Linking alpha-synuclein phosphorylation to reactive oxygen species formation and mitochondrial dysfunction in SH-SY5Y cells

Author:

Perfeito Rita,Lázaro Diana F.,Outeiro Tiago F.,Rego A. Cristina

Funder

FCT

COMPETE—Programa Operacional Factores de Competitividade”, QREN

European Union

EMBO

DFG Center for Nanoscale Microscopy

Molecular Physiology of the Brain

Publisher

Elsevier BV

Subject

Cell Biology,Cellular and Molecular Neuroscience,Molecular Biology

Reference56 articles.

1. Phosphorylation of Ser-129 is the dominant pathological modification of alpha-synuclein in familial and sporadic Lewy body disease;Anderson;J. Biol. Chem.,2006

2. Alpha-synuclein p.H50Q, a novel pathogenic mutation for Parkinson's disease;Appel-Cresswell;Mov. Disord.,2013

3. Phosphorylation does not prompt, nor prevent, the formation of alpha-synuclein toxic species in a rat model of Parkinson's disease;Azeredo da;Hum. Mol. Genet.,2009

4. PLK2 modulates α-synuclein aggregation in yeast and mammalian cells;Basso;Mol. Neurobiol.,2013

5. Disturbance of iron metabolism as a contributing factor to SN hyperechogenicity in Parkinson's disease: implications for idiopathic and monogenetic forms;Berg;Neurochem. Res.,2007

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