Alpha-synuclein suppresses mitochondrial protease ClpP to trigger mitochondrial oxidative damage and neurotoxicity.
Springer Berlin Heidelberg; https://doi.org/10.1007/s00401-019-01993-2.
Protein Damage in Aging and Age-Related Diseases.
Open Biology; https://doi.org/10.1098/rsob.180249.
Proline- and Arginine-Rich Peptides as Flexible Allosteric Modulators of Human Proteasome Activity.
Journal of Medicinal Chemistry; DOI: 10.1021/acs.jmedchem.8b01025.
Novel Mannitol-Based Small Molecules for Inhibiting Aggregation of α-Synuclein Amyloids in Parkinson's Disease.
Frontiers; https://doi.org/10.3389/fmolb.2019.00016.
Electrochemical Detection of Interaction between Copper(II) and Peptides Related to Pathological α-Synuclein Mutants.
Anal Chem.; DOI: 10.1021/acs.analchem.8b03612.
Characterization of pathology-inducing α-synuclein species from human diseased brain tissue.
bioRxiv; doi: https://doi.org/10.1101/588335.
Interferon-γ Potentiates α-Synuclein-induced Neurotoxicity Linked to Toll-like Receptors 2 and 3 and Tumor Necrosis Factor-α in Murine Astrocytes..
Mol Neurobiol.; DOI: 10.1007/s12035-019-1567-5.
Identification of a New α-Synuclein Aggregation Inhibitor via Mass Spectrometry Based Screening.
ACS Chem. Neurosci.; https://doi.org/10.1021/acschemneuro.9b00092.
Reduction of Immunoreactivity Against the C-Terminal Region of the Intracellular α-Synuclein by Exogenous α-Synuclein Aggregates: Possibility of Conformational Changes..
Journal of Parkinson’s Disease; doi: 10.3233/JPD-160835..
Effect of naturally occurring α-synuclein-antibodies on toxic α-synuclein-fragments.
Neuroscience Letters; https://doi.org/10.1016/j.neulet.2019.04.004.