Dr. Oueslati is an Assistant Professor in the Department of Molecular Medicine at Laval University, Director of the Molecular and Cellular Neurodegeneration Laboratory at the CHU Research Center in Quebec City, and a member of the management committee of l’Axe de Neurosciences-CHUL.
Dr. Oueslati obtained his Advanced Studies Diploma (ASD) in Neurobiology (2004), as well as his Doctorate in neuroscience (2008) at the Université de la Méditerranée Aix-Marseille – Faculté des Sciences de Luminy, Marseille-France. He then joined The Brain and Mind Institute at l’École Polytechnique Fédérale de Lausanne (EPFL), Switzerland, for a Postdoctoral fellowship in the group of Dr. Hilal A. Lashuel (2008-2014). After a short experience in the pharmaceutical industry at the ‘EPFL Innovation Parc’, he joined Laval University as Associate Professor (2014), and then as Assistant Professor in June 2015.
The research program developed by Dr. Oueslati and his colleagues aims to understand the involvement of protein misfolding and aggregation in neurodegenerative diseases, including Parkinson’s and Alzheimer’s disease.
More specifically, Dr. Oueslati’s group are developing two lines of research:
- Role of post-translational modifications in the regulation of aggregation and protein toxicity in neurodegenerative diseases. The goal of this line of research is to understand how chemical modifications (e.g. phosphorylation) affect the aggregation and toxicity of certain proteins in the brain, including alpha-synuclein protein in Parkinson’s disease, and tau and amyloid beta proteins in Alzheimer’s disease. The results of this project will allow, on the one hand to identify new markers for the early detection of neurodegenerative diseases, and on the other hand, they will allow to develop new therapeutic targets for these crippling diseases.
- Role of prion propagation in the initiation and progression of neurodegenerative diseases. The goal of this project is to investigate how proteins involved in neurodegenerative diseases are able to spread from one neuron to another, and from one region of the brain to another, like prion disease. This spread of pathogenic proteins appears to play an important role in the initiation and progression of Parkinson’s disease and related diseases. The dissection of the molecular and cellular bases of this pathological propagation will allow to develop new therapeutic approaches that aim at stopping, or at least slowing, the progression of these neurodegenerative diseases.
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Mimicking phosphorylation at serine 87 inhibits the aggregation of human α-synuclein and protects against its toxicity in a rat model of Parkinson's disease
Journal ArticleJ Neurosci, 32 (5), 2012.
Role of post-translational modifications in modulating the structure, function and toxicity of alpha-synuclein: implications for Parkinson's disease pathogenesis and therapies
Journal ArticleProg Brain Res, 183 , 2010.
Phosphorylation at S87 is enhanced in synucleinopathies, inhibits alpha-synuclein oligomerization, and influences synuclein-membrane interactions
Journal ArticleJ Neurosci, 30 (9), 2010.
Phosphorylation of synucleins by members of the Polo-like kinase family
Journal ArticleJ Biol Chem, 285 (4), 2010.
Different functional basal ganglia subcircuits associated with anti-akinetic and dyskinesiogenic effects of antiparkinsonian therapies
Journal ArticleNeurobiol Dis, 36 (1), 2009.
High-frequency stimulation of the subthalamic nucleus potentiates L-DOPA-induced neurochemical changes in the striatum in a rat model of Parkinson's disease
Journal ArticleJ Neurosci, 27 (9), 2007.
Chronic high-frequency stimulation of the subthalamic nucleus and L-DOPA treatment in experimental parkinsonism: effects on motor behaviour and striatal glutamate transmission
Journal ArticleEur J Neurosci, 24 (6), 2006.
Dysfunction of the cortico-basal ganglia-cortical loop in a rat model of early parkinsonism is reversed by metabotropic glutamate receptor 5 antagonism
Journal ArticleEur J Neurosci, 22 (11), 2005.
Active projects
- Deciphering the physiological role of alpha-synuclein aggregation in the central nervous system, from 2023-04-01 to 2028-03-31
- Effects of post-translational modifications on intracellular alpha-synuclein oligomerization, from 2023-02-01 to 2024-01-31
- Implication de l’alpha-synucléine dans la pathogenèse et les traitements de la maladie de Parkinson, from 2020-07-01 to 2024-06-30
- Unveiling the role of alpha-synuclein clustering and Lewy body formation in Parkinson’s disease pathogenesis using an optogenetic-mediated protein aggregation system, from 2019-04-01 to 2024-03-31
- Use of optogenetic-TDP43 to shed light on the dying-back hypothesis in ALS, from 2022-04-01 to 2023-09-30
Recently finished projects
- Investigation of the synergistic role of PLK2 and alpha-synuclein in the regulation of neuronal homeostasis and functions., from 2016-04-01 to 2023-03-31