Site-specific glycation of Aβ1-42 affects fibril formation and is neurotoxic.
Alzheimer Disease
/ metabolism
Amyloid
/ metabolism
Amyloid beta-Peptides
/ chemical synthesis
Apoptosis
/ drug effects
Cell Line, Tumor
Glycosylation
Humans
Lysine
/ analogs & derivatives
Membrane Potential, Mitochondrial
/ drug effects
Mitochondria
/ metabolism
Peptide Fragments
/ chemical synthesis
Protein Aggregates
Protein Conformation, beta-Strand
Protein Stability
Singlet Oxygen
/ metabolism
Alzheimer disease
N-ϵ-(carboxyethyl)lysine (CEL)
advanced glycated end product (AGE)
amyloid-β (Aβ)
fibril
glycation
mitochondria
neurodegeneration
protein aggregation
Journal
The Journal of biological chemistry
ISSN: 1083-351X
Titre abrégé: J Biol Chem
Pays: United States
ID NLM: 2985121R
Informations de publication
Date de publication:
31 05 2019
31 05 2019
Historique:
received:
28
11
2018
revised:
12
04
2019
pubmed:
19
4
2019
medline:
19
2
2020
entrez:
19
4
2019
Statut:
ppublish
Résumé
Aβ1-42 is involved in Alzheimer's disease (AD) pathogenesis and is prone to glycation, an irreversible process where proteins accumulate advanced glycated end products (AGEs).
Identifiants
pubmed: 30996005
pii: S0021-9258(20)36402-4
doi: 10.1074/jbc.RA118.006846
pmc: PMC6552435
doi:
Substances chimiques
Amyloid
0
Amyloid beta-Peptides
0
N(6)-carboxyethyllysine
0
Peptide Fragments
0
Protein Aggregates
0
amyloid beta-protein (1-42)
0
Singlet Oxygen
17778-80-2
Lysine
K3Z4F929H6
Banques de données
PDB
['2BEG']
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
8806-8818Informations de copyright
© 2019 Ng et al.
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