Zobrazeno 1 - 10
of 58
pro vyhledávání: '"Giuseppina Tesco"'
Autor:
WonHee Kim, Liang Ma, Selene Lomoio, Rachel Willen, Sylvia Lombardo, Jinghui Dong, Philip G. Haydon, Giuseppina Tesco
Publikováno v:
Molecular Neurodegeneration, Vol 13, Iss 1, Pp 1-22 (2018)
Abstract Background β-site amyloid precursor protein cleaving enzyme 1 (BACE1) is the rate-limiting enzyme in the production of amyloid beta (Aβ), the toxic peptide that accumulates in the brains of Alzheimer’s disease (AD) patients. Our previous
Externí odkaz:
https://doaj.org/article/7258624d78f2453a9df25d037112256f
Autor:
Kendall R Walker, Amit Modgil, David Albrecht, Selene Lomoio, Philip G Haydon, Stephen J Moss, Giuseppina Tesco
Publikováno v:
PLoS ONE, Vol 11, Iss 5, p e0155799 (2016)
Golgi-localized γ-ear-containing ARF binding protein 3 (GGA3) is a monomeric clathrin adaptor that has been shown to regulate the trafficking of the Beta-site APP-cleaving enzyme (BACE1), which is required for production of the Alzheimer's disease (
Externí odkaz:
https://doaj.org/article/f97a36937c584f06ae853a52e5cb0fbf
Publikováno v:
PLoS ONE, Vol 7, Iss 1, p e29940 (2012)
Memory loss is one of the hallmark symptoms of Alzheimer's disease (AD). It has been proposed that soluble amyloid-beta (Abeta) oligomers acutely impair neuronal function and thereby memory. We here report that natural Abeta oligomers acutely impair
Externí odkaz:
https://doaj.org/article/01db4b76c0334c5684ae5c0262f982cb
Autor:
Selene Lomoio, Ravi S. Pandey, Nicolas Rouleau, Beatrice Menicacci, WonHee Kim, William L. Cantley, Philip G. Haydon, David A. Bennett, Tracy L. Young-Pearse, Gregory W. Carter, David L. Kaplan, Giuseppina Tesco
BackgroundCurrent models to study Alzheimer’s disease (AD) include cell cultures and animal models. Human diseases, however, are often poorly reproduced in animal models. Developing techniques to differentiate human brain cells from induced pluripo
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::0df38cc1e2d0dcc039217844e20f208d
https://doi.org/10.1101/2022.07.21.501004
https://doi.org/10.1101/2022.07.21.501004
Autor:
William L. Cantley, David L. Kaplan, Giuseppina Tesco, Emily Peirent, Min D. Tang-Schomer, Chuang Du, Dominic Kleinknecht, Thomas DePalma, Selene Lomoio, Martin Hunter
Publikováno v:
ACS Biomater Sci Eng
Three-dimensional in vitro cell culture models, particularly for the central nervous system, allow for the exploration of mechanisms of organ development, cellular interactions, and disease progression within defined environments. Here we describe th
Autor:
WonHee Kim, Selene Lomoio, Edward K. Robinson, Giuseppina Tesco, Matthew E. Kennedy, Kevin Z. Ho, Rudolph E. Tanzi, Rachel Willen, Dmitry Prokopenko
Publikováno v:
Sci Transl Med
Axonal dystrophy, indicative of perturbed axonal transport, occurs early during Alzheimer’s disease (AD) pathogenesis. Little is known about the mechanisms underlying this initial sign of the pathology. This study proves that Golgi-localized γ-ear
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3d52c53f890587c8ff4a5f7839cbee36
https://europepmc.org/articles/PMC8612295/
https://europepmc.org/articles/PMC8612295/
Autor:
WonHee Kim, Sylvia Lombardo, Giuseppina Tesco, Matthew E. Kennedy, Andrew J. Tarr, Thomas W. Rosahl, Philip G. Haydon, Tingyi Cao, Martina Chiacchiaretta, Griffin Sigal, Weiming Xia
Publikováno v:
Scientific Reports, Vol 9, Iss 1, Pp 1-14 (2019)
Scientific Reports
Scientific Reports
BACE1 is the first enzyme involved in APP processing, thus it is a strong therapeutic target candidate for Alzheimer’s disease. The observation of deleterious phenotypes in BACE1 Knock-out (KO) mouse models (germline and conditional) raised some co
Publikováno v:
The Journal of Biological Chemistry
Neural cell adhesion molecules 1 (NCAM1) and 2 (NCAM2) belong to the cell adhesion molecules of the immunoglobulin superfamily and have been shown to regulate formation, maturation, and maintenance of synapses. NCAM1 and NCAM2 undergo proteolysis, bu
Autor:
Giuseppina Tesco, Kerstin Voelkl, Sandra Karch, Fang Zheng, Christian Alzheimer, Carla D’Avanzo, Selene Lomoio, Doo Yeon Kim, Benedikt Zott, Michele Constanze Kyncl, Tobias Huth, Stephanie Hartmann
The β-secretase β-site APP-cleaving enzyme 1 (BACE1) is deemed a major culprit in Alzheimer's disease, but accumulating evidence indicates that there is more to the enzyme than driving the amyloidogenic processing of the amyloid precursor protein.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1c4521f2d6197551e7d556fb55d838ae
https://europepmc.org/articles/PMC5895038/
https://europepmc.org/articles/PMC5895038/
Autor:
Selene Lomoio, Sylvia Lombardo, WonHee Kim, Jinghui Dong, Giuseppina Tesco, Rachel Willen, Liang Ma, Philip G. Haydon
Publikováno v:
Molecular Neurodegeneration
Molecular Neurodegeneration, Vol 13, Iss 1, Pp 1-22 (2018)
Molecular Neurodegeneration, Vol 13, Iss 1, Pp 1-22 (2018)
Background β-site amyloid precursor protein cleaving enzyme 1 (BACE1) is the rate-limiting enzyme in the production of amyloid beta (Aβ), the toxic peptide that accumulates in the brains of Alzheimer’s disease (AD) patients. Our previous studies