S
Susanna Suomensaari
Researcher at Sunesis Pharmaceuticals
Publications - 3
Citations - 1969
Susanna Suomensaari is an academic researcher from Sunesis Pharmaceuticals. The author has contributed to research in topics: P3 peptide & Amyloid precursor protein. The author has an hindex of 3, co-authored 3 publications receiving 1917 citations.
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Purification and cloning of amyloid precursor protein beta-secretase from human brain.
Sukanto Sinha,John P. Anderson,Robin Barbour,Guriqbal S. Basi,Russell J. Caccavello,David Davis,Minhtam Doan,Harry F. Dovey,Normand Frigon,Jin Hong,Kirsten L. Jacobson-Croak,Nancy Jewett,Pamela S. Keim,J. Knops,Ivan Lieberburg,Michael Power,Hua Tan,Gwen Tatsuno,Jay Tung,Dale Schenk,Peter Seubert,Susanna Suomensaari,Shuwen Wang,Donald A. Walker,Jun Zhao,Lisa McConlogue,Varghese John +26 more
TL;DR: A membrane-bound enzyme activity that cleaves full-length APP at the β-secretase cleavage site is described and found to be the predominant β-cleavage activity in human brain, and it is found that human brain β- secretase is a new membrane- bound aspartic proteinase.
Journal ArticleDOI
Cell-type and Amyloid Precursor Protein-type Specific Inhibition of Aβ Release by Bafilomycin A1, a Selective Inhibitor of Vacuolar ATPases
TL;DR: Intacellular acidic processes are rate-limiting for β-secretase cleavage and Aβ production from SW APP, but not WT APP, in the peripheral 293 cell line, indicating that such acidic processes also play a rate- Limiting role in Aβ release from human central nervous system-derived cells, including HMBC.
Journal ArticleDOI
Retention of the Alzheimer's Amyloid Precursor Fragment C99 in the Endoplasmic Reticulum Prevents Formation of Amyloid β-Peptide
William A. Maltese,Susan E. Wilson,Yizheng Tan,Susanna Suomensaari,Sukanto Sinha,Robin Barbour,Lisa McConlogue +6 more
TL;DR: It is indicated that the ER is not a major intracellular site for γ-secretase cleavage of C99, and the results suggest that presenilins may acquire the characteristics of ιsecretase after leaving the ER, possibly by assembling with other proteins in peripheral membranes.