Zobrazeno 1 - 10
of 34
pro vyhledávání: '"Suzanne Y. Guénette"'
Publikováno v:
Frontiers in Molecular Neuroscience
Understanding the molecular mechanisms underlying amyloid precursor protein family (APP/APP-like proteins, APLP) function in the nervous system can be achieved by studying the APP/APLP interactome. In this review article, we focused on intracellular
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::72cb45c5ced7ad4219a37ccc590c4f09
https://doi.org/10.3389/fnmol.2017.00087
https://doi.org/10.3389/fnmol.2017.00087
Autor:
Paul Strecker, Marco B. Rust, Suzanne Y. Guénette, Tabea A. Mundinger, Christina Mehrfeld, Elisa G. Krächan, Martin Korte, Andreas Görlich, Stefan Kins, Joachim Herz, Susann Ludewig
Publikováno v:
Scientific Reports
The FE65 adaptor proteins (FE65, FE65L1 and FE65L2) bind proteins that function in diverse cellular pathways and are essential for specific biological processes. Mice lacking both FE65 and FE65L1 exhibit ectopic neuronal positioning in the cortex and
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2d205a567e8bdad67335df6a2cea99f6
https://pubmed.ncbi.nlm.nih.gov/27734846
https://pubmed.ncbi.nlm.nih.gov/27734846
Publikováno v:
Journal of Neurochemistry. 119:377-388
Amyloid precursor protein (APP) family members and their proteolytic products are implicated in normal nervous system function and Alzheimer's disease pathogenesis. APP processing and Aβ secretion are regulated by neuronal activity. Various data sug
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::098c0c1e700b0531be6865b00f820420
https://doi.org/10.1111/j.1471-4159.2011.07419.x
https://doi.org/10.1111/j.1471-4159.2011.07419.x
Autor:
Henri J. Huttunen, Doo Yeon Kim, Cory Barren, Camilla Peach, Suzanne Y. Guénette, Weiming Xia, Rudolph E. Tanzi, Christopher Greco, Dora M. Kovacs
Publikováno v:
Journal of Biological Chemistry. 282:28285-28295
Alzheimer disease-associated beta-amyloid peptide is generated from its precursor protein APP. By using the yeast two-hybrid assay, here we identified HtrA2/Omi, a stress-responsive chaperone-protease as a protein binding to the N-terminal cysteineri
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::855954449e06848654017b42b2fc98ca
https://doi.org/10.1074/jbc.m702951200
https://doi.org/10.1074/jbc.m702951200
Autor:
Suzanne Y. Guénette, Zhanyan Fu, Stefano Vicini, Hyang-Sook Hoe, G. William Rebeck, Laura Ann Magill
Publikováno v:
Journal of Biological Chemistry. 281:24521-24530
The adaptor protein FE65 interacts with the beta-amyloid precursor protein (APP) via its C-terminal phosphotyrosine binding (PTB) domain and affects APP processing and Abeta production. Our previous data demonstrate that the apoE receptor ApoEr2 co-p
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b8f4a5bbff4b528d6a7aa7e6cccfcde0
https://doi.org/10.1074/jbc.m600728200
https://doi.org/10.1074/jbc.m600728200
Autor:
Suzanne Y. Guénette, Yang Chang, Joachim Herz, Thomas Hiesberger, Robert E. Hammer, James A. Richardson, Elizabeth A. Eckman, Christopher B. Eckman
Publikováno v:
The EMBO Journal. 25:420-431
Targeted deletion of two members of the FE65 family of adaptor proteins, FE65 and FE65L1, results in cortical dysplasia. Heterotopias resembling those found in cobblestone lissencephalies in which neuroepithelial cells migrate into superficial layers
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::460585ae22e444220ab3659b9d0833ae
https://doi.org/10.1038/sj.emboj.7600926
https://doi.org/10.1038/sj.emboj.7600926
Autor:
Elizabeth A. Eckman, Rudolph E. Tanzi, Yang Chang, Giuseppina Tesco, William J. Jeong, Suzanne Y. Guénette, Loren Lindsley, Christopher B. Eckman
Publikováno v:
Journal of Biological Chemistry. 278:51100-51107
Members of the FE65 family of adaptor proteins, FE65, FE65L1, and FE65L2, bind the C-terminal region of the amyloid precursor protein (APP). Overexpression of FE65 and FE65L1 was previously reported to increase the levels of alpha-secretase-derived A
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4bdf53f334191912b88bf74d522630fc
https://doi.org/10.1074/jbc.m309561200
https://doi.org/10.1074/jbc.m309561200
Autor:
Suzanne Y. Guénette
Publikováno v:
NeuroMolecular Medicine. 4:147-160
Mutations that result in an increased generation of amyloid beta peptide (Abeta) account for less than 5% of Alzheimer's disease (AD). Data suggesting that late onset AD risk factors play a role in Abeta turnover in the brain have shifted some of the
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4534997a23f927e8af54daa1af82d78a
https://doi.org/10.1385/nmm:4:3:147
https://doi.org/10.1385/nmm:4:3:147
Publikováno v:
Journal of Neurochemistry. 82:755-762
The FE65 adaptor protein family was identified in two-hybrid screens as proteins that bind the cytoplasmic domain of the amyloid precursor protein (APP). Studies have shown that FE65 binding to APP modulates APP processing. Increased levels of alpha-
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::47e2677012f6f6905226565be4489cc6
https://doi.org/10.1046/j.1471-4159.2002.01009.x
https://doi.org/10.1046/j.1471-4159.2002.01009.x
Autor:
Suzanne Y. Guénette, Anja Capell, Rudolph E. Tanzi, Jing Chen, Amber Ferland, Christian Haass
Publikováno v:
Journal of Neurochemistry. 73:985-993
The amyloid precursor protein (APP) is processed in the secretory and endocytic pathways, where both the neuroprotective alpha-secretase-derived secreted APP (APPs alpha) and the Alzheimer's disease-associated beta-amyloid peptide are generated. All
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::826c87e26c29905a14fee72bdadf1de7
https://doi.org/10.1046/j.1471-4159.1999.0730985.x
https://doi.org/10.1046/j.1471-4159.1999.0730985.x