta. 1823(1):29-39. pdf file link (^Corresponding author).


45. Couthouis, J.*, M.P. Hart*, J. Shorter*, M. DeJesus-Hernandez, R. Erion, R.E. Oristano, X.A. Liu, D. Ramos, N. Jethava, D. Hosangadi, J. Epstein, A. Chiang, Z. Diaz, T. Nakaya, F. Ibrahim, H.J. Kim, J.A. Solski, K.L. Williams, J. Mojsilovic-Petrovic, C. Ingre, K. Boylan, N. Graff-Radford, D. Dickson, D. Clay-Falcone, L. Elman, L. McCluskey, R. Greene, R.G. Kalb, V.M.Y. Lee, J.Q. Trojanowski, A.C. Ludolph, W. Robberecht, P.M. Andersen, G.A. Nicholson, I.P. Blair, O.D. King, N.M. Bonini, V. Van Deerlin, R. Rademakers, Z. Mourelatos, and A.D. Gitler. (2011). A yeast functional screen predicts new candidate ALS disease genes. Proc. Natl. Acad. Sci. U.S.A. 108(52):20881-90. pdf file link cover (*Authors contributed equally to this work).

44. Shorter, J^. (2011). The mammalian disaggregase machinery: Hsp110 synergizes with Hsp70 and Hsp40 to catalyze protein disaggregation and reactivation in a cell-free system. PLoS ONE. 6(10):e26319. pdf file link (^Corresponding author).

43. Sweeny, E.A., M.E. DeSantis, and J. Shorter^. (2011). Purification of Hsp104, a protein disaggregase. J. Vis. Exp. 55:e3190 doi:10.3791/3190 pdf file link (^Corresponding author).

42. Shorter, J^. (2011). Amyloid remodeling by Hsp104, in Protein Chaperones and Protection from Neurodegeneration (ed. Witt, S.N.). Chapter 7: 235-259. (John Wiley & Sons, Inc.). pdf file link (^Corresponding author).

41. Gitler, A.D.^, and J. Shorter^. (2011). RNA-binding proteins with prion-like domains in ALS and FTLD-U. Prion. 5(3):179-187. pdf file link cover (^Co-corresponding author).

40. Jackrel, M.E., and J. Shorter^. (2011). Shock and awe: unleashing the heat shock response to treat Huntington disease. J. Clin. Invest. 121(8):2972-2975. pdf file link (^Corresponding author).

39. Sun, Z., Z. Diaz, X. Fang, M.P. Hart, A. Chesi, J. Shorter^, and A.D. Gitler^. (2011). Molecular determinants and genetic modifiers of aggregation and toxicity for the ALS disease protein FUS/TLS. PLoS Biol. 9(4):e1000614. pdf file link (^Co-Corresponding author).


38. Duennwald, M.L.^, and J. Shorter^. (2010). Countering amyloid polymorphism and drug resistance with minimal drug cocktails. Prion. 4(4): 244-251. pdf file link (^Co-Corresponding author).

37. Shorter, J.^ (2010). Emergence and natural selection of drug-resistant prions. Mol. Biosyst. 6(7):1115-1130. pdf file link (^Corresponding author).

36. Cushman, M., B.S. Johnson, O.D. King, A.D. Gitler^, and J. Shorter^. (2010). Prion-like disorders: blurring the divide between transmissibility and infectivity. J. Cell Sci. 123(8):1191-1201. pdf file link (^Co-Corresponding author).

35. Vashist, S., M. Cushman, and J. Shorter^. (2010). Applying Hsp104 to protein-misfolding disorders. Biochem. Cell Biol. 88(1):1-13. pdf file link (^Corresponding author).


34. Roberts, B.E., M.L. Duennwald^, H. Wang, C. Chung, N.P. Lopreiato, E.A. Sweeny, M.N. Knight, and J. Shorter^. (2009). A synergistic small-molecule combination directly eradicates diverse prion strain structures. Nat. Chem. Biol. 5(12):936-946. pdf file link (^Co-Corresponding author).

33. Watt, B., G. van Niel, D.M. Fowler, I. Hurbain, K.C. Luk, S.E. Stayrook, M.A. Lemmon, G. Raposo, J. Shorter, J.W. Kelly, and M.S. Marks. (2009). N-terminal domains elicit formation of functional Pmel17 amyloid fibrils. J. Biol. Chem. 284(51):35543-35555. pdf file link cover

32. Johnson, B.S., D. Snead, J.J. Lee, J. M. McCaffery, J. Shorter^, and A.D. Gitler^. (2009). TDP-43 is intrinsically aggregation-prone and Amyotrophic Lateral Sclerosis-linked mutations accelerate aggregation and increase toxicity. J. Biol. Chem. 284(30):20329-39. pdf file link (^Co-Corresponding author).

31. Wendler, P., J. Shorter, D. Snead, C. Plisson, D.K. Clare, S. Lindquist, and H.R. Saibil. (2009). Motor mechanism for protein threading through Hsp104. Mol. Cell. 34(1):81-92. pdf file link


30. Sweeny, E.A., and J. Shorter^. (2008). Prion proteostasis: Hsp104 meets its supporting cast. Prion. 2(4):135-40. pdf file link (^Corresponding author)

29. Skinner, J.J., S. Wood, J. Shorter, S.W. Englander, and B.E. Black. (2008). The Mad2 partial unfolding model: regulating mitosis through Mad2 conformational switching. J. Cell Biol. 183(5):761-768. pdf file link

28. Shorter, J.^, and S. Lindquist. (2008). Hsp104, Hsp70 and Hsp40 interplay regulates formation, growth and elimination of Sup35 prions. EMBO J. 27 (20):2712–2724. pdf file link (^Corresponding author).

27. Lo Bianco, C.*, J. Shorter*^, E. Régulier, H. Lashuel, T. Iwatsubo, S. Lindquist, and P. Aebischer^. (2008). Hsp104 antagonizes alpha-synuclein aggregation and reduces dopaminergic degeneration in a rat model of Parkinson’s disease. J. Clin. Invest. 118(9):3087-3097. pdf file link (*Authors contributed equally to this work. ^Co-Corresponding author)

26. Maday, S., E. Anderson, H.C. Chang, J. Shorter, A. Satoh, J. Sfakianos, H. Foelsch, J.M. Anderson, Z. Walther, and I. Mellman. (2008). A PDZ-binding motif controls basolateral targeting of syndecan-1 along the biosynthetic pathway in polarized epithelial cells. Traffic. 9(11):1915–1924. pdf file link

25. Roberts, B.E. and J. Shorter^. (2008). Escaping Amyloid Fate. Nat. Struct. Mol. Biol. 15(6):544-546. pdf file link (^Corresponding author)

24. Wang, H., M.L. Duennwald, B.E. Roberts, L.M. Rozeboom, Y.L. Zhang, A.D. Steele, R. Krishnan, L.J. Su, D. Griffin, S. Mukhopadhyay, E.J. Hennessy, P. Weigele, B.J. Blanchard, J. King, A.A. Deniz, S.L. Buchwald, V.M. Ingram, S. Lindquist^, and J. Shorter^. (2008). Direct and selective elimination of specific prions and amyloids by 4,5-dianilinophthalimide and analogs. Proc. Natl. Acad. Sci. U.S.A. 105(20):7159-7164. pdf file link (^Co-Corresponding author)

23. Sadlish H., H. Rampelt, J. Shorter, R.D. Wegrzyn, C. Andréasson, S. Lindquist, and B. Bukau. (2008). Hsp110 chaperones regulate prion formation and propagation in S. cerevisiae by two discrete activities. PLoS ONE. 3(3):e1763. pdf file link

22. Shorter, J.^ (2008). Hsp104: a weapon to combat diverse neurodegenerative disorders. Neurosignals. 16(1):63-74. pdf file link cover (^Corresponding author)

21. Gitler, A.D., B.J. Bevis, J. Shorter , K.E. Strathearn, S. Hamamichi, L.J. Su, K.A. Caldwell, G.A. Caldwell, J.C. Rochet, J.M. McCaffery, C. Barlowe, and S. Lindquist. (2008). The Parkinson's disease protein alpha-synuclein disrupts cellular Rab homeostasis. Proc. Natl. Acad. Sci. U.S.A. 105(1):145-150. pdf file link


20. Wendler, P., J. Shorter, C. Plisson, A.G. Cashikar, S. Lindquist, and H.R. Saibil. (2007). Atypical AAA+ subunit packing creates an expanded cavity for disaggregation by the protein-remodeling factor Hsp104. Cell. 131(7):1366-1377. pdf file link

19. Gitler, A. D.^, and J. Shorter^ (2007). Prime time for alpha-synuclein. J. Neurosci. 27(10):2433-2434. pdf file link (^Co-Corresponding author)

18. Doyle, S. M.*, J. Shorter*, M. Zolkiewski, J.R. Hoskins, S. Lindquist, and S. Wickner. (2007). Asymmetric deceleration of ClpB or Hsp104 ATPase activity unleashes protein-remodeling activity. Nat. Struct. Mol. Biol. 14(2):114-122. pdf file link (*Authors contributed equally to this work)


17. Shorter, J., and S. Lindquist. (2006). Destruction or potentiation of different prions catalyzed by similar Hsp104 remodeling activities. Mol. Cell. 23(3):425-438. pdf file link


16. Shorter, J.^, and S. Lindquist^. (2005). Prions as adaptive conduits of memory and inheritance. Nat. Rev. Genetics. 6(6):435-450. pdf file link (^Co-Corresponding author)

15. Beard, M.B., A. Satoh, J. Shorter, and G. Warren. (2005). A cryptic Rab1-binding site in the p115 tethering protein. J. Biol. Chem. 280(27):25840-25848. pdf file link

14. Shorter, J., and S. Lindquist. (2005). Navigating the ClpB channel to solution. Nat. Struct. Mol. Biol. 12(1):4-6. pdf file link


13. Shorter, J., and S. Lindquist. (2004). Hsp104 catalyzes formation and elimination of self-replicating Sup35 prion conformers. Science. 304(5678):1793-1797. pdf file link


12. Wang, Y., J. Seemann, M. Pypaert, J. Shorter, and G. Warren. (2003). A direct role for GRASP65 as a mitotically regulated Golgi stacking factor. EMBO J. 22(13):3279-90. pdf file link


11. Shorter, J.^, and G. Warren^. (2002). Golgi Architecture and Inheritance. Annu. Rev. Cell Dev. Biol. 18:379-420. pdf file link (^Co-Corresponding author)

10. Müller, J.M.*, J. Shorter*, R. Newman, K. Deinhardt, Y. Sagiv, Z. Elazar, G. Warren, and D.T. Shima. (2002). Sequential SNARE disassembly and GATE-16/GOS-28 complex assembly mediated by distinct NSF activities drives Golgi membrane fusion. J. Cell Biol. 157(7):1161-1173. pdf file link (*Authors contributed equally to this work)

9. Shorter, J., M.B. Beard, J. Seemann, A.B. Dirac-Svejstrup, and G. Warren. (2002). Sequential tethering of Golgins and catalysis of SNAREpin assembly by the vesicle-tethering protein p115. J. Cell Biol. 157(1):45-62. pdf file link


8. Dirac-Svejstrup, A.B., J. Shorter, M.G. Waters, and G. Warren. (2000). Phosphorylation of the vesicle-tethering protein p115 by a casein kinase II-like enzyme is required for Golgi reassembly from isolated mitotic fragments. J. Cell Biol. 150(3):475-488. pdf file link

7. Meyer, H. H., J.G. Shorter, J. Seemann, D. Pappin, and G. Warren. (2000). A complex of mammalian ufd1 and npl4 links the AAA-ATPase, p97, to ubiquitin and nuclear transport pathways. EMBO J. 19(10):2181-2192. pdf file link

6. Shorter, J. (2000). Molecular mechanisms regulating Golgi architecture during the mammalian cell division cycle. Ph.D. Thesis (University of London).

5. Barr, F.A., and J. Shorter. (2000). Membrane traffic: do cones mark sites of fission? Curr. Biol. 10(4):R141-144. pdf file link

4. Lesa, G.M., J. Seemann, J. Shorter, J. Vandekerckhove, and G. Warren. (2000). The amino-terminal domain of the Golgi protein Giantin interacts directly with the vesicle-tethering protein p115. J. Biol. Chem. 275(4):2831-2836. pdf file link


3. Müller, J.M., C. Rabouille, R. Newman, J. Shorter, P. Freemont, G. Schiavo, G. Warren, and D.T. Shima. (1999). An NSF function distinct from ATPase-dependent SNARE disassembly is essential for Golgi membrane fusion. Nat. Cell Biol. 1(6):335-340. pdf file link

2. Shorter, J., R. Watson, M.E. Giannakou, M. Clarke, G. Warren, and F.A. Barr. (1999). GRASP55, a second mammalian GRASP protein involved in the stacking of Golgi cisternae in a cell-free system. EMBO J. 18(18):4949-4960. pdf file link

1. Shorter, J.^, and G. Warren. (1999). A role for the vesicle tethering protein, p115, in the post-mitotic stacking of reassembling Golgi cisternae in a cell-free system. J. Cell Biol. 146(1):57-70. pdf file link (^Corresponding author)

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Department of Biochemistry & Biophysics

University of Pennsylvania