Reverse engineering Lewy bodies: how far have we come and how far can we go?
Lewy bodies (LBs) are α-synuclein (α-syn)-rich intracellular inclusions that are an important
pathological hallmark of Parkinson disease and several other neurodegenerative diseases …
pathological hallmark of Parkinson disease and several other neurodegenerative diseases …
[HTML][HTML] Do Lewy bodies contain alpha-synuclein fibrils? and Does it matter? A brief history and critical analysis of recent reports
HA Lashuel - Neurobiology of disease, 2020 - Elsevier
Several lines of evidence from neuropathological studies, human genetics, in vitro
aggregation studies and cellular and animal models support the hypothesis that aSyn plays …
aggregation studies and cellular and animal models support the hypothesis that aSyn plays …
Lewy pathology in Parkinson's disease consists of crowded organelles and lipid membranes
Parkinson's disease, the most common age-related movement disorder, is a progressive
neurodegenerative disease with unclear etiology. Key neuropathological hallmarks are …
neurodegenerative disease with unclear etiology. Key neuropathological hallmarks are …
The process of Lewy body formation, rather than simply α-synuclein fibrillization, is one of the major drivers of neurodegeneration
AL Mahul-Mellier, J Burtscher… - Proceedings of the …, 2020 - National Acad Sciences
Parkinson's disease (PD) is characterized by the accumulation of misfolded and aggregated
α-synuclein (α-syn) into intraneuronal inclusions named Lewy bodies (LBs). Although it is …
α-synuclein (α-syn) into intraneuronal inclusions named Lewy bodies (LBs). Although it is …
Two new polymorphic structures of human full-length alpha-synuclein fibrils solved by cryo-electron microscopy
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 …
diseases including Parkinson's disease (PD). Previously, we reported the structure of alpha …
Seeding the aggregation of TDP-43 requires post-fibrillization proteolytic cleavage
Despite the strong evidence linking the transactive response DNA-binding protein 43 (TDP-
43) aggregation to the pathogenesis of frontotemporal lobar degeneration with TDP-43 …
43) aggregation to the pathogenesis of frontotemporal lobar degeneration with TDP-43 …
Regulation of α-synuclein by chaperones in mammalian cells
BM Burmann, JA Gerez, I Matečko-Burmann… - Nature, 2020 - nature.com
Neurodegeneration in patients with Parkinson's disease is correlated with the occurrence of
Lewy bodies—intracellular inclusions that contain aggregates of the intrinsically disordered …
Lewy bodies—intracellular inclusions that contain aggregates of the intrinsically disordered …
[HTML][HTML] How specific are the conformation-specific α-synuclein antibodies? Characterization and validation of 16 α-synuclein conformation-specific antibodies using …
ST Kumar, S Jagannath, C Francois… - Neurobiology of …, 2020 - Elsevier
Increasing evidence suggests that alpha-synuclein (α-syn) oligomers are obligate
intermediates in the pathway involved in α-syn fibrillization and Lewy body (LB) formation …
intermediates in the pathway involved in α-syn fibrillization and Lewy body (LB) formation …
The subcellular arrangement of alpha-synuclein proteoforms in the Parkinson's disease brain as revealed by multicolor STED microscopy
TE Moors, CA Maat, D Niedieker, D Mona… - Acta …, 2021 - Springer
Various post-translationally modified (PTM) proteoforms of alpha-synuclein (aSyn)—
including C-terminally truncated (CTT) and Serine 129 phosphorylated (Ser129-p) aSyn …
including C-terminally truncated (CTT) and Serine 129 phosphorylated (Ser129-p) aSyn …
O-GlcNAc forces an α-synuclein amyloid strain with notably diminished seeding and pathology
Amyloid-forming proteins such α-synuclein and tau, which are implicated in Alzheimer's and
Parkinson's disease, can form different fibril structures or strains with distinct toxic properties …
Parkinson's disease, can form different fibril structures or strains with distinct toxic properties …