Cargando…
Partially oxidized DJ-1 inhibits α-synuclein nucleation and remodels mature α-synuclein fibrils in vitro
DJ-1 is a deglycase enzyme which exhibits a redox-sensitive chaperone-like activity. The partially oxidized state of DJ-1 is active in inhibiting the aggregation of α-synuclein, a key protein associated with Parkinson’s disease. The underlying molecular mechanism behind α-synuclein aggregation inhib...
Autores principales: | Kumar, Roshan, Kumar, Sanjay, Hanpude, Pranita, Singh, Abhishek Kumar, Johari, Tanu, Majumder, Sushanta, Maiti, Tushar Kanti |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Nature Publishing Group UK
2019
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6821844/ https://www.ncbi.nlm.nih.gov/pubmed/31701024 http://dx.doi.org/10.1038/s42003-019-0644-7 |
Ejemplares similares
-
S-nitrosylation of UCHL1 induces its structural instability and promotes α-synuclein aggregation
por: Kumar, Roshan, et al.
Publicado: (2017) -
DJ-1 Acts as a Scavenger of α-Synuclein Oligomers and Restores Monomeric Glycated α-Synuclein
por: Atieh, Tamr B., et al.
Publicado: (2021) -
Ubiquitin recognition of BAP1: understanding its enzymatic function
por: Hanpude, Pranita, et al.
Publicado: (2017) -
Cancer associated missense mutations in BAP1 catalytic domain induce amyloidogenic aggregation: A new insight in enzymatic inactivation
por: Bhattacharya, Sushmita, et al.
Publicado: (2015) -
α-Synuclein and DJ-1 as Potential Biological Fluid Biomarkers for Parkinson’s Disease
por: Waragai, Masaaki, et al.
Publicado: (2010)