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Charlotte M. Fare
Researcher at University of Pennsylvania
Publications - 21
Citations - 784
Charlotte M. Fare is an academic researcher from University of Pennsylvania. The author has contributed to research in topics: Nuclear transport & Biology. The author has an hindex of 7, co-authored 13 publications receiving 400 citations.
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Journal ArticleDOI
Nuclear-Import Receptors Reverse Aberrant Phase Transitions of RNA-Binding Proteins with Prion-like Domains
Lin Guo,Hong Joo Kim,Hejia Wang,John Monaghan,Fernande Freyermuth,Julie C. Sung,Kevin J. O'Donovan,Charlotte M. Fare,Zamia Diaz,Nikita Singh,Zi Chao Zhang,Zi Chao Zhang,Maura Coughlin,Elizabeth A. Sweeny,Morgan E. DeSantis,Meredith E. Jackrel,Christopher B. Rodell,Jason A. Burdick,Oliver D. King,Aaron D. Gitler,Clotilde Lagier-Tourenne,Udai Bhan Pandey,Yuh Min Chook,J. Paul Taylor,J. Paul Taylor,James Shorter +25 more
TL;DR: Karyopherin-β2 prevents RBPs with PY-NLSs accumulating in stress granules, restores nuclear RBP localization and function, and rescues degeneration caused by disease-linked FUS and hnRNPA2, establishing that NIRs therapeutically restore RBP homeostasis and mitigate neurodegeneration.
Journal ArticleDOI
Loss of Dynamic RNA Interaction and Aberrant Phase Separation Induced by Two Distinct Types of ALS/FTD-Linked FUS Mutations.
Amirhossein Ghanbari Niaki,Jaya Sarkar,Xinyi Cai,Kevin Rhine,Velinda Vidaurre,Brian Guy,Miranda N Hurst,Jong-Chan Lee,Hye Ran Koh,Hye Ran Koh,Lin Guo,Lin Guo,Charlotte M. Fare,James Shorter,Sua Myong,Sua Myong +15 more
TL;DR: It is demonstrated that wild-type FUS binds single-stranded RNA stoichiometrically in a length-dependent manner and that multimers induce highly dynamic interactions with RNA, giving rise to small and fluid condensates.
Journal ArticleDOI
Higher-order organization of biomolecular condensates.
TL;DR: In this article, a review of the underlying physical and chemical processes that generate internal condensate architectures is presented, and the authors discuss how specific condensat organization is critical for specific biological functions.
Journal ArticleDOI
ALS/FTLD-Linked Mutations in FUS Glycine Residues Cause Accelerated Gelation and Reduced Interactions with Wild-Type FUS.
Kevin Rhine,Monika A. Makurath,James Liu,James Liu,Sophie Skanchy,Christian Lopez,Kevin F. Catalan,Ye Ma,Charlotte M. Fare,James Shorter,Taekjip Ha,Yann R. Chemla,Sua Myong,Sua Myong +13 more
TL;DR: It is demonstrated that ALS/FTLD-linked FUS mutations in glycine (G) strikingly drive formation of droplets that do not readily interact withWT FUS, whereas arginine (R) mutants form mixed condensates with WT FUS.
Journal ArticleDOI
Nuclear Import Receptors Directly Bind to Arginine-Rich Dipeptide Repeat Proteins and Suppress Their Pathological Interactions
Saskia Hutten,Sinem Usluer,Benjamin Bourgeois,Francesca Simonetti,Hana M. Odeh,Charlotte M. Fare,Mareike Czuppa,Marian Hruska-Plochan,Mario Hofweber,Magdalini Polymenidou,James Shorter,Dieter Edbauer,Tobias Madl,Dorothee Dormann +13 more
TL;DR: It is shown that arginine-rich DPRs (poly-GR and poly-PR) bind directly to multiple importins and, in excess, promote their insolubility and condensation, and suggest that importins can decrease toxicity of arginin- rich DPRs by suppressing their pathological interactions.