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.
CHUL
2705, boulevard Laurier
T2-05
Québec, Québec
Canada G1V 4G2
28 entries « 2 of 3 »

Oueslati A

Implication of Alpha-Synuclein Phosphorylation at S129 in Synucleinopathies: What Have We Learned in the Last Decade?

Journal Article

J Parkinsons Dis, 6 (1), 2016.

Abstract | Links:

Fares MB, Maco B, Oueslati A, Rockenstein E, Ninkina N, Buchman VL, Masliah E, Lashuel HA

Induction of de novo α-synuclein fibrillization in a neuronal model for Parkinson's disease

Journal Article

Proc Natl Acad Sci U S A, 113 (7), 2016.

Abstract | Links:

Jeon I, Cicchetti F, Cisbani G, Lee S, Li E, Bae J, Lee N, Li L, Im W, Kim M, Kim HS, Oh SH, Kim TA, Ko JJ, Aube B, Oueslati A, Kim YJ, Song J

Human-to-mouse prion-like propagation of mutant huntingtin protein

Journal Article

Acta Neuropathol, 132 (4), 2016.

Abstract | Links:

Oueslati A, Lovisa B, Perrin J, Wagnieres G, van den Bergh H, Tardy Y, Lashuel HA

Photobiomodulation Suppresses Alpha-Synuclein-Induced Toxicity in an AAV-Based Rat Genetic Model of Parkinson's Disease

Journal Article

PLoS One, 10 (10), 2015.

Abstract | Links:

Mbefo M, Fares MB, Paleologou K, Oueslati A, Yin G, Tenreiro S, Pinto M, Outeiro T, Zweckstetter M, Masliah E, Lashuel HA

Parkinson disease mutant E46K enhances α-synuclein phosphorylation in mammalian cell lines, in yeast, and in vivo

Journal Article

J Biol Chem, 290 (15), 2015.

Abstract | Links:

Oueslati A, Ximerakis M, Vekrellis K

Protein Transmission, Seeding and Degradation: Key Steps for α-Synuclein Prion-Like Propagation

Journal Article

Exp Neurobiol, 23 (4), 2014.

Abstract | Links:

Khalaf O, Fauvet B, Oueslati A, Dikiy I, Mahul-Mellier AL, Ruggeri FS, Mbefo MK, Vercruysse F, Dietler G, Lee SJ, Eliezer D, Lashuel HA

The H50Q mutation enhances α-synuclein aggregation, secretion, and toxicity

Journal Article

J Biol Chem, 289 (32), 2014.

Abstract | Links:

Mahul-Mellier AL, Fauvet B, Gysbers A, Dikiy I, Oueslati A, Georgeon S, Lamontanara AJ, Bisquertt A, Eliezer D, Masliah E, Halliday G, Hantschel O, Lashuel HA

c-Abl phosphorylates α-synuclein and regulates its degradation: implication for α-synuclein clearance and contribution to the pathogenesis of Parkinson's disease

Journal Article

Hum Mol Genet, 23 (11), 2014.

Abstract | Links:

Lashuel HA, Overk CR, Oueslati A, Masliah E

The many faces of α-synuclein: from structure and toxicity to therapeutic target

Journal Article

Nat Rev Neurosci, 14 (1), 2013.

Abstract | Links:

Oueslati A, Schneider BL, Aebischer P, Lashuel HA

Polo-like kinase 2 regulates selective autophagic α-synuclein clearance and suppresses its toxicity in vivo

Journal Article

Proc Natl Acad Sci U S A, 110 (41), 2013.

Abstract | Links:

28 entries « 2 of 3 »
Signaler des ajouts ou des modifications

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
Data provided by the Université Laval research projects registery