S
Sarah A. Sagi
Researcher at University of California, San Diego
Publications - 20
Citations - 4026
Sarah A. Sagi is an academic researcher from University of California, San Diego. The author has contributed to research in topics: Amyloid precursor protein & G protein-coupled receptor. The author has an hindex of 15, co-authored 19 publications receiving 3945 citations. Previous affiliations of Sarah A. Sagi include Mayo Clinic.
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Journal ArticleDOI
A subset of NSAIDs lower amyloidogenic Aβ42 independently of cyclooxygenase activity
Sascha Weggen,Jason L. Eriksen,Pritam Das,Sarah A. Sagi,Rong Wang,Claus U. Pietrzik,Kirk A. Findlay,Tawnya E. Smith,Michael P. Murphy,Thomas Bulter,David E. Kang,Numa R. Marquez-Sterling,Todd E. Golde,Edward H. Koo +13 more
TL;DR: It is reported that the NSAIDs ibuprofen, indomethacin and sulindac sulphide preferentially decrease the highly amyloidogenic Aβ42 peptide (the 42-residue isoform of the amyloids-β peptide) produced from a variety of cultured cells by as much as 80%.
Journal ArticleDOI
NSAIDs and enantiomers of flurbiprofen target γ-secretase and lower Aβ42 in vivo
Jason L. Eriksen,Sarah A. Sagi,Tawnya E. Smith,Sascha Weggen,Pritam Das,Daniel C. McLendon,Victor V. Ozols,Kevin W. Jessing,Kenton H. Zavitz,Edward H. Koo,Todd E. Golde +10 more
TL;DR: R-flurbiprofen reduces Aβ42 levels by targeting γ-secretase and has reduced side effects related to inhibition of cyclooxygenase (COX), it is an excellent candidate for clinical testing as an A β42 lowering agent.
Journal ArticleDOI
The role of Rho in G protein-coupled receptor signal transduction.
TL;DR: G alpha 12/13 can bind and activate Rho-specific guanine nucleotide exchange factors, providing a mechanism by which GPCRs that couple to G alpha12/13 could activate RHo and its downstream responses.
Journal ArticleDOI
Substrate-targeting γ-secretase modulators
Thomas Kukar,Thomas B. Ladd,Maralyssa Bann,Patrick C. Fraering,Patrick C. Fraering,Rajeshwar Narlawar,Ghulam M. Maharvi,Brent Healy,Robert Chapman,Alfred T. Welzel,Robert W. Price,Brenda D. Moore,Vijayaraghavan Rangachari,Bernadette Cusack,Jason L. Eriksen,Karen Jansen-West,Christophe Verbeeck,Debra Yager,Christopher B. Eckman,Wenjuan Ye,Sarah A. Sagi,Barbara A. Cottrell,Justin W. Torpey,Terrone L. Rosenberry,Abdul H. Fauq,Michael S. Wolfe,Boris Schmidt,Dominic M. Walsh,Edward H. Koo,Todd E. Golde +29 more
TL;DR: Findings indicate that substrate targeting by GSMs mechanistically links two therapeutic actions: alteration in Aβ42 production and inhibition of amyloid-β aggregation, which may synergistically reduce amyloids-β deposition in Alzheimer’s disease.
Journal ArticleDOI
Diverse compounds mimic Alzheimer disease–causing mutations by augmenting Aβ42 production
Thomas Kukar,Michael P. Murphy,Michael P. Murphy,Jason L. Eriksen,Sarah A. Sagi,Sascha Weggen,Sascha Weggen,Tawnya E. Smith,Thomas B. Ladd,Murad Ali Khan,Rajashaker Kache,Jenny Beard,Mark K. Dodson,Sami L. Merit,Victor V. Ozols,Panos Z. Anastasiadis,Pritam Das,Abdul H. Fauq,Edward H. Koo,Todd E. Golde +19 more
TL;DR: In this article, the authors identify a number of compounds that raise Aβ42 levels in the brain, including fenofibrate, an antilipidemic agent, and celecoxib, a COX-2-selective NSAID.