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Nathaniel Safren
Researcher at University of Maryland, Baltimore
Publications - 4
Citations - 308
Nathaniel Safren is an academic researcher from University of Maryland, Baltimore. The author has contributed to research in topics: Huntington's disease & Motor neuron. The author has an hindex of 4, co-authored 4 publications receiving 281 citations.
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Journal ArticleDOI
Pattern of ubiquilin pathology in ALS and FTLD indicates presence of C9ORF72 hexanucleotide expansion
Johannes Brettschneider,Johannes Brettschneider,Vivianna M. Van Deerlin,John L. Robinson,Linda K. Kwong,Edward B. Lee,Yousuf O. Ali,Nathaniel Safren,Mervyn J. Monteiro,Jon B. Toledo,Lauren Elman,Leo McCluskey,David J. Irwin,Murray Grossman,Laura Molina-Porcel,Virginia M.-Y. Lee,John Q. Trojanowski +16 more
TL;DR: The study indicates a pathophysiological link between C9ORF72 expansions and UBQLN proteins in ALS and FTLD-TDP that is associated with alterations in clinical phenotype, and suggests that the presence of C9ORN72 repeat expansions may indicate a worse prognosis in ALS.
Journal ArticleDOI
Motor neuron disease, TDP-43 pathology, and memory deficits in mice expressing ALS-FTD-linked UBQLN2 mutations.
Nhat T. T. Le,Lydia Chang,Irina Kovlyagina,Polymnia Georgiou,Nathaniel Safren,Kerstin E. Braunstein,Mark D. Kvarta,Adam M. Van Dyke,Tara A. LeGates,Thomas Philips,Brett M. Morrison,Scott M. Thompson,Adam C. Puche,Todd D. Gould,Jeffrey D. Rothstein,Philip C. Wong,Mervyn J. Monteiro +16 more
TL;DR: It is shown that lines of mice expressing either the ALS–FTD-linked P497S or P506T UBQLN2 mutations have cognitive deficits, shortened lifespans, and develop motor neuron disease, mimicking the human disease.
Journal ArticleDOI
Ubiquilin-1 overexpression increases the lifespan and delays accumulation of Huntingtin aggregates in the R6/2 mouse model of Huntington's disease.
Nathaniel Safren,Amina El Ayadi,Lydia Chang,Chantelle E. Terrillion,Todd D. Gould,Darren Boehning,Mervyn J. Monteiro +6 more
TL;DR: It is demonstrated that overexpression of ubiqulin-1, which facilitates protein clearance through the proteasome and autophagy pathways, reduces huntingtin aggregates and toxicity in mammalian cell and invertebrate models of HD, and that restoration of ubiquilin levels would delay HD symptoms and pathology.
Journal ArticleDOI
Signature changes in ubiquilin expression in the R6/2 mouse model of Huntington’s disease
TL;DR: It is demonstrated that all ubiquilin proteins are involved in HD pathology and that distinct changes in the signature of Ubiquilin-4 expression could be useful for monitoring end-stage of HD disease.