Results 61 to 70 of about 31,365 (260)
Advanced Science, EarlyView.Genetic and pharmacological inhibition of SLC11A1 functioning as an H+/Fe2+ antiporter–mediated lysosomal iron accumulation in microglia promotes lysosomal lumen acidification, increases CTSD expression, enhances lysosomal myelin debris uptake and degradation, and promotes repair following white matter stroke. ABSTRACT White matter stroke (WMS) results
Lingling Qiu +11 more
wiley +1 more source
Advanced Science, EarlyView.Time‐resolved SAXS reveals how physiologically relevant metal ions shape the earliest conformational responses of monomeric α‐synuclein. Fe3+ induces rapid compaction, Cu2+ generates heterogeneous and partially folded ensembles, while Mn2+ and Zn2+ cause only modest changes.
Rebecca Sternke‐Hoffmann +3 more
wiley +1 more source
Engineered GM1 Intersects Between Mitochondrial and Synaptic Pathways to Ameliorate ALS Pathology
Advanced Science, EarlyView.Amyotrophic Lateral Sclerosis (ALS) is a fatal neurodegenerative disease driven by genetic and molecular disruptions affecting energy balance, protein homeostasis, and stress responses in nerve cells. Studies using human and rodent models identified convergent defects in mitochondria and synaptic function.
Federica Pilotto +11 more
wiley +1 more source
Cutaneous Alpha-Synuclein From Paraffin Embedded Autopsy Specimens in Parkinson’s Disease
Journal of Parkinson’s Disease, 2017 Background: Parkinson disease (PD) is neurodegenerative disorder characterized by tremor, rigidity and bradykinesia and pathologically by the deposition of alpha-synuclein within different tissues. We, and others, have reported the detection of cutaneous
Christopher H. Gibbons +2 more
doaj +1 more source
Frontiers in Neuroscience, 2019 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
Cristina Cariulo +15 more
doaj +1 more source
C. elegans model identifies genetic modifiers of alpha-synuclein inclusion formation during aging. [PDF]
PLoS Genetics, 2008 Inclusions in the brain containing alpha-synuclein are the pathological hallmark of Parkinson's disease, but how these inclusions are formed and how this links to disease is poorly understood. We have developed a C.
Tjakko J van Ham +5 more
doaj +1 more source
Alpha-Synuclein Interactions with Membranes
, 2011 Synucleinopathies are a group of neurodegenerative disorders that share common pathological intracellular deposits that contain aggregates of the protein ┙-synuclein. Substantial evidence suggests that fibril formation by ┙-synuclein is a critical step in the development of Parkinson's disease (PD).
Pirc, Katja, Poklar Ulrih, Nataša
openaire +4 more sources
A Nanoparticle‐Integrated Complete Manufacturing Pipeline of Chemically Engineered Exosomes
Advanced Science, EarlyView.We report a novel manufacture technology of chemically engineered exosomes. The four steps of manufacturing, i.e., biogenesis, loading, isolation, and storage, are integrated by the use of a nanoparticle. The manufacture technology incorporates three innovative components, i.e., a new nano‐bio effect, a new composite nanoparticle, and a new isolation ...
Xiaowei Wen +13 more
wiley +1 more source
Advanced Science, EarlyView.Time‐restricted feeding (TRF) exerts protein‐dependent neuroprotective effects in an MPTP‐induced Parkinson's disease model. In casein‐fed mice, TRF improves gut barrier integrity and reduces neuroinflammation, possibly via modulation of Allobaculum and BCAAs.
Ting Li +12 more
wiley +1 more source
F1000Research, 2014 The accumulation of misfolded a-synuclein is mechanistically linked to neurodegeneration in Parkinson’s disease (PD) and other alpha-synucleinopathies. However, how alpha-synuclein causes neurodegeneration is unresolved.
Yan Liu +5 more
doaj +1 more source