Publications by authors named "C Betzer"
Article Synopsis
- The MJF-14 PLA is a new technique for detecting α-synuclein aggregates, demonstrating high specificity and sensitivity for non-Lewy body pathology.
- This assay shows a strong correlation between α-synuclein aggregation and specific conditions in both cell cultures and human neuronal samples linked to neurodegenerative diseases.
- The findings indicate that a significant amount of α-synuclein pathology occurs before the formation of Lewy bodies in diseases such as Parkinson's, suggesting the need for further research using brain samples.
Alpha-synuclein (α-syn) aggregation and immune activation represent hallmark pathological events in Parkinson's disease (PD). The PD-associated immune response encompasses both brain and peripheral immune cells, although little is known about the immune proteins relevant for such a response. We propose that the upregulation of CD163 observed in blood monocytes and in the responsive microglia in PD patients is a protective mechanism in the disease.
View Article and Find Full Text PDFBackground: There is a long-standing tradition of honours education in the field of nursing, dating back to the early 1960s in the United States. However, its adoption in European and particularly Scandinavian egalitarian educational contexts is relatively recent.
Purpose: This scoping review aims to provide an analysis of the global utilisation and distribution of honours education within the field of nursing.
Alpha-synuclein (aSN) is a membrane-associated and intrinsically disordered protein, well known for pathological aggregation in neurodegeneration. However, the physiological function of aSN is disputed. Pull-down experiments have pointed to plasma membrane Ca -ATPase (PMCA) as a potential interaction partner.
View Article and Find Full Text PDFArticle Synopsis
- α-synuclein (α-syn), which accumulates in Lewy body inclusions observed in Parkinson's disease, exists in different states influencing synaptic vesicle release, but its membrane-binding mechanisms remain unclear.
- Protein kinase R (PKR) phosphorylates α-syn at key residues, particularly Thr64 and Thr72, which reduces its binding to lipid membranes and affects its interactions with synaptic vesicles.
- Modified α-syn with these phosphomimetic mutations not only prevents aggregation and propagation of toxic α-syn forms but could also provide a target for therapeutic strategies in diseases characterized by α-syn pathology.