S
Suzanne Y. Guénette
Researcher at Harvard University
Publications - 27
Citations - 5769
Suzanne Y. Guénette is an academic researcher from Harvard University. The author has contributed to research in topics: Amyloid precursor protein & P3 peptide. The author has an hindex of 19, co-authored 27 publications receiving 5538 citations.
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Journal ArticleDOI
Candidate gene for the chromosome 1 familial Alzheimer's disease locus
Ephrat Levy-Lahad,Wilma Wasco,Parvoneh Poorkaj,Donna M. Romano,Junko Oshima,Warren H. Pettingell,Chang En Yu,P. D. Jondro,Stephen D. Schmidt,Kai Wang,Annette C. Crowley,Ying-Hui Fu,Suzanne Y. Guénette,David J. Galas,Ellen Nemens,Ellen M. Wijsman,Thomas D. Bird,Gerard D. Schellenberg,Rudolph E. Tanzi +18 more
TL;DR: The presence of missense mutations in AD subjects in two highly similar genes strongly supports the hypothesis that mutations in both are pathogenic.
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Insulin-degrading enzyme regulates the levels of insulin, amyloid β-protein, and the β-amyloid precursor protein intracellular domain in vivo
Wesley Farris,Stefan Mansourian,Yang Chang,Loren Lindsley,Elizabeth A. Eckman,Matthew P. Frosch,Christopher B. Eckman,Rudolph E. Tanzi,Dennis J. Selkoe,Suzanne Y. Guénette +9 more
TL;DR: In vivo findings suggest that IDE hypofunction may underlie or contribute to some forms of AD and DM2 and provide a mechanism for the recently recognized association among hyperinsulinemia, diabetes, and AD.
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The Intracellular Domain of the β-Amyloid Precursor Protein Is Stabilized by Fe65 and Translocates to the Nucleus in a Notch-like Manner
TL;DR: The results demonstrate that the cytoplasmic domain of APP is a highly labile fragment that is stabilized by forming complexes with Fe65 and can then enter the nucleus in neurons and non-neural cells and strongly support the hypothesis that APP signals in the nucleusIn a manner analogous to the function of Notch.
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The gene defects responsible for familial Alzheimer's disease.
TL;DR: While the exact mechanisms by which the known FAD gene changes lead to the onset of AD remain unclear, the available data indicate that novel therapies aimed at curbing the generation, aggregation, and deposition of A beta would appear to carry the greatest potential for the effective treatment of this formidable disease.
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Association of a novel human FE65-like protein with the cytoplasmic domain of the beta-amyloid precursor protein
TL;DR: The existence of a human FE65 gene family and evidence supporting specific interactions between members of the beta PP and FE65 protein families are reported and sequence analysis of the FE65 human gene family reveals the presence of two phosphotyrosine interaction (PI) domains.