J
James Shorter
Researcher at University of Pennsylvania
Publications - 211
Citations - 20145
James Shorter is an academic researcher from University of Pennsylvania. The author has contributed to research in topics: Neurodegeneration & Protein aggregation. The author has an hindex of 65, co-authored 180 publications receiving 16242 citations. Previous affiliations of James Shorter include Lincoln's Inn & Massachusetts Institute of Technology.
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Journal ArticleDOI
Protein Phase Separation: A New Phase in Cell Biology.
Steven Boeynaems,Steven Boeynaems,Simon Alberti,Nicolas L. Fawzi,Tanja Mittag,Magdalini Polymenidou,Frederic Rousseau,Frederic Rousseau,Joost Schymkowitz,Joost Schymkowitz,James Shorter,Benjamin Wolozin,Ludo Van Den Bosch,Peter Tompa,Peter Tompa,Monika Fuxreiter +15 more
TL;DR: A combination of techniques from cell biology, biophysics, physical chemistry, structural biology, and bioinformatics are starting to help establish the molecular principles of an emerging field, thus paving the way for exciting discoveries, including novel therapeutic approaches for the treatment of age-related disorders.
Journal ArticleDOI
Mutations in prion-like domains in hnRNPA2B1 and hnRNPA1 cause multisystem proteinopathy and ALS
Hong Joo Kim,Nam Chul Kim,Yong Dong Wang,Emily A. Scarborough,Jennifer Moore,Zamia Diaz,Kyle S. MacLea,Brian D. Freibaum,Songqing Li,Amandine Molliex,Anderson P. Kanagaraj,Robert A. Carter,Kevin B. Boylan,Aleksandra Wojtas,Rosa Rademakers,Jack L. Pinkus,Steven A. Greenberg,John Q. Trojanowski,Bryan J. Traynor,Bradley N. Smith,Simon Topp,Athina Soragia Gkazi,Jack W. Miller,Christopher Shaw,Michael Kottlors,Janbernd Kirschner,Alan Pestronk,Yun Li,Alice Flynn Ford,Aaron D. Gitler,Michael Benatar,Oliver D. King,Virginia Kimonis,Eric D. Ross,Conrad C. Weihl,James Shorter,J. Paul Taylor +36 more
TL;DR: Dysregulated polymerization caused by a potent mutant steric zipper motif in a PrLD can initiate degenerative disease and related proteins with PrLDs should be considered candidates for initiating and perhaps propagating proteinopathies of muscle, brain, motor neuron and bone.
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Stress granules as crucibles of ALS pathogenesis
TL;DR: This work has shown that TDP-43 and FUS and several related RNA-binding proteins harbor aggregation-promoting prion-like domains that allow them to rapidly self-associate, critical for the formation and dynamics of cellular ribonucleoprotein granules, the crucibles of RNA metabolism and homeostasis.
Journal ArticleDOI
TDP-43 Is Intrinsically Aggregation-prone, and Amyotrophic Lateral Sclerosis-linked Mutations Accelerate Aggregation and Increase Toxicity
Brian S. Johnson,David Snead,Jonathan Lee,J. Michael McCaffery,James Shorter,Aaron D. Gitler +5 more
TL;DR: It is reported that, in the absence of other components, TDP-43 spontaneously forms aggregates bearing remarkable ultrastructural similarities to TDP -43 deposits in degenerating neurons of ALS FTLD-U patients.
Journal ArticleDOI
The tip of the iceberg: RNA-binding proteins with prion-like domains in neurodegenerative disease
TL;DR: Simple prion-like transfer mechanisms involving the prion domains of RNA-binding proteins could underlie the classical non-cell-autonomous emanation of neurodegenerative pathology from originating epicenters to neighboring portions of the nervous system.