Explanipedia

Ambroxol displaces α-synuclein from the membrane and inhibits the formation of early protein-lipid coaggregates† Open

Jesper E. Dreier, Alisdair Stevenson, Elliot Carles, Thomas C. T. Michaels, Céline Galvagnion · 2025

Parkinson’s disease (PD) is a neurological disorder characterized by neuronal loss and the deposition of α -synuclein-lipid coaggregates in the brain of patients as well as disruptions in lipid metabolism. Mutations in the gene GBA , which…

Global kinetic model of lipid-induced α -synuclein aggregation and its inhibition by small molecules Open

Alisdair Stevenson, Roxine Staats, Alexander J. Dear, David Voderholzer, Jesper E. Dreier , et al. · 2025

The aggregation of α -synuclein into amyloid fibrils is a hallmark of Parkinson’s disease. This process has been shown to directly involve interactions between proteins and lipid surfaces when the latter are present. Despite this importanc…

Ambroxol displaces α-synuclein from the membrane and inhibits the formation of early protein–lipid coaggregates Open

Jesper E. Dreier, Alisdair Stevenson, Elliot Carles, Katharina Schott, Thomas C. T. Michaels , et al. · 2025

Ambroxol, a small molecule known to stabilise Glucocerebrosidase, can act directly on α-synuclein–lipid coaggregation into amyloid fibrils, a process associated with Parkinson's disease, by preventing the formation of early protein–lipid o…

Divergent effects of pathological α-synuclein truncations and mutations on phase separation Open

Soumik Ray, Cecilia Chiodaroli, Azad Farzadfard, Antonín Kunka, Karin Schott , et al. · 2024

Phase separated condensates can accelerate α-synuclein (α-Syn) amyloid fibril formation implicated in Parkinson’s disease pathogenesis. The effects of pathological modifications, i.e., truncations and familial mutations on the thermodynami…

Global kinetic model of lipid-inducedα-synuclein aggregation and its inhibition by small molecules Open

Alisdair Stevenson, Roxine Staats, Alexander J. Dear, David Voderholzer, Georg Meisl , et al. · 2024

The aggregation of α -synuclein into amyloid fibrils is a hallmark of Parkinson’s disease. This process has been shown to directly involve interactions between proteins and lipid surfaces when the latter are present. Despite this importanc…

Shared and Distinct Lipid Profiles in amygdala from Sporadic and GBA-associated Parkinson’s Diseases Open

Sonia Sanz Muñoz, Frederik Ravnkilde Marlet, Mesut Bilgin, Jesper E. Dreier, Erwan Bézard , et al. · 2024

Parkinson’s Disease (PD) is a neurodegenerative disorder characterised by the deposition of protein-lipid inclusions, containing alpha-synuclein, neuronal cell loss and disruptions in lipid metabolism such as those associated with GBA muta…

Lipid levels correlate with neuronal and dopaminergic markers during the differentiation of SH-SY5Y cells Open

Frederik Ravnkilde Marlet, Sonia Sanz Muñoz, Nefeli Sotiraki, Jannik Nicklas Eliasen, Jakob Woessmann , et al. · 2024

Parkinson's Disease (PD) is characterised by the loss of dopaminergic neurons and the deposition of protein inclusions called Lewy Bodies (LBs). LBs are heterogeneous structures composed of protein and lipid molecules and their main consti…

Lipid levels correlate with neuronal and dopaminergic markers during the differentiation of SH-SY5Y cells Open

Frederik Ravnkilde Marlet, Sonia Sanz Muñoz, Nefeli Sotiraki, Jannik Nicklas Eliasen, Jakob Woessmann , et al. · 2023

Parkinson’s Disease (PD) is characterized by the loss of dopaminergic neurons and the deposition in the remaining cells of protein inclusions called Lewy Bodies (LBs). LBs are heterogeneous structures composed of protein and lipid molecule…

Structural characterisation of α-synuclein-membrane interactions and the resulting aggregation using small angle scattering Open

Céline Galvagnion, Abigail Barclay, Katarzyna Makasewicz, Frederik Ravnkilde Marlet, Martine Moulin , et al. · 2023

The presence of amyloid fibrils is a hallmark of several neurodegenerative diseases. Some amyloidogenic proteins, such as α-synuclein and amyloid β, can interact with lipids, and this interaction can strongly favor the formation of amyloid…

N-Terminal Acetylation of α-Synuclein Slows down Its Aggregation Process and Alters the Morphology of the Resulting Aggregates Open

Rosie Bell, Rebecca J. Thrush, Marta Castellana-Cruz, Marc Oeller, Roxine Staats , et al. · 2022

Parkinson's disease is associated with the aberrant aggregation of α-synuclein. Although the causes of this process are still unclear, post-translational modifications of α-synuclein are likely to play a modulatory role. Since α-synuclein …

Editorial: Amyloid-Membrane Interactions in Protein Misfolding Disorders: From Basic Mechanisms to Therapy Open

Neville Vassallo, Céline Galvagnion, Eva Y. · 2022

EDITORIAL article Front. Cell Dev. Biol., 25 February 2022 | https://doi.org/10.3389/fcell.2022.870791

Capillary flow experiments for thermodynamic and kinetic characterization of protein liquid-liquid phase separation Open

Emil G. P. Stender, Soumik Ray, Rasmus K. Norrild, Jacob Aunstrup Larsen, Daniel Petersen , et al. · 2021

Sphingolipid changes in Parkinson L444P GBA mutation fibroblasts promote α-synuclein aggregation Open

Céline Galvagnion, Frederik Ravnkilde Marlet, Silvia Cerri, Anthony H.V. Schapira, Fabio Blandini , et al. · 2021

Intraneuronal accumulation of aggregated α-synuclein is a pathological hallmark of Parkinson’s disease. Therefore, mechanisms capable of promoting α-synuclein deposition bear important pathogenetic implications. Mutations of the glucocereb…

Sphingolipid changes in Parkinson L444P GBA mutation fibroblasts promote α-synuclein aggregation Open

Céline Galvagnion, Silvia Cerri, Anthony H.V. Schapira, Fabio Blandini, Donato A. Di Monte · 2020

Intraneuronal accumulation of aggregated α-synuclein is a pathological hallmark of Parkinson’s disease. Therefore, mechanisms capable of promoting α-synuclein deposition bear important pathogenetic implications. Mutations of the glucocereb…

Lipid Dynamics and Phase Transition within α-Synuclein Amyloid Fibrils Open

Céline Galvagnion, Daniel Topgaard, Katarzyna Makasewicz, Alexander K. Buell, Sara Linse , et al. · 2019

The deposition of coassemblies made of the small presynaptic protein, α-synuclein, and lipids in the brains of patients is the hallmark of Parkinson's disease. In this study, we used natural abundance ¹³C and ³¹P magi…

An engineered monomer binding-protein for α-synuclein efficiently inhibits the proliferation of amyloid fibrils Open

Emil Dandanell Agerschou, Patrick Flagmeier, Theodora Saridaki, Céline Galvagnion, Daniel Komnig , et al. · 2019

Removing or preventing the formation of -synuclein aggregates is a plausible strategy against Parkinson’s disease. To this end, we have engineered the -wrapin AS69 to bind monomeric -synuclein with high affinity. In cultured cells, A…

Author response: An engineered monomer binding-protein for α-synuclein efficiently inhibits the proliferation of amyloid fibrils Open

Emil Dandanell Agerschou, Patrick Flagmeier, Theodora Saridaki, Céline Galvagnion, Daniel Komnig , et al. · 2019

Article Figures and data Abstract Introduction Results Discussion Materials and methods Appendix 1 Appendix 2 Appendix 3 Data availability References Decision letter Author response Article and author information Metrics Abstract Removing …

Author response: An engineered monomer binding-protein for α-synuclein efficiently inhibits the proliferation of amyloid fibrils Open

Emil Dandanell Agerschou, Patrick Flagmeier, Theodora Saridaki, Céline Galvagnion, Daniel Komnig , et al. · 2019

Article Figures and data Abstract Introduction Results Discussion Materials and methods Appendix 1 Appendix 2 Appendix 3 Data availability References Decision letter Author response Article and author information Metrics Abstract Removing …

An engineered monomer binding-protein forα-synuclein efficiently inhibits the proliferation of amyloid fibrils Open

Emil Dandanell Agerschou, Theodora Saridaki, Patrick Flagmeier, Céline Galvagnion, Daniel Komnig , et al. · 2019

Removing or preventing the formation of α -synuclein aggregates is a plausible strategy against Parkinson’s disease. To this end we have engineered the β -wrapin AS69 to bind monomeric α -synuclein with high affinity. In cultured cells, AS…

Multistep Inhibition of α-Synuclein Aggregation and Toxicity in Vitro and in Vivo by Trodusquemine Open

Michele Perni, Patrick Flagmeier, Ryan Limbocker, Roberta Cascella, Francesco A. Aprile , et al. · 2018

The aggregation of α-synuclein, an intrinsically disordered protein that is highly abundant in neurons, is closely associated with the onset and progression of Parkinson's disease. We have shown previously that the aminosterol squalamine c…

Cholesterol catalyses Aβ42 aggregation through a heterogeneous nucleation pathway in the presence of lipid membranes Open

Johnny Habchi, Sean Chia, Céline Galvagnion, Thomas C. T. Michaels, Mathias M. J. Bellaiche , et al. · 2018

C-terminal truncation of α-synuclein promotes amyloid fibril amplification at physiological pH Open

Ingrid M. van der Wateren, Tuomas P. J. Knowles, Alexander K. Buell, Christopher M. Dobson, Céline Galvagnion · 2018

C-terminal truncations shift the pH range at which α-synuclein secondary nucleation occurs from acidic to neutral values.

Kinetic barriers to α-synuclein protofilament formation and conversion into mature fibrils Open

James W. Brown, Georg Meisl, Tuomas P. J. Knowles, Alexander K. Buell, Christopher M. Dobson , et al. · 2018

An increase in temperature allows the conversion of α-synuclein lipid-induced proto-fibrils to mature fibrils by overcoming the associated energy barrier.

The Role of Lipids Interacting with α-Synuclein in the Pathogenesis of Parkinson’s Disease Open

Céline Galvagnion · 2017

α-synuclein is a small protein abundantly expressed in the brain and mainly located in synaptic terminals. The conversion of α-synuclein into oligomers and fibrils is the hallmark of a range of neurodegenerative disorders including Parkins…

A natural product inhibits the initiation of α-synuclein aggregation and suppresses its toxicity Open

Michele Perni, Céline Galvagnion, Alexander S. Maltsev, Georg Meisl, Martin Müller , et al. · 2017

Significance Parkinson’s disease is characterized by the presence in brain tissues of aberrant aggregates primarily formed by the protein α-synuclein. It has been difficult, however, to identify compounds capable of preventing the formatio…

β-Synuclein suppresses both the initiation and amplification steps of α-synuclein aggregation via competitive binding to surfaces Open

James W. Brown, Alexander K. Buell, Thomas C. T. Michaels, Georg Meisl, Jacqueline A. Carozza , et al. · 2016

Mutations associated with familial Parkinson’s disease alter the initiation and amplification steps of α-synuclein aggregation Open

Patrick Flagmeier, Georg Meisl, Michele Vendruscolo, Tuomas P. J. Knowles, Christopher M. Dobson , et al. · 2016

Significance Proteinaceous deposits composed primarily of amyloid fibrils of α-synuclein are a hallmark of a range of neurological disorders including Parkinson’s disease. Mutations of the gene encoding α-synuclein have been associated wit…

Chemical properties of lipids strongly affect the kinetics of the membrane-induced aggregation of α-synuclein Open

Céline Galvagnion, James W. Brown, Myriam Ouberaï, Patrick Flagmeier, Michele Vendruscolo , et al. · 2016

Significance Parkinson’s disease is the second most prevalent neurodegenerative disorder and is characterized by the presence in the brains of patients of proteinaceous deposits whose main component is α-synuclein. This protein interacts w…

Discovery of a small-molecule binder of the oncoprotein gankyrin that modulates gankyrin activity in the cell Open

Anasuya Chattopadhyay, Cornelius J. O’Connor, Fengzhi Zhang, Céline Galvagnion, Warren R. J. D. Galloway , et al. · 2016

The inverted free energy landscape of an intrinsically disordered peptide by simulations and experiments Open

Daniele Granata, Fahimeh Baftizadeh, Johnny Habchi, Céline Galvagnion, Alfonso De Simone , et al. · 2015

The free energy landscape theory has been very successful in rationalizing the folding behaviour of globular proteins, as this representation provides intuitive information on the number of states involved in the folding process, their pop…

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