A5065084452- Alzheimer's disease research and treatments
- Neuroinflammation and Neurodegeneration Mechanisms
- Parkinson's Disease Mechanisms and Treatments
- Cholinesterase and Neurodegenerative Diseases
- Cellular transport and secretion
- Amyotrophic Lateral Sclerosis Research
- Prion Diseases and Protein Misfolding
- Inflammation biomarkers and pathways
- Neurological Disease Mechanisms and Treatments
- Computational Drug Discovery Methods
- Nuclear Receptors and Signaling
- Neurogenetic and Muscular Disorders Research
- Amyloidosis: Diagnosis, Treatment, Outcomes
- S100 Proteins and Annexins
- Neurological diseases and metabolism
- Dementia and Cognitive Impairment Research
- 14-3-3 protein interactions
- Peptidase Inhibition and Analysis
- Drug Transport and Resistance Mechanisms
- Mitochondrial Function and Pathology
- Ubiquitin and proteasome pathways
- Endoplasmic Reticulum Stress and Disease
- Neuroscience and Neuropharmacology Research
- Glycosylation and Glycoproteins Research
- Genetic Neurodegenerative Diseases
Ludwig-Maximilians-Universität München
2016-2025
German Center for Neurodegenerative Diseases
2016-2025
Munich Cluster for Systems Neurology
2016-2025
Synergy University
2023
Leipzig University
2023
University of Sheffield
2023
Imperial College London
2023
University of Regensburg
2023
Shenzhen Institutes of Advanced Technology
2022
Center for Inherited Blood Disorders
2022
Unusual Aggregates Several recent papers have revealed the unexpected genetic and pathological overlap between frontotemporal lobar degeneration (FTLD) amyotrophic lateral sclerosis (ALS). The most common cause is GGGGCC hexanucleotide repeat expansion upstream of C9orf72 coding region affecting about 10% all patients. It currently unknown how might lead to neurodegeneration. patients show two distinct types ubiquitinated inclusions in central nervous system, one which was identified as...
Amyloid β peptide (Aβ), the principal proteinaceous component of amyloid plaques in brains Alzheimer’s disease patients, is derived by proteolytic cleavage precursor protein (APP). Proteolytic APP a putative α-secretase within Aβ sequence precludes formation amyloidogenic peptides and leads to release soluble APPsα into medium. By overexpression d isintegrin nd m etalloprotease (ADAM), classified as ADAM 10, HEK 293 cells, basal kinase C-stimulated activity was increased severalfold. The...
Formation of senile plaques containing the β-amyloid peptide (Aβ) derived from amyloid precursor protein (APP) is an invariant feature Alzheimer's disease (AD). APP cleaved either by β-secretase or α-secretase to initiate amyloidogenic (release Aβ) nonamyloidogenic processing APP, respectively. A key understanding AD unravel how access these enzymes regulated. Here, we demonstrate that lipid rafts are critically involved in regulating Aβ generation. Reducing cholesterol levels N2a cells...
The neurodegeneration observed in Alzheimer's disease has been associated with synaptic dismantling and progressive decrease neuronal activity. We tested this hypothesis vivo by using two-photon Ca2+ imaging a mouse model of disease. Although activity was seen 29% layer 2/3 cortical neurons, 21% neurons displayed an unexpected increase the frequency spontaneous transients. These "hyperactive" were found exclusively near plaques amyloid beta-depositing mice. hyperactivity appeared to be due...
Loss of TREM2 function impairs phagocytosis and correlates with decreased soluble in biological fluids patients neurodegenerative disorders.
Although BACE1 (beta-site amyloid precursor protein–cleaving enzyme 1) is essential for the generation of amyloid-b peptide in Alzheimer's disease, its physiological function unclear. We found that very high levels were expressed at time points when peripheral nerves become myelinated. Deficiency resulted accumulation unprocessed neuregulin 1 (NRG1), an axonally factor required glial cell development and myelination. –/– mice displayed hypomyelination aberrant axonal segregation...
Mutations in the alpha-synuclein (alphaSYN) gene are associated with rare cases of familial Parkinson's disease, and alphaSYN is a major component Lewy bodies neurites. Here we have investigated localization wild-type mutant [A30P]alphaSYN as well betaSYN at cellular subcellular level. Our direct comparative study demonstrates extensive synaptic colocalization human mouse brain. In sucrose gradient equilibrium centrifugation assay, portion floated into lower density fractions, which also...
Degeneration of dopaminergic neurons in the substantia nigra is characteristic for Parkinson's disease (PD), second most common neurodegenerative disorder. Mitochondrial dysfunction believed to contribute etiology PD. Although cases are sporadic, recent evidence points a number genes involved familial variants Among them, loss-of-function phosphatase and tensin homolog-induced kinase 1 (PINK1; PARK6) associated with rare autosomal recessive parkinsonism. In HeLa cells, RNA...
α-Synuclein has been implicated in the pathogenesis of Parkinson's disease, since rare autosomal dominant mutations are associated with early onset disease and α-synuclein was found to be a major constituent Lewy bodies. We have analyzed expression transfected cell lines. In pulse-chase experiments appeared stable over long periods (<i>t</i> <mml:math><mml:mrow><mml:mn>1</mml:mn></mml:mrow><mml:mrow><mml:mn>2</mml:mn></mml:mrow></mml:math> 54 h) no endoproteolytic processing observed....