Possible mechanisms of polyphosphate-induced amyloid fibril formation of β
amorphous aggregation
amyloid fibrillation
dialysis-related amyloidosis
polyphosphates
supersaturation
Journal
Proceedings of the National Academy of Sciences of the United States of America
ISSN: 1091-6490
Titre abrégé: Proc Natl Acad Sci U S A
Pays: United States
ID NLM: 7505876
Informations de publication
Date de publication:
25 06 2019
25 06 2019
Historique:
pubmed:
12
6
2019
medline:
27
3
2020
entrez:
12
6
2019
Statut:
ppublish
Résumé
Polyphosphate (polyP), which is found in various microorganisms and human cells, is an anionic biopolymer consisting of inorganic phosphates linked by high-energy phosphate bonds. Previous studies revealed that polyPs strongly promoted the amyloid formation of several amyloidogenic proteins; however, the mechanism of polyP-induced amyloid formation remains unclear. In the present study using β
Identifiants
pubmed: 31182591
pii: 1819813116
doi: 10.1073/pnas.1819813116
pmc: PMC6600944
doi:
Substances chimiques
Amyloid
0
Polyphosphates
0
beta 2-Microglobulin
0
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
12833-12838Déclaration de conflit d'intérêts
The authors declare no conflict of interest.
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