Hilal Lashuel

Nationalité: USA

Formation

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1994 – 2000 Texas A&M University and The Scripps Research Institute
Dirigée par Prof. Jeffery W. Kelly

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1990 – 1994 City University of New York, Brooklyn College

A Site-Specific Organometallic Approach for Installing Tyrosine Phosphorylation Mimics to Decipher the Role of Phosphorylation in Alpha-Synuclein (aSyn) Aggregation and Seeding

S. MandalX. LinA. V. GemelliM. SinghA.-L. Mahul Mellier  et al.

2025

A Microfluidic Platform for Whole-Membrane Integrity Profiling in Live Neuronal Cells

C. GuiducciT. J. RyserA. KricheneN. MarchiF. R. Espinal  et al.

2025

Defined human tri-lineage brain microtissues

T. UenakaS. JungI. KumarK. VodehnalM. Rastogi  et al.

2025

Self-driving microscopy detects the onset of protein aggregation and enables intelligent Brillouin imaging

K. A. IbrahimC. CathalaC. BevilacquaL. FelettiR. Prevedel  et al.

Nature Communications. 2025. DOI : 10.1038/s41467-025-60912-0.

Mapping the Structural Landscape of Amyloid Fibrils to Guide Polymorph-Specific Therapeutics

A. SadekB. E. CorreiaH. A. Lashuel

2025

Huntingtin inclusion bodies have distinct immunophenotypes and ubiquitination profiles in the Huntington’s disease human cerebral cortex

M. E. V. SwansonA. Y. S. TanL. J. TippettC. TurnerM. A. Curtis  et al.

Scientific Reports. 2025. DOI : 10.1038/s41598-025-00465-w.

Amyotrophic lateral sclerosis caused by TARDBP mutations: from genetics to TDP-43 proteinopathy

R. BalendraJ. SreedharanM. HalleggerR. LuisierH. A. Lashuel  et al.

The Lancet Neurology. 2025. DOI : 10.1016/S1474-4422(25)00109-7.

Alpha-synuclein seed amplification assays: Data sharing, standardization needed for clinical use

H. A. LashuelD. J. SurmeierT. SimuniK. MerchantB. Caughey  et al.

Science Advances. 2025. DOI : 10.1126/sciadv.adt7195.

<i>Multi‐Targeting</i> Makrozyklische Peptide als Nanomolare Inhibitoren der Selbst‐ und Kreuznukleation der Amyloiden Selbstassemblierung von α‐Synuclein

S. HornungD. P. VoglD. NaltsasB. D. VoltaM. Ballmann  et al.

Angewandte Chemie. 2025. DOI : 10.1002/ange.202422834.

Multi-Targeting Macrocyclic Peptides as Nanomolar Inhibitors of Self- and Cross-Seeded Amyloid Self-Assembly of α-Synuclein

S. HornungD. P. VoglD. NaltsasB. D. VoltaM. Ballmann  et al.

ANGEWANDTE CHEMIE-INTERNATIONAL EDITION. 2025. DOI : 10.1002/anie.202422834.

Qatar national cancer care and research: pioneering strategies for global health excellence

M. B. H. Al-ThaniM. SubramanianN. HalabiS. Bujassoum Al BaderJ. Shan  et al.

The Lancet Oncology. 2025. DOI : 10.1016/s1470-2045(25)00132-9.

Uses of aerolysin nanopores

C. CaoM. Dal PeraroH. Lashuel

WO2025003492 . 2025.

Intelligent and Self-Driving Microscopy of Protein Aggregation in Neurodegenerative Diseases

K. Ibrahim / A. RadenovicH. Lashuel (Dir.)

Lausanne, EPFL, 2025. DOI : 10.5075/epfl-thesis-11337.

Nanoplasmonic Infrared Microarray Sensor Enabling Structural Protein Biomarker-Based Drug Screening for Neurodegenerative Diseases

D. KavungalE. MorroS. T. KumarB. DagliH. Lashuel  et al.

Advanced science (Weinheim, Baden-Wurttemberg, Germany). 2025. DOI : 10.1002/advs.202500320.

Nanoplasmonic infrared biosensors enabling detection of misfolded protein biomarkers and drug screening for neurodegenerative diseases

D. Kavungal / H. AltugH. Lashuel (Dir.)

Lausanne, EPFL, 2025. DOI : 10.5075/epfl-thesis-10478.

Towards Conformational Targeting of Alpha-Synuclein Fibrils

A. S. S. Z. M. Sadek / B. E. Ferreira De Sousa CorreiaH. Lashuel (Dir.)

Lausanne, EPFL, 2025. DOI : 10.5075/epfl-thesis-10710.

Mouse α-synuclein fibrils are structurally and functionally distinct from human fibrils associated with Lewy body diseases

A. SokratianY. ZhouM. TatliK. J. BurbidgeE. Xu  et al.

Science advances. 2024. DOI : 10.1126/sciadv.adq3539.

Research Priorities on the Role of α-Synuclein in Parkinson's Disease Pathogenesis

J. BurréR. H. EdwardsG. HallidayA. E. LangH. A. Lashuel  et al.

Movement disorders : official journal of the Movement Disorder Society. 2024. DOI : 10.1002/mds.29897.

A Versatile Method for Site-Specific Chemical Installation of Aromatic Posttranslational Modification Analogs into Proteins

X. LinS. MandalR. V. NithunR. KollaB. Bouri  et al.

Journal of the American Chemical Society. 2024. DOI : 10.1021/jacs.4c08416.

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

Z. ZhangC. GehinL. A. AbriataM. Dal PeraroH. Lashuel

Acs Chemical Neuroscience. 2024. DOI : 10.1021/acschemneuro.4c00091.

Mouse α-synuclein fibrils are structurally and functionally distinct from human fibrils associated with Lewy body diseases

A. SokratianY. ZhouM. TatliK. J. BurbidgeE. Xu  et al.

2024

Post-translational glycosylation diminishes α-synuclein pathology formation

M. PrattH. Lashuel

Nature Chemical Biology. 2024. DOI : 10.1038/s41589-024-01553-0.

O-GlcNAc forces an α-synuclein amyloid strain with notably diminished seeding and pathology

A. T. BalanaA.-L. Mahul-MellierB. A. NguyenM. HorvathA. Javed  et al.

Nature Chemical Biology. 2024. DOI : 10.1038/s41589-024-01551-2.

Development and validation of an expanded antibody toolset that captures alpha-synuclein pathological diversity in Lewy body diseases (vol 10, 19, 2024)

M. F. AltayS. T. KumarJ. BurtscherS. JagannathC. Strand  et al.

NPJ PARKINSONS DISEASE. 2024. DOI : 10.1038/s41531-024-00634-0.

Targeting TDP-43 Proteinopathies in Neurodegeneration by its Native-State Stabilization

L. Yang / H. Lashuel (Dir.)

Lausanne, EPFL, 2024. DOI : 10.5075/epfl-thesis-10555.

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

G. LimorenkoM. TatliR. KollaS. NazarovM.-T. Weil  et al.

Nature Communications. 2024. DOI : 10.1038/s41467-024-48976-w.

Deep learning augmented nanoplasmonic infrared sensor for structural protein biomarker-based detection of neurodegenerative diseases

D. KavungalP. MagalhãesS. T. KumarR. KollaH. Lashuel  et al.

2024. 21 Nanoscale Imaging, Sensing, and Actuation for Biomedical Applications, San Francisco, United States, 2024-01-28 - 2024-01-28. DOI : 10.1117/12.3003239.

Investigating the intra-molecular and inter-molecular effects of post-translational modifications on intrinsically disordered protein regions and structured protein regions

Z. Zhang / M. Dal PeraroH. Lashuel (Dir.)

Lausanne, EPFL, 2024. DOI : 10.5075/epfl-thesis-10530.

Effective Inhibition of TDP-43 Aggregation by Native State Stabilization

L. YangY. JasiqiA. ZettorO. VadasJ. Chiaravalli  et al.

Angewandte Chemie International Edition. 2024. DOI : 10.1002/anie.202314587.

Transactive response dna-binding protein 43kda (tdp-43) mutants and uses thereof

L. YangH. Lashuel

WO2024223615 . 2024.

Exploring the therapeutic potential of Huntingtin native state stabilization through targeting its interacting partners

E. Morro / H. Lashuel (Dir.)

Lausanne, EPFL, 2024. DOI : 10.5075/epfl-thesis-10915.

Method of preparation of amyloidogenic protein aggregates and uses thereof

G. LimorenkoH. Lashuel

WO2024094597 . 2024.

Dielectrophoretic Manipulation of Biological Species: Novel Microfluidic Approaches to Study Cell-Cell Interactions and the Role of Alpha-Synuclein in Neurodegeneration

T. J. Ryser / C. GuiducciH. Lashuel (Dir.)

Lausanne, EPFL, 2024. DOI : 10.5075/epfl-thesis-10597.

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

L. YangY. JasiqiH. Lashuel

Acs Chemical Neuroscience. 2023. DOI : 10.1021/acschemneuro.3c00691.

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

C. CaoP. MagalhaesL. F. KrappJ. F. B. JuarezS. F. Mayer  et al.

Acs Nano. 2023. DOI : 10.1021/acsnano.3c08623.

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

M. F. AltayS. T. KumarJ. BurtscherS. JagannathC. Strand  et al.

Npj Parkinsons Disease. 2023. DOI : 10.1038/s41531-023-00604-y.

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

G. LimorenkoM. TatliR. KollaS. NazarovM.-T. Weil  et al.

Nature Communications. 2023. DOI : 10.1038/s41467-023-39314-7.

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

Y. SinghC. TrautweinJ. RomaniM. S. S. SalkerP. H. H. Neckel  et al.

Molecular Neurodegeneration. 2023. DOI : 10.1186/s13024-023-00628-1.

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

D. KavungalP. MagalhaesS. T. KumarR. KollaH. A. Lashuel  et al.

Science Advances. 2023. DOI : 10.1126/sciadv.adg9644.

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

S. T. KumarS. NazarovS. PortaN. MaharjanU. Cendrowska  et al.

Nature Neuroscience. 2023. DOI : 10.1038/s41593-023-01341-4.

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

E. LoseroS. JagannathM. PezzoliV. GoblotH. Babashah  et al.

Scientific Reports. 2023. DOI : 10.1038/s41598-023-32235-x.

Deconstructing and Reconstructing the Complexity of Tau pathology

G. Limorenko / H. Lashuel (Dir.)

Lausanne, EPFL, 2023. DOI : 10.5075/epfl-thesis-9911.

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

M. F. AltayA. K. L. LiuJ. L. HoltonL. ParkkinenH. A. Lashuel

Acta Neuropathologica Communications. 2022. DOI : 10.1186/s40478-022-01468-8.

Revisiting the specificity and ability of phospho-S129 antibodies to capture alpha-synuclein biochemical and pathological diversity

H. A. LashuelA.-L. Mahul-MellierS. NovelloR. N. HegdeY. Jasiqi  et al.

Npj Parkinsons Disease. 2022. DOI : 10.1038/s41531-022-00388-7.

N-terminal mutant huntingtin deposition correlates with CAG repeat length and symptom onset, but not neuronal loss in Huntington's disease

F. E. LayburnA. Y. S. TanN. F. MehrabiM. A. CurtisL. J. Tippett  et al.

Neurobiology Of Disease. 2022. DOI : 10.1016/j.nbd.2022.105884.

Pathological substrate of memory impairment in multiple system atrophy

Y. MikiK. TanjiK. ShinnaiM. T. TanakaF. Altay  et al.

Neuropathology And Applied Neurobiology. 2022. DOI : 10.1111/nan.12844.

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

D. NaltsasS. HornungD. VoglJ. LudwigA. Molenaar  et al.

2022.

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

P. MagalhaesH. A. Lashuel

Npj Parkinsons Disease. 2022. DOI : 10.1038/s41531-022-00357-0.

On-Demand Nanoliter Sampling Probe for the Collection of Brain Fluid

J. TeixidorS. NovelloD. OrtizL. MeninH. A. Lashuel  et al.

Analytical Chemistry. 2022. DOI : 10.1021/acs.analchem.2c01577.

Structural Basis of Huntingtin Fibril Polymorphism Revealed by Cryogenic Electron Microscopy of Exon 1 HTT Fibrils

S. NazarovA. ChikiD. BoudeffaH. A. Lashuel

Journal Of The American Chemical Society. 2022. DOI : 10.1021/jacs.2c00509.

Remembering John Q Trojanowski, in his own words: A life dedicated to discovering building blocks and using them to build bridges of knowledge, collaboration, and discovery

H. A. Lashuel

Npj Parkinsons Disease. 2022. DOI : 10.1038/s41531-022-00310-1.

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

S. T. KumarA.-L. Mahul-MellierR. N. HegdeG. RiviereR. Moons  et al.

Science Advances. 2022. DOI : 10.1126/sciadv.abn0044.

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

B. SonustunM. F. AltayC. StrandK. EbanksG. Hondhamuni  et al.

Cells. 2022. DOI : 10.3390/cells11050906.

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

Z. ZhangA. ChikiC. GehinR. KollaL. A. Abriata  et al.

2022. p. 38 - 38. DOI : 10.1016/j.bpj.2021.11.2495.

An integrative approach to elucidate the mechanisms and dynamics of Huntingtin aggregation and inclusion formation in neuronal models of Huntington's Disease

N. A. D. Riguet / H. Lashuel (Dir.)

Lausanne, EPFL, 2022. DOI : 10.5075/epfl-thesis-9296.

Capturing the heterogeneity of alpha-synuclein pathology in synucleinopathies

M. F. Altay / H. Lashuel (Dir.)

Lausanne, EPFL, 2022. DOI : 10.5075/epfl-thesis-8480.

Towards elucidating the structural and cellular determinants of a-synuclein seeding and toxicity

S. Jagannath / H. Lashuel (Dir.)

Lausanne, EPFL, 2022. DOI : 10.5075/epfl-thesis-9365.

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

G. LimorenkoH. A. Lashuel

Chemical Society Reviews. 2022. DOI : 10.1039/d1cs00127b.

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

J. C. ShillcockJ. HastingsN. RiguetH. A. Lashuel

Computational and Structural Biotechnology Journal. 2022. DOI : 10.1016/j.csbj.2021.12.017.

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

L. PetriccaN. ChikiL. Hanna-El-DaherL. AeschbachR. Burai  et al.

Journal Of Parkinsons Disease. 2022. DOI : 10.3233/JPD-223285.

To target Tau pathologies, we must embrace and reconstruct their complexities

G. LimorenkoH. A. Lashuel

Neurobiology Of Disease. 2021. DOI : 10.1016/j.nbd.2021.105536.

Nuclear and cytoplasmic huntingtin inclusions exhibit distinct biochemical composition, interactome and ultrastructural properties

N. RiguetA.-L. Mahul-MellierN. MaharjanJ. BurtscherM. Croisier  et al.

Nature Communications. 2021. DOI : 10.1038/s41467-021-26684-z.

Fatal attraction-The role of hypoxia when alpha-synuclein gets intimate with mitochondria

J. BurtscherM. M. K. SyedM. A. KellerH. A. LashuelG. P. Millet

Neurobiology Of Aging. 2021. DOI : 10.1016/j.neurobiolaging.2021.07.017.

The Nt17 Domain and its Helical Conformation Regulate the Aggregation, Cellular Properties and Neurotoxicity of Mutant Huntingtin Exon 1

S. ViewegA.-L. Mahul MellierF. S. RuggeriN. RiguetS. M. Deguire  et al.

Journal of Molecular Biology. 2021. DOI : 10.1016/j.jmb.2021.167222.

Pharmacological characterization of mutant huntingtin aggregate-directed PET imaging tracer candidates

F. HerrmannM. HessmannS. SchaertlK. Berg-RosseburgC. J. Brown  et al.

Scientific Reports. 2021. DOI : 10.1038/s41598-021-97334-z.

Investigating Crosstalk Among PTMs Provides Novel Insight Into the Structural Basis Underlying the Differential Effects of Nt17 PTMs on Mutant Httex1 Aggregation

A. ChikiZ. ZhangK. RajasekharL. A. AbriataI. Rostami  et al.

Frontiers in Molecular Biosciences. 2021. DOI : 10.3389/fmolb.2021.686086.

Alpha-synuclein research: defining strategic moves in the battle against Parkinson's disease

L. M. A. OliveiraT. GasserR. EdwardsM. ZweckstetterR. Melki  et al.

Npj Parkinsons Disease. 2021. DOI : 10.1038/s41531-021-00203-9.

A New Chemoenzymatic Semisynthetic Approach Provides Insight into the Role of Phosphorylation beyond Exon1 of Huntingtin and Reveals N-Terminal Fragment Length-Dependent Distinct Mechanisms of Aggregation

R. KollaG. PushparathinamJ. RicciA. ReifI. Rostami  et al.

Journal of the American Chemical Society. 2021. DOI : 10.1021/jacs.1c03108.

Rethinking protein aggregation and drug discovery in neurodegenerative diseases: Why we need to embrace complexity?

H. Lashuel

Current Opinion in Chemical Biology. 2021. DOI : 10.1016/j.cbpa.2021.05.006.

Lewy body-associated proteins: Victims, instigators, or innocent bystanders? The case of AIMP2 and alpha-synuclein

H. A. LashuelS. Novello

Neurobiology of Disease. 2021. DOI : 10.1016/j.nbd.2021.105417.

Parkinson mice show functional and molecular changes in the gut long before motoric disease onset

M. GriesA. ChristmannS. SchulteM. WeylandS. Rommel  et al.

Molecular Neurodegeneration. 2021. DOI : 10.1186/s13024-021-00439-2.

Enforced dimerization between XBP1s and ATF6f enhances the protective effects of the UPR in models of neurodegeneration

R. L. VidalD. SepulvedaP. Troncoso-EscuderoP. Garcia-HuertaC. Gonzalez  et al.

Molecular Therapy. 2021. DOI : 10.1016/j.ymthe.2021.01.033.

Correlative light and electron microscopy suggests that mutant huntingtin dysregulates the endolysosomal pathway in presymptomatic Huntington's disease

Y. ZhouT. R. PeskettC. LandlesJ. B. WarnerK. Sathasivam  et al.

Acta Neuropathologica Communications. 2021. DOI : 10.1186/s40478-021-01172-z.

Alpha-Synuclein oligomerization and aggregation: All models are useful but only if we know what they model This is the reply to a comment "Alpha-synuclein oligomerization and aggregation: A model will always be a model" on the original article "Monitoring alpha-synuclein oligomerization and aggregation using bimolecular fluorescence complementation assays: What you see is not always what you get". The articles are accompanied by a Preface "How good are cellular models?".

H. A. Lashuel

Journal of Neurochemistry (JNC). 2021. DOI : 10.1111/jnc.15275.

Hypoxia Conditioning as a Promising Therapeutic Target in Parkinson's Disease?

J. BurtscherM. M. K. SyedH. A. LashuelG. P. Millet

Movement Disorders. 2021. DOI : 10.1002/mds.28544.

Reverse engineering Lewy bodies: how far have we come and how far can we go?

M. B. FaresS. JagannathH. Lashuel

Nature Reviews Neuroscience. 2021. DOI : 10.1038/s41583-020-00416-6.

Monitoring alpha-synuclein oligomerization and aggregation using bimolecular fluorescence complementation assays: What you see is not always what you get

B. FreyA. AlOkdaM. P. JacksonN. RiguetJ. A. Duce  et al.

Journal of Neurochemistry (JNC). 2021. DOI : 10.1111/jnc.15147.

Site-Specific Phosphorylation of Huntingtin Exon 1 Recombinant Proteins Enabled by the Discovery of Novel Kinases

A. ChikiJ. RicciR. HegdeL. A. AbriataA. Reif  et al.

Chembiochem. 2020. DOI : 10.1002/cbic.202000508.

How specific are the conformation-specific α-synuclein antibodies? Characterization and validation of 16 α-synuclein conformation-specific antibodies using well-characterized preparations of α-synuclein monomers, fibrils and oligomers with distinct structures and morphology

S. K. ThangarajS. JagannathC. FrancoisH. VandersticheleE. Stoops  et al.

Neurobiology of Disease. 2020. DOI : 10.1016/j.nbd.2020.105086.

TBK1 phosphorylates mutant Huntingtin and suppresses its aggregation and toxicity in Huntington's disease models

R. N. HegdeA. ChikiL. PetriccaP. MartufiN. Arbez  et al.

The EMBO Journal. 2020. DOI : 10.15252/embj.2020104671.

Half a century of amyloids: past, present and future

P. C. KeR. ZhouL. C. SerpellR. RiekT. P. J. Knowles  et al.

Chemical Society Reviews. 2020. DOI : 10.1039/C9CS00199A.

Do Lewy bodies contain alpha-synuclein fibrils? and Does it matter? A brief history and critical analysis of recent reports

H. A. Lashuel

Neurobiology Of Disease. 2020. DOI : 10.1016/j.nbd.2020.104876.

Phosphorylation of the overlooked tyrosine 310 regulates the structure, aggregation, and microtubule- and lipid-binding properties of Tau

N. Ait-BouziadA. ChikiG. LimorenkoS. XiaoD. Eliezer  et al.

Journal of Biological Chemistry. 2020. DOI : 10.1074/jbc.RA119.012517.

Extent of N-terminus exposure of monomeric alpha-synuclein determines its aggregation propensity

A. D. StephensM. ZacharopoulouR. MoonsG. FuscoN. Seetaloo  et al.

Nature Communications. 2020. DOI : 10.1038/s41467-020-16564-3.

Education and research are essential for lasting peace in Yemen

F. ZakhamO. VapalahtiH. A. Lashual

Lancet. 2020. DOI : 10.1016/S0140-6736(20)30162-8.

Unraveling the complexity of amyloid polymorphism using gold nanoparticles and cryo-EM

U. CendrowskaP. J. SilvaN. Ait-BouziadM. MuellerZ. P. Guven  et al.

Proceedings Of The National Academy Of Sciences Of The United States Of America (PNAS). 2020. DOI : 10.1073/pnas.1916176117.

The busy lives of academics have hidden costs — and universities must take better care of their faculty members

H. Lashuel

Nature Careers Community. 2020. DOI : 10.1038/d41586-020-00661-w.

A simple, versatile and robust centrifugation-based filtration protocol for the isolation and quantification of alpha-synuclein monomers, oligomers and fibrils: Towards improving experimental reproducibility in alpha-synuclein research

S. T. KumarS. DonzelliA. ChikiM. M. K. SyedH. A. Lashuel

Journal of Neurochemistry (JNC). 2020. DOI : 10.1111/jnc.14955.

The process of Lewy body formation, rather than simply α-synuclein fibrillization, is one of the major drivers of neurodegeneration

A.-L. Mahul-MellierJ. BurtscherN. MaharjanL. WeerensM. Croisier  et al.

Proceedings Of The National Academy Of Sciences Of The United States Of America (PNAS). 2020. DOI : 10.1073/pnas.1913904117.

Site-Specific Hyperphosphorylation Inhibits, Rather than Promotes, Tau Fibrillization, Seeding Capacity, and Its Microtubule Binding

M. Haj-YahyaP. GopinathK. RajasekharH. MirbahaM. I. Diamond  et al.

Angewandte Chemie International Edition. 2020. DOI : 10.1002/anie.201913001.

Ultrasensitive quantitative measurement of huntingtin phosphorylation at residue S13

C. CariuloM. VeraniP. MartufiR. IngenitoM. Finotto  et al.

Biochemical And Biophysical Research Communications. 2020. DOI : 10.1016/j.bbrc.2019.09.097.

What about faculty?

H. A. Lashuel

Elife. 2020. DOI : 10.7554/eLife.54551.

Gold nanoparticles as a new tool in amyloid studies

U. B. Cendrowska / F. StellacciH. Lashuel (Dir.)

Lausanne, EPFL, 2020. DOI : 10.5075/epfl-thesis-7471.

Pronounced α-synuclein pathology in a seeding-based mouse model is not sufficient to induce mitochondrial respiration deficits in the striatum and amygdala

J. BurtscherJ.-C. CopinC. SandiH. Lashuel

eNeuro. 2020. DOI : 10.1523/ENEURO.0110-20.2020.

Development of novel methods and tools to decipher the huntingtin post-translation modifications code

A. Chiki / H. Lashuel (Dir.)

Lausanne, EPFL, 2020. DOI : 10.5075/epfl-thesis-7537.

The Role of Post-translational Modifications on the Energy Landscape of Huntingtin N-Terminus

H. YalincaC. J. C. GehinV. OleinikovasH. A. LashuelF. L. Gervasio  et al.

Frontiers in Molecular Biosciences. 2019. DOI : 10.3389/fmolb.2019.00095.

Phospho-S129 Alpha-Synuclein Is Present in Human Plasma but Not in Cerebrospinal Fluid as Determined by an Ultrasensitive Immunoassay

C. CariuloP. MartufiM. VeraniL. AzzolliniG. Bruni  et al.

Frontiers in Neuroscience. 2019. DOI : 10.3389/fnins.2019.00889.

Investigation of alpha-synuclein post-translational modifications in idiopathic Parkinson's disease and multiple system atrophy

B. SonustunC. StrandS. FotiT. T. WarnerH. Lashuel  et al.

2019. 120th Meeting of the British-Neuropathological-Society (BNS) / Developmental Neuropathology Symposium, London, ENGLAND, Mar 06-08, 2019. p. 19 - 19.

Single Posttranslational Modifications in the Central Repeat Domains of Tau4 Impact its Aggregation and Tubulin Binding

D. EllmerM. BrehsM. Haj-YahyaH. A. LashuelC. F. W. Becker

Angewandte Chemie International Edition. 2019. DOI : 10.1002/anie.201805238.

alpha-Synuclein O-GlcNAcylation alters aggregation and toxicity, revealing certain residues as potential inhibitors of Parkinson's disease

P. M. LevineA. GalesicA. T. BalanaA.-L. Mahul-MellierM. X. Navarro  et al.

Proceedings Of The National Academy Of Sciences Of The United States Of America (PNAS). 2019. DOI : 10.1073/pnas.1808845116.

A method for preparing phfs-like tau aggregates

H. A. LashuelN. Ait-Bouziad

US11629175 ; US2021238242 ; EP3784687 ; WO2019207164 . 2019.

Exploring the role of post-translational modifications in regulating α-synuclein interactions by studying the effects of phosphorylation on nanobody binding

F. El TurkE. De GenstT. GuilliamsB. C. D. FauvetJ. Kiwi  et al.

Proteins Science. 2018. DOI : 10.1002/pro.3412.

Generation of Native, Untagged Huntingtin Exon1 Monomer and Fibrils Using a SUMO Fusion Strategy

A. ReifA. ChikiJ. RicciH. Lashuel

Journal of Visualized Experiments. 2018. DOI : 10.3791/57506.

Combined Multi-Plane Tomographic Phase Retrieval and Stochastic Optical Fluctuation Imaging for 4D Cell Microscopy

A. DesclouxK. GrußmayerE. BostanT. LukesA. Bouwens  et al.

Nature Photonics. 2018. DOI : 10.1038/s41566-018-0109-4.

Monomeric Huntingtin Exon 1 Has Similar Overall Structural Features for Wild-Type and Pathological Polyglutamine Lengths

J. B. Warner IVK. RuffP. Siong TanE. A. LemkeR. V. Pappu  et al.

Journal of the American Chemical Society. 2017. DOI : 10.1021/jacs.7b06659.

Sequence and structural determinants of Tau aggregation and seeding capacity: Implications for Neurofibrillary Tangle formation and Tau toxicity in Alzheimer's disease

N. Ait Bouziad / H. Lashuel (Dir.)

Lausanne, EPFL, 2017. DOI : 10.5075/epfl-thesis-7985.

Ganciclovir derivatives for modulating innate and adaptive immunity and for use in immunotherapy

R. BuraiH. A. LashuelV. MathurA. Wyss-Coray

US9809597 ; US2017050967 . 2017.

Human and eco-toxicological impacts of organometallic halide perovskites

R. I. Benmessaoud / L. ForróH. Lashuel (Dir.)

Lausanne, EPFL, 2017. DOI : 10.5075/epfl-thesis-7595.

Mutant Exon1 Huntingtin Aggregation is Regulated by T3 Phosphorylation-Induced Structural Changes and Crosstalk between T3 Phosphorylation and Acetylation at K6

A. ChikiS. M. DeGuireF. S. RuggeriD. SanfeliceA. Ansaloni  et al.

Angewandte Chemie (International ed. in English). 2017. DOI : 10.1002/anie.201611750.

The America I believe in

H. A. Lashuel

Science. 2017. DOI : 10.1126/science.355.6326.766.

Activation of the STING-dependent type I interferon response reduces microglial reactivity and neuroinflammation

V. MathusR. BuraiR. VestL. BonannoB. Lehallier  et al.

Neuron. 2017. DOI : 10.1016/j.neuron.2017.11.032.

Amyloid Single Cell Cytotoxicity Assays by Nanomotion Detection

F. RuggeriA.-L. MahulS. KasasH. LashuelG. Longo  et al.

Cell Death Discovery. 2017. DOI : 10.1038/cddiscovery.2017.53.

Polyglutamine expansion affects huntingtin conformation in multiple Huntington’s disease models

M. DaldinV. FodaleC. CariuloL. AzzolliniM. Verani  et al.

Scientific Reports. 2017. DOI : 10.1038/s41598-017-05336-7.

Membrane scission driven by the PROPPIN Atg18

N. GopaldassB. FauvetH. LashuelA. RouxA. Mayer

Embo Journal. 2017. DOI : 10.15252/embj.201796859.

The role of the polyglutamine and N-terminal domains in regulating the aggregation and structural properties of Huntingtin Exon 1

S. Vieweg / H. Lashuel (Dir.)

Lausanne, EPFL, 2017. DOI : 10.5075/epfl-thesis-7374.

The mechanism of sirtuin 2-mediated exacerbation of alpha-synuclein toxicity in models of Parkinson disease

R. M. de OliveiraH. Vicente MirandaL. FrancelleR. PinhoÉ. M. Szegö  et al.

PLoS Biology. 2017. DOI : 10.1371/journal.pbio.2000374.

Glycation potentiates α-synuclein-associated neurodegeneration in synucleinopathies

H. Vicente MirandaÉ. M. SzegoL. M. A. OliveiraC. BredaE. Darendelioglu  et al.

Brain : a journal of neurology. 2017. DOI : 10.1093/brain/awx056.

Polyglutamine Length Dependent Structural Properties and Phase Behavior of Huntingtin Exon 1

K. M. RuffJ. B. WarnerA. E. PoseyP. S. TanE. A. Lemke  et al.

2017. 58th Annual Meeting of the Biophysical-Society, San Francisco, CA, FEB 15-19, 2014. p. 511A - 511A. DOI : 10.1016/j.bpj.2016.11.2762.

A user's guide for α-synuclein biomarker studies in biological fluids: Perianalytical considerations

B. MollenhauerR. BatrlaO. El-AgnafD. R. GalaskoH. A. Lashuel  et al.

Movement Disorders. 2017. DOI : 10.1002/mds.27090.

Discovery and characterization of novel stable tau oligomeric complexes: Implications for the role of Tau/phospholipid interactions in regulating its functions in health and disease

N. Ait-BouziadG. LvA. L. Mahul-MellierS. XiaoG. Zorludemir  et al.

Nature Communications. 2017. DOI : 10.1038/s41467-017-01575-4.

An Intein-based Strategy for the Production of Tag-free Huntingtin Exon 1 Proteins Enables New Insights into the Polyglutamine Dependence of Httex1 Aggregation and Fibril Formation

S. ViewegA. AnsaloniZ.-M. WangJ. B. WarnerH. A. Lashuel

Journal of Biological Chemistry. 2016. DOI : 10.1074/jbc.M116.713982.

A New Caged-Glutamine Derivative as a Tool To Control the Assembly of Glutamine-Containing Amyloidogenic Peptides

L. AwadN. JejelavaR. BuraiH. A. Lashuel

Chembiochem : a European journal of chemical biology. 2016. DOI : 10.1002/cbic.201600474.

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

M.-B. FaresB. MacoA. OueslatiE. RockensteinN. Ninkina  et al.

Proceedings Of The National Academy Of Sciences Of The United States Of America (PNAS). 2016. DOI : 10.1073/pnas.1512876113.

Microtubule-Binding R3 Fragment from Tau Self-Assembles into Giant Multistranded Amyloid Ribbons

J. AdamcikA. Sanchez-FerrerN. Ait-BouziadN. P. ReynoldsH. A. Lashuel  et al.

Angewandte Chemie International Edition. 2016. DOI : 10.1002/anie.201508968.

Health hazards of methylammonium lead iodide based perovskites: cytotoxicity studies

I. R. BenmessaoudA.-L. Mahul-MellierE. HorváthB. MacoM. Spina  et al.

Toxicol. Res.. 2016. DOI : 10.1039/C5TX00303B.

Semisynthetic and in Vitro Phosphorylation of Alpha-Synuclein at Y39 Promotes Functional Partly Helical Membrane-Bound States Resembling Those Induced by PD Mutations

I. DikiyB. FauvetA. JovicicA.-L. Mahul-MellierC. Desobry  et al.

Acs Chemical Biology. 2016. DOI : 10.1021/acschembio.6b00539.

Novel therapeutic strategy for neurodegeneration by blocking Aβ seeding mediated aggregation in models of Alzheimer's disease

S. EleuteriS. Di GiovanniE. RockensteinM. ManteA. Adame  et al.

Neurobiology of disease. 2015. DOI : 10.1016/j.nbd.2014.08.017.

Fibril growth and seeding capacity play key roles in α-synuclein-mediated apoptotic cell death

Mahul-MellierF. VercruysseB. MacoN. Ait-BouziadM. De Roo  et al.

Cell death and differentiation. 2015. DOI : 10.1038/cdd.2015.79.

Recapitulating De Novo Alpha-Synuclein Fibrillization in a Novel Neuronal Model of Parkinson's Disease

M.-B. Fares / H. Lashuel (Dir.)

Lausanne, EPFL, 2015. DOI : 10.5075/epfl-thesis-6679.

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

A. OueslatiB. LovisaJ. PerrinG. WagnièresH. van den Bergh  et al.

PloS One. 2015. DOI : 10.1371/journal.pone.0140880.

Semisynthesis and Enzymatic Preparation of Post-translationally Modified α-Synuclein

B. FauvetH. A. Lashuel

Methods in molecular biology (Clifton, N.J.). 2015. DOI : 10.1007/978-1-4939-2978-8_1.

Elucidating the Role of Site-Specific Nitration of alpha-Synuclein in the Pathogenesis of Parkinson's Disease via Protein Semisynthesis and Mutagenesis

R. BuraiN. Ait-BouziadA. ChikiH. A. Lashuel

Journal Of The American Chemical Society. 2015. DOI : 10.1021/ja5131726.

Influence of the β-sheet content on the mechanical properties of aggregates during amyloid fibrillization

F. S. RuggeriJ. AdamcikJ. S. JeongH. A. LashuelR. Mezzenga  et al.

Angewandte Chemie (International ed. in English). 2015. DOI : 10.1002/anie.201409050.

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

M. K. MbefoM.-B. FaresK. PaleologouA. OueslatiG. Yin  et al.

Journal of Biological Chemistry. 2015. DOI : 10.1074/jbc.M114.610774.

Structural differences of amyloid-beta fibrils revealed by antibodies from phage display

P. DrosteA. FrenzelM. SteinwandT. PelatP. Thullier  et al.

Bmc Biotechnology. 2015. DOI : 10.1186/s12896-015-0146-8.

Parkinson's Disease Genes VPS35 and EIF4G1 Interact Genetically and Converge on α-Synuclein

N. DhungelS. EleuteriL.-B. LiN. J. KramerJ. W. Chartron  et al.

Neuron. 2015. DOI : 10.1016/j.neuron.2014.11.027.

The novel Parkinson's disease linked mutation G51D attenuates in vitro aggregation and membrane binding of alpha-synuclein, and enhances its secretion and nuclear localization in cells

M.-B. FaresN. Ait-BouziadI. DikiyM. K. MbefoA. Jovicic  et al.

Human Molecular Genetics. 2014. DOI : 10.1093/hmg/ddu165.

Reversible attachment of Cell-Penetrating Peptides for the efficient delivery of α-synuclein to HeLa cells and primary cortical neurons

C. Desobry / H. Lashuel (Dir.)

Lausanne, EPFL, 2014. DOI : 10.5075/epfl-thesis-6412.

One-Pot Semisynthesis of Exon 1 of the Huntingtin Protein: New Tools for Elucidating the Role of Posttranslational Modifications in the Pathogenesis of Huntington's Disease

A. AnsaloniZ.-M. WangJ. S. JeongF. S. RuggeriG. Dietler  et al.

Angewandte Chemie International Edition. 2014. DOI : 10.1002/anie.201307510.

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

A.-L. Mahul-MellierB. FauvetA. GysbersI. DikiyA. Oueslati  et al.

Human Molecular Genetics. 2014. DOI : 10.1093/hmg/ddt674.

Protein semisynthesis and total synthesis approaches to elucidate the role of Alpha-Synuclein post-translational modifications

B. C. D. Fauvet / H. Lashuel (Dir.)

Lausanne, EPFL, 2014. DOI : 10.5075/epfl-thesis-6187.

The role of S129 phosphorylation in regulating the cellular properties and secretion of alpha-synuclein : implication for alpha-synuclein function in health and disease

M. Mbefo Kamdem / H. Lashuel (Dir.)

Lausanne, EPFL, 2014. DOI : 10.5075/epfl-thesis-6110.

The role of fibril formation and growth in a-synuclein mediated extracellular toxicity

F. Vercruysse / H. Lashuel (Dir.)

Lausanne, EPFL, 2014. DOI : 10.5075/epfl-thesis-6106.

NOVEL MECHANISM-BASED INHIBITORS OF A beta AGGREGATION AND TOXICITY

H. A. LashuelS. EleuteriS. Di GiovanniE. RockensteinM. Mante  et al.

2014. 6th International Conference on Alzheimers Disease and Related Disorders in the Middle East, Istanbul, TURKEY, OCT 25-27, 2013. p. 720 - 721.

Elucidating the role of N-terminal phosphorylation in regulating the structure and the aggregation propensities of Huntingtin exon 1 using a semisynthetic strategy

A. Ansaloni / H. Lashuel (Dir.)

Lausanne, EPFL, 2014. DOI : 10.5075/epfl-thesis-6188.

Alpha-synuclein Post-translational Modifications as Potential Biomarkers for Parkinson Disease and Other Synucleinopathies

A. W. SchmidB. FauvetM. MoniatteH. A. Lashuel

Molecular & Cellular Proteomics. 2013. DOI : 10.1074/mcp.R113.032730.

Oxidative and nitrative alpha-synuclein modifications and proteostatic stress: implications for disease mechanisms and interventions in synucleinopathies

S. SchildknechtH. R. GerdingC. KarremanM. DrescherH. A. Lashuel  et al.

Journal of Neurochemistry (JNC). 2013. DOI : 10.1111/jnc.12226.

Novel Mechanistic Insight into the Molecular Basis of Amyloid Polymorphism and Secondary Nucleation during Amyloid Formation

J. S. JeongA. AnsaloniR. MezzengaH. A. LashuelG. Dietler

Journal of Molecular Biology. 2013. DOI : 10.1016/j.jmb.2013.02.005.

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

H. A. LashuelC. R. OverkA. OueslatiE. Masliah

Nature reviews. Neuroscience. 2013. DOI : 10.1038/nrn3406.

Real-time Amyloid Aggregation Monitoring with a Photonic Crystal-based Approach

S. SantiV. MusiE. DescroviV. PaederJ. Di Francesco  et al.

ChemPhysChem. 2013. DOI : 10.1002/cphc.201300633.

Synthetic polyubiquitinated α-Synuclein reveals important insights into the roles of the ubiquitin chain in regulating its pathophysiology

M. Haj-YahyaB. FauvetY. Herman-BachinskyM. HejjaouiS. N. Bavikar  et al.

Proceedings Of The National Academy Of Sciences Of The United States Of America (PNAS). 2013. DOI : 10.1073/pnas.1315654110.

One-pot total chemical synthesis of human α-synuclein

B. FauvetS. M. ButterfieldJ. FuksA. BrikH. A. Lashuel

Chemical Communications (ChemComm). 2013. DOI : 10.1039/c3cc45353g.

Parkin depletion delays motor decline dose-dependently without overtly affecting neuropathology in alpha-synuclein transgenic mice

M. FournierA. RouxJ. GarrigueM.-P. MurielP. Blanche  et al.

BMC neuroscience. 2013. DOI : 10.1186/1471-2202-14-135.

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

A. OueslatiB. L. SchneiderP. AebischerH. A. Lashuel

Proceedings Of The National Academy Of Sciences Of The United States Of America (PNAS). 2013. DOI : 10.1073/pnas.1309991110.

Reactive oxidative species enhance amyloid toxicity in APP/PS1 mouse neurons

B. YangX. SunH. LashuelY. Zhang

Neuroscience Bulletin. 2012. DOI : 10.1007/s12264-012-1239-1.

Characterization of Molecular Determinants of the Conformational Stability of Macrophage Migration Inhibitory Factor: Leucine 46 Hydrophobic Pocket

F. El-TurkB. FauvetA. AshrafiH. Ouertatani-SakouhiM.-K. Cho  et al.

PLoS ONE. 2012. DOI : 10.1371/journal.pone.0045024.

Discovery of a novel aggregation domain in the huntingtin protein: implications for the mechanisms of Htt aggregation and toxicity

Z.-M. WangH. A. Lashuel

Angewandte Chemie (International ed. in English). 2012. DOI : 10.1002/anie.201206561.

α-Synuclein in central nervous system and from erythrocytes, mammalian cells, and Escherichia coli exists predominantly as disordered monomer

B. FauvetM. K. MbefoM.-B. FaresC. DesobryS. Michael  et al.

Journal of Biological Chemistry. 2012. DOI : 10.1074/jbc.M111.318949.

Elucidating the role of C-terminal post-translational modifications using protein semisynthesis strategies: α-synuclein phosphorylation at tyrosine 125

M. HejjaouiS. ButterfieldB. FauvetF. VercruysseJ. Cui  et al.

Journal of the American Chemical Society. 2012. DOI : 10.1021/ja210866j.

Chemical strategies for controlling protein folding and elucidating the molecular mechanisms of amyloid formation and toxicity

S. ButterfieldM. HejjaouiB. FauvetL. AwadH. A. Lashuel

Journal of Molecular Biology. 2012. DOI : 10.1016/j.jmb.2012.01.051.

Measurement of intrinsic properties of amyloid fibrils by the peak force QNM method

J. AdamcikC. LaraI. UsovJ. S. JeongF. S. Ruggeri  et al.

Nanoscale. 2012. DOI : 10.1039/c2nr30768e.

Characterization of semisynthetic and naturally Nα-acetylated α-synuclein in vitro and in intact cells: implications for aggregation and cellular properties of α-synuclein

B. FauvetM.-B. FaresF. SamuelI. DikiyA. Tandon  et al.

Journal of Biological Chemistry. 2012. DOI : 10.1074/jbc.M112.383711.

Elucidating the role of post-translational modifications of alpha-synuclein using semisynthesis : phosphorylation at Tyrosine 125 and monoubiquitination at Lysine 6

M. Hejjaoui / H. Lashuel (Dir.)

Lausanne, EPFL, 2012. DOI : 10.5075/epfl-thesis-5494.

Discovery and Structure Activity Relationship of Small Molecule Inhibitors of Toxic β-Amyloid-42 Fibril Formation

H. KrothA. AnsaloniY. VariscoA. JanN. Sreenivasachary  et al.

Journal of Biological Chemistry. 2012. DOI : 10.1074/jbc.M112.357665.

The Size of the Proteasomal Substrate Determines Whether Its Degradation Will Be Mediated by Mono- or Polyubiquitylation

N. ShabekY. Herman-BachinskyS. BuchsbaumO. LewinsonM. Haj-Yahya  et al.

Molecular cell. 2012. DOI : 10.1016/j.molcel.2012.07.011.

Establishing the links between Aβ aggregation and cytotoxicity in vitro using biophysical approaches

A. JanH. A. Lashuel

Methods in molecular biology (Clifton, N.J.). 2012. DOI : 10.1007/978-1-61779-551-0_16.

Phosphorylation of α-synuclein is crucial in compensating for proteasomal dysfunction

H. S. ChoiH. LiewA. JangY.-M. KimH. Lashuel  et al.

Biochemical and biophysical research communications. 2012. DOI : 10.1016/j.bbrc.2012.06.159.

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

A. OueslatiK. E. PaleologouB. L. SchneiderP. AebischerH. A. Lashuel

The Journal of neuroscience : the official journal of the Society for Neuroscience. 2012. DOI : 10.1523/JNEUROSCI.3784-11.2012.

Chemical Biology of alpha-synuclein: The role post-translational modification in the pathogenesis of Parkinson's disease & related disorders

H. A. Lashuel

2011. 22nd American Peptide Symposium, San Diego, CA, Jun 25-30, 2011. p. 413 - 413.

Semisynthesis and Total Chemical Synthesis of alpha-synuclein to study Post-Translational Modifications in Health and Disease

B. FauvetS. M. ButterfieldM. HejjaouiD. OlschewskiM. Prudent  et al.

2011. 22nd American Peptide Symposium, San Diego, CA, Jun 25-30, 2011. p. 523 - 523.

Arab world needs its science diaspora

H. A. LashuelW. K. Al-Delaimy

Nature. 2011. DOI : 10.1038/472418d.

Novel chemical tools to facilitate the synthesis and control the folding and Self-assembly of amyloid-forming polypeptides

L. AwadN. JejelavaA. BrikH. Lashuel

2011. 22nd American Peptide Symposium, San Diego, CA, Jun 25-30, 2011. p. 430 - 430.

Method and compositions for inhibition of macrophage migration inhibitory factor (mif)

H. LashuelH. Ouertatani-sakouhi

WO2011066864 . 2011.

Phosphorylation of alpha-Synuclein at Y125 and S129 Alters Its Metal Binding Properties: Implications for Understanding the Role of alpha-Synuclein in the Pathogenesis of Parkinson's Disease and Related Disorders

Y. LuM. PrudentB. FauvetH. A. LashuelH. H. Girault

Acs Chemical Neuroscience. 2011. DOI : 10.1021/cn200074d.

Characterization and application of novel chemical tools to control folding and amyloid formation

N. Jejelava

2011

Amyloidogenic protein-membrane interactions: mechanistic insight from model systems

S. M. ButterfieldH. A. Lashuel

Angewandte Chemie (International ed. in English). 2010. DOI : 10.1002/anie.200906670.

Elucidating the Role of Quaternary Structure in Modulating Macrophage Migration Inhibitory Factor (MIF) Functions

F. El Turk / H. Lashuel (Dir.)

Lausanne, EPFL, 2010. DOI : 10.5075/epfl-thesis-4632.

Parkinson-related parkin reduces α-Synuclein phosphorylation in a gene transfer model

P. J. KhandelwalS. B. DumanisL. R. FengK. Maguire-ZeissG. Rebeck  et al.

Molecular neurodegeneration. 2010. DOI : 10.1186/1750-1326-5-47.

Phosphorylation of synucleins by members of the Polo-like kinase family

M. MbefoK. PaleologouA. BoucharabaA. OueslatiH. Schell  et al.

Journal of Biological Chemistry. 2010. DOI : 10.1074/jbc.M109.081950.

Stable  -Synuclein Oligomers Strongly Inhibit Chaperone Activity of the Hsp70 System by Weak Interactions with J-domain Co-chaperones

M.-P. HinaultA. F. H. CuendetR. U. H. MattooM. MensiG. Dietler  et al.

Journal of Biological Chemistry. 2010. DOI : 10.1074/jbc.M110.127753.

Role of post-translational modifications in modulating the structure, function and toxicity of alpha-synuclein: implications for Parkinson's disease pathogenesis and therapies

A. OueslatiM. FournierH. A. Lashuel

Progress in brain research. 2010. DOI : 10.1016/S0079-6123(10)83007-9.

An integrative in silico methodology for the identification of modulators of macrophage migration inhibitory factor (MIF) tautomerase activity

F. El TurkB. FauvetH. Ouertatani-SakouhiA. LugariS. Betzi  et al.

Bioorganic & medicinal chemistry. 2010. DOI : 10.1016/j.bmc.2010.05.010.

Identification and characterization of novel classes of macrophage migration inhibitory factor (MIF) inhibitors with distinct mechanisms of action

H. Ouertatani-SakouhiF. El-TurkB. FauvetM.-K. ChoD. Pinar Karpinar  et al.

Journal of Biological Chemistry. 2010. DOI : 10.1074/jbc.M110.113951.

Entacapone and tolcapone, two catechol O-methyltransferase inhibitors, block fibril formation of alpha-synuclein and beta-amyloid and protect against amyloid-induced toxicity

S. Di GiovanniS. EleuteriK. E. PaleologouG. YinM. Zweckstetter  et al.

Journal of Biological Chemistry. 2010. DOI : 10.1074/jbc.M109.080390.

Amyloid-beta aggregates cause alterations of astrocytic metabolic phenotype: impact on neuronal viability

I. AllamanM. GavilletM. BélangerT. LarocheD. Viertl  et al.

The Journal of neuroscience : the official journal of the Society for Neuroscience. 2010. DOI : 10.1523/JNEUROSCI.5098-09.2010.

The anti-Parkinsonian drug selegiline delays the nucleation phase of α-synuclein aggregation leading to the formation of nontoxic species

C. A. BragaC. FollmerF. L. PalhanoE. KhattarM. S. Freitas  et al.

Journal of Molecular Biology. 2010. DOI : 10.1016/j.jmb.2010.10.027.

Small Molecule Based Approaches to Inhibit Macrophage Migration Inhibitory Factor (MIF) Activities and Elucidate its Role in Health and Disease

H. Ouertatani-Sakouhi / H. Lashuel (Dir.)

Lausanne, EPFL, 2010. DOI : 10.5075/epfl-thesis-4633.

Phosphorylation at S87 is enhanced in synucleinopathies, inhibits alpha-synuclein oligomerization, and influences synuclein-membrane interactions

K. E. PaleologouA. OueslatiG. ShakkedC. C. RospigliosiH.-Y. Kim  et al.

The Journal of neuroscience : the official journal of the Society for Neuroscience. 2010. DOI : 10.1523/JNEUROSCI.5922-09.2010.

Preparation and characterization of toxic Abeta aggregates for structural and functional studies in Alzheimer's disease research

A. JanD. M. HartleyH. A. Lashuel

Nature protocols. 2010. DOI : 10.1038/nprot.2010.72.

Kinetic-based high-throughput screening assay to discover novel classes of macrophage migration inhibitory factor inhibitors

H. Ouertatani-SakouhiM. LiuF. El-TurkG. D. CunyM. A. Glicksman  et al.

Journal of biomolecular screening. 2010. DOI : 10.1177/1087057110363825.

Nucleation Dependent Polymerization of Amyloid-ß (Aß) as an Important Determinant of Aß Amyloid Formation and Neurotoxicity : Implications for the Pathogenesis of Alzheimer's Disease and Design of Therapies

M. A. Jan Qureshi / H. Lashuel (Dir.)

Lausanne, EPFL, 2010. DOI : 10.5075/epfl-thesis-4773.

Amyloids go genomic: insights regarding the sequence determinants of prion formation from genome-wide studies

H. A. LashuelR. V. Pappu

Chembiochem : a European journal of chemical biology. 2009. DOI : 10.1002/cbic.200900373.

Dissecting the mechanisms of tissue transglutaminase-induced cross-linking of alpha-synuclein: implications for the pathogenesis of Parkinson disease

A. W. SchmidD. ChiappeV. PignatV. GrimmingerI. Hang  et al.

Journal of Biological Chemistry. 2009. DOI : 10.1074/jbc.M809067200.

Structural properties of pore-forming oligomers of alpha-synuclein

H. Y. KimM. K. ChoA. KumarE. MaierC. Siebenharr  et al.

Journal of the American Chemical Society. 2009. DOI : 10.1021/ja9077599.

Switch-peptides as folding precursors in self-assembling peptides and amyloid fibrillogenesis

M. S. CamusR. MimnaA. SchmidA. ChandravarkarG. Tuchscherer  et al.

Advances in experimental medicine and biology. 2009. DOI : 10.1007/978-0-387-73657-0_126.

Highly efficient and chemoselective peptide ubiquitylation

K. S. Ajish KumarM. Haj-YahyaD. OlschewskiH. A. LashuelA. Brik

Angewandte Chemie (International ed. in English). 2009. DOI : 10.1002/anie.200902936.

A new class of isothiocyanate-based irreversible inhibitors of macrophage migration inhibitory factor

H. Ouertatani-SakouhiF. El-TurkB. FauvetT. RogerD. Le Roy  et al.

Biochemistry. 2009. DOI : 10.1021/bi900957e.

E46K Parkinson's-linked mutation enhances C-terminal-to-N-terminal contacts in alpha-synuclein

C. C. RospigliosiS. McClendonA. W. SchmidT. F. RamlallP. Barré  et al.

Journal of Molecular Biology. 2009. DOI : 10.1016/j.jmb.2009.03.065.

Parkin deficiency delays motor decline and disease manifestation in a mouse model of synucleinopathy

M. FournierJ. VitteJ. GarrigueD. LanguiJ.-P. Dullin  et al.

PloS One. 2009. DOI : 10.1371/journal.pone.0006629.

The role of post-translational modification (phosphorylation) in modulating alpha-synuclein, structure, aggregation and toxicity

H. A. Lashuel

2009. 4th European-Society-for-Neurochemistry Conference on Advances in Molecular Mechanisms of Neurological Disorders, Leipzig, GERMANY, Jul 11-14, 2009. p. 61 - 61.

Structure and function of the molecular chaperone Hsp104 from yeast

V. Grimminger-MarquardtH. A. Lashuel

Biopolymers. 2009. DOI : 10.1002/bip.21301.

Amyloid-Beta Modifies Astrocytic Metabolic Phenotype

I. AllamanM. GavilletM. BelangerT. LarocheD. Viertl  et al.

22nd Biennial Meeting of the International-Society-of-Neurochemistry/Asian-Pacific-Society-for-Neurochemistry, Busan, SOUTH KOREA, Aug 23-29, 2009.

Apomorphine inhibitors of amyloid-beta (abeta) fibril formation and their use in amyloidosis based disease

H. A. LashuelD. E. Callaway

US2008096909 ; US2003187011 . 2008.

Phosphorylation at Ser-129 but not the phosphomimics S129E/D inhibits the fibrillation of alpha-synuclein

K. E. PaleologouA. W. SchmidC. C. RospigliosiH.-Y. KimG. R. Lamberto  et al.

Journal of Biological Chemistry. 2008. DOI : 10.1074/jbc.M800747200.

Switch-peptides: design and characterization of controllable super-amyloid-forming host-guest peptides as tools for identifying anti-amyloid agents

M.-S. CamusS. Dos SantosA. ChandravarkarB. MandalA. W. Schmid  et al.

Chembiochem : a European journal of chemical biology. 2008. DOI : 10.1002/cbic.200800245.

Hsp104 targets multiple intermediates on the amyloid pathway and suppresses the seeding capacity of Abeta fibrils and protofibrils

M. ArimonV. GrimmingerF. SanzH. A. Lashuel

Journal of Molecular Biology. 2008. DOI : 10.1016/j.jmb.2008.09.063.

Inhibition of alpha-synuclein fibrillization by dopamine is mediated by interactions with five C-terminal residues and with E83 in the NAC region

F. E. HerreraA. ChesiK. E. PaleologouA. SchmidA. Munoz  et al.

PloS One. 2008. DOI : 10.1371/journal.pone.0003394.

Switch peptide via Staudinger reaction

N. NepomniaschiyV. GrimmingerA. CohenS. DiGiovanniH. A. Lashuel  et al.

Organic Letters. 2008. DOI : 10.1021/ol802268e.

The conformational flexibility of the carboxy terminal residues 105-114 is a key modulator of the catalytic activity and stability of macrophage migration inhibitory factor

F. El-TurkM. CascellaH. Ouertatani-SakouhiR. L. NarayananL. Leng  et al.

Biochemistry. 2008. DOI : 10.1021/bi800603x.

The ratio of monomeric to aggregated forms of Abeta40 and Abeta42 is an important determinant of amyloid-beta aggregation, fibrillogenesis, and toxicity

A. JanO. GokceR. Luthi-CarterH. A. Lashuel

Journal of Biological Chemistry. 2008. DOI : 10.1074/jbc.M803159200.

Hsp104 antagonizes alpha-synuclein aggregation and reduces dopaminergic degeneration in a rat model of Parkinson disease

C. Lo BiancoJ. ShorterE. RégulierH. LashuelT. Iwatsubo  et al.

The Journal of clinical investigation. 2008. DOI : 10.1172/JCI35781.

Disruption of amyloid-derived peptide assemblies through the controlled induction of a beta-sheet to alpha-helix transformation: application of the switch concept

R. MimnaM.-S. CamusA. SchmidG. TuchschererH. A. Lashuel  et al.

Angewandte Chemie International Edition. 2007. DOI : 10.1002/anie.200603681.

The impact of the E46K mutation on the properties of alpha-synuclein in its monomeric and oligomeric states

R. A. FredenburgC. RospigliosiR. K. MerayJ. C. KesslerH. A. Lashuel  et al.

Biochemistry. 2007. DOI : 10.1021/bi7000246.

Dopamine affects the stability, hydration, and packing of protofibrils and fibrils of the wild type and variants of alpha-synuclein

C. FollmerL. RomãoC. M. EinsiedlerT. C. R. PortoF. A. Lara  et al.

Biochemistry. 2007. DOI : 10.1021/bi061871+.

Branched KLVFF tetramers strongly potentiate inhibition of beta-amyloid aggregation

S. M. ChafekarH. MaldaM. MerkxE. W. MeijerD. Viertl  et al.

Chembiochem : a European journal of chemical biology. 2007. DOI : 10.1002/cbic.200700338.

Switch-peptides as folding precursors in self-assembling peptides and amyloid fibrillogenesis

G. TuchschererA. ChandravarkarM.-S. CamusJ. BerardK. Murat  et al.

Biopolymers. 2007. DOI : 10.1002/bip.20663.

A century-old debate on protein aggregation and neurodegeneration enters the clinic

P. T. LansburyH. A. Lashuel

Nature. 2006. DOI : 10.1038/nature05290.

Are amyloid diseases caused by protein aggregates that mimic bacterial pore-forming toxins?

H. A. LashuelP. T. Lansbury

Quarterly reviews of biophysics. 2006. DOI : 10.1017/S0033583506004422.

Rescuing defective vesicular trafficking protects against alpha-synuclein toxicity in cellular and animal models of Parkinson's disease

H. A. LashuelH. Hirling

ACS chemical biology. 2006. DOI : 10.1021/cb600331e.

Switch-peptides: from conformational studies to Alzheimer's disease

L. SaucedeS. Dos SantosA. ChandravarkarB. MandalR. Mimna  et al.

CHIMIA. 2006. DOI : 10.2533/000942906777674921.

Islam: governments need to reform education and build a scientific culture

H. A. LashuelN. Zawia

Nature. 2006. DOI : 10.1038/444545a.

The materials science of protein aggregation

D. L. CoxH. A. LashuelK. Y. C. LeeR. R. R. Singh

MRS Bulletin. 2005. DOI : 10.1557/mrs2005.123.

Amyloid fibril formation by macrophage migration inhibitory factor

H. A. LashuelB. AljabariE. M. SigurdssonC. N. MetzL. Leng  et al.

Biochemical and biophysical research communications. 2005. DOI : 10.1016/j.bbrc.2005.10.040.

Lead (Pb) exposure and its effect on APP proteolysis and Abeta aggregation

M. R. BashaM. MuraliH. K. SiddiqiK. GhosalO. K. Siddiqi  et al.

The FASEB journal : official publication of the Federation of American Societies for Experimental Biology. 2005. DOI : 10.1096/fj.05-4375fje.

In vitro preparation of prefibrillar intermediates of amyloid-beta and alpha-synuclein

H. A. LashuelD. Grillo-Bosch

Methods in molecular biology (Clifton, N.J.). 2005. DOI : 10.1385/1-59259-874-9:019.

Molecular electron microscopy approaches to elucidating the mechanisms of protein fibrillogenesis

H. A. LashuelJ. S. Wall

Methods in molecular biology (Clifton, N.J.). 2005. DOI : 10.1385/1-59259-874-9:081.

Membrane permeabilization: a common mechanism in protein-misfolding diseases

H. A. Lashuel

Science of aging knowledge environment : SAGE KE. 2005. DOI : 10.1126/sageke.2005.38.pe28.

From hexamer to amyloid: marginal stability of apolipoprotein SAA2.2 leads to in vitro fibril formation at physiological temperature

L. WangH. A. LashuelW. Colón

Amyloid : the international journal of experimental and clinical investigation : the official journal of the International Society of Amyloidosis. 2005. DOI : 10.1080/13506120500223084.

Production and characterization of astrocyte-derived human apolipoprotein E isoforms from immortalized astrocytes and their interactions with amyloid-beta

M. MorikawaJ. D. FryerP. M. SullivanE. A. ChristopherS. E. Wahrle  et al.

Neurobiology of disease. 2005. DOI : 10.1016/j.nbd.2004.11.005.

Quaternary structure, protein dynamics, and synaptic function of SAP97 controlled by L27 domain interactions

T. NakagawaK. FutaiH. A. LashuelI. LoK. Okamoto  et al.

Neuron. 2004. DOI : 10.1016/j.neuron.2004.10.012.

Interactions among alpha-synuclein, dopamine, and biomembranes: some clues for understanding neurodegeneration in Parkinson's disease

J.-C. RochetT. F. OuteiroK. A. ConwayT. T. DingM. J. Volles  et al.

Journal of molecular neuroscience : MN. 2004. DOI : 10.1385/JMN:23:1-2:023.

Apomorphine inhibitors of amyloid-beta (abeta) fibril formation and their use in amyloidosis based disease

H. A. LashuelD. E. Callaway

WO03053356 ; AU2002357911 ; AU2002357911 ; WO03053356 ; CA2479263 . 2003.

Hydration and packing are crucial to amyloidogenesis as revealed by pressure studies on transthyretin variants that either protect or worsen amyloid disease

A. D. Ferrão-GonzalesL. PalmieriM. ValoryJ. L. SilvaH. Lashuel  et al.

Journal of Molecular Biology. 2003. DOI : 10.1016/S0022-2836(03)00368-1.

Dissociation of amyloid fibrils of alpha-synuclein and transthyretin by pressure reveals their reversible nature and the formation of water-excluded cavities

D. FoguelM. C. SuarezA. D. Ferrão-GonzalesT. C. R. PortoL. Palmieri  et al.

Proceedings Of The National Academy Of Sciences Of The United States Of America (PNAS). 2003. DOI : 10.1073/pnas.1734009100.

Mixtures of wild-type and a pathogenic (E22G) form of Abeta40 in vitro accumulate protofibrils, including amyloid pores

H. A. LashuelD. M. HartleyB. M. PetreJ. S. WallM. N. Simon  et al.

Journal of Molecular Biology. 2003. DOI : 10.1016/S0022-2836(03)00927-6.

Discovery of inhibitors that elucidate the role of UCH-L1 activity in the H1299 lung cancer cell line

Y. LiuH. A. LashuelS. ChoiX. XingA. Case  et al.

Chemistry & biology. 2003. DOI : 10.1016/j.chembiol.2003.08.010.

Abeta protofibrils possess a stable core structure resistant to hydrogen exchange

I. KheterpalH. A. LashuelD. M. HartleyT. WalzP. T. Lansbury  et al.

Biochemistry. 2003. DOI : 10.1021/bi0357816.

hA molecular switch in amyloid assembly: Met35 and amyloid beta-protein oligomerization

G. BitanB. TarusS. S. VollersH. A. LashuelM. M. Condron  et al.

Journal of the American Chemical Society. 2003. DOI : 10.1021/ja0349296.

New class of inhibitors of amyloid-beta fibril formation. Implications for the mechanism of pathogenesis in Alzheimer's disease

H. A. LashuelD. M. HartleyD. BalakhanehA. AggarwalS. Teichberg  et al.

Journal of Biological Chemistry. 2002. DOI : 10.1074/jbc.M206593200.

The UCH-L1 gene encodes two opposing enzymatic activities that affect alpha-synuclein degradation and Parkinson's disease susceptibility

Y. LiuL. FallonH. A. LashuelZ. LiuP. T. Lansbury

Cell. 2002. DOI : 10.1016/S0092-8674(02)01012-7.

Murine apolipoprotein serum amyloid A in solution forms a hexamer containing a central channel

L. WangH. A. LashuelT. WalzW. Colon

Proceedings Of The National Academy Of Sciences Of The United States Of America (PNAS). 2002. DOI : 10.1073/pnas.252508399.

Neurodegenerative disease: amyloid pores from pathogenic mutations

H. A. LashuelD. HartleyB. M. PetreT. WalzP. T. Lansbury

Nature. 2002. DOI : 10.1038/418291a.

Alpha-synuclein, especially the Parkinson's disease-associated mutants, forms pore-like annular and tubular protofibrils

H. A. LashuelB. M. PetreJ. WallM. SimonR. J. Nowak  et al.

Journal of Molecular Biology. 2002. DOI : 10.1016/S0022-2836(02)00735-0.

Synthesis, structure, and activity of diclofenac analogues as transthyretin amyloid fibril formation inhibitors

V. B. OzaC. SmithP. RamanE. K. KoepfH. A. Lashuel  et al.

Journal of medicinal chemistry. 2002. DOI : 10.1021/jm010257n.

Protofilaments, filaments, ribbons, and fibrils from peptidomimetic self-assembly: Implications for amyloid fibril formation and materials science

H. A. LashuelS. R. LaBrenzL. WooL. C. SerpellJ. W. Kelly

Journal of the American Chemical Society. 2000. DOI : 10.1021/ja9937831.

Nuclear import factors importin alpha and importin beta undergo mutually induced conformational changes upon association

G. CingolaniH. A. LashuelL. GeraceC. W. Müller

FEBS letters. 2000. DOI : 10.1016/S0014-5793(00)02154-2.

A glimpse of a possible amyloidogenic intermediate of transthyretin

K. LiuH. S. ChoH. A. LashuelJ. W. KellyD. E. Wemmer

Nature structural biology. 2000. DOI : 10.1038/78980.

The nucleation of monomeric parallel beta-sheet-like structures and their self-assembly in aqueous solution

P. ChitnumsubW. R. FioriH. A. LashuelH. DiazJ. W. Kelly

Bioorganic & medicinal chemistry. 1999. DOI : 10.1016/S0968-0896(98)00222-3.

The most pathogenic transthyretin variant, L55P, forms amyloid fibrils under acidic conditions and protofilaments under physiological conditions

H. A. LashuelC. WurthL. WooJ. W. Kelly

Biochemistry. 1999. DOI : 10.1021/bi991021c.

Characterization of the transthyretin acid denaturation pathways by analytical ultracentrifugation: implications for wild-type, V30M, and L55P amyloid fibril formation

H. A. LashuelZ. LaiJ. W. Kelly

Biochemistry. 1999. DOI : 10.1021/bi981876+.

Association between the first two immunoglobulin-like domains of the neural cell adhesion molecule N-CAM

A. R. AtkinsM. J. OsborneH. A. LashuelG. M. EdelmanP. E. Wright  et al.

FEBS letters. 1999. DOI : 10.1016/S0014-5793(99)00554-2.

Comparative characterization of a wild type and transmembrane domain-deleted fatty acid amide hydrolase: identification of the transmembrane domain as a site for oligomerization

M. P. PatricelliH. A. LashuelD. K. GiangJ. W. KellyB. F. Cravatt

Biochemistry. 1998. DOI : 10.1021/bi981733n.

Inhibiting transthyretin conformational changes that lead to amyloid fibril formation

S. A. PetersonT. KlabundeH. A. LashuelH. PurkeyJ. C. Sacchettini  et al.

Proceedings Of The National Academy Of Sciences Of The United States Of America (PNAS). 1998. DOI : 10.1073/pnas.95.22.12956.

Recombinant human retinol-binding protein refolding, native disulfide formation, and characterization

Y. XieH. A. LashuelG. J. MiroyS. DiklerJ. W. Kelly

Protein expression and purification. 1998. DOI : 10.1006/prep.1998.0944.

Anti-amyloidogenic agents

G. J. MiroyJ. W. KellyZ. LaiH. A. LashuelS. A. Peterson

WO9827972 ; WO9827972 ; AU5727798 ; WO9827972 . 1998.

Complete inhibition of Cdk/cyclin by one molecule of p21(Cip1)

L. HengstU. GöpfertH. A. LashuelS. I. Reed

Genes & development. 1998. DOI : 10.1101/gad.12.24.3882.

Guanidine hydrochloride-induced denaturation and refolding of transthyretin exhibits a marked hysteresis: equilibria with high kinetic barriers

Z. LaiJ. McCullochH. A. LashuelJ. W. Kelly

Biochemistry. 1997. DOI : 10.1021/bi963195p.

Transthyretin quaternary and tertiary structural changes facilitate misassembly into amyloid

J. W. KellyW. ColonZ. LaiH. A. LashuelJ. McCulloch  et al.

Advances in protein chemistry. 1997. DOI : 10.1016/S0065-3233(08)60321-6.

Oligomerization properties of GCN4 leucine zipper e and g position mutants

X. ZengH. ZhuH. A. LashuelJ. C. Hu

Protein science : a publication of the Protein Society. 1997. DOI : 10.1002/pro.5560061016.

Inhibiting transthyretin amyloid fibril formation via protein stabilization

G. J. MiroyZ. LaiH. A. LashuelS. A. PetersonC. Strang  et al.

Proceedings Of The National Academy Of Sciences Of The United States Of America (PNAS). 1996. DOI : 10.1073/pnas.93.26.15051.

A Site-Specific Organometallic Approach for Installing Tyrosine Phosphorylation Mimics to Decipher the Role of Phosphorylation in Alpha-Synuclein (aSyn) Aggregation and Seeding

S. MandalX. LinA. V. GemelliM. SinghA.-L. Mahul Mellier  et al.

2025

A Microfluidic Platform for Whole-Membrane Integrity Profiling in Live Neuronal Cells

C. GuiducciT. J. RyserA. KricheneN. MarchiF. R. Espinal  et al.

2025

Defined human tri-lineage brain microtissues

T. UenakaS. JungI. KumarK. VodehnalM. Rastogi  et al.

2025

Self-driving microscopy detects the onset of protein aggregation and enables intelligent Brillouin imaging

K. A. IbrahimC. CathalaC. BevilacquaL. FelettiR. Prevedel  et al.

Nature Communications. 2025. DOI : 10.1038/s41467-025-60912-0.

Mapping the Structural Landscape of Amyloid Fibrils to Guide Polymorph-Specific Therapeutics

A. SadekB. E. CorreiaH. A. Lashuel

2025

Huntingtin inclusion bodies have distinct immunophenotypes and ubiquitination profiles in the Huntington’s disease human cerebral cortex

M. E. V. SwansonA. Y. S. TanL. J. TippettC. TurnerM. A. Curtis  et al.

Scientific Reports. 2025. DOI : 10.1038/s41598-025-00465-w.

Amyotrophic lateral sclerosis caused by TARDBP mutations: from genetics to TDP-43 proteinopathy

R. BalendraJ. SreedharanM. HalleggerR. LuisierH. A. Lashuel  et al.

The Lancet Neurology. 2025. DOI : 10.1016/S1474-4422(25)00109-7.

Alpha-synuclein seed amplification assays: Data sharing, standardization needed for clinical use

H. A. LashuelD. J. SurmeierT. SimuniK. MerchantB. Caughey  et al.

Science Advances. 2025. DOI : 10.1126/sciadv.adt7195.

<i>Multi‐Targeting</i> Makrozyklische Peptide als Nanomolare Inhibitoren der Selbst‐ und Kreuznukleation der Amyloiden Selbstassemblierung von α‐Synuclein

S. HornungD. P. VoglD. NaltsasB. D. VoltaM. Ballmann  et al.

Angewandte Chemie. 2025. DOI : 10.1002/ange.202422834.

Multi-Targeting Macrocyclic Peptides as Nanomolar Inhibitors of Self- and Cross-Seeded Amyloid Self-Assembly of α-Synuclein

S. HornungD. P. VoglD. NaltsasB. D. VoltaM. Ballmann  et al.

ANGEWANDTE CHEMIE-INTERNATIONAL EDITION. 2025. DOI : 10.1002/anie.202422834.

Qatar national cancer care and research: pioneering strategies for global health excellence

M. B. H. Al-ThaniM. SubramanianN. HalabiS. Bujassoum Al BaderJ. Shan  et al.

The Lancet Oncology. 2025. DOI : 10.1016/s1470-2045(25)00132-9.

Uses of aerolysin nanopores

C. CaoM. Dal PeraroH. Lashuel

WO2025003492 . 2025.

Intelligent and Self-Driving Microscopy of Protein Aggregation in Neurodegenerative Diseases

K. Ibrahim / A. RadenovicH. Lashuel (Dir.)

Lausanne, EPFL, 2025. DOI : 10.5075/epfl-thesis-11337.

Nanoplasmonic Infrared Microarray Sensor Enabling Structural Protein Biomarker-Based Drug Screening for Neurodegenerative Diseases

D. KavungalE. MorroS. T. KumarB. DagliH. Lashuel  et al.

Advanced science (Weinheim, Baden-Wurttemberg, Germany). 2025. DOI : 10.1002/advs.202500320.

Nanoplasmonic infrared biosensors enabling detection of misfolded protein biomarkers and drug screening for neurodegenerative diseases

D. Kavungal / H. AltugH. Lashuel (Dir.)

Lausanne, EPFL, 2025. DOI : 10.5075/epfl-thesis-10478.

Towards Conformational Targeting of Alpha-Synuclein Fibrils

A. S. S. Z. M. Sadek / B. E. Ferreira De Sousa CorreiaH. Lashuel (Dir.)

Lausanne, EPFL, 2025. DOI : 10.5075/epfl-thesis-10710.

Mouse α-synuclein fibrils are structurally and functionally distinct from human fibrils associated with Lewy body diseases

A. SokratianY. ZhouM. TatliK. J. BurbidgeE. Xu  et al.

Science advances. 2024. DOI : 10.1126/sciadv.adq3539.

Research Priorities on the Role of α-Synuclein in Parkinson's Disease Pathogenesis

J. BurréR. H. EdwardsG. HallidayA. E. LangH. A. Lashuel  et al.

Movement disorders : official journal of the Movement Disorder Society. 2024. DOI : 10.1002/mds.29897.

A Versatile Method for Site-Specific Chemical Installation of Aromatic Posttranslational Modification Analogs into Proteins

X. LinS. MandalR. V. NithunR. KollaB. Bouri  et al.

Journal of the American Chemical Society. 2024. DOI : 10.1021/jacs.4c08416.

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

Z. ZhangC. GehinL. A. AbriataM. Dal PeraroH. Lashuel

Acs Chemical Neuroscience. 2024. DOI : 10.1021/acschemneuro.4c00091.

Mouse α-synuclein fibrils are structurally and functionally distinct from human fibrils associated with Lewy body diseases

A. SokratianY. ZhouM. TatliK. J. BurbidgeE. Xu  et al.

2024

Post-translational glycosylation diminishes α-synuclein pathology formation

M. PrattH. Lashuel

Nature Chemical Biology. 2024. DOI : 10.1038/s41589-024-01553-0.

O-GlcNAc forces an α-synuclein amyloid strain with notably diminished seeding and pathology

A. T. BalanaA.-L. Mahul-MellierB. A. NguyenM. HorvathA. Javed  et al.

Nature Chemical Biology. 2024. DOI : 10.1038/s41589-024-01551-2.

Development and validation of an expanded antibody toolset that captures alpha-synuclein pathological diversity in Lewy body diseases (vol 10, 19, 2024)

M. F. AltayS. T. KumarJ. BurtscherS. JagannathC. Strand  et al.

NPJ PARKINSONS DISEASE. 2024. DOI : 10.1038/s41531-024-00634-0.

Targeting TDP-43 Proteinopathies in Neurodegeneration by its Native-State Stabilization

L. Yang / H. Lashuel (Dir.)

Lausanne, EPFL, 2024. DOI : 10.5075/epfl-thesis-10555.

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

G. LimorenkoM. TatliR. KollaS. NazarovM.-T. Weil  et al.

Nature Communications. 2024. DOI : 10.1038/s41467-024-48976-w.

Deep learning augmented nanoplasmonic infrared sensor for structural protein biomarker-based detection of neurodegenerative diseases

D. KavungalP. MagalhãesS. T. KumarR. KollaH. Lashuel  et al.

2024. 21 Nanoscale Imaging, Sensing, and Actuation for Biomedical Applications, San Francisco, United States, 2024-01-28 - 2024-01-28. DOI : 10.1117/12.3003239.

Investigating the intra-molecular and inter-molecular effects of post-translational modifications on intrinsically disordered protein regions and structured protein regions

Z. Zhang / M. Dal PeraroH. Lashuel (Dir.)

Lausanne, EPFL, 2024. DOI : 10.5075/epfl-thesis-10530.

Effective Inhibition of TDP-43 Aggregation by Native State Stabilization

L. YangY. JasiqiA. ZettorO. VadasJ. Chiaravalli  et al.

Angewandte Chemie International Edition. 2024. DOI : 10.1002/anie.202314587.

Transactive response dna-binding protein 43kda (tdp-43) mutants and uses thereof

L. YangH. Lashuel

WO2024223615 . 2024.

Exploring the therapeutic potential of Huntingtin native state stabilization through targeting its interacting partners

E. Morro / H. Lashuel (Dir.)

Lausanne, EPFL, 2024. DOI : 10.5075/epfl-thesis-10915.

Method of preparation of amyloidogenic protein aggregates and uses thereof

G. LimorenkoH. Lashuel

WO2024094597 . 2024.

Dielectrophoretic Manipulation of Biological Species: Novel Microfluidic Approaches to Study Cell-Cell Interactions and the Role of Alpha-Synuclein in Neurodegeneration

T. J. Ryser / C. GuiducciH. Lashuel (Dir.)

Lausanne, EPFL, 2024. DOI : 10.5075/epfl-thesis-10597.

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

L. YangY. JasiqiH. Lashuel

Acs Chemical Neuroscience. 2023. DOI : 10.1021/acschemneuro.3c00691.

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

C. CaoP. MagalhaesL. F. KrappJ. F. B. JuarezS. F. Mayer  et al.

Acs Nano. 2023. DOI : 10.1021/acsnano.3c08623.

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

M. F. AltayS. T. KumarJ. BurtscherS. JagannathC. Strand  et al.

Npj Parkinsons Disease. 2023. DOI : 10.1038/s41531-023-00604-y.

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

G. LimorenkoM. TatliR. KollaS. NazarovM.-T. Weil  et al.

Nature Communications. 2023. DOI : 10.1038/s41467-023-39314-7.

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

Y. SinghC. TrautweinJ. RomaniM. S. S. SalkerP. H. H. Neckel  et al.

Molecular Neurodegeneration. 2023. DOI : 10.1186/s13024-023-00628-1.

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

D. KavungalP. MagalhaesS. T. KumarR. KollaH. A. Lashuel  et al.

Science Advances. 2023. DOI : 10.1126/sciadv.adg9644.

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

S. T. KumarS. NazarovS. PortaN. MaharjanU. Cendrowska  et al.

Nature Neuroscience. 2023. DOI : 10.1038/s41593-023-01341-4.

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

E. LoseroS. JagannathM. PezzoliV. GoblotH. Babashah  et al.

Scientific Reports. 2023. DOI : 10.1038/s41598-023-32235-x.

Deconstructing and Reconstructing the Complexity of Tau pathology

G. Limorenko / H. Lashuel (Dir.)

Lausanne, EPFL, 2023. DOI : 10.5075/epfl-thesis-9911.

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

M. F. AltayA. K. L. LiuJ. L. HoltonL. ParkkinenH. A. Lashuel

Acta Neuropathologica Communications. 2022. DOI : 10.1186/s40478-022-01468-8.

Revisiting the specificity and ability of phospho-S129 antibodies to capture alpha-synuclein biochemical and pathological diversity

H. A. LashuelA.-L. Mahul-MellierS. NovelloR. N. HegdeY. Jasiqi  et al.

Npj Parkinsons Disease. 2022. DOI : 10.1038/s41531-022-00388-7.

N-terminal mutant huntingtin deposition correlates with CAG repeat length and symptom onset, but not neuronal loss in Huntington's disease

F. E. LayburnA. Y. S. TanN. F. MehrabiM. A. CurtisL. J. Tippett  et al.

Neurobiology Of Disease. 2022. DOI : 10.1016/j.nbd.2022.105884.

Pathological substrate of memory impairment in multiple system atrophy

Y. MikiK. TanjiK. ShinnaiM. T. TanakaF. Altay  et al.

Neuropathology And Applied Neurobiology. 2022. DOI : 10.1111/nan.12844.

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

D. NaltsasS. HornungD. VoglJ. LudwigA. Molenaar  et al.

2022.

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

P. MagalhaesH. A. Lashuel

Npj Parkinsons Disease. 2022. DOI : 10.1038/s41531-022-00357-0.

On-Demand Nanoliter Sampling Probe for the Collection of Brain Fluid

J. TeixidorS. NovelloD. OrtizL. MeninH. A. Lashuel  et al.

Analytical Chemistry. 2022. DOI : 10.1021/acs.analchem.2c01577.

Structural Basis of Huntingtin Fibril Polymorphism Revealed by Cryogenic Electron Microscopy of Exon 1 HTT Fibrils

S. NazarovA. ChikiD. BoudeffaH. A. Lashuel

Journal Of The American Chemical Society. 2022. DOI : 10.1021/jacs.2c00509.

Remembering John Q Trojanowski, in his own words: A life dedicated to discovering building blocks and using them to build bridges of knowledge, collaboration, and discovery

H. A. Lashuel

Npj Parkinsons Disease. 2022. DOI : 10.1038/s41531-022-00310-1.

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

S. T. KumarA.-L. Mahul-MellierR. N. HegdeG. RiviereR. Moons  et al.

Science Advances. 2022. DOI : 10.1126/sciadv.abn0044.

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

B. SonustunM. F. AltayC. StrandK. EbanksG. Hondhamuni  et al.

Cells. 2022. DOI : 10.3390/cells11050906.

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

Z. ZhangA. ChikiC. GehinR. KollaL. A. Abriata  et al.

2022. p. 38 - 38. DOI : 10.1016/j.bpj.2021.11.2495.

An integrative approach to elucidate the mechanisms and dynamics of Huntingtin aggregation and inclusion formation in neuronal models of Huntington's Disease

N. A. D. Riguet / H. Lashuel (Dir.)

Lausanne, EPFL, 2022. DOI : 10.5075/epfl-thesis-9296.

Capturing the heterogeneity of alpha-synuclein pathology in synucleinopathies

M. F. Altay / H. Lashuel (Dir.)

Lausanne, EPFL, 2022. DOI : 10.5075/epfl-thesis-8480.

Towards elucidating the structural and cellular determinants of a-synuclein seeding and toxicity

S. Jagannath / H. Lashuel (Dir.)

Lausanne, EPFL, 2022. DOI : 10.5075/epfl-thesis-9365.

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

G. LimorenkoH. A. Lashuel

Chemical Society Reviews. 2022. DOI : 10.1039/d1cs00127b.

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

J. C. ShillcockJ. HastingsN. RiguetH. A. Lashuel

Computational and Structural Biotechnology Journal. 2022. DOI : 10.1016/j.csbj.2021.12.017.

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

L. PetriccaN. ChikiL. Hanna-El-DaherL. AeschbachR. Burai  et al.

Journal Of Parkinsons Disease. 2022. DOI : 10.3233/JPD-223285.

To target Tau pathologies, we must embrace and reconstruct their complexities

G. LimorenkoH. A. Lashuel

Neurobiology Of Disease. 2021. DOI : 10.1016/j.nbd.2021.105536.

Nuclear and cytoplasmic huntingtin inclusions exhibit distinct biochemical composition, interactome and ultrastructural properties

N. RiguetA.-L. Mahul-MellierN. MaharjanJ. BurtscherM. Croisier  et al.

Nature Communications. 2021. DOI : 10.1038/s41467-021-26684-z.

Fatal attraction-The role of hypoxia when alpha-synuclein gets intimate with mitochondria

J. BurtscherM. M. K. SyedM. A. KellerH. A. LashuelG. P. Millet

Neurobiology Of Aging. 2021. DOI : 10.1016/j.neurobiolaging.2021.07.017.

The Nt17 Domain and its Helical Conformation Regulate the Aggregation, Cellular Properties and Neurotoxicity of Mutant Huntingtin Exon 1

S. ViewegA.-L. Mahul MellierF. S. RuggeriN. RiguetS. M. Deguire  et al.

Journal of Molecular Biology. 2021. DOI : 10.1016/j.jmb.2021.167222.

Pharmacological characterization of mutant huntingtin aggregate-directed PET imaging tracer candidates

F. HerrmannM. HessmannS. SchaertlK. Berg-RosseburgC. J. Brown  et al.

Scientific Reports. 2021. DOI : 10.1038/s41598-021-97334-z.

Investigating Crosstalk Among PTMs Provides Novel Insight Into the Structural Basis Underlying the Differential Effects of Nt17 PTMs on Mutant Httex1 Aggregation

A. ChikiZ. ZhangK. RajasekharL. A. AbriataI. Rostami  et al.

Frontiers in Molecular Biosciences. 2021. DOI : 10.3389/fmolb.2021.686086.

Alpha-synuclein research: defining strategic moves in the battle against Parkinson's disease

L. M. A. OliveiraT. GasserR. EdwardsM. ZweckstetterR. Melki  et al.

Npj Parkinsons Disease. 2021. DOI : 10.1038/s41531-021-00203-9.

A New Chemoenzymatic Semisynthetic Approach Provides Insight into the Role of Phosphorylation beyond Exon1 of Huntingtin and Reveals N-Terminal Fragment Length-Dependent Distinct Mechanisms of Aggregation

R. KollaG. PushparathinamJ. RicciA. ReifI. Rostami  et al.

Journal of the American Chemical Society. 2021. DOI : 10.1021/jacs.1c03108.

Rethinking protein aggregation and drug discovery in neurodegenerative diseases: Why we need to embrace complexity?

H. Lashuel

Current Opinion in Chemical Biology. 2021. DOI : 10.1016/j.cbpa.2021.05.006.

Lewy body-associated proteins: Victims, instigators, or innocent bystanders? The case of AIMP2 and alpha-synuclein

H. A. LashuelS. Novello

Neurobiology of Disease. 2021. DOI : 10.1016/j.nbd.2021.105417.

Parkinson mice show functional and molecular changes in the gut long before motoric disease onset

M. GriesA. ChristmannS. SchulteM. WeylandS. Rommel  et al.

Molecular Neurodegeneration. 2021. DOI : 10.1186/s13024-021-00439-2.

Enforced dimerization between XBP1s and ATF6f enhances the protective effects of the UPR in models of neurodegeneration

R. L. VidalD. SepulvedaP. Troncoso-EscuderoP. Garcia-HuertaC. Gonzalez  et al.

Molecular Therapy. 2021. DOI : 10.1016/j.ymthe.2021.01.033.

Correlative light and electron microscopy suggests that mutant huntingtin dysregulates the endolysosomal pathway in presymptomatic Huntington's disease

Y. ZhouT. R. PeskettC. LandlesJ. B. WarnerK. Sathasivam  et al.

Acta Neuropathologica Communications. 2021. DOI : 10.1186/s40478-021-01172-z.

Alpha-Synuclein oligomerization and aggregation: All models are useful but only if we know what they model This is the reply to a comment "Alpha-synuclein oligomerization and aggregation: A model will always be a model" on the original article "Monitoring alpha-synuclein oligomerization and aggregation using bimolecular fluorescence complementation assays: What you see is not always what you get". The articles are accompanied by a Preface "How good are cellular models?".

H. A. Lashuel

Journal of Neurochemistry (JNC). 2021. DOI : 10.1111/jnc.15275.

Hypoxia Conditioning as a Promising Therapeutic Target in Parkinson's Disease?

J. BurtscherM. M. K. SyedH. A. LashuelG. P. Millet

Movement Disorders. 2021. DOI : 10.1002/mds.28544.

Reverse engineering Lewy bodies: how far have we come and how far can we go?

M. B. FaresS. JagannathH. Lashuel

Nature Reviews Neuroscience. 2021. DOI : 10.1038/s41583-020-00416-6.

Monitoring alpha-synuclein oligomerization and aggregation using bimolecular fluorescence complementation assays: What you see is not always what you get

B. FreyA. AlOkdaM. P. JacksonN. RiguetJ. A. Duce  et al.

Journal of Neurochemistry (JNC). 2021. DOI : 10.1111/jnc.15147.

Site-Specific Phosphorylation of Huntingtin Exon 1 Recombinant Proteins Enabled by the Discovery of Novel Kinases

A. ChikiJ. RicciR. HegdeL. A. AbriataA. Reif  et al.

Chembiochem. 2020. DOI : 10.1002/cbic.202000508.

How specific are the conformation-specific α-synuclein antibodies? Characterization and validation of 16 α-synuclein conformation-specific antibodies using well-characterized preparations of α-synuclein monomers, fibrils and oligomers with distinct structures and morphology

S. K. ThangarajS. JagannathC. FrancoisH. VandersticheleE. Stoops  et al.

Neurobiology of Disease. 2020. DOI : 10.1016/j.nbd.2020.105086.

TBK1 phosphorylates mutant Huntingtin and suppresses its aggregation and toxicity in Huntington's disease models

R. N. HegdeA. ChikiL. PetriccaP. MartufiN. Arbez  et al.

The EMBO Journal. 2020. DOI : 10.15252/embj.2020104671.

Half a century of amyloids: past, present and future

P. C. KeR. ZhouL. C. SerpellR. RiekT. P. J. Knowles  et al.

Chemical Society Reviews. 2020. DOI : 10.1039/C9CS00199A.

Do Lewy bodies contain alpha-synuclein fibrils? and Does it matter? A brief history and critical analysis of recent reports

H. A. Lashuel

Neurobiology Of Disease. 2020. DOI : 10.1016/j.nbd.2020.104876.

Phosphorylation of the overlooked tyrosine 310 regulates the structure, aggregation, and microtubule- and lipid-binding properties of Tau

N. Ait-BouziadA. ChikiG. LimorenkoS. XiaoD. Eliezer  et al.

Journal of Biological Chemistry. 2020. DOI : 10.1074/jbc.RA119.012517.

Extent of N-terminus exposure of monomeric alpha-synuclein determines its aggregation propensity

A. D. StephensM. ZacharopoulouR. MoonsG. FuscoN. Seetaloo  et al.

Nature Communications. 2020. DOI : 10.1038/s41467-020-16564-3.

Education and research are essential for lasting peace in Yemen

F. ZakhamO. VapalahtiH. A. Lashual

Lancet. 2020. DOI : 10.1016/S0140-6736(20)30162-8.

Unraveling the complexity of amyloid polymorphism using gold nanoparticles and cryo-EM

U. CendrowskaP. J. SilvaN. Ait-BouziadM. MuellerZ. P. Guven  et al.

Proceedings Of The National Academy Of Sciences Of The United States Of America (PNAS). 2020. DOI : 10.1073/pnas.1916176117.

The busy lives of academics have hidden costs — and universities must take better care of their faculty members

H. Lashuel

Nature Careers Community. 2020. DOI : 10.1038/d41586-020-00661-w.

A simple, versatile and robust centrifugation-based filtration protocol for the isolation and quantification of alpha-synuclein monomers, oligomers and fibrils: Towards improving experimental reproducibility in alpha-synuclein research

S. T. KumarS. DonzelliA. ChikiM. M. K. SyedH. A. Lashuel

Journal of Neurochemistry (JNC). 2020. DOI : 10.1111/jnc.14955.

The process of Lewy body formation, rather than simply α-synuclein fibrillization, is one of the major drivers of neurodegeneration

A.-L. Mahul-MellierJ. BurtscherN. MaharjanL. WeerensM. Croisier  et al.

Proceedings Of The National Academy Of Sciences Of The United States Of America (PNAS). 2020. DOI : 10.1073/pnas.1913904117.

Site-Specific Hyperphosphorylation Inhibits, Rather than Promotes, Tau Fibrillization, Seeding Capacity, and Its Microtubule Binding

M. Haj-YahyaP. GopinathK. RajasekharH. MirbahaM. I. Diamond  et al.

Angewandte Chemie International Edition. 2020. DOI : 10.1002/anie.201913001.

Ultrasensitive quantitative measurement of huntingtin phosphorylation at residue S13

C. CariuloM. VeraniP. MartufiR. IngenitoM. Finotto  et al.

Biochemical And Biophysical Research Communications. 2020. DOI : 10.1016/j.bbrc.2019.09.097.

What about faculty?

H. A. Lashuel

Elife. 2020. DOI : 10.7554/eLife.54551.

Gold nanoparticles as a new tool in amyloid studies

U. B. Cendrowska / F. StellacciH. Lashuel (Dir.)

Lausanne, EPFL, 2020. DOI : 10.5075/epfl-thesis-7471.

Pronounced α-synuclein pathology in a seeding-based mouse model is not sufficient to induce mitochondrial respiration deficits in the striatum and amygdala

J. BurtscherJ.-C. CopinC. SandiH. Lashuel

eNeuro. 2020. DOI : 10.1523/ENEURO.0110-20.2020.

Development of novel methods and tools to decipher the huntingtin post-translation modifications code

A. Chiki / H. Lashuel (Dir.)

Lausanne, EPFL, 2020. DOI : 10.5075/epfl-thesis-7537.

The Role of Post-translational Modifications on the Energy Landscape of Huntingtin N-Terminus

H. YalincaC. J. C. GehinV. OleinikovasH. A. LashuelF. L. Gervasio  et al.

Frontiers in Molecular Biosciences. 2019. DOI : 10.3389/fmolb.2019.00095.

Phospho-S129 Alpha-Synuclein Is Present in Human Plasma but Not in Cerebrospinal Fluid as Determined by an Ultrasensitive Immunoassay

C. CariuloP. MartufiM. VeraniL. AzzolliniG. Bruni  et al.

Frontiers in Neuroscience. 2019. DOI : 10.3389/fnins.2019.00889.

Investigation of alpha-synuclein post-translational modifications in idiopathic Parkinson's disease and multiple system atrophy

B. SonustunC. StrandS. FotiT. T. WarnerH. Lashuel  et al.

2019. 120th Meeting of the British-Neuropathological-Society (BNS) / Developmental Neuropathology Symposium, London, ENGLAND, Mar 06-08, 2019. p. 19 - 19.

Single Posttranslational Modifications in the Central Repeat Domains of Tau4 Impact its Aggregation and Tubulin Binding

D. EllmerM. BrehsM. Haj-YahyaH. A. LashuelC. F. W. Becker

Angewandte Chemie International Edition. 2019. DOI : 10.1002/anie.201805238.

alpha-Synuclein O-GlcNAcylation alters aggregation and toxicity, revealing certain residues as potential inhibitors of Parkinson's disease

P. M. LevineA. GalesicA. T. BalanaA.-L. Mahul-MellierM. X. Navarro  et al.

Proceedings Of The National Academy Of Sciences Of The United States Of America (PNAS). 2019. DOI : 10.1073/pnas.1808845116.

A method for preparing phfs-like tau aggregates

H. A. LashuelN. Ait-Bouziad

US11629175 ; US2021238242 ; EP3784687 ; WO2019207164 . 2019.

Exploring the role of post-translational modifications in regulating α-synuclein interactions by studying the effects of phosphorylation on nanobody binding

F. El TurkE. De GenstT. GuilliamsB. C. D. FauvetJ. Kiwi  et al.

Proteins Science. 2018. DOI : 10.1002/pro.3412.

Generation of Native, Untagged Huntingtin Exon1 Monomer and Fibrils Using a SUMO Fusion Strategy

A. ReifA. ChikiJ. RicciH. Lashuel

Journal of Visualized Experiments. 2018. DOI : 10.3791/57506.

Combined Multi-Plane Tomographic Phase Retrieval and Stochastic Optical Fluctuation Imaging for 4D Cell Microscopy

A. DesclouxK. GrußmayerE. BostanT. LukesA. Bouwens  et al.

Nature Photonics. 2018. DOI : 10.1038/s41566-018-0109-4.

Monomeric Huntingtin Exon 1 Has Similar Overall Structural Features for Wild-Type and Pathological Polyglutamine Lengths

J. B. Warner IVK. RuffP. Siong TanE. A. LemkeR. V. Pappu  et al.

Journal of the American Chemical Society. 2017. DOI : 10.1021/jacs.7b06659.

Sequence and structural determinants of Tau aggregation and seeding capacity: Implications for Neurofibrillary Tangle formation and Tau toxicity in Alzheimer's disease

N. Ait Bouziad / H. Lashuel (Dir.)

Lausanne, EPFL, 2017. DOI : 10.5075/epfl-thesis-7985.

Ganciclovir derivatives for modulating innate and adaptive immunity and for use in immunotherapy

R. BuraiH. A. LashuelV. MathurA. Wyss-Coray

US9809597 ; US2017050967 . 2017.

Human and eco-toxicological impacts of organometallic halide perovskites

R. I. Benmessaoud / L. ForróH. Lashuel (Dir.)

Lausanne, EPFL, 2017. DOI : 10.5075/epfl-thesis-7595.

Mutant Exon1 Huntingtin Aggregation is Regulated by T3 Phosphorylation-Induced Structural Changes and Crosstalk between T3 Phosphorylation and Acetylation at K6

A. ChikiS. M. DeGuireF. S. RuggeriD. SanfeliceA. Ansaloni  et al.

Angewandte Chemie (International ed. in English). 2017. DOI : 10.1002/anie.201611750.

The America I believe in

H. A. Lashuel

Science. 2017. DOI : 10.1126/science.355.6326.766.

Activation of the STING-dependent type I interferon response reduces microglial reactivity and neuroinflammation

V. MathusR. BuraiR. VestL. BonannoB. Lehallier  et al.

Neuron. 2017. DOI : 10.1016/j.neuron.2017.11.032.

Amyloid Single Cell Cytotoxicity Assays by Nanomotion Detection

F. RuggeriA.-L. MahulS. KasasH. LashuelG. Longo  et al.

Cell Death Discovery. 2017. DOI : 10.1038/cddiscovery.2017.53.

Polyglutamine expansion affects huntingtin conformation in multiple Huntington’s disease models

M. DaldinV. FodaleC. CariuloL. AzzolliniM. Verani  et al.

Scientific Reports. 2017. DOI : 10.1038/s41598-017-05336-7.

Membrane scission driven by the PROPPIN Atg18

N. GopaldassB. FauvetH. LashuelA. RouxA. Mayer

Embo Journal. 2017. DOI : 10.15252/embj.201796859.

The role of the polyglutamine and N-terminal domains in regulating the aggregation and structural properties of Huntingtin Exon 1

S. Vieweg / H. Lashuel (Dir.)

Lausanne, EPFL, 2017. DOI : 10.5075/epfl-thesis-7374.

The mechanism of sirtuin 2-mediated exacerbation of alpha-synuclein toxicity in models of Parkinson disease

R. M. de OliveiraH. Vicente MirandaL. FrancelleR. PinhoÉ. M. Szegö  et al.

PLoS Biology. 2017. DOI : 10.1371/journal.pbio.2000374.

Glycation potentiates α-synuclein-associated neurodegeneration in synucleinopathies

H. Vicente MirandaÉ. M. SzegoL. M. A. OliveiraC. BredaE. Darendelioglu  et al.

Brain : a journal of neurology. 2017. DOI : 10.1093/brain/awx056.

Polyglutamine Length Dependent Structural Properties and Phase Behavior of Huntingtin Exon 1

K. M. RuffJ. B. WarnerA. E. PoseyP. S. TanE. A. Lemke  et al.

2017. 58th Annual Meeting of the Biophysical-Society, San Francisco, CA, FEB 15-19, 2014. p. 511A - 511A. DOI : 10.1016/j.bpj.2016.11.2762.

A user's guide for α-synuclein biomarker studies in biological fluids: Perianalytical considerations

B. MollenhauerR. BatrlaO. El-AgnafD. R. GalaskoH. A. Lashuel  et al.

Movement Disorders. 2017. DOI : 10.1002/mds.27090.

Discovery and characterization of novel stable tau oligomeric complexes: Implications for the role of Tau/phospholipid interactions in regulating its functions in health and disease

N. Ait-BouziadG. LvA. L. Mahul-MellierS. XiaoG. Zorludemir  et al.

Nature Communications. 2017. DOI : 10.1038/s41467-017-01575-4.

An Intein-based Strategy for the Production of Tag-free Huntingtin Exon 1 Proteins Enables New Insights into the Polyglutamine Dependence of Httex1 Aggregation and Fibril Formation

S. ViewegA. AnsaloniZ.-M. WangJ. B. WarnerH. A. Lashuel

Journal of Biological Chemistry. 2016. DOI : 10.1074/jbc.M116.713982.

A New Caged-Glutamine Derivative as a Tool To Control the Assembly of Glutamine-Containing Amyloidogenic Peptides

L. AwadN. JejelavaR. BuraiH. A. Lashuel

Chembiochem : a European journal of chemical biology. 2016. DOI : 10.1002/cbic.201600474.

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

M.-B. FaresB. MacoA. OueslatiE. RockensteinN. Ninkina  et al.

Proceedings Of The National Academy Of Sciences Of The United States Of America (PNAS). 2016. DOI : 10.1073/pnas.1512876113.

Microtubule-Binding R3 Fragment from Tau Self-Assembles into Giant Multistranded Amyloid Ribbons

J. AdamcikA. Sanchez-FerrerN. Ait-BouziadN. P. ReynoldsH. A. Lashuel  et al.

Angewandte Chemie International Edition. 2016. DOI : 10.1002/anie.201508968.

Health hazards of methylammonium lead iodide based perovskites: cytotoxicity studies

I. R. BenmessaoudA.-L. Mahul-MellierE. HorváthB. MacoM. Spina  et al.

Toxicol. Res.. 2016. DOI : 10.1039/C5TX00303B.

Semisynthetic and in Vitro Phosphorylation of Alpha-Synuclein at Y39 Promotes Functional Partly Helical Membrane-Bound States Resembling Those Induced by PD Mutations

I. DikiyB. FauvetA. JovicicA.-L. Mahul-MellierC. Desobry  et al.

Acs Chemical Biology. 2016. DOI : 10.1021/acschembio.6b00539.

Novel therapeutic strategy for neurodegeneration by blocking Aβ seeding mediated aggregation in models of Alzheimer's disease

S. EleuteriS. Di GiovanniE. RockensteinM. ManteA. Adame  et al.

Neurobiology of disease. 2015. DOI : 10.1016/j.nbd.2014.08.017.

Fibril growth and seeding capacity play key roles in α-synuclein-mediated apoptotic cell death

Mahul-MellierF. VercruysseB. MacoN. Ait-BouziadM. De Roo  et al.

Cell death and differentiation. 2015. DOI : 10.1038/cdd.2015.79.

Recapitulating De Novo Alpha-Synuclein Fibrillization in a Novel Neuronal Model of Parkinson's Disease

M.-B. Fares / H. Lashuel (Dir.)

Lausanne, EPFL, 2015. DOI : 10.5075/epfl-thesis-6679.

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

A. OueslatiB. LovisaJ. PerrinG. WagnièresH. van den Bergh  et al.

PloS One. 2015. DOI : 10.1371/journal.pone.0140880.

Semisynthesis and Enzymatic Preparation of Post-translationally Modified α-Synuclein

B. FauvetH. A. Lashuel

Methods in molecular biology (Clifton, N.J.). 2015. DOI : 10.1007/978-1-4939-2978-8_1.

Elucidating the Role of Site-Specific Nitration of alpha-Synuclein in the Pathogenesis of Parkinson's Disease via Protein Semisynthesis and Mutagenesis

R. BuraiN. Ait-BouziadA. ChikiH. A. Lashuel

Journal Of The American Chemical Society. 2015. DOI : 10.1021/ja5131726.

Influence of the β-sheet content on the mechanical properties of aggregates during amyloid fibrillization

F. S. RuggeriJ. AdamcikJ. S. JeongH. A. LashuelR. Mezzenga  et al.

Angewandte Chemie (International ed. in English). 2015. DOI : 10.1002/anie.201409050.

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

M. K. MbefoM.-B. FaresK. PaleologouA. OueslatiG. Yin  et al.

Journal of Biological Chemistry. 2015. DOI : 10.1074/jbc.M114.610774.

Structural differences of amyloid-beta fibrils revealed by antibodies from phage display

P. DrosteA. FrenzelM. SteinwandT. PelatP. Thullier  et al.

Bmc Biotechnology. 2015. DOI : 10.1186/s12896-015-0146-8.

Parkinson's Disease Genes VPS35 and EIF4G1 Interact Genetically and Converge on α-Synuclein

N. DhungelS. EleuteriL.-B. LiN. J. KramerJ. W. Chartron  et al.

Neuron. 2015. DOI : 10.1016/j.neuron.2014.11.027.

The novel Parkinson's disease linked mutation G51D attenuates in vitro aggregation and membrane binding of alpha-synuclein, and enhances its secretion and nuclear localization in cells

M.-B. FaresN. Ait-BouziadI. DikiyM. K. MbefoA. Jovicic  et al.

Human Molecular Genetics. 2014. DOI : 10.1093/hmg/ddu165.

Reversible attachment of Cell-Penetrating Peptides for the efficient delivery of α-synuclein to HeLa cells and primary cortical neurons

C. Desobry / H. Lashuel (Dir.)

Lausanne, EPFL, 2014. DOI : 10.5075/epfl-thesis-6412.

One-Pot Semisynthesis of Exon 1 of the Huntingtin Protein: New Tools for Elucidating the Role of Posttranslational Modifications in the Pathogenesis of Huntington's Disease

A. AnsaloniZ.-M. WangJ. S. JeongF. S. RuggeriG. Dietler  et al.

Angewandte Chemie International Edition. 2014. DOI : 10.1002/anie.201307510.

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

A.-L. Mahul-MellierB. FauvetA. GysbersI. DikiyA. Oueslati  et al.

Human Molecular Genetics. 2014. DOI : 10.1093/hmg/ddt674.

Protein semisynthesis and total synthesis approaches to elucidate the role of Alpha-Synuclein post-translational modifications

B. C. D. Fauvet / H. Lashuel (Dir.)

Lausanne, EPFL, 2014. DOI : 10.5075/epfl-thesis-6187.

The role of S129 phosphorylation in regulating the cellular properties and secretion of alpha-synuclein : implication for alpha-synuclein function in health and disease

M. Mbefo Kamdem / H. Lashuel (Dir.)

Lausanne, EPFL, 2014. DOI : 10.5075/epfl-thesis-6110.

The role of fibril formation and growth in a-synuclein mediated extracellular toxicity

F. Vercruysse / H. Lashuel (Dir.)

Lausanne, EPFL, 2014. DOI : 10.5075/epfl-thesis-6106.

NOVEL MECHANISM-BASED INHIBITORS OF A beta AGGREGATION AND TOXICITY

H. A. LashuelS. EleuteriS. Di GiovanniE. RockensteinM. Mante  et al.

2014. 6th International Conference on Alzheimers Disease and Related Disorders in the Middle East, Istanbul, TURKEY, OCT 25-27, 2013. p. 720 - 721.

Elucidating the role of N-terminal phosphorylation in regulating the structure and the aggregation propensities of Huntingtin exon 1 using a semisynthetic strategy

A. Ansaloni / H. Lashuel (Dir.)

Lausanne, EPFL, 2014. DOI : 10.5075/epfl-thesis-6188.

Alpha-synuclein Post-translational Modifications as Potential Biomarkers for Parkinson Disease and Other Synucleinopathies

A. W. SchmidB. FauvetM. MoniatteH. A. Lashuel

Molecular & Cellular Proteomics. 2013. DOI : 10.1074/mcp.R113.032730.

Oxidative and nitrative alpha-synuclein modifications and proteostatic stress: implications for disease mechanisms and interventions in synucleinopathies

S. SchildknechtH. R. GerdingC. KarremanM. DrescherH. A. Lashuel  et al.

Journal of Neurochemistry (JNC). 2013. DOI : 10.1111/jnc.12226.

Novel Mechanistic Insight into the Molecular Basis of Amyloid Polymorphism and Secondary Nucleation during Amyloid Formation

J. S. JeongA. AnsaloniR. MezzengaH. A. LashuelG. Dietler

Journal of Molecular Biology. 2013. DOI : 10.1016/j.jmb.2013.02.005.

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

H. A. LashuelC. R. OverkA. OueslatiE. Masliah

Nature reviews. Neuroscience. 2013. DOI : 10.1038/nrn3406.

Real-time Amyloid Aggregation Monitoring with a Photonic Crystal-based Approach

S. SantiV. MusiE. DescroviV. PaederJ. Di Francesco  et al.

ChemPhysChem. 2013. DOI : 10.1002/cphc.201300633.

Synthetic polyubiquitinated α-Synuclein reveals important insights into the roles of the ubiquitin chain in regulating its pathophysiology

M. Haj-YahyaB. FauvetY. Herman-BachinskyM. HejjaouiS. N. Bavikar  et al.

Proceedings Of The National Academy Of Sciences Of The United States Of America (PNAS). 2013. DOI : 10.1073/pnas.1315654110.

One-pot total chemical synthesis of human α-synuclein

B. FauvetS. M. ButterfieldJ. FuksA. BrikH. A. Lashuel

Chemical Communications (ChemComm). 2013. DOI : 10.1039/c3cc45353g.

Parkin depletion delays motor decline dose-dependently without overtly affecting neuropathology in alpha-synuclein transgenic mice

M. FournierA. RouxJ. GarrigueM.-P. MurielP. Blanche  et al.

BMC neuroscience. 2013. DOI : 10.1186/1471-2202-14-135.

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

A. OueslatiB. L. SchneiderP. AebischerH. A. Lashuel

Proceedings Of The National Academy Of Sciences Of The United States Of America (PNAS). 2013. DOI : 10.1073/pnas.1309991110.

Reactive oxidative species enhance amyloid toxicity in APP/PS1 mouse neurons

B. YangX. SunH. LashuelY. Zhang

Neuroscience Bulletin. 2012. DOI : 10.1007/s12264-012-1239-1.

Characterization of Molecular Determinants of the Conformational Stability of Macrophage Migration Inhibitory Factor: Leucine 46 Hydrophobic Pocket

F. El-TurkB. FauvetA. AshrafiH. Ouertatani-SakouhiM.-K. Cho  et al.

PLoS ONE. 2012. DOI : 10.1371/journal.pone.0045024.

Discovery of a novel aggregation domain in the huntingtin protein: implications for the mechanisms of Htt aggregation and toxicity

Z.-M. WangH. A. Lashuel

Angewandte Chemie (International ed. in English). 2012. DOI : 10.1002/anie.201206561.

α-Synuclein in central nervous system and from erythrocytes, mammalian cells, and Escherichia coli exists predominantly as disordered monomer

B. FauvetM. K. MbefoM.-B. FaresC. DesobryS. Michael  et al.

Journal of Biological Chemistry. 2012. DOI : 10.1074/jbc.M111.318949.

Elucidating the role of C-terminal post-translational modifications using protein semisynthesis strategies: α-synuclein phosphorylation at tyrosine 125

M. HejjaouiS. ButterfieldB. FauvetF. VercruysseJ. Cui  et al.

Journal of the American Chemical Society. 2012. DOI : 10.1021/ja210866j.

Chemical strategies for controlling protein folding and elucidating the molecular mechanisms of amyloid formation and toxicity

S. ButterfieldM. HejjaouiB. FauvetL. AwadH. A. Lashuel

Journal of Molecular Biology. 2012. DOI : 10.1016/j.jmb.2012.01.051.

Measurement of intrinsic properties of amyloid fibrils by the peak force QNM method

J. AdamcikC. LaraI. UsovJ. S. JeongF. S. Ruggeri  et al.

Nanoscale. 2012. DOI : 10.1039/c2nr30768e.

Characterization of semisynthetic and naturally Nα-acetylated α-synuclein in vitro and in intact cells: implications for aggregation and cellular properties of α-synuclein

B. FauvetM.-B. FaresF. SamuelI. DikiyA. Tandon  et al.

Journal of Biological Chemistry. 2012. DOI : 10.1074/jbc.M112.383711.

Elucidating the role of post-translational modifications of alpha-synuclein using semisynthesis : phosphorylation at Tyrosine 125 and monoubiquitination at Lysine 6

M. Hejjaoui / H. Lashuel (Dir.)

Lausanne, EPFL, 2012. DOI : 10.5075/epfl-thesis-5494.

Discovery and Structure Activity Relationship of Small Molecule Inhibitors of Toxic β-Amyloid-42 Fibril Formation

H. KrothA. AnsaloniY. VariscoA. JanN. Sreenivasachary  et al.

Journal of Biological Chemistry. 2012. DOI : 10.1074/jbc.M112.357665.

The Size of the Proteasomal Substrate Determines Whether Its Degradation Will Be Mediated by Mono- or Polyubiquitylation

N. ShabekY. Herman-BachinskyS. BuchsbaumO. LewinsonM. Haj-Yahya  et al.

Molecular cell. 2012. DOI : 10.1016/j.molcel.2012.07.011.

Establishing the links between Aβ aggregation and cytotoxicity in vitro using biophysical approaches

A. JanH. A. Lashuel

Methods in molecular biology (Clifton, N.J.). 2012. DOI : 10.1007/978-1-61779-551-0_16.

Phosphorylation of α-synuclein is crucial in compensating for proteasomal dysfunction

H. S. ChoiH. LiewA. JangY.-M. KimH. Lashuel  et al.

Biochemical and biophysical research communications. 2012. DOI : 10.1016/j.bbrc.2012.06.159.

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

A. OueslatiK. E. PaleologouB. L. SchneiderP. AebischerH. A. Lashuel

The Journal of neuroscience : the official journal of the Society for Neuroscience. 2012. DOI : 10.1523/JNEUROSCI.3784-11.2012.

Chemical Biology of alpha-synuclein: The role post-translational modification in the pathogenesis of Parkinson's disease & related disorders

H. A. Lashuel

2011. 22nd American Peptide Symposium, San Diego, CA, Jun 25-30, 2011. p. 413 - 413.

Semisynthesis and Total Chemical Synthesis of alpha-synuclein to study Post-Translational Modifications in Health and Disease

B. FauvetS. M. ButterfieldM. HejjaouiD. OlschewskiM. Prudent  et al.

2011. 22nd American Peptide Symposium, San Diego, CA, Jun 25-30, 2011. p. 523 - 523.

Arab world needs its science diaspora

H. A. LashuelW. K. Al-Delaimy

Nature. 2011. DOI : 10.1038/472418d.

Novel chemical tools to facilitate the synthesis and control the folding and Self-assembly of amyloid-forming polypeptides

L. AwadN. JejelavaA. BrikH. Lashuel

2011. 22nd American Peptide Symposium, San Diego, CA, Jun 25-30, 2011. p. 430 - 430.

Method and compositions for inhibition of macrophage migration inhibitory factor (mif)

H. LashuelH. Ouertatani-sakouhi

WO2011066864 . 2011.

Phosphorylation of alpha-Synuclein at Y125 and S129 Alters Its Metal Binding Properties: Implications for Understanding the Role of alpha-Synuclein in the Pathogenesis of Parkinson's Disease and Related Disorders

Y. LuM. PrudentB. FauvetH. A. LashuelH. H. Girault

Acs Chemical Neuroscience. 2011. DOI : 10.1021/cn200074d.

Characterization and application of novel chemical tools to control folding and amyloid formation

N. Jejelava

2011

Amyloidogenic protein-membrane interactions: mechanistic insight from model systems

S. M. ButterfieldH. A. Lashuel

Angewandte Chemie (International ed. in English). 2010. DOI : 10.1002/anie.200906670.

Elucidating the Role of Quaternary Structure in Modulating Macrophage Migration Inhibitory Factor (MIF) Functions

F. El Turk / H. Lashuel (Dir.)

Lausanne, EPFL, 2010. DOI : 10.5075/epfl-thesis-4632.

Parkinson-related parkin reduces α-Synuclein phosphorylation in a gene transfer model

P. J. KhandelwalS. B. DumanisL. R. FengK. Maguire-ZeissG. Rebeck  et al.

Molecular neurodegeneration. 2010. DOI : 10.1186/1750-1326-5-47.

Phosphorylation of synucleins by members of the Polo-like kinase family

M. MbefoK. PaleologouA. BoucharabaA. OueslatiH. Schell  et al.

Journal of Biological Chemistry. 2010. DOI : 10.1074/jbc.M109.081950.

Stable  -Synuclein Oligomers Strongly Inhibit Chaperone Activity of the Hsp70 System by Weak Interactions with J-domain Co-chaperones

M.-P. HinaultA. F. H. CuendetR. U. H. MattooM. MensiG. Dietler  et al.

Journal of Biological Chemistry. 2010. DOI : 10.1074/jbc.M110.127753.

Role of post-translational modifications in modulating the structure, function and toxicity of alpha-synuclein: implications for Parkinson's disease pathogenesis and therapies

A. OueslatiM. FournierH. A. Lashuel

Progress in brain research. 2010. DOI : 10.1016/S0079-6123(10)83007-9.

An integrative in silico methodology for the identification of modulators of macrophage migration inhibitory factor (MIF) tautomerase activity

F. El TurkB. FauvetH. Ouertatani-SakouhiA. LugariS. Betzi  et al.

Bioorganic & medicinal chemistry. 2010. DOI : 10.1016/j.bmc.2010.05.010.

Identification and characterization of novel classes of macrophage migration inhibitory factor (MIF) inhibitors with distinct mechanisms of action

H. Ouertatani-SakouhiF. El-TurkB. FauvetM.-K. ChoD. Pinar Karpinar  et al.

Journal of Biological Chemistry. 2010. DOI : 10.1074/jbc.M110.113951.

Entacapone and tolcapone, two catechol O-methyltransferase inhibitors, block fibril formation of alpha-synuclein and beta-amyloid and protect against amyloid-induced toxicity

S. Di GiovanniS. EleuteriK. E. PaleologouG. YinM. Zweckstetter  et al.

Journal of Biological Chemistry. 2010. DOI : 10.1074/jbc.M109.080390.

Amyloid-beta aggregates cause alterations of astrocytic metabolic phenotype: impact on neuronal viability

I. AllamanM. GavilletM. BélangerT. LarocheD. Viertl  et al.

The Journal of neuroscience : the official journal of the Society for Neuroscience. 2010. DOI : 10.1523/JNEUROSCI.5098-09.2010.

The anti-Parkinsonian drug selegiline delays the nucleation phase of α-synuclein aggregation leading to the formation of nontoxic species

C. A. BragaC. FollmerF. L. PalhanoE. KhattarM. S. Freitas  et al.

Journal of Molecular Biology. 2010. DOI : 10.1016/j.jmb.2010.10.027.

Small Molecule Based Approaches to Inhibit Macrophage Migration Inhibitory Factor (MIF) Activities and Elucidate its Role in Health and Disease

H. Ouertatani-Sakouhi / H. Lashuel (Dir.)

Lausanne, EPFL, 2010. DOI : 10.5075/epfl-thesis-4633.

Phosphorylation at S87 is enhanced in synucleinopathies, inhibits alpha-synuclein oligomerization, and influences synuclein-membrane interactions

K. E. PaleologouA. OueslatiG. ShakkedC. C. RospigliosiH.-Y. Kim  et al.

The Journal of neuroscience : the official journal of the Society for Neuroscience. 2010. DOI : 10.1523/JNEUROSCI.5922-09.2010.

Preparation and characterization of toxic Abeta aggregates for structural and functional studies in Alzheimer's disease research

A. JanD. M. HartleyH. A. Lashuel

Nature protocols. 2010. DOI : 10.1038/nprot.2010.72.

Kinetic-based high-throughput screening assay to discover novel classes of macrophage migration inhibitory factor inhibitors

H. Ouertatani-SakouhiM. LiuF. El-TurkG. D. CunyM. A. Glicksman  et al.

Journal of biomolecular screening. 2010. DOI : 10.1177/1087057110363825.

Nucleation Dependent Polymerization of Amyloid-ß (Aß) as an Important Determinant of Aß Amyloid Formation and Neurotoxicity : Implications for the Pathogenesis of Alzheimer's Disease and Design of Therapies

M. A. Jan Qureshi / H. Lashuel (Dir.)

Lausanne, EPFL, 2010. DOI : 10.5075/epfl-thesis-4773.

Amyloids go genomic: insights regarding the sequence determinants of prion formation from genome-wide studies

H. A. LashuelR. V. Pappu

Chembiochem : a European journal of chemical biology. 2009. DOI : 10.1002/cbic.200900373.

Dissecting the mechanisms of tissue transglutaminase-induced cross-linking of alpha-synuclein: implications for the pathogenesis of Parkinson disease

A. W. SchmidD. ChiappeV. PignatV. GrimmingerI. Hang  et al.

Journal of Biological Chemistry. 2009. DOI : 10.1074/jbc.M809067200.

Structural properties of pore-forming oligomers of alpha-synuclein

H. Y. KimM. K. ChoA. KumarE. MaierC. Siebenharr  et al.

Journal of the American Chemical Society. 2009. DOI : 10.1021/ja9077599.

Switch-peptides as folding precursors in self-assembling peptides and amyloid fibrillogenesis

M. S. CamusR. MimnaA. SchmidA. ChandravarkarG. Tuchscherer  et al.

Advances in experimental medicine and biology. 2009. DOI : 10.1007/978-0-387-73657-0_126.

Highly efficient and chemoselective peptide ubiquitylation

K. S. Ajish KumarM. Haj-YahyaD. OlschewskiH. A. LashuelA. Brik

Angewandte Chemie (International ed. in English). 2009. DOI : 10.1002/anie.200902936.

A new class of isothiocyanate-based irreversible inhibitors of macrophage migration inhibitory factor

H. Ouertatani-SakouhiF. El-TurkB. FauvetT. RogerD. Le Roy  et al.

Biochemistry. 2009. DOI : 10.1021/bi900957e.

E46K Parkinson's-linked mutation enhances C-terminal-to-N-terminal contacts in alpha-synuclein

C. C. RospigliosiS. McClendonA. W. SchmidT. F. RamlallP. Barré  et al.

Journal of Molecular Biology. 2009. DOI : 10.1016/j.jmb.2009.03.065.

Parkin deficiency delays motor decline and disease manifestation in a mouse model of synucleinopathy

M. FournierJ. VitteJ. GarrigueD. LanguiJ.-P. Dullin  et al.

PloS One. 2009. DOI : 10.1371/journal.pone.0006629.

The role of post-translational modification (phosphorylation) in modulating alpha-synuclein, structure, aggregation and toxicity

H. A. Lashuel

2009. 4th European-Society-for-Neurochemistry Conference on Advances in Molecular Mechanisms of Neurological Disorders, Leipzig, GERMANY, Jul 11-14, 2009. p. 61 - 61.

Structure and function of the molecular chaperone Hsp104 from yeast

V. Grimminger-MarquardtH. A. Lashuel

Biopolymers. 2009. DOI : 10.1002/bip.21301.

Amyloid-Beta Modifies Astrocytic Metabolic Phenotype

I. AllamanM. GavilletM. BelangerT. LarocheD. Viertl  et al.

22nd Biennial Meeting of the International-Society-of-Neurochemistry/Asian-Pacific-Society-for-Neurochemistry, Busan, SOUTH KOREA, Aug 23-29, 2009.

Apomorphine inhibitors of amyloid-beta (abeta) fibril formation and their use in amyloidosis based disease

H. A. LashuelD. E. Callaway

US2008096909 ; US2003187011 . 2008.

Phosphorylation at Ser-129 but not the phosphomimics S129E/D inhibits the fibrillation of alpha-synuclein

K. E. PaleologouA. W. SchmidC. C. RospigliosiH.-Y. KimG. R. Lamberto  et al.

Journal of Biological Chemistry. 2008. DOI : 10.1074/jbc.M800747200.

Switch-peptides: design and characterization of controllable super-amyloid-forming host-guest peptides as tools for identifying anti-amyloid agents

M.-S. CamusS. Dos SantosA. ChandravarkarB. MandalA. W. Schmid  et al.

Chembiochem : a European journal of chemical biology. 2008. DOI : 10.1002/cbic.200800245.

Hsp104 targets multiple intermediates on the amyloid pathway and suppresses the seeding capacity of Abeta fibrils and protofibrils

M. ArimonV. GrimmingerF. SanzH. A. Lashuel

Journal of Molecular Biology. 2008. DOI : 10.1016/j.jmb.2008.09.063.

Inhibition of alpha-synuclein fibrillization by dopamine is mediated by interactions with five C-terminal residues and with E83 in the NAC region

F. E. HerreraA. ChesiK. E. PaleologouA. SchmidA. Munoz  et al.

PloS One. 2008. DOI : 10.1371/journal.pone.0003394.

Switch peptide via Staudinger reaction

N. NepomniaschiyV. GrimmingerA. CohenS. DiGiovanniH. A. Lashuel  et al.

Organic Letters. 2008. DOI : 10.1021/ol802268e.

The conformational flexibility of the carboxy terminal residues 105-114 is a key modulator of the catalytic activity and stability of macrophage migration inhibitory factor

F. El-TurkM. CascellaH. Ouertatani-SakouhiR. L. NarayananL. Leng  et al.

Biochemistry. 2008. DOI : 10.1021/bi800603x.

The ratio of monomeric to aggregated forms of Abeta40 and Abeta42 is an important determinant of amyloid-beta aggregation, fibrillogenesis, and toxicity

A. JanO. GokceR. Luthi-CarterH. A. Lashuel

Journal of Biological Chemistry. 2008. DOI : 10.1074/jbc.M803159200.

Hsp104 antagonizes alpha-synuclein aggregation and reduces dopaminergic degeneration in a rat model of Parkinson disease

C. Lo BiancoJ. ShorterE. RégulierH. LashuelT. Iwatsubo  et al.

The Journal of clinical investigation. 2008. DOI : 10.1172/JCI35781.

Disruption of amyloid-derived peptide assemblies through the controlled induction of a beta-sheet to alpha-helix transformation: application of the switch concept

R. MimnaM.-S. CamusA. SchmidG. TuchschererH. A. Lashuel  et al.

Angewandte Chemie International Edition. 2007. DOI : 10.1002/anie.200603681.

The impact of the E46K mutation on the properties of alpha-synuclein in its monomeric and oligomeric states

R. A. FredenburgC. RospigliosiR. K. MerayJ. C. KesslerH. A. Lashuel  et al.

Biochemistry. 2007. DOI : 10.1021/bi7000246.

Dopamine affects the stability, hydration, and packing of protofibrils and fibrils of the wild type and variants of alpha-synuclein

C. FollmerL. RomãoC. M. EinsiedlerT. C. R. PortoF. A. Lara  et al.

Biochemistry. 2007. DOI : 10.1021/bi061871+.

Branched KLVFF tetramers strongly potentiate inhibition of beta-amyloid aggregation

S. M. ChafekarH. MaldaM. MerkxE. W. MeijerD. Viertl  et al.

Chembiochem : a European journal of chemical biology. 2007. DOI : 10.1002/cbic.200700338.

Switch-peptides as folding precursors in self-assembling peptides and amyloid fibrillogenesis

G. TuchschererA. ChandravarkarM.-S. CamusJ. BerardK. Murat  et al.

Biopolymers. 2007. DOI : 10.1002/bip.20663.

A century-old debate on protein aggregation and neurodegeneration enters the clinic

P. T. LansburyH. A. Lashuel

Nature. 2006. DOI : 10.1038/nature05290.

Are amyloid diseases caused by protein aggregates that mimic bacterial pore-forming toxins?

H. A. LashuelP. T. Lansbury

Quarterly reviews of biophysics. 2006. DOI : 10.1017/S0033583506004422.

Rescuing defective vesicular trafficking protects against alpha-synuclein toxicity in cellular and animal models of Parkinson's disease

H. A. LashuelH. Hirling

ACS chemical biology. 2006. DOI : 10.1021/cb600331e.

Switch-peptides: from conformational studies to Alzheimer's disease

L. SaucedeS. Dos SantosA. ChandravarkarB. MandalR. Mimna  et al.

CHIMIA. 2006. DOI : 10.2533/000942906777674921.

Islam: governments need to reform education and build a scientific culture

H. A. LashuelN. Zawia

Nature. 2006. DOI : 10.1038/444545a.

The materials science of protein aggregation

D. L. CoxH. A. LashuelK. Y. C. LeeR. R. R. Singh

MRS Bulletin. 2005. DOI : 10.1557/mrs2005.123.

Amyloid fibril formation by macrophage migration inhibitory factor

H. A. LashuelB. AljabariE. M. SigurdssonC. N. MetzL. Leng  et al.

Biochemical and biophysical research communications. 2005. DOI : 10.1016/j.bbrc.2005.10.040.

Lead (Pb) exposure and its effect on APP proteolysis and Abeta aggregation

M. R. BashaM. MuraliH. K. SiddiqiK. GhosalO. K. Siddiqi  et al.

The FASEB journal : official publication of the Federation of American Societies for Experimental Biology. 2005. DOI : 10.1096/fj.05-4375fje.

In vitro preparation of prefibrillar intermediates of amyloid-beta and alpha-synuclein

H. A. LashuelD. Grillo-Bosch

Methods in molecular biology (Clifton, N.J.). 2005. DOI : 10.1385/1-59259-874-9:019.

Molecular electron microscopy approaches to elucidating the mechanisms of protein fibrillogenesis

H. A. LashuelJ. S. Wall

Methods in molecular biology (Clifton, N.J.). 2005. DOI : 10.1385/1-59259-874-9:081.

Membrane permeabilization: a common mechanism in protein-misfolding diseases

H. A. Lashuel

Science of aging knowledge environment : SAGE KE. 2005. DOI : 10.1126/sageke.2005.38.pe28.

From hexamer to amyloid: marginal stability of apolipoprotein SAA2.2 leads to in vitro fibril formation at physiological temperature

L. WangH. A. LashuelW. Colón

Amyloid : the international journal of experimental and clinical investigation : the official journal of the International Society of Amyloidosis. 2005. DOI : 10.1080/13506120500223084.

Production and characterization of astrocyte-derived human apolipoprotein E isoforms from immortalized astrocytes and their interactions with amyloid-beta

M. MorikawaJ. D. FryerP. M. SullivanE. A. ChristopherS. E. Wahrle  et al.

Neurobiology of disease. 2005. DOI : 10.1016/j.nbd.2004.11.005.

Quaternary structure, protein dynamics, and synaptic function of SAP97 controlled by L27 domain interactions

T. NakagawaK. FutaiH. A. LashuelI. LoK. Okamoto  et al.

Neuron. 2004. DOI : 10.1016/j.neuron.2004.10.012.

Interactions among alpha-synuclein, dopamine, and biomembranes: some clues for understanding neurodegeneration in Parkinson's disease

J.-C. RochetT. F. OuteiroK. A. ConwayT. T. DingM. J. Volles  et al.

Journal of molecular neuroscience : MN. 2004. DOI : 10.1385/JMN:23:1-2:023.

Apomorphine inhibitors of amyloid-beta (abeta) fibril formation and their use in amyloidosis based disease

H. A. LashuelD. E. Callaway

WO03053356 ; AU2002357911 ; AU2002357911 ; WO03053356 ; CA2479263 . 2003.

Hydration and packing are crucial to amyloidogenesis as revealed by pressure studies on transthyretin variants that either protect or worsen amyloid disease

A. D. Ferrão-GonzalesL. PalmieriM. ValoryJ. L. SilvaH. Lashuel  et al.

Journal of Molecular Biology. 2003. DOI : 10.1016/S0022-2836(03)00368-1.

Dissociation of amyloid fibrils of alpha-synuclein and transthyretin by pressure reveals their reversible nature and the formation of water-excluded cavities

D. FoguelM. C. SuarezA. D. Ferrão-GonzalesT. C. R. PortoL. Palmieri  et al.

Proceedings Of The National Academy Of Sciences Of The United States Of America (PNAS). 2003. DOI : 10.1073/pnas.1734009100.

Mixtures of wild-type and a pathogenic (E22G) form of Abeta40 in vitro accumulate protofibrils, including amyloid pores

H. A. LashuelD. M. HartleyB. M. PetreJ. S. WallM. N. Simon  et al.

Journal of Molecular Biology. 2003. DOI : 10.1016/S0022-2836(03)00927-6.

Discovery of inhibitors that elucidate the role of UCH-L1 activity in the H1299 lung cancer cell line

Y. LiuH. A. LashuelS. ChoiX. XingA. Case  et al.

Chemistry & biology. 2003. DOI : 10.1016/j.chembiol.2003.08.010.

Abeta protofibrils possess a stable core structure resistant to hydrogen exchange

I. KheterpalH. A. LashuelD. M. HartleyT. WalzP. T. Lansbury  et al.

Biochemistry. 2003. DOI : 10.1021/bi0357816.

hA molecular switch in amyloid assembly: Met35 and amyloid beta-protein oligomerization

G. BitanB. TarusS. S. VollersH. A. LashuelM. M. Condron  et al.

Journal of the American Chemical Society. 2003. DOI : 10.1021/ja0349296.

New class of inhibitors of amyloid-beta fibril formation. Implications for the mechanism of pathogenesis in Alzheimer's disease

H. A. LashuelD. M. HartleyD. BalakhanehA. AggarwalS. Teichberg  et al.

Journal of Biological Chemistry. 2002. DOI : 10.1074/jbc.M206593200.

The UCH-L1 gene encodes two opposing enzymatic activities that affect alpha-synuclein degradation and Parkinson's disease susceptibility

Y. LiuL. FallonH. A. LashuelZ. LiuP. T. Lansbury

Cell. 2002. DOI : 10.1016/S0092-8674(02)01012-7.

Murine apolipoprotein serum amyloid A in solution forms a hexamer containing a central channel

L. WangH. A. LashuelT. WalzW. Colon

Proceedings Of The National Academy Of Sciences Of The United States Of America (PNAS). 2002. DOI : 10.1073/pnas.252508399.

Neurodegenerative disease: amyloid pores from pathogenic mutations

H. A. LashuelD. HartleyB. M. PetreT. WalzP. T. Lansbury

Nature. 2002. DOI : 10.1038/418291a.

Alpha-synuclein, especially the Parkinson's disease-associated mutants, forms pore-like annular and tubular protofibrils

H. A. LashuelB. M. PetreJ. WallM. SimonR. J. Nowak  et al.

Journal of Molecular Biology. 2002. DOI : 10.1016/S0022-2836(02)00735-0.

Synthesis, structure, and activity of diclofenac analogues as transthyretin amyloid fibril formation inhibitors

V. B. OzaC. SmithP. RamanE. K. KoepfH. A. Lashuel  et al.

Journal of medicinal chemistry. 2002. DOI : 10.1021/jm010257n.

Protofilaments, filaments, ribbons, and fibrils from peptidomimetic self-assembly: Implications for amyloid fibril formation and materials science

H. A. LashuelS. R. LaBrenzL. WooL. C. SerpellJ. W. Kelly

Journal of the American Chemical Society. 2000. DOI : 10.1021/ja9937831.

Nuclear import factors importin alpha and importin beta undergo mutually induced conformational changes upon association

G. CingolaniH. A. LashuelL. GeraceC. W. Müller

FEBS letters. 2000. DOI : 10.1016/S0014-5793(00)02154-2.

A glimpse of a possible amyloidogenic intermediate of transthyretin

K. LiuH. S. ChoH. A. LashuelJ. W. KellyD. E. Wemmer

Nature structural biology. 2000. DOI : 10.1038/78980.

The nucleation of monomeric parallel beta-sheet-like structures and their self-assembly in aqueous solution

P. ChitnumsubW. R. FioriH. A. LashuelH. DiazJ. W. Kelly

Bioorganic & medicinal chemistry. 1999. DOI : 10.1016/S0968-0896(98)00222-3.

The most pathogenic transthyretin variant, L55P, forms amyloid fibrils under acidic conditions and protofilaments under physiological conditions

H. A. LashuelC. WurthL. WooJ. W. Kelly

Biochemistry. 1999. DOI : 10.1021/bi991021c.

Characterization of the transthyretin acid denaturation pathways by analytical ultracentrifugation: implications for wild-type, V30M, and L55P amyloid fibril formation

H. A. LashuelZ. LaiJ. W. Kelly

Biochemistry. 1999. DOI : 10.1021/bi981876+.

Association between the first two immunoglobulin-like domains of the neural cell adhesion molecule N-CAM

A. R. AtkinsM. J. OsborneH. A. LashuelG. M. EdelmanP. E. Wright  et al.

FEBS letters. 1999. DOI : 10.1016/S0014-5793(99)00554-2.

Comparative characterization of a wild type and transmembrane domain-deleted fatty acid amide hydrolase: identification of the transmembrane domain as a site for oligomerization

M. P. PatricelliH. A. LashuelD. K. GiangJ. W. KellyB. F. Cravatt

Biochemistry. 1998. DOI : 10.1021/bi981733n.

Inhibiting transthyretin conformational changes that lead to amyloid fibril formation

S. A. PetersonT. KlabundeH. A. LashuelH. PurkeyJ. C. Sacchettini  et al.

Proceedings Of The National Academy Of Sciences Of The United States Of America (PNAS). 1998. DOI : 10.1073/pnas.95.22.12956.

Recombinant human retinol-binding protein refolding, native disulfide formation, and characterization

Y. XieH. A. LashuelG. J. MiroyS. DiklerJ. W. Kelly

Protein expression and purification. 1998. DOI : 10.1006/prep.1998.0944.

Anti-amyloidogenic agents

G. J. MiroyJ. W. KellyZ. LaiH. A. LashuelS. A. Peterson

WO9827972 ; WO9827972 ; AU5727798 ; WO9827972 . 1998.

Complete inhibition of Cdk/cyclin by one molecule of p21(Cip1)

L. HengstU. GöpfertH. A. LashuelS. I. Reed

Genes & development. 1998. DOI : 10.1101/gad.12.24.3882.

Guanidine hydrochloride-induced denaturation and refolding of transthyretin exhibits a marked hysteresis: equilibria with high kinetic barriers

Z. LaiJ. McCullochH. A. LashuelJ. W. Kelly

Biochemistry. 1997. DOI : 10.1021/bi963195p.

Transthyretin quaternary and tertiary structural changes facilitate misassembly into amyloid

J. W. KellyW. ColonZ. LaiH. A. LashuelJ. McCulloch  et al.

Advances in protein chemistry. 1997. DOI : 10.1016/S0065-3233(08)60321-6.

Oligomerization properties of GCN4 leucine zipper e and g position mutants

X. ZengH. ZhuH. A. LashuelJ. C. Hu

Protein science : a publication of the Protein Society. 1997. DOI : 10.1002/pro.5560061016.

Inhibiting transthyretin amyloid fibril formation via protein stabilization

G. J. MiroyZ. LaiH. A. LashuelS. A. PetersonC. Strang  et al.

Proceedings Of The National Academy Of Sciences Of The United States Of America (PNAS). 1996. DOI : 10.1073/pnas.93.26.15051.