A cell-based high-throughput screening method to directly examine transthyretin amyloid fibril formation at neutral pH.
Amyloid
/ drug effects
Amyloid Neuropathies, Familial
/ metabolism
Apomorphine
/ pharmacology
Cells, Cultured
Drug Repositioning
High-Throughput Screening Assays
/ methods
Humans
Hydrogen-Ion Concentration
Inflammation
/ genetics
Neuroglia
/ metabolism
Neurons
/ metabolism
Prealbumin
/ chemistry
Protein Conformation
Proteolysis
Pyrvinium Compounds
/ pharmacology
Trypsin
/ metabolism
amyloid
amyloid disrupters
apomorphine hydrochloride
drug discovery
drug screening
protein aggregation
protein conformation
pyrvinium pamoate
transthyretin (TTR)
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:
19 07 2019
19 07 2019
Historique:
received:
01
02
2019
revised:
31
05
2019
pubmed:
7
6
2019
medline:
3
4
2020
entrez:
7
6
2019
Statut:
ppublish
Résumé
Transthyretin (TTR) is a major amyloidogenic protein associated with hereditary (ATTRm) and nonhereditary (ATTRwt) intractable systemic transthyretin amyloidosis. The pathological mechanisms of ATTR-associated amyloid fibril formation are incompletely understood, and there is a need for identifying compounds that target ATTR. C-terminal TTR fragments are often present in amyloid-laden tissues of most patients with ATTR amyloidosis, and on the basis of
Identifiants
pubmed: 31167790
pii: S0021-9258(20)30252-0
doi: 10.1074/jbc.RA119.007851
pmc: PMC6643022
doi:
Substances chimiques
Amyloid
0
Prealbumin
0
Pyrvinium Compounds
0
pyrvinium
6B9991FLU3
Trypsin
EC 3.4.21.4
Apomorphine
N21FAR7B4S
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
11259-11275Informations de copyright
© 2019 Ueda et al.
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