Presenilin-2 and Calcium Handling: Molecules, Organelles, Cells and Brain Networks.


Journal

Cells
ISSN: 2073-4409
Titre abrégé: Cells
Pays: Switzerland
ID NLM: 101600052

Informations de publication

Date de publication:
25 09 2020
Historique:
received: 31 08 2020
revised: 15 09 2020
accepted: 18 09 2020
entrez: 30 9 2020
pubmed: 1 10 2020
medline: 22 6 2021
Statut: epublish

Résumé

Presenilin-2 (PS2) is one of the three proteins that are dominantly mutated in familial Alzheimer's disease (FAD). It forms the catalytic core of the γ-secretase complex-a function shared with its homolog presenilin-1 (PS1)-the enzyme ultimately responsible of amyloid-β (Aβ) formation. Besides its enzymatic activity, PS2 is a multifunctional protein, being specifically involved, independently of γ-secretase activity, in the modulation of several cellular processes, such as Ca

Identifiants

pubmed: 32992716
pii: cells9102166
doi: 10.3390/cells9102166
pmc: PMC7601421
pii:
doi:

Substances chimiques

Multiprotein Complexes 0
Mutant Proteins 0
Presenilin-1 0
Presenilin-2 0
Flavin-Adenine Dinucleotide 146-14-5
Amyloid Precursor Protein Secretases EC 3.4.-
Calcium SY7Q814VUP

Types de publication

Journal Article Research Support, Non-U.S. Gov't Review

Langues

eng

Sous-ensembles de citation

IM

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Auteurs

Paola Pizzo (P)

Department of Biomedical Sciences, University of Padua, Via U. Bassi 58/B, 35131 Padua, Italy.
Neuroscience Institute, Italian National Research Council (CNR), Via U. Bassi 58/B, 35131 Padua, Italy.

Emy Basso (E)

Department of Biomedical Sciences, University of Padua, Via U. Bassi 58/B, 35131 Padua, Italy.
Neuroscience Institute, Italian National Research Council (CNR), Via U. Bassi 58/B, 35131 Padua, Italy.

Riccardo Filadi (R)

Department of Biomedical Sciences, University of Padua, Via U. Bassi 58/B, 35131 Padua, Italy.
Neuroscience Institute, Italian National Research Council (CNR), Via U. Bassi 58/B, 35131 Padua, Italy.

Elisa Greotti (E)

Department of Biomedical Sciences, University of Padua, Via U. Bassi 58/B, 35131 Padua, Italy.
Neuroscience Institute, Italian National Research Council (CNR), Via U. Bassi 58/B, 35131 Padua, Italy.

Alessandro Leparulo (A)

Department of Biomedical Sciences, University of Padua, Via U. Bassi 58/B, 35131 Padua, Italy.

Diana Pendin (D)

Department of Biomedical Sciences, University of Padua, Via U. Bassi 58/B, 35131 Padua, Italy.
Neuroscience Institute, Italian National Research Council (CNR), Via U. Bassi 58/B, 35131 Padua, Italy.

Nelly Redolfi (N)

Department of Biomedical Sciences, University of Padua, Via U. Bassi 58/B, 35131 Padua, Italy.

Michela Rossini (M)

Department of Biomedical Sciences, University of Padua, Via U. Bassi 58/B, 35131 Padua, Italy.

Nicola Vajente (N)

Department of Biomedical Sciences, University of Padua, Via U. Bassi 58/B, 35131 Padua, Italy.
Neuroscience Institute, Italian National Research Council (CNR), Via U. Bassi 58/B, 35131 Padua, Italy.

Tullio Pozzan (T)

Department of Biomedical Sciences, University of Padua, Via U. Bassi 58/B, 35131 Padua, Italy.
Neuroscience Institute, Italian National Research Council (CNR), Via U. Bassi 58/B, 35131 Padua, Italy.
Venetian Institute of Molecular Medicine (VIMM), Via G. Orus 2B, 35131 Padua, Italy.

Cristina Fasolato (C)

Department of Biomedical Sciences, University of Padua, Via U. Bassi 58/B, 35131 Padua, Italy.

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Classifications MeSH