Faculty profile

Abid Oueslati

ResearcherUniversité Laval

This profile is built from public research funding records (CIHR, NSERC and SSHRC) and PubMed. We have not imported them from a Université Laval directory, so their courses may be missing. Find their university profile.

Abid Oueslati

Researcher

Health Sciences

Université Laval

Quebec City, Quebec, Canada

Supervision signals

Has led research grants, which requires an independent research appointment. Ask their department whether they supervise graduate students.
19 publications in the last five years, latest in 2026.
Senior (last) author on 14 recent papers, a sign of leading a research group.
Principal investigator on 4 research grants (2 CIHR, 2 NSERC), most recently in 2026.

These signals come from public records, including CIHR, NSERC and SSHRC funding decisions. Ask the professor or the graduate program whether they are taking new students.

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Collaborators

Grants

Publications by year

Counts cover the works listed on the university profile; citation counts come from Dimensions.

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Signals and details

Research

Alpha-Synuclein Optogenetic Protein Aggregation Animal Models Ipsc-Derived Neurons Animal Model Cellular Model Live Imaging

Latest papers

Modeling Parkinson's pathology in human iPSC dopaminergic neurons uncovers key mechanisms of Lewy body formation and heterogeneity.
Science advances · 2026
WDR44 drives de novo α-synuclein aggregation at the lysosomal membrane and promotes neuronal dysfunction in Parkinson's Disease.
bioRxiv : the preprint server for biology · 2026 · senior author
The emerging role of polo-like kinase 2 in Alzheimer's disease.
Experimental neurology · 2026 · senior author

All 29 publications

Latest funding

Decoding endolysosomal pathways driving pathological alpha Synuclein aggregation in Parkinson's Disease
CIHR · 2026 · Nominated PI
$1,082,476
Deciphering the physiological role of alpha-synuclein aggregation in the central nervous system
NSERC · 2023 · Principal investigator
$70,000
Unveiling the role of alpha-synuclein clustering and Lewy body formation in Parkinson's disease pathogenesis using an optogenetic-mediated protein aggregation system
CIHR · 2018 · Nominated PI
$726,750

All 4 grants and awards

29 publications.

Modeling Parkinson's pathology in human iPSC dopaminergic neurons uncovers key mechanisms of Lewy body formation and heterogeneity.

Mahul-Mellier AL, van den Heuvel L, Teixeira M, Boussouf MLN, Oudinot G, Thonet A, Speri D, Jasiqi Y, Ulrich C, Sheta R, Idi W, Croisier M, Clerc-Rosset S, Blanc J, Knott G, Oueslati A, Lashuel HA

Science advances2026

DOI: 10.1126/sciadv.aed8851 PMID: 42430493

WDR44 drives de novo α-synuclein aggregation at the lysosomal membrane and promotes neuronal dysfunction in Parkinson's Disease.

Teixeira M, Sheta R, Bérard M, Insinna C, Mahul-Mellier AL, Delmas CVL, Lépinay E, Idi W, Ricard A, Del Cid-Pellitero E, Trabolsi C, Gobeil S, Canron MH, Bézard E, Rajput A, Cicchetti F, Parent M, Fon EA, Ramalingam N, Dettmer U, Calon F, Westlake C, Lashuel HA, Oueslati A

bioRxiv : the preprint server for biology2026Senior author

DOI: 10.64898/2026.04.03.716340 PMID: 41993512

The emerging role of polo-like kinase 2 in Alzheimer's disease.

Martínez-Drudis L, Sheta R, Musiol D, Teixeira M, Oueslati A

Experimental neurology2026Senior author

DOI: 10.1016/j.expneurol.2026.115806 PMID: 42107623

Protocol for dissecting the aggregation-prone protein interactome with optogenetic-induced aggregation and biotin labeling proximity assay.

Teixeira M, Musiol D, Lambert JP, Oueslati A

STAR protocols2026Senior author

DOI: 10.1016/j.xpro.2025.104303 PMID: 41456280

The impact of tau deletion on Huntington's disease: An in vivo perspective.

Lepinay E, Saint-Pierre M, Teixeira M, Snapyan M, Oueslati A, Parent M, Alpaugh M, Cicchetti F

Molecular therapy : the journal of the American Society of Gene Therapy2026

DOI: 10.1016/j.ymthe.2025.11.033 PMID: 41318997

Optogenetic-induced α-synuclein accumulation reveals early synaptic dysfunction in experimental models of Parkinson's disease.

Rodriguez-Aller R, Romero-Quineche B, Morissette M, Sheta R, Di Paolo T, Saghatelyan A, Oueslati A

NPJ Parkinson's disease2025Senior author

DOI: 10.1038/s41531-025-01201-x PMID: 41390775

Interplay between lipid droplets and alpha-synuclein: implication in Parkinson's disease pathogenesis.

Idi W, Sheta R, Oueslati A

Frontiers in molecular neuroscience2025Senior author

DOI: 10.3389/fnmol.2025.1681039 PMID: 41404624

Combining light-induced aggregation and biotin proximity labeling implicates endolysosomal proteins in early α-synuclein oligomerization.

Teixeira M, Sheta R, Musiol D, Ranjakasoa V, Loehr J, Lambert JP, Oueslati A

iScience2025Senior author

DOI: 10.1016/j.isci.2025.112823 PMID: 40612512

Behavioral analysis of motor and non-motor impairment in rodent models of Parkinson's disease.

Sheta R, Bérard M, Musiol D, Martínez-Drudis L, Oueslati A

Frontiers in aging neuroscience2024Senior author

DOI: 10.3389/fnagi.2024.1464706 PMID: 39763579

Pharmacological inhibition of PLK2 kinase activity mitigates cognitive decline but aggravates APP pathology in a sex-dependent manner in APP/PS1 mouse model of Alzheimer's disease.

Martínez-Drudis L, Bérard M, Musiol D, Rivest S, Oueslati A

Heliyon2024Senior author

DOI: 10.1016/j.heliyon.2024.e39571 PMID: 39498012

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Abid Oueslati

Research

Latest papers

Latest funding

Modeling Parkinson's pathology in human iPSC dopaminergic neurons uncovers key mechanisms of Lewy body formation and heterogeneity.

WDR44 drives de novo α-synuclein aggregation at the lysosomal membrane and promotes neuronal dysfunction in Parkinson's Disease.

The emerging role of polo-like kinase 2 in Alzheimer's disease.

Protocol for dissecting the aggregation-prone protein interactome with optogenetic-induced aggregation and biotin labeling proximity assay.

The impact of tau deletion on Huntington's disease: An in vivo perspective.

Optogenetic-induced α-synuclein accumulation reveals early synaptic dysfunction in experimental models of Parkinson's disease.

Interplay between lipid droplets and alpha-synuclein: implication in Parkinson's disease pathogenesis.

Combining light-induced aggregation and biotin proximity labeling implicates endolysosomal proteins in early α-synuclein oligomerization.

Behavioral analysis of motor and non-motor impairment in rodent models of Parkinson's disease.

Pharmacological inhibition of PLK2 kinase activity mitigates cognitive decline but aggravates APP pathology in a sex-dependent manner in APP/PS1 mouse model of Alzheimer's disease.

Decoding endolysosomal pathways driving pathological alpha Synuclein aggregation in Parkinson's Disease

Deciphering the physiological role of alpha-synuclein aggregation in the central nervous system

Unveiling the role of alpha-synuclein clustering and Lewy body formation in Parkinson's disease pathogenesis using an optogenetic-mediated protein aggregation system

Investigation of the synergistic role of PLK2 and alpha-synuclein in the regulation of neuronal homeostasis and functions

Frequent collaborators

Francesca Cicchetti

Steve Lacroix

Jean-Philippe Lambert

Paul Isenring

Serge Rivest

Martin Parent

Ray Truant

Marie-Ève Tremblay

Armen Saghatelyan

Marie-Ève Tremblay

Etienne Hébert Chatelain

Denis Soulet

Frédéric Calon

Mohamed Chahine

Armen Saghatelyan

Abid Oueslati

Research

Latest papers

Latest funding

Modeling Parkinson's pathology in human iPSC dopaminergic neurons uncovers key mechanisms of Lewy body formation and heterogeneity.

WDR44 drives de novo &#x3b1;-synuclein aggregation at the lysosomal membrane and promotes neuronal dysfunction in Parkinson's Disease.

The emerging role of polo-like kinase 2 in Alzheimer's disease.

Protocol for dissecting the aggregation-prone protein interactome with optogenetic-induced aggregation and biotin labeling proximity assay.

The impact of tau deletion on Huntington's disease: An in vivo perspective.

Optogenetic-induced &#x3b1;-synuclein accumulation reveals early synaptic dysfunction in experimental models of Parkinson's disease.

Interplay between lipid droplets and alpha-synuclein: implication in Parkinson's disease pathogenesis.

Combining light-induced aggregation and biotin proximity labeling implicates endolysosomal proteins in early &#x3b1;-synuclein oligomerization.

Behavioral analysis of motor and non-motor impairment in rodent models of Parkinson's disease.

Pharmacological inhibition of PLK2 kinase activity mitigates cognitive decline but aggravates APP pathology in a sex-dependent manner in APP/PS1 mouse model of Alzheimer's disease.

Decoding endolysosomal pathways driving pathological alpha Synuclein aggregation in Parkinson's Disease

Deciphering the physiological role of alpha-synuclein aggregation in the central nervous system

Unveiling the role of alpha-synuclein clustering and Lewy body formation in Parkinson's disease pathogenesis using an optogenetic-mediated protein aggregation system

Investigation of the synergistic role of PLK2 and alpha-synuclein in the regulation of neuronal homeostasis and functions

Frequent collaborators

Francesca Cicchetti

Steve Lacroix

Jean-Philippe Lambert

Paul Isenring

Serge Rivest

Martin Parent

Ray Truant

Marie-Ève Tremblay

Armen Saghatelyan

Marie-Ève Tremblay

Etienne Hébert Chatelain

Denis Soulet

Frédéric Calon

Mohamed Chahine

Armen Saghatelyan

WDR44 drives de novo α-synuclein aggregation at the lysosomal membrane and promotes neuronal dysfunction in Parkinson's Disease.

Optogenetic-induced α-synuclein accumulation reveals early synaptic dysfunction in experimental models of Parkinson's disease.

Combining light-induced aggregation and biotin proximity labeling implicates endolysosomal proteins in early α-synuclein oligomerization.