Hilal Lashuel
hilal.lashuel@epfl.ch +41 21 693 96 91 http://lashuel-lab.epfl.ch
Nationalité: USA
Date de naissance: 15.01.1973
+41 21 693 96 91
EPFL
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SSV-ENS
Web site: Site web: https://sv.epfl.ch/education
+41 21 693 96 91
EPFL
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Web site: Site web: https://sv.epfl.ch/professeurs-honoraires
Publications
Publications Infoscience
Huntingtin inclusion bodies have distinct immunophenotypes and ubiquitination profiles in the Huntington’s disease human cerebral cortex
Scientific Reports. 2025. DOI : 10.1038/s41598-025-00465-w.Amyotrophic lateral sclerosis caused by TARDBP mutations: from genetics to TDP-43 proteinopathy
The Lancet Neurology. 2025. DOI : 10.1016/S1474-4422(25)00109-7.Alpha-synuclein seed amplification assays: Data sharing, standardization needed for clinical use
Science Advances. 2025. DOI : 10.1126/sciadv.adt7195.Multi-Targeting Macrocyclic Peptides as Nanomolar Inhibitors of Self- and Cross-Seeded Amyloid Self-Assembly of α-Synuclein
ANGEWANDTE CHEMIE-INTERNATIONAL EDITION. 2025. DOI : 10.1002/anie.202422834.Intelligent and Self-Driving Microscopy of Protein Aggregation in Neurodegenerative Diseases
Lausanne, EPFL, 2025. DOI : 10.5075/epfl-thesis-11337.Nanoplasmonic infrared biosensors enabling detection of misfolded protein biomarkers and drug screening for neurodegenerative diseases
Lausanne, EPFL, 2025. DOI : 10.5075/epfl-thesis-10478.Uses of aerolysin nanopores
WO2025003492 . 2025.Mouse α-synuclein fibrils are structurally and functionally distinct from human fibrils associated with Lewy body diseases
Science advances. 2024. DOI : 10.1126/sciadv.adq3539.Research Priorities on the Role of α-Synuclein in Parkinson's Disease Pathogenesis
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
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
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
2024Post-translational glycosylation diminishes α-synuclein pathology formation
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
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)
NPJ PARKINSONS DISEASE. 2024. DOI : 10.1038/s41531-024-00634-0.Transactive response dna-binding protein 43kda (tdp-43) mutants and uses thereof
WO2024223615 . 2024.Exploring the therapeutic potential of Huntingtin native state stabilization through targeting its interacting partners
Lausanne, EPFL, 2024. DOI : 10.5075/epfl-thesis-10915.Effective Inhibition of TDP-43 Aggregation by Native State Stabilization
Angewandte Chemie International Edition. 2024. DOI : 10.1002/anie.202314587.Deep learning augmented nanoplasmonic infrared sensor for structural protein biomarker-based detection of neurodegenerative diseases
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.Dielectrophoretic Manipulation of Biological Species: Novel Microfluidic Approaches to Study Cell-Cell Interactions and the Role of Alpha-Synuclein in Neurodegeneration
Lausanne, EPFL, 2024. DOI : 10.5075/epfl-thesis-10597.Method of preparation of amyloidogenic protein aggregates and uses thereof
WO2024094597 . 2024.Investigating the intra-molecular and inter-molecular effects of post-translational modifications on intrinsically disordered protein regions and structured protein regions
Lausanne, EPFL, 2024. DOI : 10.5075/epfl-thesis-10530.Author Correction: Fully co-factor-free ClearTau platform produces seeding-competent Tau fibrils for reconstructing pathological Tau aggregates
Nature Communications. 2024. DOI : 10.1038/s41467-024-48976-w.Targeting TDP-43 Proteinopathies in Neurodegeneration by its Native-State Stabilization
Lausanne, EPFL, 2024. DOI : 10.5075/epfl-thesis-10555.Recombinant Full-Length TDP-43 Oligomers Retain Their Ability to Bind RNAs, Are Not Toxic, and Do Not Seed TDP-43 Aggregation in Vitro
Acs Chemical Neuroscience. 2023. DOI : 10.1021/acschemneuro.3c00691.Deep Learning-Assisted Single-Molecule Detection of Protein Post-translational Modifications with a Biological Nanopore
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
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
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
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
Science Advances. 2023. DOI : 10.1126/sciadv.adg9644.Seeding the aggregation of TDP-43 requires post-fibrillization proteolytic cleavage
Nature Neuroscience. 2023. DOI : 10.1038/s41593-023-01341-4.Neuronal growth on high-aspect-ratio diamond nanopillar arrays for biosensing applications
Scientific Reports. 2023. DOI : 10.1038/s41598-023-32235-x.Deconstructing and Reconstructing the Complexity of Tau pathology
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
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
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
Neurobiology Of Disease. 2022. DOI : 10.1016/j.nbd.2022.105884.Pathological substrate of memory impairment in multiple system atrophy
Neuropathology And Applied Neurobiology. 2022. DOI : 10.1111/nan.12844.Identification of key segments of IAPP/aSyn cross-amyloid interactions
2022.Opportunities and challenges of alpha-synuclein as a potential biomarker for Parkinson's disease and other synucleinopathies
Npj Parkinsons Disease. 2022. DOI : 10.1038/s41531-022-00357-0.On-Demand Nanoliter Sampling Probe for the Collection of Brain Fluid
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
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
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
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
Cells. 2022. DOI : 10.3390/cells11050906.The role of PTM crosstalks in Httex1 structure, aggregation and membrane interaction
2022. p. 38 - 38. DOI : 10.1016/j.bpj.2021.11.2495.Capturing the heterogeneity of alpha-synuclein pathology in synucleinopathies
Lausanne, EPFL, 2022. DOI : 10.5075/epfl-thesis-8480.Comparative Analysis of Total Alpha-Synuclein (alpha SYN) Immunoassays Reveals That They Do Not Capture the Diversity of Modified alpha SYN Proteoforms
Journal Of Parkinsons Disease. 2022. DOI : 10.3233/JPD-223285.An integrative approach to elucidate the mechanisms and dynamics of Huntingtin aggregation and inclusion formation in neuronal models of Huntington's Disease
Lausanne, EPFL, 2022. DOI : 10.5075/epfl-thesis-9296.Towards elucidating the structural and cellular determinants of a-synuclein seeding and toxicity
Lausanne, EPFL, 2022. DOI : 10.5075/epfl-thesis-9365.Non-monotonic fibril surface occlusion by GFP tags from coarse-grained molecular simulations
Computational and Structural Biotechnology Journal. 2022. DOI : 10.1016/j.csbj.2021.12.017.Revisiting the grammar of Tau aggregation and pathology formation: how new insights from brain pathology are shaping how we study and target Tauopathies
Chemical Society Reviews. 2022. DOI : 10.1039/d1cs00127b.To target Tau pathologies, we must embrace and reconstruct their complexities
Neurobiology Of Disease. 2021. DOI : 10.1016/j.nbd.2021.105536.Nuclear and cytoplasmic huntingtin inclusions exhibit distinct biochemical composition, interactome and ultrastructural properties
Nature Communications. 2021. DOI : 10.1038/s41467-021-26684-z.Fatal attraction-The role of hypoxia when alpha-synuclein gets intimate with mitochondria
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
Journal of Molecular Biology. 2021. DOI : 10.1016/j.jmb.2021.167222.Pharmacological characterization of mutant huntingtin aggregate-directed PET imaging tracer candidates
Scientific Reports. 2021. DOI : 10.1038/s41598-021-97334-z.Alpha-synuclein research: defining strategic moves in the battle against Parkinson's disease
Npj Parkinsons Disease. 2021. DOI : 10.1038/s41531-021-00203-9.Investigating Crosstalk Among PTMs Provides Novel Insight Into the Structural Basis Underlying the Differential Effects of Nt17 PTMs on Mutant Httex1 Aggregation
Frontiers in Molecular Biosciences. 2021. DOI : 10.3389/fmolb.2021.686086.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
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?
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
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
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
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
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?".
Journal Of Neurochemistry. 2021. DOI : 10.1111/jnc.15275.Hypoxia Conditioning as a Promising Therapeutic Target in Parkinson's Disease?
Movement Disorders. 2021. DOI : 10.1002/mds.28544.Reverse engineering Lewy bodies: how far have we come and how far can we go?
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
Journal of Neurochemistry. 2021. DOI : 10.1111/jnc.15147.Site-Specific Phosphorylation of Huntingtin Exon 1 Recombinant Proteins Enabled by the Discovery of Novel Kinases
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
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
The EMBO Journal. 2020. DOI : 10.15252/embj.2020104671.Half a century of amyloids: past, present and future
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
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
Journal of Biological Chemistry. 2020. DOI : 10.1074/jbc.RA119.012517.Extent of N-terminus exposure of monomeric alpha-synuclein determines its aggregation propensity
Nature Communications. 2020. DOI : 10.1038/s41467-020-16564-3.Education and research are essential for lasting peace in Yemen
Lancet. 2020. DOI : 10.1016/S0140-6736(20)30162-8.Unraveling the complexity of amyloid polymorphism using gold nanoparticles and cryo-EM
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
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
Journal Of Neurochemistry. 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
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
Angewandte Chemie International Edition. 2020. DOI : 10.1002/anie.201913001.Ultrasensitive quantitative measurement of huntingtin phosphorylation at residue S13
Biochemical And Biophysical Research Communications. 2020. DOI : 10.1016/j.bbrc.2019.09.097.What about faculty?
Elife. 2020. DOI : 10.7554/eLife.54551.Development of novel methods and tools to decipher the huntingtin post-translation modifications code
Lausanne, EPFL, 2020. DOI : 10.5075/epfl-thesis-7537.Gold nanoparticles as a new tool in amyloid studies
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
eNeuro. 2020. DOI : 10.1523/ENEURO.0110-20.2020.The Role of Post-translational Modifications on the Energy Landscape of Huntingtin N-Terminus
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
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
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
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
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
US11629175 ; US2021238242 ; EP3784687 ; WO2019207164 . 2019.Generation of Native, Untagged Huntingtin Exon1 Monomer and Fibrils Using a SUMO Fusion Strategy
Journal of Visualized Experiments. 2018. DOI : 10.3791/57506.Exploring the role of post-translational modifications in regulating α-synuclein interactions by studying the effects of phosphorylation on nanobody binding
Proteins Science. 2018. DOI : 10.1002/pro.3412.Combined Multi-Plane Tomographic Phase Retrieval and Stochastic Optical Fluctuation Imaging for 4D Cell Microscopy
Nature Photonics. 2018. DOI : 10.1038/s41566-018-0109-4.Amyloid Single Cell Cytotoxicity Assays by Nanomotion Detection
Cell Death Discovery. 2017. DOI : 10.1038/cddiscovery.2017.53.A user's guide for α-synuclein biomarker studies in biological fluids: Perianalytical considerations
Movement Disorders. 2017. DOI : 10.1002/mds.27090.Monomeric Huntingtin Exon 1 Has Similar Overall Structural Features for Wild-Type and Pathological Polyglutamine Lengths
Journal of the American Chemical Society. 2017. DOI : 10.1021/jacs.7b06659.Membrane scission driven by the PROPPIN Atg18
Embo Journal. 2017. DOI : 10.15252/embj.201796859.Polyglutamine expansion affects huntingtin conformation in multiple Huntington’s disease models
Scientific Reports. 2017. DOI : 10.1038/s41598-017-05336-7.Activation of the STING-dependent type I interferon response reduces microglial reactivity and neuroinflammation
Neuron. 2017. DOI : 10.1016/j.neuron.2017.11.032.Polyglutamine Length Dependent Structural Properties and Phase Behavior of Huntingtin Exon 1
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.Glycation potentiates α-synuclein-associated neurodegeneration in synucleinopathies
Brain : a journal of neurology. 2017. DOI : 10.1093/brain/awx056.The mechanism of sirtuin 2-mediated exacerbation of alpha-synuclein toxicity in models of Parkinson disease
PLoS Biology. 2017. DOI : 10.1371/journal.pbio.2000374.Mutant Exon1 Huntingtin Aggregation is Regulated by T3 Phosphorylation-Induced Structural Changes and Crosstalk between T3 Phosphorylation and Acetylation at K6
Angewandte Chemie (International ed. in English). 2017. DOI : 10.1002/anie.201611750.The role of the polyglutamine and N-terminal domains in regulating the aggregation and structural properties of Huntingtin Exon 1
Lausanne, EPFL, 2017. DOI : 10.5075/epfl-thesis-7374.Human and eco-toxicological impacts of organometallic halide perovskites
Lausanne, EPFL, 2017. DOI : 10.5075/epfl-thesis-7595.The America I believe in
Science. 2017. DOI : 10.1126/science.355.6326.766.Ganciclovir derivatives for modulating innate and adaptive immunity and for use in immunotherapy
US9809597 ; US2017050967 . 2017.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
Nature Communications. 2017. DOI : 10.1038/s41467-017-01575-4.Sequence and structural determinants of Tau aggregation and seeding capacity: Implications for Neurofibrillary Tangle formation and Tau toxicity in Alzheimer's disease
Lausanne, EPFL, 2017. DOI : 10.5075/epfl-thesis-7985.A New Caged-Glutamine Derivative as a Tool To Control the Assembly of Glutamine-Containing Amyloidogenic Peptides
Chembiochem : a European journal of chemical biology. 2016. DOI : 10.1002/cbic.201600474.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
Journal of Biological Chemistry. 2016. DOI : 10.1074/jbc.M116.713982.Microtubule-Binding R3 Fragment from Tau Self-Assembles into Giant Multistranded Amyloid Ribbons
Angewandte Chemie International Edition. 2016. DOI : 10.1002/anie.201508968.Semisynthetic and in Vitro Phosphorylation of Alpha-Synuclein at Y39 Promotes Functional Partly Helical Membrane-Bound States Resembling Those Induced by PD Mutations
Acs Chemical Biology. 2016. DOI : 10.1021/acschembio.6b00539.Health hazards of methylammonium lead iodide based perovskites: cytotoxicity studies
Toxicol. Res.. 2016. DOI : 10.1039/C5TX00303B.Induction of de novo α-synuclein fibrillization in a neuronal model for Parkinson's disease
Proceedings Of The National Academy Of Sciences Of The United States Of America (PNAS). 2016. DOI : 10.1073/pnas.1512876113.Parkinson's Disease Genes VPS35 and EIF4G1 Interact Genetically and Converge on α-Synuclein
Neuron. 2015. DOI : 10.1016/j.neuron.2014.11.027.Fibril growth and seeding capacity play key roles in α-synuclein-mediated apoptotic cell death
Cell death and differentiation. 2015. DOI : 10.1038/cdd.2015.79.Novel therapeutic strategy for neurodegeneration by blocking Aβ seeding mediated aggregation in models of Alzheimer's disease
Neurobiology of disease. 2015. DOI : 10.1016/j.nbd.2014.08.017.Parkinson disease mutant E46K enhances α-synuclein phosphorylation in mammalian cell lines, in yeast, and in vivo
Journal of Biological Chemistry. 2015. DOI : 10.1074/jbc.M114.610774.Elucidating the Role of Site-Specific Nitration of alpha-Synuclein in the Pathogenesis of Parkinson's Disease via Protein Semisynthesis and Mutagenesis
Journal Of The American Chemical Society. 2015. DOI : 10.1021/ja5131726.Semisynthesis and Enzymatic Preparation of Post-translationally Modified α-Synuclein
Methods in molecular biology (Clifton, N.J.). 2015. DOI : 10.1007/978-1-4939-2978-8_1.Recapitulating De Novo Alpha-Synuclein Fibrillization in a Novel Neuronal Model of Parkinson's Disease
Lausanne, EPFL, 2015. DOI : 10.5075/epfl-thesis-6679.Influence of the β-sheet content on the mechanical properties of aggregates during amyloid fibrillization
Angewandte Chemie (International ed. in English). 2015. DOI : 10.1002/anie.201409050.Photobiomodulation Suppresses Alpha-Synuclein-Induced Toxicity in an AAV-Based Rat Genetic Model of Parkinson's Disease
PloS One. 2015. DOI : 10.1371/journal.pone.0140880.Structural differences of amyloid-beta fibrils revealed by antibodies from phage display
Bmc Biotechnology. 2015. DOI : 10.1186/s12896-015-0146-8.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
Human Molecular Genetics. 2014. DOI : 10.1093/hmg/ddu165.The role of fibril formation and growth in a-synuclein mediated extracellular toxicity
Lausanne, EPFL, 2014. DOI : 10.5075/epfl-thesis-6106.Protein semisynthesis and total synthesis approaches to elucidate the role of Alpha-Synuclein post-translational modifications
Lausanne, EPFL, 2014. DOI : 10.5075/epfl-thesis-6187.c-Abl phosphorylates α-synuclein and regulates its degradation: implication for α-synuclein clearance and contribution to the pathogenesis of Parkinson's disease
Human molecular genetics. 2014. DOI : 10.1093/hmg/ddt674.NOVEL MECHANISM-BASED INHIBITORS OF A beta AGGREGATION AND TOXICITY
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
Lausanne, EPFL, 2014. DOI : 10.5075/epfl-thesis-6188.The role of S129 phosphorylation in regulating the cellular properties and secretion of alpha-synuclein : implication for alpha-synuclein function in health and disease
Lausanne, EPFL, 2014. DOI : 10.5075/epfl-thesis-6110.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
Angewandte Chemie International Edition. 2014. DOI : 10.1002/anie.201307510.Reversible attachment of Cell-Penetrating Peptides for the efficient delivery of α-synuclein to HeLa cells and primary cortical neurons
Lausanne, EPFL, 2014. DOI : 10.5075/epfl-thesis-6412.Polo-like kinase 2 regulates selective autophagic α-synuclein clearance and suppresses its toxicity in vivo
Proceedings Of The National Academy Of Sciences Of The United States Of America (PNAS). 2013. DOI : 10.1073/pnas.1309991110.Alpha-synuclein Post-translational Modifications as Potential Biomarkers for Parkinson Disease and Other Synucleinopathies
Molecular & Cellular Proteomics. 2013. DOI : 10.1074/mcp.R113.032730.Real-time Amyloid Aggregation Monitoring with a Photonic Crystal-based Approach
ChemPhysChem. 2013. DOI : 10.1002/cphc.201300633.Parkin depletion delays motor decline dose-dependently without overtly affecting neuropathology in alpha-synuclein transgenic mice
BMC neuroscience. 2013. DOI : 10.1186/1471-2202-14-135.One-pot total chemical synthesis of human α-synuclein
Chemical Communications (ChemComm). 2013. DOI : 10.1039/c3cc45353g.Novel Mechanistic Insight into the Molecular Basis of Amyloid Polymorphism and Secondary Nucleation during Amyloid Formation
Journal of molecular biology. 2013. DOI : 10.1016/j.jmb.2013.02.005.Synthetic polyubiquitinated α-Synuclein reveals important insights into the roles of the ubiquitin chain in regulating its pathophysiology
Proceedings Of The National Academy Of Sciences Of The United States Of America (PNAS). 2013. DOI : 10.1073/pnas.1315654110.The many faces of α-synuclein: from structure and toxicity to therapeutic target
Nature reviews. Neuroscience. 2013. DOI : 10.1038/nrn3406.Oxidative and nitrative alpha-synuclein modifications and proteostatic stress: implications for disease mechanisms and interventions in synucleinopathies
Journal of neurochemistry. 2013. DOI : 10.1111/jnc.12226.Phosphorylation of α-synuclein is crucial in compensating for proteasomal dysfunction
Biochemical and biophysical research communications. 2012. DOI : 10.1016/j.bbrc.2012.06.159.Discovery of a novel aggregation domain in the huntingtin protein: implications for the mechanisms of Htt aggregation and toxicity
Angewandte Chemie (International ed. in English). 2012. DOI : 10.1002/anie.201206561.Reactive oxidative species enhance amyloid toxicity in APP/PS1 mouse neurons
Neuroscience Bulletin. 2012. DOI : 10.1007/s12264-012-1239-1.Chemical strategies for controlling protein folding and elucidating the molecular mechanisms of amyloid formation and toxicity
Journal of molecular biology. 2012. DOI : 10.1016/j.jmb.2012.01.051.Elucidating the role of C-terminal post-translational modifications using protein semisynthesis strategies: α-synuclein phosphorylation at tyrosine 125
Journal of the American Chemical Society. 2012. DOI : 10.1021/ja210866j.Characterization of semisynthetic and naturally Nα-acetylated α-synuclein in vitro and in intact cells: implications for aggregation and cellular properties of α-synuclein
Journal of Biological Chemistry. 2012. DOI : 10.1074/jbc.M112.383711.Establishing the links between Aβ aggregation and cytotoxicity in vitro using biophysical approaches
Methods in molecular biology (Clifton, N.J.). 2012. DOI : 10.1007/978-1-61779-551-0_16.Measurement of intrinsic properties of amyloid fibrils by the peak force QNM method
Nanoscale. 2012. DOI : 10.1039/c2nr30768e.The Size of the Proteasomal Substrate Determines Whether Its Degradation Will Be Mediated by Mono- or Polyubiquitylation
Molecular cell. 2012. DOI : 10.1016/j.molcel.2012.07.011.Elucidating the role of post-translational modifications of alpha-synuclein using semisynthesis : phosphorylation at Tyrosine 125 and monoubiquitination at Lysine 6
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
Journal of Biological Chemistry. 2012. DOI : 10.1074/jbc.M112.357665.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
The Journal of neuroscience : the official journal of the Society for Neuroscience. 2012. DOI : 10.1523/JNEUROSCI.3784-11.2012.Characterization of Molecular Determinants of the Conformational Stability of Macrophage Migration Inhibitory Factor: Leucine 46 Hydrophobic Pocket
PLoS ONE. 2012. DOI : 10.1371/journal.pone.0045024.α-Synuclein in central nervous system and from erythrocytes, mammalian cells, and Escherichia coli exists predominantly as disordered monomer
Journal of Biological Chemistry. 2012. DOI : 10.1074/jbc.M111.318949.Semisynthesis and Total Chemical Synthesis of alpha-synuclein to study Post-Translational Modifications in Health and Disease
2011. 22nd American Peptide Symposium, San Diego, CA, Jun 25-30, 2011. p. 523 - 523.Chemical Biology of alpha-synuclein: The role post-translational modification in the pathogenesis of Parkinson's disease & related disorders
2011. 22nd American Peptide Symposium, San Diego, CA, Jun 25-30, 2011. p. 413 - 413.Novel chemical tools to facilitate the synthesis and control the folding and Self-assembly of amyloid-forming polypeptides
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)
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
Acs Chemical Neuroscience. 2011. DOI : 10.1021/cn200074d.Arab world needs its science diaspora
Nature. 2011. DOI : 10.1038/472418d.Characterization and application of novel chemical tools to control folding and amyloid formation
2011Nucleation 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
Lausanne, EPFL, 2010. DOI : 10.5075/epfl-thesis-4773.Entacapone and tolcapone, two catechol O-methyltransferase inhibitors, block fibril formation of alpha-synuclein and beta-amyloid and protect against amyloid-induced toxicity
Journal of Biological Chemistry. 2010. DOI : 10.1074/jbc.M109.080390.Phosphorylation at S87 is enhanced in synucleinopathies, inhibits alpha-synuclein oligomerization, and influences synuclein-membrane interactions
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
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
Journal of biomolecular screening. 2010. DOI : 10.1177/1087057110363825.Amyloid-beta aggregates cause alterations of astrocytic metabolic phenotype: impact on neuronal viability
The Journal of neuroscience : the official journal of the Society for Neuroscience. 2010. DOI : 10.1523/JNEUROSCI.5098-09.2010.Small Molecule Based Approaches to Inhibit Macrophage Migration Inhibitory Factor (MIF) Activities and Elucidate its Role in Health and Disease
Lausanne, EPFL, 2010. DOI : 10.5075/epfl-thesis-4633.Phosphorylation of synucleins by members of the Polo-like kinase family
Journal of Biological Chemistry. 2010. DOI : 10.1074/jbc.M109.081950.An integrative in silico methodology for the identification of modulators of macrophage migration inhibitory factor (MIF) tautomerase activity
Bioorganic & medicinal chemistry. 2010. DOI : 10.1016/j.bmc.2010.05.010.The anti-Parkinsonian drug selegiline delays the nucleation phase of α-synuclein aggregation leading to the formation of nontoxic species
Journal of molecular biology. 2010. DOI : 10.1016/j.jmb.2010.10.027.Identification and characterization of novel classes of macrophage migration inhibitory factor (MIF) inhibitors with distinct mechanisms of action
Journal of Biological Chemistry. 2010. DOI : 10.1074/jbc.M110.113951.Elucidating the Role of Quaternary Structure in Modulating Macrophage Migration Inhibitory Factor (MIF) Functions
Lausanne, EPFL, 2010. DOI : 10.5075/epfl-thesis-4632.Amyloidogenic protein-membrane interactions: mechanistic insight from model systems
Angewandte Chemie (International ed. in English). 2010. DOI : 10.1002/anie.200906670.Parkinson-related parkin reduces α-Synuclein phosphorylation in a gene transfer model
Molecular neurodegeneration. 2010. DOI : 10.1186/1750-1326-5-47.Role of post-translational modifications in modulating the structure, function and toxicity of alpha-synuclein: implications for Parkinson's disease pathogenesis and therapies
Progress in brain research. 2010. DOI : 10.1016/S0079-6123(10)83007-9.Stable -Synuclein Oligomers Strongly Inhibit Chaperone Activity of the Hsp70 System by Weak Interactions with J-domain Co-chaperones
Journal of Biological Chemistry. 2010. DOI : 10.1074/jbc.M110.127753.A new class of isothiocyanate-based irreversible inhibitors of macrophage migration inhibitory factor
Biochemistry. 2009. DOI : 10.1021/bi900957e.E46K Parkinson's-linked mutation enhances C-terminal-to-N-terminal contacts in alpha-synuclein
Journal of molecular biology. 2009. DOI : 10.1016/j.jmb.2009.03.065.Structural properties of pore-forming oligomers of alpha-synuclein
Journal of the American Chemical Society. 2009. DOI : 10.1021/ja9077599.Parkin deficiency delays motor decline and disease manifestation in a mouse model of synucleinopathy
PloS One. 2009. DOI : 10.1371/journal.pone.0006629.Switch-peptides as folding precursors in self-assembling peptides and amyloid fibrillogenesis
Advances in experimental medicine and biology. 2009. DOI : 10.1007/978-0-387-73657-0_126.The role of post-translational modification (phosphorylation) in modulating alpha-synuclein, structure, aggregation and toxicity
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
Biopolymers. 2009. DOI : 10.1002/bip.21301.Amyloid-Beta Modifies Astrocytic Metabolic Phenotype
22nd Biennial Meeting of the International-Society-of-Neurochemistry/Asian-Pacific-Society-for-Neurochemistry, Busan, SOUTH KOREA, Aug 23-29, 2009.Dissecting the mechanisms of tissue transglutaminase-induced cross-linking of alpha-synuclein: implications for the pathogenesis of Parkinson disease
Journal of Biological Chemistry. 2009. DOI : 10.1074/jbc.M809067200.Highly efficient and chemoselective peptide ubiquitylation
Angewandte Chemie (International ed. in English). 2009. DOI : 10.1002/anie.200902936.Amyloids go genomic: insights regarding the sequence determinants of prion formation from genome-wide studies
Chembiochem : a European journal of chemical biology. 2009. DOI : 10.1002/cbic.200900373.Hsp104 antagonizes alpha-synuclein aggregation and reduces dopaminergic degeneration in a rat model of Parkinson disease
The Journal of clinical investigation. 2008. DOI : 10.1172/JCI35781.Apomorphine inhibitors of amyloid-beta (abeta) fibril formation and their use in amyloidosis based disease
US2008096909 ; US2003187011 . 2008.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
Biochemistry. 2008. DOI : 10.1021/bi800603x.Inhibition of alpha-synuclein fibrillization by dopamine is mediated by interactions with five C-terminal residues and with E83 in the NAC region
PloS One. 2008. DOI : 10.1371/journal.pone.0003394.Switch peptide via Staudinger reaction
Organic Letters. 2008. DOI : 10.1021/ol802268e.Phosphorylation at Ser-129 but not the phosphomimics S129E/D inhibits the fibrillation of alpha-synuclein
Journal of Biological Chemistry. 2008. DOI : 10.1074/jbc.M800747200.The ratio of monomeric to aggregated forms of Abeta40 and Abeta42 is an important determinant of amyloid-beta aggregation, fibrillogenesis, and toxicity
Journal of Biological Chemistry. 2008. DOI : 10.1074/jbc.M803159200.Switch-peptides: design and characterization of controllable super-amyloid-forming host-guest peptides as tools for identifying anti-amyloid agents
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
Journal of molecular biology. 2008. DOI : 10.1016/j.jmb.2008.09.063.Switch-peptides as folding precursors in self-assembling peptides and amyloid fibrillogenesis
Biopolymers. 2007. DOI : 10.1002/bip.20663.Branched KLVFF tetramers strongly potentiate inhibition of beta-amyloid aggregation
Chembiochem : a European journal of chemical biology. 2007. DOI : 10.1002/cbic.200700338.Dopamine affects the stability, hydration, and packing of protofibrils and fibrils of the wild type and variants of alpha-synuclein
Biochemistry. 2007. DOI : 10.1021/bi061871+.The impact of the E46K mutation on the properties of alpha-synuclein in its monomeric and oligomeric states
Biochemistry. 2007. DOI : 10.1021/bi7000246.Disruption of amyloid-derived peptide assemblies through the controlled induction of a beta-sheet to alpha-helix transformation: application of the switch concept
Angewandte Chemie International Edition. 2007. DOI : 10.1002/anie.200603681.Switch-peptides: from conformational studies to Alzheimer's disease
CHIMIA. 2006. DOI : 10.2533/000942906777674921.Are amyloid diseases caused by protein aggregates that mimic bacterial pore-forming toxins?
Quarterly reviews of biophysics. 2006. DOI : 10.1017/S0033583506004422.A century-old debate on protein aggregation and neurodegeneration enters the clinic
Nature. 2006. DOI : 10.1038/nature05290.Islam: governments need to reform education and build a scientific culture
Nature. 2006. DOI : 10.1038/444545a.Rescuing defective vesicular trafficking protects against alpha-synuclein toxicity in cellular and animal models of Parkinson's disease
ACS chemical biology. 2006. DOI : 10.1021/cb600331e.Production and characterization of astrocyte-derived human apolipoprotein E isoforms from immortalized astrocytes and their interactions with amyloid-beta
Neurobiology of disease. 2005. DOI : 10.1016/j.nbd.2004.11.005.In vitro preparation of prefibrillar intermediates of amyloid-beta and alpha-synuclein
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
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
Science of aging knowledge environment : SAGE KE. 2005. DOI : 10.1126/sageke.2005.38.pe28.The materials science of protein aggregation
MRS Bulletin. 2005. DOI : 10.1557/mrs2005.123.From hexamer to amyloid: marginal stability of apolipoprotein SAA2.2 leads to in vitro fibril formation at physiological temperature
Amyloid : the international journal of experimental and clinical investigation : the official journal of the International Society of Amyloidosis. 2005. DOI : 10.1080/13506120500223084.Lead (Pb) exposure and its effect on APP proteolysis and Abeta aggregation
The FASEB journal : official publication of the Federation of American Societies for Experimental Biology. 2005. DOI : 10.1096/fj.05-4375fje.Amyloid fibril formation by macrophage migration inhibitory factor
Biochemical and biophysical research communications. 2005. DOI : 10.1016/j.bbrc.2005.10.040.Quaternary structure, protein dynamics, and synaptic function of SAP97 controlled by L27 domain interactions
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
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
WO03053356 ; AU2002357911 ; AU2002357911 ; WO03053356 ; CA2479263 . 2003.Discovery of inhibitors that elucidate the role of UCH-L1 activity in the H1299 lung cancer cell line
Chemistry & biology. 2003. DOI : 10.1016/j.chembiol.2003.08.010.hA molecular switch in amyloid assembly: Met35 and amyloid beta-protein oligomerization
Journal of the American Chemical Society. 2003. DOI : 10.1021/ja0349296.Abeta protofibrils possess a stable core structure resistant to hydrogen exchange
Biochemistry. 2003. DOI : 10.1021/bi0357816.Dissociation of amyloid fibrils of alpha-synuclein and transthyretin by pressure reveals their reversible nature and the formation of water-excluded cavities
Proceedings Of The National Academy Of Sciences Of The United States Of America (PNAS). 2003. DOI : 10.1073/pnas.1734009100.Hydration and packing are crucial to amyloidogenesis as revealed by pressure studies on transthyretin variants that either protect or worsen amyloid disease
Journal of molecular biology. 2003. DOI : 10.1016/S0022-2836(03)00368-1.Mixtures of wild-type and a pathogenic (E22G) form of Abeta40 in vitro accumulate protofibrils, including amyloid pores
Journal of molecular biology. 2003. DOI : 10.1016/S0022-2836(03)00927-6.New class of inhibitors of amyloid-beta fibril formation. Implications for the mechanism of pathogenesis in Alzheimer's disease
Journal of Biological Chemistry. 2002. DOI : 10.1074/jbc.M206593200.Murine apolipoprotein serum amyloid A in solution forms a hexamer containing a central channel
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
Nature. 2002. DOI : 10.1038/418291a.Alpha-synuclein, especially the Parkinson's disease-associated mutants, forms pore-like annular and tubular protofibrils
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
Journal of medicinal chemistry. 2002. DOI : 10.1021/jm010257n.The UCH-L1 gene encodes two opposing enzymatic activities that affect alpha-synuclein degradation and Parkinson's disease susceptibility
Cell. 2002. DOI : 10.1016/S0092-8674(02)01012-7.A glimpse of a possible amyloidogenic intermediate of transthyretin
Nature structural biology. 2000. DOI : 10.1038/78980.Nuclear import factors importin alpha and importin beta undergo mutually induced conformational changes upon association
FEBS letters. 2000. DOI : 10.1016/S0014-5793(00)02154-2.Protofilaments, filaments, ribbons, and fibrils from peptidomimetic self-assembly: Implications for amyloid fibril formation and materials science
Journal of the American Chemical Society. 2000. DOI : 10.1021/ja9937831.The most pathogenic transthyretin variant, L55P, forms amyloid fibrils under acidic conditions and protofilaments under physiological conditions
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
Biochemistry. 1999. DOI : 10.1021/bi981876+.Association between the first two immunoglobulin-like domains of the neural cell adhesion molecule N-CAM
FEBS letters. 1999. DOI : 10.1016/S0014-5793(99)00554-2.The nucleation of monomeric parallel beta-sheet-like structures and their self-assembly in aqueous solution
Bioorganic & medicinal chemistry. 1999. DOI : 10.1016/S0968-0896(98)00222-3.Comparative characterization of a wild type and transmembrane domain-deleted fatty acid amide hydrolase: identification of the transmembrane domain as a site for oligomerization
Biochemistry. 1998. DOI : 10.1021/bi981733n.Anti-amyloidogenic agents
WO9827972 ; WO9827972 ; AU5727798 ; WO9827972 . 1998.Complete inhibition of Cdk/cyclin by one molecule of p21(Cip1)
Genes & development. 1998. DOI : 10.1101/gad.12.24.3882.Inhibiting transthyretin conformational changes that lead to amyloid fibril formation
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
Protein expression and purification. 1998. DOI : 10.1006/prep.1998.0944.Transthyretin quaternary and tertiary structural changes facilitate misassembly into amyloid
Advances in protein chemistry. 1997. DOI : 10.1016/S0065-3233(08)60321-6.Oligomerization properties of GCN4 leucine zipper e and g position mutants
Protein science : a publication of the Protein Society. 1997. DOI : 10.1002/pro.5560061016.Guanidine hydrochloride-induced denaturation and refolding of transthyretin exhibits a marked hysteresis: equilibria with high kinetic barriers
Biochemistry. 1997. DOI : 10.1021/bi963195p.Inhibiting transthyretin amyloid fibril formation via protein stabilization
Proceedings Of The National Academy Of Sciences Of The United States Of America (PNAS). 1996. DOI : 10.1073/pnas.93.26.15051.Infoscience
Huntingtin inclusion bodies have distinct immunophenotypes and ubiquitination profiles in the Huntington’s disease human cerebral cortex
Scientific Reports. 2025. DOI : 10.1038/s41598-025-00465-w.Amyotrophic lateral sclerosis caused by TARDBP mutations: from genetics to TDP-43 proteinopathy
The Lancet Neurology. 2025. DOI : 10.1016/S1474-4422(25)00109-7.Alpha-synuclein seed amplification assays: Data sharing, standardization needed for clinical use
Science Advances. 2025. DOI : 10.1126/sciadv.adt7195.Multi-Targeting Macrocyclic Peptides as Nanomolar Inhibitors of Self- and Cross-Seeded Amyloid Self-Assembly of α-Synuclein
ANGEWANDTE CHEMIE-INTERNATIONAL EDITION. 2025. DOI : 10.1002/anie.202422834.Intelligent and Self-Driving Microscopy of Protein Aggregation in Neurodegenerative Diseases
Lausanne, EPFL, 2025. DOI : 10.5075/epfl-thesis-11337.Nanoplasmonic infrared biosensors enabling detection of misfolded protein biomarkers and drug screening for neurodegenerative diseases
Lausanne, EPFL, 2025. DOI : 10.5075/epfl-thesis-10478.Uses of aerolysin nanopores
WO2025003492 . 2025.Mouse α-synuclein fibrils are structurally and functionally distinct from human fibrils associated with Lewy body diseases
Science advances. 2024. DOI : 10.1126/sciadv.adq3539.Research Priorities on the Role of α-Synuclein in Parkinson's Disease Pathogenesis
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
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
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
2024Post-translational glycosylation diminishes α-synuclein pathology formation
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
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)
NPJ PARKINSONS DISEASE. 2024. DOI : 10.1038/s41531-024-00634-0.Transactive response dna-binding protein 43kda (tdp-43) mutants and uses thereof
WO2024223615 . 2024.Exploring the therapeutic potential of Huntingtin native state stabilization through targeting its interacting partners
Lausanne, EPFL, 2024. DOI : 10.5075/epfl-thesis-10915.Effective Inhibition of TDP-43 Aggregation by Native State Stabilization
Angewandte Chemie International Edition. 2024. DOI : 10.1002/anie.202314587.Deep learning augmented nanoplasmonic infrared sensor for structural protein biomarker-based detection of neurodegenerative diseases
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.Dielectrophoretic Manipulation of Biological Species: Novel Microfluidic Approaches to Study Cell-Cell Interactions and the Role of Alpha-Synuclein in Neurodegeneration
Lausanne, EPFL, 2024. DOI : 10.5075/epfl-thesis-10597.Method of preparation of amyloidogenic protein aggregates and uses thereof
WO2024094597 . 2024.Investigating the intra-molecular and inter-molecular effects of post-translational modifications on intrinsically disordered protein regions and structured protein regions
Lausanne, EPFL, 2024. DOI : 10.5075/epfl-thesis-10530.Author Correction: Fully co-factor-free ClearTau platform produces seeding-competent Tau fibrils for reconstructing pathological Tau aggregates
Nature Communications. 2024. DOI : 10.1038/s41467-024-48976-w.Targeting TDP-43 Proteinopathies in Neurodegeneration by its Native-State Stabilization
Lausanne, EPFL, 2024. DOI : 10.5075/epfl-thesis-10555.Recombinant Full-Length TDP-43 Oligomers Retain Their Ability to Bind RNAs, Are Not Toxic, and Do Not Seed TDP-43 Aggregation in Vitro
Acs Chemical Neuroscience. 2023. DOI : 10.1021/acschemneuro.3c00691.Deep Learning-Assisted Single-Molecule Detection of Protein Post-translational Modifications with a Biological Nanopore
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
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
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
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
Science Advances. 2023. DOI : 10.1126/sciadv.adg9644.Seeding the aggregation of TDP-43 requires post-fibrillization proteolytic cleavage
Nature Neuroscience. 2023. DOI : 10.1038/s41593-023-01341-4.Neuronal growth on high-aspect-ratio diamond nanopillar arrays for biosensing applications
Scientific Reports. 2023. DOI : 10.1038/s41598-023-32235-x.Deconstructing and Reconstructing the Complexity of Tau pathology
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
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
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
Neurobiology Of Disease. 2022. DOI : 10.1016/j.nbd.2022.105884.Pathological substrate of memory impairment in multiple system atrophy
Neuropathology And Applied Neurobiology. 2022. DOI : 10.1111/nan.12844.Identification of key segments of IAPP/aSyn cross-amyloid interactions
2022.Opportunities and challenges of alpha-synuclein as a potential biomarker for Parkinson's disease and other synucleinopathies
Npj Parkinsons Disease. 2022. DOI : 10.1038/s41531-022-00357-0.On-Demand Nanoliter Sampling Probe for the Collection of Brain Fluid
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
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
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
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
Cells. 2022. DOI : 10.3390/cells11050906.The role of PTM crosstalks in Httex1 structure, aggregation and membrane interaction
2022. p. 38 - 38. DOI : 10.1016/j.bpj.2021.11.2495.Capturing the heterogeneity of alpha-synuclein pathology in synucleinopathies
Lausanne, EPFL, 2022. DOI : 10.5075/epfl-thesis-8480.Comparative Analysis of Total Alpha-Synuclein (alpha SYN) Immunoassays Reveals That They Do Not Capture the Diversity of Modified alpha SYN Proteoforms
Journal Of Parkinsons Disease. 2022. DOI : 10.3233/JPD-223285.An integrative approach to elucidate the mechanisms and dynamics of Huntingtin aggregation and inclusion formation in neuronal models of Huntington's Disease
Lausanne, EPFL, 2022. DOI : 10.5075/epfl-thesis-9296.Towards elucidating the structural and cellular determinants of a-synuclein seeding and toxicity
Lausanne, EPFL, 2022. DOI : 10.5075/epfl-thesis-9365.Non-monotonic fibril surface occlusion by GFP tags from coarse-grained molecular simulations
Computational and Structural Biotechnology Journal. 2022. DOI : 10.1016/j.csbj.2021.12.017.Revisiting the grammar of Tau aggregation and pathology formation: how new insights from brain pathology are shaping how we study and target Tauopathies
Chemical Society Reviews. 2022. DOI : 10.1039/d1cs00127b.To target Tau pathologies, we must embrace and reconstruct their complexities
Neurobiology Of Disease. 2021. DOI : 10.1016/j.nbd.2021.105536.Nuclear and cytoplasmic huntingtin inclusions exhibit distinct biochemical composition, interactome and ultrastructural properties
Nature Communications. 2021. DOI : 10.1038/s41467-021-26684-z.Fatal attraction-The role of hypoxia when alpha-synuclein gets intimate with mitochondria
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
Journal of Molecular Biology. 2021. DOI : 10.1016/j.jmb.2021.167222.Pharmacological characterization of mutant huntingtin aggregate-directed PET imaging tracer candidates
Scientific Reports. 2021. DOI : 10.1038/s41598-021-97334-z.Alpha-synuclein research: defining strategic moves in the battle against Parkinson's disease
Npj Parkinsons Disease. 2021. DOI : 10.1038/s41531-021-00203-9.Investigating Crosstalk Among PTMs Provides Novel Insight Into the Structural Basis Underlying the Differential Effects of Nt17 PTMs on Mutant Httex1 Aggregation
Frontiers in Molecular Biosciences. 2021. DOI : 10.3389/fmolb.2021.686086.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
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?
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
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
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
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
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?".
Journal Of Neurochemistry. 2021. DOI : 10.1111/jnc.15275.Hypoxia Conditioning as a Promising Therapeutic Target in Parkinson's Disease?
Movement Disorders. 2021. DOI : 10.1002/mds.28544.Reverse engineering Lewy bodies: how far have we come and how far can we go?
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
Journal of Neurochemistry. 2021. DOI : 10.1111/jnc.15147.Site-Specific Phosphorylation of Huntingtin Exon 1 Recombinant Proteins Enabled by the Discovery of Novel Kinases
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
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
The EMBO Journal. 2020. DOI : 10.15252/embj.2020104671.Half a century of amyloids: past, present and future
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
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
Journal of Biological Chemistry. 2020. DOI : 10.1074/jbc.RA119.012517.Extent of N-terminus exposure of monomeric alpha-synuclein determines its aggregation propensity
Nature Communications. 2020. DOI : 10.1038/s41467-020-16564-3.Education and research are essential for lasting peace in Yemen
Lancet. 2020. DOI : 10.1016/S0140-6736(20)30162-8.Unraveling the complexity of amyloid polymorphism using gold nanoparticles and cryo-EM
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
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
Journal Of Neurochemistry. 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
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
Angewandte Chemie International Edition. 2020. DOI : 10.1002/anie.201913001.Ultrasensitive quantitative measurement of huntingtin phosphorylation at residue S13
Biochemical And Biophysical Research Communications. 2020. DOI : 10.1016/j.bbrc.2019.09.097.What about faculty?
Elife. 2020. DOI : 10.7554/eLife.54551.Development of novel methods and tools to decipher the huntingtin post-translation modifications code
Lausanne, EPFL, 2020. DOI : 10.5075/epfl-thesis-7537.Gold nanoparticles as a new tool in amyloid studies
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
eNeuro. 2020. DOI : 10.1523/ENEURO.0110-20.2020.The Role of Post-translational Modifications on the Energy Landscape of Huntingtin N-Terminus
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
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
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
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
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
US11629175 ; US2021238242 ; EP3784687 ; WO2019207164 . 2019.Generation of Native, Untagged Huntingtin Exon1 Monomer and Fibrils Using a SUMO Fusion Strategy
Journal of Visualized Experiments. 2018. DOI : 10.3791/57506.Exploring the role of post-translational modifications in regulating α-synuclein interactions by studying the effects of phosphorylation on nanobody binding
Proteins Science. 2018. DOI : 10.1002/pro.3412.Combined Multi-Plane Tomographic Phase Retrieval and Stochastic Optical Fluctuation Imaging for 4D Cell Microscopy
Nature Photonics. 2018. DOI : 10.1038/s41566-018-0109-4.Amyloid Single Cell Cytotoxicity Assays by Nanomotion Detection
Cell Death Discovery. 2017. DOI : 10.1038/cddiscovery.2017.53.A user's guide for α-synuclein biomarker studies in biological fluids: Perianalytical considerations
Movement Disorders. 2017. DOI : 10.1002/mds.27090.Monomeric Huntingtin Exon 1 Has Similar Overall Structural Features for Wild-Type and Pathological Polyglutamine Lengths
Journal of the American Chemical Society. 2017. DOI : 10.1021/jacs.7b06659.Membrane scission driven by the PROPPIN Atg18
Embo Journal. 2017. DOI : 10.15252/embj.201796859.Polyglutamine expansion affects huntingtin conformation in multiple Huntington’s disease models
Scientific Reports. 2017. DOI : 10.1038/s41598-017-05336-7.Activation of the STING-dependent type I interferon response reduces microglial reactivity and neuroinflammation
Neuron. 2017. DOI : 10.1016/j.neuron.2017.11.032.Polyglutamine Length Dependent Structural Properties and Phase Behavior of Huntingtin Exon 1
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.Glycation potentiates α-synuclein-associated neurodegeneration in synucleinopathies
Brain : a journal of neurology. 2017. DOI : 10.1093/brain/awx056.The mechanism of sirtuin 2-mediated exacerbation of alpha-synuclein toxicity in models of Parkinson disease
PLoS Biology. 2017. DOI : 10.1371/journal.pbio.2000374.Mutant Exon1 Huntingtin Aggregation is Regulated by T3 Phosphorylation-Induced Structural Changes and Crosstalk between T3 Phosphorylation and Acetylation at K6
Angewandte Chemie (International ed. in English). 2017. DOI : 10.1002/anie.201611750.The role of the polyglutamine and N-terminal domains in regulating the aggregation and structural properties of Huntingtin Exon 1
Lausanne, EPFL, 2017. DOI : 10.5075/epfl-thesis-7374.Human and eco-toxicological impacts of organometallic halide perovskites
Lausanne, EPFL, 2017. DOI : 10.5075/epfl-thesis-7595.The America I believe in
Science. 2017. DOI : 10.1126/science.355.6326.766.Ganciclovir derivatives for modulating innate and adaptive immunity and for use in immunotherapy
US9809597 ; US2017050967 . 2017.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
Nature Communications. 2017. DOI : 10.1038/s41467-017-01575-4.Sequence and structural determinants of Tau aggregation and seeding capacity: Implications for Neurofibrillary Tangle formation and Tau toxicity in Alzheimer's disease
Lausanne, EPFL, 2017. DOI : 10.5075/epfl-thesis-7985.A New Caged-Glutamine Derivative as a Tool To Control the Assembly of Glutamine-Containing Amyloidogenic Peptides
Chembiochem : a European journal of chemical biology. 2016. DOI : 10.1002/cbic.201600474.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
Journal of Biological Chemistry. 2016. DOI : 10.1074/jbc.M116.713982.Microtubule-Binding R3 Fragment from Tau Self-Assembles into Giant Multistranded Amyloid Ribbons
Angewandte Chemie International Edition. 2016. DOI : 10.1002/anie.201508968.Semisynthetic and in Vitro Phosphorylation of Alpha-Synuclein at Y39 Promotes Functional Partly Helical Membrane-Bound States Resembling Those Induced by PD Mutations
Acs Chemical Biology. 2016. DOI : 10.1021/acschembio.6b00539.Health hazards of methylammonium lead iodide based perovskites: cytotoxicity studies
Toxicol. Res.. 2016. DOI : 10.1039/C5TX00303B.Induction of de novo α-synuclein fibrillization in a neuronal model for Parkinson's disease
Proceedings Of The National Academy Of Sciences Of The United States Of America (PNAS). 2016. DOI : 10.1073/pnas.1512876113.Parkinson's Disease Genes VPS35 and EIF4G1 Interact Genetically and Converge on α-Synuclein
Neuron. 2015. DOI : 10.1016/j.neuron.2014.11.027.Fibril growth and seeding capacity play key roles in α-synuclein-mediated apoptotic cell death
Cell death and differentiation. 2015. DOI : 10.1038/cdd.2015.79.Novel therapeutic strategy for neurodegeneration by blocking Aβ seeding mediated aggregation in models of Alzheimer's disease
Neurobiology of disease. 2015. DOI : 10.1016/j.nbd.2014.08.017.Parkinson disease mutant E46K enhances α-synuclein phosphorylation in mammalian cell lines, in yeast, and in vivo
Journal of Biological Chemistry. 2015. DOI : 10.1074/jbc.M114.610774.Elucidating the Role of Site-Specific Nitration of alpha-Synuclein in the Pathogenesis of Parkinson's Disease via Protein Semisynthesis and Mutagenesis
Journal Of The American Chemical Society. 2015. DOI : 10.1021/ja5131726.Semisynthesis and Enzymatic Preparation of Post-translationally Modified α-Synuclein
Methods in molecular biology (Clifton, N.J.). 2015. DOI : 10.1007/978-1-4939-2978-8_1.Recapitulating De Novo Alpha-Synuclein Fibrillization in a Novel Neuronal Model of Parkinson's Disease
Lausanne, EPFL, 2015. DOI : 10.5075/epfl-thesis-6679.Influence of the β-sheet content on the mechanical properties of aggregates during amyloid fibrillization
Angewandte Chemie (International ed. in English). 2015. DOI : 10.1002/anie.201409050.Photobiomodulation Suppresses Alpha-Synuclein-Induced Toxicity in an AAV-Based Rat Genetic Model of Parkinson's Disease
PloS One. 2015. DOI : 10.1371/journal.pone.0140880.Structural differences of amyloid-beta fibrils revealed by antibodies from phage display
Bmc Biotechnology. 2015. DOI : 10.1186/s12896-015-0146-8.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
Human Molecular Genetics. 2014. DOI : 10.1093/hmg/ddu165.The role of fibril formation and growth in a-synuclein mediated extracellular toxicity
Lausanne, EPFL, 2014. DOI : 10.5075/epfl-thesis-6106.Protein semisynthesis and total synthesis approaches to elucidate the role of Alpha-Synuclein post-translational modifications
Lausanne, EPFL, 2014. DOI : 10.5075/epfl-thesis-6187.c-Abl phosphorylates α-synuclein and regulates its degradation: implication for α-synuclein clearance and contribution to the pathogenesis of Parkinson's disease
Human molecular genetics. 2014. DOI : 10.1093/hmg/ddt674.NOVEL MECHANISM-BASED INHIBITORS OF A beta AGGREGATION AND TOXICITY
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
Lausanne, EPFL, 2014. DOI : 10.5075/epfl-thesis-6188.The role of S129 phosphorylation in regulating the cellular properties and secretion of alpha-synuclein : implication for alpha-synuclein function in health and disease
Lausanne, EPFL, 2014. DOI : 10.5075/epfl-thesis-6110.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
Angewandte Chemie International Edition. 2014. DOI : 10.1002/anie.201307510.Reversible attachment of Cell-Penetrating Peptides for the efficient delivery of α-synuclein to HeLa cells and primary cortical neurons
Lausanne, EPFL, 2014. DOI : 10.5075/epfl-thesis-6412.Polo-like kinase 2 regulates selective autophagic α-synuclein clearance and suppresses its toxicity in vivo
Proceedings Of The National Academy Of Sciences Of The United States Of America (PNAS). 2013. DOI : 10.1073/pnas.1309991110.Alpha-synuclein Post-translational Modifications as Potential Biomarkers for Parkinson Disease and Other Synucleinopathies
Molecular & Cellular Proteomics. 2013. DOI : 10.1074/mcp.R113.032730.Real-time Amyloid Aggregation Monitoring with a Photonic Crystal-based Approach
ChemPhysChem. 2013. DOI : 10.1002/cphc.201300633.Parkin depletion delays motor decline dose-dependently without overtly affecting neuropathology in alpha-synuclein transgenic mice
BMC neuroscience. 2013. DOI : 10.1186/1471-2202-14-135.One-pot total chemical synthesis of human α-synuclein
Chemical Communications (ChemComm). 2013. DOI : 10.1039/c3cc45353g.Novel Mechanistic Insight into the Molecular Basis of Amyloid Polymorphism and Secondary Nucleation during Amyloid Formation
Journal of molecular biology. 2013. DOI : 10.1016/j.jmb.2013.02.005.Synthetic polyubiquitinated α-Synuclein reveals important insights into the roles of the ubiquitin chain in regulating its pathophysiology
Proceedings Of The National Academy Of Sciences Of The United States Of America (PNAS). 2013. DOI : 10.1073/pnas.1315654110.The many faces of α-synuclein: from structure and toxicity to therapeutic target
Nature reviews. Neuroscience. 2013. DOI : 10.1038/nrn3406.Oxidative and nitrative alpha-synuclein modifications and proteostatic stress: implications for disease mechanisms and interventions in synucleinopathies
Journal of neurochemistry. 2013. DOI : 10.1111/jnc.12226.Phosphorylation of α-synuclein is crucial in compensating for proteasomal dysfunction
Biochemical and biophysical research communications. 2012. DOI : 10.1016/j.bbrc.2012.06.159.Discovery of a novel aggregation domain in the huntingtin protein: implications for the mechanisms of Htt aggregation and toxicity
Angewandte Chemie (International ed. in English). 2012. DOI : 10.1002/anie.201206561.Reactive oxidative species enhance amyloid toxicity in APP/PS1 mouse neurons
Neuroscience Bulletin. 2012. DOI : 10.1007/s12264-012-1239-1.Chemical strategies for controlling protein folding and elucidating the molecular mechanisms of amyloid formation and toxicity
Journal of molecular biology. 2012. DOI : 10.1016/j.jmb.2012.01.051.Elucidating the role of C-terminal post-translational modifications using protein semisynthesis strategies: α-synuclein phosphorylation at tyrosine 125
Journal of the American Chemical Society. 2012. DOI : 10.1021/ja210866j.Characterization of semisynthetic and naturally Nα-acetylated α-synuclein in vitro and in intact cells: implications for aggregation and cellular properties of α-synuclein
Journal of Biological Chemistry. 2012. DOI : 10.1074/jbc.M112.383711.Establishing the links between Aβ aggregation and cytotoxicity in vitro using biophysical approaches
Methods in molecular biology (Clifton, N.J.). 2012. DOI : 10.1007/978-1-61779-551-0_16.Measurement of intrinsic properties of amyloid fibrils by the peak force QNM method
Nanoscale. 2012. DOI : 10.1039/c2nr30768e.The Size of the Proteasomal Substrate Determines Whether Its Degradation Will Be Mediated by Mono- or Polyubiquitylation
Molecular cell. 2012. DOI : 10.1016/j.molcel.2012.07.011.Elucidating the role of post-translational modifications of alpha-synuclein using semisynthesis : phosphorylation at Tyrosine 125 and monoubiquitination at Lysine 6
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
Journal of Biological Chemistry. 2012. DOI : 10.1074/jbc.M112.357665.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
The Journal of neuroscience : the official journal of the Society for Neuroscience. 2012. DOI : 10.1523/JNEUROSCI.3784-11.2012.Characterization of Molecular Determinants of the Conformational Stability of Macrophage Migration Inhibitory Factor: Leucine 46 Hydrophobic Pocket
PLoS ONE. 2012. DOI : 10.1371/journal.pone.0045024.α-Synuclein in central nervous system and from erythrocytes, mammalian cells, and Escherichia coli exists predominantly as disordered monomer
Journal of Biological Chemistry. 2012. DOI : 10.1074/jbc.M111.318949.Semisynthesis and Total Chemical Synthesis of alpha-synuclein to study Post-Translational Modifications in Health and Disease
2011. 22nd American Peptide Symposium, San Diego, CA, Jun 25-30, 2011. p. 523 - 523.Chemical Biology of alpha-synuclein: The role post-translational modification in the pathogenesis of Parkinson's disease & related disorders
2011. 22nd American Peptide Symposium, San Diego, CA, Jun 25-30, 2011. p. 413 - 413.Novel chemical tools to facilitate the synthesis and control the folding and Self-assembly of amyloid-forming polypeptides
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)
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
Acs Chemical Neuroscience. 2011. DOI : 10.1021/cn200074d.Arab world needs its science diaspora
Nature. 2011. DOI : 10.1038/472418d.Characterization and application of novel chemical tools to control folding and amyloid formation
2011Nucleation 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
Lausanne, EPFL, 2010. DOI : 10.5075/epfl-thesis-4773.Entacapone and tolcapone, two catechol O-methyltransferase inhibitors, block fibril formation of alpha-synuclein and beta-amyloid and protect against amyloid-induced toxicity
Journal of Biological Chemistry. 2010. DOI : 10.1074/jbc.M109.080390.Phosphorylation at S87 is enhanced in synucleinopathies, inhibits alpha-synuclein oligomerization, and influences synuclein-membrane interactions
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
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
Journal of biomolecular screening. 2010. DOI : 10.1177/1087057110363825.Amyloid-beta aggregates cause alterations of astrocytic metabolic phenotype: impact on neuronal viability
The Journal of neuroscience : the official journal of the Society for Neuroscience. 2010. DOI : 10.1523/JNEUROSCI.5098-09.2010.Small Molecule Based Approaches to Inhibit Macrophage Migration Inhibitory Factor (MIF) Activities and Elucidate its Role in Health and Disease
Lausanne, EPFL, 2010. DOI : 10.5075/epfl-thesis-4633.Phosphorylation of synucleins by members of the Polo-like kinase family
Journal of Biological Chemistry. 2010. DOI : 10.1074/jbc.M109.081950.An integrative in silico methodology for the identification of modulators of macrophage migration inhibitory factor (MIF) tautomerase activity
Bioorganic & medicinal chemistry. 2010. DOI : 10.1016/j.bmc.2010.05.010.The anti-Parkinsonian drug selegiline delays the nucleation phase of α-synuclein aggregation leading to the formation of nontoxic species
Journal of molecular biology. 2010. DOI : 10.1016/j.jmb.2010.10.027.Identification and characterization of novel classes of macrophage migration inhibitory factor (MIF) inhibitors with distinct mechanisms of action
Journal of Biological Chemistry. 2010. DOI : 10.1074/jbc.M110.113951.Elucidating the Role of Quaternary Structure in Modulating Macrophage Migration Inhibitory Factor (MIF) Functions
Lausanne, EPFL, 2010. DOI : 10.5075/epfl-thesis-4632.Amyloidogenic protein-membrane interactions: mechanistic insight from model systems
Angewandte Chemie (International ed. in English). 2010. DOI : 10.1002/anie.200906670.Parkinson-related parkin reduces α-Synuclein phosphorylation in a gene transfer model
Molecular neurodegeneration. 2010. DOI : 10.1186/1750-1326-5-47.Role of post-translational modifications in modulating the structure, function and toxicity of alpha-synuclein: implications for Parkinson's disease pathogenesis and therapies
Progress in brain research. 2010. DOI : 10.1016/S0079-6123(10)83007-9.Stable -Synuclein Oligomers Strongly Inhibit Chaperone Activity of the Hsp70 System by Weak Interactions with J-domain Co-chaperones
Journal of Biological Chemistry. 2010. DOI : 10.1074/jbc.M110.127753.A new class of isothiocyanate-based irreversible inhibitors of macrophage migration inhibitory factor
Biochemistry. 2009. DOI : 10.1021/bi900957e.E46K Parkinson's-linked mutation enhances C-terminal-to-N-terminal contacts in alpha-synuclein
Journal of molecular biology. 2009. DOI : 10.1016/j.jmb.2009.03.065.Structural properties of pore-forming oligomers of alpha-synuclein
Journal of the American Chemical Society. 2009. DOI : 10.1021/ja9077599.Parkin deficiency delays motor decline and disease manifestation in a mouse model of synucleinopathy
PloS One. 2009. DOI : 10.1371/journal.pone.0006629.Switch-peptides as folding precursors in self-assembling peptides and amyloid fibrillogenesis
Advances in experimental medicine and biology. 2009. DOI : 10.1007/978-0-387-73657-0_126.The role of post-translational modification (phosphorylation) in modulating alpha-synuclein, structure, aggregation and toxicity
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
Biopolymers. 2009. DOI : 10.1002/bip.21301.Amyloid-Beta Modifies Astrocytic Metabolic Phenotype
22nd Biennial Meeting of the International-Society-of-Neurochemistry/Asian-Pacific-Society-for-Neurochemistry, Busan, SOUTH KOREA, Aug 23-29, 2009.Dissecting the mechanisms of tissue transglutaminase-induced cross-linking of alpha-synuclein: implications for the pathogenesis of Parkinson disease
Journal of Biological Chemistry. 2009. DOI : 10.1074/jbc.M809067200.Highly efficient and chemoselective peptide ubiquitylation
Angewandte Chemie (International ed. in English). 2009. DOI : 10.1002/anie.200902936.Amyloids go genomic: insights regarding the sequence determinants of prion formation from genome-wide studies
Chembiochem : a European journal of chemical biology. 2009. DOI : 10.1002/cbic.200900373.Hsp104 antagonizes alpha-synuclein aggregation and reduces dopaminergic degeneration in a rat model of Parkinson disease
The Journal of clinical investigation. 2008. DOI : 10.1172/JCI35781.Apomorphine inhibitors of amyloid-beta (abeta) fibril formation and their use in amyloidosis based disease
US2008096909 ; US2003187011 . 2008.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
Biochemistry. 2008. DOI : 10.1021/bi800603x.Inhibition of alpha-synuclein fibrillization by dopamine is mediated by interactions with five C-terminal residues and with E83 in the NAC region
PloS One. 2008. DOI : 10.1371/journal.pone.0003394.Switch peptide via Staudinger reaction
Organic Letters. 2008. DOI : 10.1021/ol802268e.Phosphorylation at Ser-129 but not the phosphomimics S129E/D inhibits the fibrillation of alpha-synuclein
Journal of Biological Chemistry. 2008. DOI : 10.1074/jbc.M800747200.The ratio of monomeric to aggregated forms of Abeta40 and Abeta42 is an important determinant of amyloid-beta aggregation, fibrillogenesis, and toxicity
Journal of Biological Chemistry. 2008. DOI : 10.1074/jbc.M803159200.Switch-peptides: design and characterization of controllable super-amyloid-forming host-guest peptides as tools for identifying anti-amyloid agents
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
Journal of molecular biology. 2008. DOI : 10.1016/j.jmb.2008.09.063.Switch-peptides as folding precursors in self-assembling peptides and amyloid fibrillogenesis
Biopolymers. 2007. DOI : 10.1002/bip.20663.Branched KLVFF tetramers strongly potentiate inhibition of beta-amyloid aggregation
Chembiochem : a European journal of chemical biology. 2007. DOI : 10.1002/cbic.200700338.Dopamine affects the stability, hydration, and packing of protofibrils and fibrils of the wild type and variants of alpha-synuclein
Biochemistry. 2007. DOI : 10.1021/bi061871+.The impact of the E46K mutation on the properties of alpha-synuclein in its monomeric and oligomeric states
Biochemistry. 2007. DOI : 10.1021/bi7000246.Disruption of amyloid-derived peptide assemblies through the controlled induction of a beta-sheet to alpha-helix transformation: application of the switch concept
Angewandte Chemie International Edition. 2007. DOI : 10.1002/anie.200603681.Switch-peptides: from conformational studies to Alzheimer's disease
CHIMIA. 2006. DOI : 10.2533/000942906777674921.Are amyloid diseases caused by protein aggregates that mimic bacterial pore-forming toxins?
Quarterly reviews of biophysics. 2006. DOI : 10.1017/S0033583506004422.A century-old debate on protein aggregation and neurodegeneration enters the clinic
Nature. 2006. DOI : 10.1038/nature05290.Islam: governments need to reform education and build a scientific culture
Nature. 2006. DOI : 10.1038/444545a.Rescuing defective vesicular trafficking protects against alpha-synuclein toxicity in cellular and animal models of Parkinson's disease
ACS chemical biology. 2006. DOI : 10.1021/cb600331e.Production and characterization of astrocyte-derived human apolipoprotein E isoforms from immortalized astrocytes and their interactions with amyloid-beta
Neurobiology of disease. 2005. DOI : 10.1016/j.nbd.2004.11.005.In vitro preparation of prefibrillar intermediates of amyloid-beta and alpha-synuclein
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
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
Science of aging knowledge environment : SAGE KE. 2005. DOI : 10.1126/sageke.2005.38.pe28.The materials science of protein aggregation
MRS Bulletin. 2005. DOI : 10.1557/mrs2005.123.From hexamer to amyloid: marginal stability of apolipoprotein SAA2.2 leads to in vitro fibril formation at physiological temperature
Amyloid : the international journal of experimental and clinical investigation : the official journal of the International Society of Amyloidosis. 2005. DOI : 10.1080/13506120500223084.Lead (Pb) exposure and its effect on APP proteolysis and Abeta aggregation
The FASEB journal : official publication of the Federation of American Societies for Experimental Biology. 2005. DOI : 10.1096/fj.05-4375fje.Amyloid fibril formation by macrophage migration inhibitory factor
Biochemical and biophysical research communications. 2005. DOI : 10.1016/j.bbrc.2005.10.040.Quaternary structure, protein dynamics, and synaptic function of SAP97 controlled by L27 domain interactions
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
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
WO03053356 ; AU2002357911 ; AU2002357911 ; WO03053356 ; CA2479263 . 2003.Discovery of inhibitors that elucidate the role of UCH-L1 activity in the H1299 lung cancer cell line
Chemistry & biology. 2003. DOI : 10.1016/j.chembiol.2003.08.010.hA molecular switch in amyloid assembly: Met35 and amyloid beta-protein oligomerization
Journal of the American Chemical Society. 2003. DOI : 10.1021/ja0349296.Abeta protofibrils possess a stable core structure resistant to hydrogen exchange
Biochemistry. 2003. DOI : 10.1021/bi0357816.Dissociation of amyloid fibrils of alpha-synuclein and transthyretin by pressure reveals their reversible nature and the formation of water-excluded cavities
Proceedings Of The National Academy Of Sciences Of The United States Of America (PNAS). 2003. DOI : 10.1073/pnas.1734009100.Hydration and packing are crucial to amyloidogenesis as revealed by pressure studies on transthyretin variants that either protect or worsen amyloid disease
Journal of molecular biology. 2003. DOI : 10.1016/S0022-2836(03)00368-1.Mixtures of wild-type and a pathogenic (E22G) form of Abeta40 in vitro accumulate protofibrils, including amyloid pores
Journal of molecular biology. 2003. DOI : 10.1016/S0022-2836(03)00927-6.New class of inhibitors of amyloid-beta fibril formation. Implications for the mechanism of pathogenesis in Alzheimer's disease
Journal of Biological Chemistry. 2002. DOI : 10.1074/jbc.M206593200.Murine apolipoprotein serum amyloid A in solution forms a hexamer containing a central channel
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
Nature. 2002. DOI : 10.1038/418291a.Alpha-synuclein, especially the Parkinson's disease-associated mutants, forms pore-like annular and tubular protofibrils
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
Journal of medicinal chemistry. 2002. DOI : 10.1021/jm010257n.The UCH-L1 gene encodes two opposing enzymatic activities that affect alpha-synuclein degradation and Parkinson's disease susceptibility
Cell. 2002. DOI : 10.1016/S0092-8674(02)01012-7.A glimpse of a possible amyloidogenic intermediate of transthyretin
Nature structural biology. 2000. DOI : 10.1038/78980.Nuclear import factors importin alpha and importin beta undergo mutually induced conformational changes upon association
FEBS letters. 2000. DOI : 10.1016/S0014-5793(00)02154-2.Protofilaments, filaments, ribbons, and fibrils from peptidomimetic self-assembly: Implications for amyloid fibril formation and materials science
Journal of the American Chemical Society. 2000. DOI : 10.1021/ja9937831.The most pathogenic transthyretin variant, L55P, forms amyloid fibrils under acidic conditions and protofilaments under physiological conditions
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
Biochemistry. 1999. DOI : 10.1021/bi981876+.Association between the first two immunoglobulin-like domains of the neural cell adhesion molecule N-CAM
FEBS letters. 1999. DOI : 10.1016/S0014-5793(99)00554-2.The nucleation of monomeric parallel beta-sheet-like structures and their self-assembly in aqueous solution
Bioorganic & medicinal chemistry. 1999. DOI : 10.1016/S0968-0896(98)00222-3.Comparative characterization of a wild type and transmembrane domain-deleted fatty acid amide hydrolase: identification of the transmembrane domain as a site for oligomerization
Biochemistry. 1998. DOI : 10.1021/bi981733n.Anti-amyloidogenic agents
WO9827972 ; WO9827972 ; AU5727798 ; WO9827972 . 1998.Complete inhibition of Cdk/cyclin by one molecule of p21(Cip1)
Genes & development. 1998. DOI : 10.1101/gad.12.24.3882.Inhibiting transthyretin conformational changes that lead to amyloid fibril formation
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
Protein expression and purification. 1998. DOI : 10.1006/prep.1998.0944.Transthyretin quaternary and tertiary structural changes facilitate misassembly into amyloid
Advances in protein chemistry. 1997. DOI : 10.1016/S0065-3233(08)60321-6.Oligomerization properties of GCN4 leucine zipper e and g position mutants
Protein science : a publication of the Protein Society. 1997. DOI : 10.1002/pro.5560061016.Guanidine hydrochloride-induced denaturation and refolding of transthyretin exhibits a marked hysteresis: equilibria with high kinetic barriers
Biochemistry. 1997. DOI : 10.1021/bi963195p.Inhibiting transthyretin amyloid fibril formation via protein stabilization
Proceedings Of The National Academy Of Sciences Of The United States Of America (PNAS). 1996. DOI : 10.1073/pnas.93.26.15051.Enseignement & Phd
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