Zobrazeno 1 - 10
of 17
pro vyhledávání: '"Selene, Lomoio"'
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:
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:
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
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
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4e7e815ae9a6664d5ce2658d42a63374
https://pubmed.ncbi.nlm.nih.gov/33304995
https://pubmed.ncbi.nlm.nih.gov/33304995
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/
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
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6fa3d63f1d63705a78ee96a8ece6f523
https://doi.org/10.1016/j.jbc.2021.100372
https://doi.org/10.1016/j.jbc.2021.100372
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
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::27429ef1be7c3dfb6e97491522e5aa46
http://europepmc.org/articles/PMC5796504
http://europepmc.org/articles/PMC5796504
Autor:
Irene López-González, Selene Lomoio, Margarita Carmona, Jesús Moreno, Aurora Pujol, Isidro Ferrer, Mario Díaz, Laura Joda, Ester Aso, Reinald Pamplona, Virginia Martín, Núria Fernández-Yagüe, Salvador Juvés, Manuel Portero-Otin
Publikováno v:
Brain Pathology. 22:636-653
Double-transgenic amyloid precursor protein/presenilin 1 (APP/PS1) mice express a chimeric mouse/human APP bearing the Swedish mutation (Mo/HuAPP695swe) and a mutant human PS1-dE9 both causative of familial Alzheimer's disease (FAD). Transgenic mice
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::0bd5b5c8d543e6023cac77ce107dd36e
https://doi.org/10.1111/j.1750-3639.2011.00560.x
https://doi.org/10.1111/j.1750-3639.2011.00560.x
Publikováno v:
Experimental Neurology. 232:114-118
In the cerebellum of adult-aging Ts65Dn mice, a murine model of Down syndrome, Purkinje cells undergo degeneration. Searching for the cause of Purkinje cell degeneration, we have studied the ubiquitin–proteasome system (UPS) in the cerebellum of ag
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7d274559030a8ac1440aaba1dfff61d4
https://doi.org/10.1016/j.expneurol.2011.08.009
https://doi.org/10.1016/j.expneurol.2011.08.009