Výsledky vyhledávání - "Enrico Ghersi"

The intracellular localization of amyloid β protein precursor (AβPP) intracellular domain associated protein-1 (AIDA-1) is regulated by AβPP and alternative splicing

Autor: Mona Abdallah, Peter Lopez, Pasquale Vito, Luciano D'Adamio, Enrico Ghersi

Publikováno v: Journal of Alzheimer's Disease. 6:67-78

The Amyloid-beta Protein Precursor (AbetaPP) is a widely expressed transmembrane protein that is extensively processed in intracellular vesicular compartments and on the cell membrane. As a result of two sequential proteolytic cleavages, AbetaPP rele

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e908a7463582c70d5199011e0024e4a7
https://doi.org/10.3233/jad-2004-6108

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Processing of β-Amyloid Precursor-like Protein-1 and -2 by γ-Secretase Regulates Transcription

Autor: Meir H. Scheinfeld, Karen Laky, Enrico Ghersi, B. J. Fowlkes, Luciano D'Adamio

Publikováno v: Journal of Biological Chemistry. 277:44195-44201

The familial Alzheimer's disease gene product beta-amyloid (Abeta) precursor protein (APP) is processed by the beta- and gamma-secretases to produce Abeta as well as AID (APP Intracellular Domain) which is derived from the extreme carboxyl terminus o

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::94ca2a5e00c70e521fd1ae4009e0ee73
https://doi.org/10.1074/jbc.m208110200

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Evidence for a role of the nerve growth factor receptor TrkA in tyrosine phosphorylation and processing of β-APP

Autor: Nicola Zambrano, Tommaso Russo, Cristina Contursi, Roberta Roncarati, Philip E. Tarr, Luciano D'Adamio, Enrico Ghersi, Cristiana Noviello, Meir H. Scheinfeld

Publikováno v: Biochemical and Biophysical Research Communications. 295:324-329

The cytoplasmic tail of the β-amyloid precursor protein (APP) contains a Y 682 ENPTY 687 sequence through which APP associates with phosphotyrosine binding (PTB) domain containing proteins in a tyrosine phosphorylation-independent manner. We have re

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8527d43dca428a514e187c46bfc46093
https://doi.org/10.1016/s0006-291x(02)00678-2

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Ligand binding and calcium influx induce distinct ectodomain/gamma-secretase-processing pathways of EphB2 receptor

Autor: Thomas Wisniewski, Rong Wang, Claudia Litterst, Enrico Ghersi, Andreas Ludwig, Junichi Shioi, Nikolaos K. Robakis, Anastasios Georgakopoulos

Publikováno v: The Journal of biological chemistry. 282(22)

Binding of EphB receptors to ephrinB ligands on the surface of adjacent cells initiates signaling cascades that regulate angiogenesis, axonal guidance, and neuronal plasticity. These functions require processing of EphB receptors and removal of EphB-

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::40304526ad2b1441d17b22f7a46b95d3
https://pubmed.ncbi.nlm.nih.gov/17428795

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O3–03–02: PS1/γ–secretase regulate the EphB–induced Src signaling

Autor: Chi-jie Xu, Nikolaos K. Robakis, Enrico Ghersi, Claudia Litterst, Anastasios Georgakopoulos, Geo Serban, Lia Baki

Publikováno v: Alzheimer's & Dementia. 2

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::1274e19a1720d7f623bd5b1f025ebbfc
https://doi.org/10.1016/j.jalz.2006.05.206

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Metalloproteinase/Presenilin1 processing of ephrinB regulates EphB-induced Src phosphorylation and signaling

Autor: Anastasios Georgakopoulos, Enrico Ghersi, Chi-jie Xu, Claudia Litterst, Nikolaos K. Robakis, Lia Baki, Geo Serban

Publikováno v: The EMBO journal. 25(6)

Bidirectional signaling triggered by interacting ephrinB receptors (EphB) and ephrinB ligands is crucial for development and function of the vascular and nervous systems. A signaling cascade triggered by this interaction involves activation of Src ki

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::249409b6c3c99fe7a2e6d3516df60231
https://pubmed.ncbi.nlm.nih.gov/16511561

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Amyloid-beta protein precursor (AbetaPP) intracellular domain-associated protein-1 proteins bind to AbetaPP and modulate its processing in an isoform-specific manner

Autor: Luciano D'Adamio, Cristiana Noviello, Enrico Ghersi

Publikováno v: The Journal of biological chemistry. 279(47)

The amyloid-beta protein precursor (AbetaPP) is a type I transmembrane molecule that undergoes several finely regulated cleavage events. The physiopathological relevance of AbetaPP derives from the fact that its aberrant processing strongly correlate

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f99968df323fc07e0a6c98e4088dd9a0
https://pubmed.ncbi.nlm.nih.gov/15347684

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Amyloid beta protein precursor is phosphorylated by JNK-1 independent of, yet facilitated by, JNK-interacting protein (JIP)-1

Autor: Luciano D'Adamio, Meir H. Scheinfeld, Peter Davies, Enrico Ghersi

Publikováno v: The Journal of biological chemistry. 278(43)

Alzheimer's disease (AD) is genetically linked to the processing of amyloid beta protein precursor (AbetaPP). Aside from being the precursor of the amyloid beta (Abeta) found in plaques in the brains of patients with AD, little is known regarding the

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8df4cc55ac7922d067f92c66bb34638e
https://pubmed.ncbi.nlm.nih.gov/12917434

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