Publications related to Multiple system atrophy

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

Hilal Lashuel, Lara Petricca, Sean Michael Deguire

Accumulation and aggregation of misfolded alpha-synuclein is believed to be a cause of Parkinson's disease (PD). Phosphorylation of alpha-synuclein at S129 is known to be associated with the pathological misfolding process, but efforts to investigate the r ...

2019

Classification of degenerative parkinsonism subtypes by support-vector-machine analysis and striatal I-123-FP-CIT indices

Dimitri Nestor Alice Van De Ville, Maria Giulia Preti

ObjectivesTo provide an automated classification method for degenerative parkinsonian syndromes (PS) based on semiquantitative I-123-FP-CIT SPECT striatal indices and support-vector-machine (SVM) analysis.Methods(123)I-FP-CIT SPECT was performed at a singl ...

Springer2019

Lewy pathology in Parkinson's disease consists of crowded organelles and lipid membranes

Jian Wang, Henning Paul-Julius Stahlberg, Amanda Jennifer Lewis

Parkinson's disease, the most common age-related movement disorder, is a progressive neurodegenerative disease with unclear etiology. Key neuropathological hallmarks are Lewy bodies and Lewy neurites: neuronal inclusions immunopositive for the protein alph ...

Springer Science and Business Media LLC2019

Membrane–Protein–Hydration Interaction of α-Synuclein with Anionic Vesicles Probed via Angle-Resolved Second-Harmonic Scattering

Sylvie Roke, Jan Dedic, Halil Ibrahim Okur

Amyloid formation of the protein α-synuclein promotes neurodegeneration in Parkinson's disease. The normal function of α-synuclein includes synaptic vesicle transport and fusion, and the protein binds strongly to negatively charged vesicles in vitro. Here, ...

2019

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

Hilal Lashuel, Anne-Laure Mahul Mellier

A compelling link is emerging between the posttranslational modification O-GlcNAc and protein aggregation. A prime example is alpha-synuclein, which forms toxic aggregates that are associated with neurodegeneration in Parkinson's and related diseases. alph ...

NATL ACAD SCIENCES2019

Two new polymorphic structures of human full-length alpha-synuclein fibrils solved by cryo-electron microscopy

Henning Paul-Julius Stahlberg, Ricardo Cesar Guerrero Ferreira, Pratibha Kumari

Intracellular inclusions rich in alpha-synuclein are a hallmark of several neuropathological diseases including Parkinson’s disease (PD). Previously, we reported the structure of alpha-synuclein fibrils (residues 1–121), composed of two protofibrils that a ...

2019

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

Hilal Lashuel, Juan Kiwi, Bruno Claude Daniel Fauvet, Anass Chiki, Farah El Turk

Intracellular deposits of α-synuclein in the form of Lewy bodies are major hallmarks of Parkinson’s disease (PD) and a range of related neurodegenerative disorders. Post-translational modifications (PTMs) of α-synuclein are increasingly thought to be major ...

2018

Cryo-EM structure of alpha-synuclein fibrils

Henning Paul-Julius Stahlberg, Ricardo Cesar Guerrero Ferreira

Parkinson's disease is a progressive neuropathological disorder that belongs to the class of synucleinopathies, in which the protein alpha-synuclein is found at abnormally high concentrations in affected neurons. Its hallmark are intracellular inclusions c ...

eLife Sciences Publications, Ltd2018

Glycation potentiates α-synuclein-associated neurodegeneration in synucleinopathies

Hilal Lashuel, Magdalena Zweckstetter, Michael Heinrich

α-Synuclein misfolding and aggregation is a hallmark in Parkinson's disease and in several other neurodegenerative diseases known as synucleinopathies. The toxic properties of α-synuclein are conserved from yeast to man, but the precise underpinnings of th ...

Oxford University Press2017

Chat with Graph Search

Ask any question about EPFL courses, lectures, exercises, research, news, etc. or try the example questions below.

DISCLAIMER: The Graph Chatbot is not programmed to provide explicit or categorical answers to your questions. Rather, it transforms your questions into API requests that are distributed across the various IT services officially administered by EPFL. Its purpose is solely to collect and recommend relevant references to content that you can explore to help you answer your questions.

Multiple system atrophy

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

Classification of degenerative parkinsonism subtypes by support-vector-machine analysis and striatal I-123-FP-CIT indices

Lewy pathology in Parkinson's disease consists of crowded organelles and lipid membranes

Membrane–Protein–Hydration Interaction of α-Synuclein with Anionic Vesicles Probed via Angle-Resolved Second-Harmonic Scattering

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

Two new polymorphic structures of human full-length alpha-synuclein fibrils solved by cryo-electron microscopy

Autophagy and LRRK2 in the Aging Brain

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

Cryo-EM structure of alpha-synuclein fibrils

Glycation potentiates α-synuclein-associated neurodegeneration in synucleinopathies

Graph Chatbot

Chat with Graph Search

Lewy pathology in Parkinson's disease consists of crowded organelles and lipid membranes

Membrane–Protein–Hydration Interaction of α-Synuclein with Anionic Vesicles Probed via Angle-Resolved Second-Harmonic Scattering

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

Two new polymorphic structures of human full-length alpha-synuclein fibrils solved by cryo-electron microscopy

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

Classification of degenerative parkinsonism subtypes by support-vector-machine analysis and striatal I-123-FP-CIT indices

Autophagy and LRRK2 in the Aging Brain

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

Glycation potentiates α-synuclein-associated neurodegeneration in synucleinopathies

Cryo-EM structure of alpha-synuclein fibrils