Cargando…
Elevated temperatures accelerate the formation of toxic amyloid fibrils of hen egg‐white lysozyme
The formation of amyloid fibrils is critical for neurodegenerative diseases. Some physiochemical conditions can promote the conversion of proteins from soluble globular shapes into insoluble well‐organized amyloid fibrils. The aim of this study was to investigate the effect of temperatures on amyloi...
Autores principales: | Feng, Zili, Li, Ying, Bai, Yu |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
John Wiley and Sons Inc.
2021
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8464291/ https://www.ncbi.nlm.nih.gov/pubmed/33978313 http://dx.doi.org/10.1002/vms3.522 |
Ejemplares similares
-
Unraveling the novel effects of aroma from small molecules in preventing hen egg white lysozyme amyloid fibril formation
por: Seraj, Zahra, et al.
Publicado: (2018) -
Manganese Ion-Induced
Amyloid Fibrillation Kinetics
of Hen Egg White-Lysozyme in Thermal and Acidic Conditions
por: Chen, Xiaodong, et al.
Publicado: (2023) -
Prolonged Glycation of Hen Egg White Lysozyme Generates Non Amyloidal Structures
por: Ghosh, Sudeshna, et al.
Publicado: (2013) -
Tannic Acid-Induced Surface-Catalyzed Secondary Nucleation during the Amyloid Fibrillation of Hen Egg-White Lysozyme
por: Tian, Jing, et al.
Publicado: (2018) -
Amyloid-Based Injectable Hydrogel Derived from Hydrolyzed
Hen Egg White Lysozyme
por: Yang, Lujuan, et al.
Publicado: (2019)