Year |
Citation |
Score |
2022 |
Fare CM, Rhine K, Lam A, Myong S, Shorter J. A minimal construct of nuclear-import receptor Karyopherin-β2 defines the regions critical for chaperone and disaggregation activity. The Journal of Biological Chemistry. 102806. PMID 36529289 DOI: 10.1016/j.jbc.2022.102806 |
0.66 |
|
2022 |
Shen H, Yanas A, Owens MC, Zhang C, Fritsch C, Fare CM, Copley KE, Shorter J, Goldman YE, Liu KF. Sexually dimorphic RNA helicases DDX3X and DDX3Y differentially regulate RNA metabolism through phase separation. Molecular Cell. PMID 35588748 DOI: 10.1016/j.molcel.2022.04.022 |
0.738 |
|
2022 |
Kim HJ, Mohassel P, Donkervoort S, Guo L, O'Donovan K, Coughlin M, Lornage X, Foulds N, Hammans SR, Foley AR, Fare CM, Ford AF, Ogasawara M, Sato A, Iida A, et al. Heterozygous frameshift variants in HNRNPA2B1 cause early-onset oculopharyngeal muscular dystrophy. Nature Communications. 13: 2306. PMID 35484142 DOI: 10.1038/s41467-022-30015-1 |
0.733 |
|
2022 |
Rhine K, Dasovich M, Yoniles J, Badiee M, Skanchy S, Ganser LR, Ge Y, Fare CM, Shorter J, Leung AKL, Myong S. Poly(ADP-ribose) drives condensation of FUS via a transient interaction. Molecular Cell. PMID 35182479 DOI: 10.1016/j.molcel.2022.01.018 |
0.604 |
|
2021 |
Odeh HM, Fare CM, Shorter J. Nuclear-import receptors counter deleterious phase transitions in neurodegenerative disease. Journal of Molecular Biology. 167220. PMID 34464655 DOI: 10.1016/j.jmb.2021.167220 |
0.788 |
|
2021 |
Beijer D, Kim HJ, Guo L, O'Donovan K, Mademan I, Deconinck T, Van Schil K, Fare CM, Drake LE, Ford AF, Kochański A, Kabzińska D, Dubuisson N, Van den Bergh P, Voermans NC, et al. Characterization of HNRNPA1 mutations defines diversity in pathogenic mechanisms and clinical presentation. Jci Insight. 6. PMID 34291734 DOI: 10.1172/jci.insight.148363 |
0.73 |
|
2021 |
Fare CM, Villani A, Drake LE, Shorter J. Higher-order organization of biomolecular condensates. Open Biology. 11: 210137. PMID 34129784 DOI: 10.1098/rsob.210137 |
0.459 |
|
2021 |
Fare CM, Shorter J. (Dis)Solving the problem of aberrant protein states. Disease Models & Mechanisms. 14. PMID 33942880 DOI: 10.1242/dmm.048983 |
0.579 |
|
2021 |
Fare CM, Shorter J. Open Access: A Role for p53 in c9ALS/FTD? Trends in Genetics : Tig. PMID 33551183 DOI: 10.1016/j.tig.2021.01.008 |
0.523 |
|
2020 |
Hutten S, Usluer S, Bourgeois B, Simonetti F, Odeh HM, Fare CM, Czuppa M, Hruska-Plochan M, Hofweber M, Polymenidou M, Shorter J, Edbauer D, Madl T, Dormann D. Nuclear Import Receptors Directly Bind to Arginine-Rich Dipeptide Repeat Proteins and Suppress Their Pathological Interactions. Cell Reports. 33: 108538. PMID 33357437 DOI: 10.1016/j.celrep.2020.108538 |
0.773 |
|
2020 |
Rhine K, Makurath MA, Liu J, Skanchy S, Lopez C, Catalan KF, Ma Y, Fare CM, Shorter J, Ha T, Chemla YR, Myong S. ALS/FTLD-Linked Mutations in FUS Glycine Residues Cause Accelerated Gelation and Reduced Interactions with Wild-Type FUS. Molecular Cell. 80: 1139. PMID 33338404 DOI: 10.1016/j.molcel.2020.11.031 |
0.531 |
|
2019 |
Niaki AG, Sarkar J, Cai X, Rhine K, Vidaurre V, Guy B, Hurst M, Lee JC, Koh HR, Guo L, Fare CM, Shorter J, Myong S. Loss of Dynamic RNA Interaction and Aberrant Phase Separation Induced by Two Distinct Types of ALS/FTD-Linked FUS Mutations. Molecular Cell. PMID 31630970 DOI: 10.1016/J.Molcel.2019.09.022 |
0.724 |
|
2019 |
Guo L, Fare CM, Shorter J. Therapeutic Dissolution of Aberrant Phases by Nuclear-Import Receptors. Trends in Cell Biology. PMID 30660504 DOI: 10.1016/J.Tcb.2018.12.004 |
0.726 |
|
2018 |
Guo L, Kim HJ, Wang H, Monaghan J, Freyermuth F, Sung JC, O'Donovan K, Fare CM, Diaz Z, Singh N, Zhang ZC, Coughlin M, Sweeny EA, DeSantis ME, Jackrel ME, et al. Nuclear-Import Receptors Reverse Aberrant Phase Transitions of RNA-Binding Proteins with Prion-like Domains. Cell. 173: 677-692.e20. PMID 29677512 DOI: 10.1016/J.Cell.2018.03.002 |
0.682 |
|
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