Amyloid Precursor Protein Dimerisation Reduces Neurite Outgrowth.
Amino Acid Sequence
Amyloid beta-Protein Precursor
/ chemistry
Biomarkers
/ metabolism
Cell Line, Tumor
Cell Shape
/ drug effects
Culture Media, Conditioned
/ pharmacology
Down-Regulation
/ genetics
Endoplasmic Reticulum
/ metabolism
Golgi Apparatus
/ metabolism
HEK293 Cells
Humans
Lentivirus
/ metabolism
MicroRNAs
/ genetics
Models, Biological
Mutation
/ genetics
Neuronal Outgrowth
/ drug effects
Phenotype
Protein Multimerization
Tubulin
/ metabolism
rhoA GTP-Binding Protein
/ metabolism
Amyloid precursor protein
Dimerisation
Function
Neurite
RhoA
microRNA
Journal
Molecular neurobiology
ISSN: 1559-1182
Titre abrégé: Mol Neurobiol
Pays: United States
ID NLM: 8900963
Informations de publication
Date de publication:
Jan 2019
Jan 2019
Historique:
received:
14
12
2017
accepted:
09
04
2018
pubmed:
21
4
2018
medline:
2
4
2019
entrez:
21
4
2018
Statut:
ppublish
Résumé
The amyloid precursor protein (APP) undergoes extensive metabolism, and its transport and proteolytic processing can be modulated by its ability to form a homodimer. We have investigated the functional consequences of stabilised APP dimer expression in cells by studying the engineered dimerisation of the APP
Identifiants
pubmed: 29675574
doi: 10.1007/s12035-018-1070-4
pii: 10.1007/s12035-018-1070-4
doi:
Substances chimiques
Amyloid beta-Protein Precursor
0
Biomarkers
0
Culture Media, Conditioned
0
MIRN34 microRNA, human
0
MicroRNAs
0
Tubulin
0
rhoA GTP-Binding Protein
EC 3.6.5.2
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
13-28Subventions
Organisme : National Health and Medical Research Council
ID : 628946
Organisme : National Health and Medical Research Council
ID : 566575
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