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Hilal Lashuel

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Publications associées (155)

Differential Effects of Post-translational Modifications on the Membrane Interaction of Huntingtin Protein

Hilal Lashuel, Matteo Dal Peraro, Luciano Andres Abriata, Charlotte Julie Caroline Gehin, Zhidian Zhang

Huntington's disease is a neurodegenerative disorder caused by an expanded polyglutamine stretch near the N-terminus of the huntingtin (HTT) protein, rendering the protein more prone to aggregate. The first 17 residues in HTT (Nt17) interact with lipid mem ...

Amer Chemical Soc2024

Fully co-factor-free ClearTau platform produces seeding-competent Tau fibrils for reconstructing pathological Tau aggregates

Henning Paul-Julius Stahlberg, Hilal Lashuel, Galina Limorenko, Rajasekhar Kolla, Meltem Tatli

The authors report a method for producing co-factor-free fibrils from all full-length Tau isoforms. The method paves the way for reconstituting pathology resembling Tau fibrils and enables screening of Tau aggregation-modifying compounds for targeted thera ...

Nature Research2023

Overexpression of human alpha-Synuclein leads to dysregulated microbiome/metabolites with ageing in a rat model of Parkinson disease

Yogesh Singh Chauhan, Hilal Lashuel, Florian Lang, Joan Romani Aumedes, Yogesh Singh

Background Braak's hypothesis states that sporadic Parkinson's disease (PD) follows a specific progression of pathology from the peripheral to the central nervous system, and this progression can be monitored by detecting the accumulation of alpha-Synuclei ...

BMC2023

Development and validation of an expanded antibody toolset that captures alpha-synuclein pathological diversity in Lewy body diseases

Hilal Lashuel, Melek Firat Altay, Johannes Burtscher, Somanath Jagannath

The abnormal aggregation and accumulation of alpha-synuclein (aSyn) in the brain is a defining hallmark of synucleinopathies. Various aSyn conformations and post-translationally modified forms accumulate in pathological inclusions and vary in abundance amo ...

Nature Portfolio2023

Recombinant Full-Length TDP-43 Oligomers Retain Their Ability to Bind RNAs, Are Not Toxic, and Do Not Seed TDP-43 Aggregation in Vitro

Hilal Lashuel, Lixin Yang, Yllza Jasiqi

TAR DNA-binding protein with 43 kD (TDP-43) is a partially disordered protein that misfolds and accumulates in the brains of patients affected by several neurodegenerative diseases. TDP-43 oligomers have been reported to form due to aberrant misfolding or ...

Amer Chemical Soc2023

Seeding the aggregation of TDP-43 requires post-fibrillization proteolytic cleavage

Hilal Lashuel, Sergey Nazarov, Niran Maharjan, Urszula Beata Cendrowska

Reconstitution of TDP-43 filaments that exhibit sequence and morphological features similar to those found in the brain helps to uncover a new mechanism for the formation and propagation of pathology in amyotrophic lateral sclerosis and other neurodegenera ...

2023

Neuronal growth on high-aspect-ratio diamond nanopillar arrays for biosensing applications

Niels Quack, Hilal Lashuel, Christophe Marcel Georges Galland, Maurizio Ferdinando Pezzoli, Somanath Jagannath, Hossein Babashah, Elena Losero

Monitoring neuronal activity with simultaneously high spatial and temporal resolution in living cell cultures is crucial to advance understanding of the development and functioning of our brain, and to gain further insights in the origin of brain disorders ...

Nature Portfolio2023

Deep Learning-Assisted Single-Molecule Detection of Protein Post-translational Modifications with a Biological Nanopore

Hilal Lashuel, Anass Chiki, Juan Francisco Bada Juarez, Matteo Dal Peraro, Lucien Fabrice Krapp, Chan Cao, Simon Finn Mayer, Pedro José Santana Ribeiro Magalhães

Protein post-translational modifications (PTMs) play a crucial role in countless biological processes, profoundly modulating protein properties on both spatial and temporal scales. Protein PTMs have also emerged as reliable biomarkers for several diseases. ...

Amer Chemical Soc2023

Artificial intelligence-coupled plasmonic infrared sensor for detection of structural protein biomarkers in neurodegenerative diseases

Hilal Lashuel, Hatice Altug, Deepthy Kavungal, Rajasekhar Kolla, Pedro José Santana Ribeiro Magalhães

Diagnosis of neurodegenerative disorders (NDDs) including Parkinson's disease and Alzheimer's disease is challenging owing to the lack of tools to detect preclinical biomarkers. The misfolding of proteins into oligomeric and fibrillar aggregates plays an i ...

AMER ASSOC ADVANCEMENT SCIENCE2023

Alpha-synuclein as a Potential Biomarker for Parkinson’s Disease and Other Synucleinopathies: Gaps, Challenges, and Opportunities

Hilal Lashuel, Pedro José Santana Ribeiro Magalhães

Parkinson's disease (PD), the second most common progressive neurodegenerative disease, develops and progresses for 10-15 years before the clinical diagnostic symptoms of the disease are manifested. Furthermore, several aspects of PD pathology overlap with ...

2022

Comparative Analysis of Total Alpha-Synuclein (alpha SYN) Immunoassays Reveals That They Do Not Capture the Diversity of Modified alpha SYN Proteoforms

Hilal Lashuel, Lorène Aeschbach, Mohamed Bilal Fares, Ritwik Burai, Layane Hanna-el-Daher, Lara Petricca

Background: The development of therapeutics for Parkinson's disease (PD) requires the establishment of biomarker assays to enable stratifying patients, monitoring disease progression, and assessing target engagement. Attempts to develop diagnostic assays b ...

IOS PRESS2022

A NAC domain mutation (E83Q) unlocks the pathogenicity of human alpha-synuclein and recapitulates its pathological diversity

Hilal Lashuel, Ramanath Narayana Hegde, Anne-Laure Mahul Mellier, Sonia Donzelli, Pedro José Santana Ribeiro Magalhães

The alpha-synuclein mutation E83Q, the first in the NAC domain of the protein, was recently identified in a patient with dementia with Lewy bodies. We investigated the effects of this mutation on the aggregation of aSyn monomers and the structure, morpholo ...

AMER ASSOC ADVANCEMENT SCIENCE2022

Pathological substrate of memory impairment in multiple system atrophy

Hilal Lashuel, Melek Firat Altay

Aims: Synaptic dysfunction in Parkinson's disease is caused by propagation of pathogenic alpha-synuclein between neurons. Previously, in multiple system atrophy (MSA), pathologically characterised by ectopic deposition of abnormal alpha-synuclein predomina ...

WILEY2022

Opportunities and challenges of alpha-synuclein as a potential biomarker for Parkinson's disease and other synucleinopathies

Hilal Lashuel, Pedro José Santana Ribeiro Magalhães

NATURE PORTFOLIO2022

Pathological Relevance of Post-Translationally Modified Alpha-Synuclein (pSer87, pSer129, nTyr39) in Idiopathic Parkinson's Disease and Multiple System Atrophy

Hilal Lashuel, Melek Firat Altay

Aggregated alpha-synuclein (alpha-synuclein) is the main component of Lewy bodies (LBs), Lewy neurites (LNs), and glial cytoplasmic inclusions (GCIs), which are pathological hallmarks of idiopathic Parkinson's disease (IPD) and multiple system atrophy (MSA ...

MDPI2022

Identification of key segments of IAPP/aSyn cross-amyloid interactions

Hilal Lashuel, Muhammed Muazzam Kamil Syed

WILEY2022

Prominent astrocytic alpha-synuclein pathology with unique post-translational modification signatures unveiled across Lewy body disorders

Hilal Lashuel, Melek Firat Altay

Alpha-synuclein (aSyn) is a pre-synaptic monomeric protein that can form aggregates in neurons in Parkinson's disease (PD), Parkinson's disease with dementia (PDD) and dementia with Lewy bodies (DLB), and in oligodendrocytes in multiple system atrophy (MSA ...

BMC2022

The role of PTM crosstalks in Httex1 structure, aggregation and membrane interaction

Hilal Lashuel, Anass Chiki, Matteo Dal Peraro, Luciano Andres Abriata, Lucien Fabrice Krapp, Driss Boudeffa, Rajasekhar Kolla, Charlotte Julie Caroline Gehin, Zhidian Zhang

CELL PRESS2022

Non-monotonic fibril surface occlusion by GFP tags from coarse-grained molecular simulations

Hilal Lashuel, Julian Charles Shillcock

The pathological growth of amyloid fibrils in neurons underlies the progression of neurodegenerative diseases including Alzheimer’s and Parkinson’s disease. Fibrils form whensoluble monomers oligomerise in the cytoplasm. Their subsequent growth occurs via ...

2022

Revisiting the grammar of Tau aggregation and pathology formation: how new insights from brain pathology are shaping how we study and target Tauopathies

Hilal Lashuel, Galina Limorenko

Converging evidence continues to point towards Tau aggregation and pathology formation as central events in the pathogenesis of Alzheimer's disease and other Tauopathies. Despite significant advances in understanding the morphological and structural proper ...

Royal Society of Chemistry2022

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