- Prion Diseases and Protein Misfolding
- RNA Research and Splicing
- Alzheimer's disease research and treatments
- Neurological diseases and metabolism
- Trace Elements in Health
- Amyotrophic Lateral Sclerosis Research
- RNA regulation and disease
- Genetics and Neurodevelopmental Disorders
- Proteins in Food Systems
- Protein Structure and Dynamics
- Heterotopic Ossification and Related Conditions
- Neurogenetic and Muscular Disorders Research
Technische Universität Dresden
2024-2025
Max Planck Institute of Molecular Cell Biology and Genetics
2024-2025
National Center for Genetic Engineering and Biotechnology
2024
St Petersburg University
2018-2021
Vavilov Institute of General Genetics
2017
SUMMARY Cytosolic aggregation of the nuclear protein TDP-43 is associated with many neurodegenerative diseases, but triggers for are still debated. Here, we demonstrate that requires a double event. One up-concentration in stress granules beyond threshold, and other oxidative stress. These two events collectively induce intra-condensate demixing, giving rise to dynamic enriched phase within granules, which subsequently transitions into pathological aggregates. Mechanistically, demixing...
Cytosolic aggregation of the RNA binding protein TDP-43 (transactive response DNA-binding 43) is a hallmark amyotrophic lateral sclerosis and frontotemporal dementia. Here, we report that during oxidative stress, becomes SUMO2/3-ylated by SUMO E3 ligase PIAS4 (protein inhibitor activated STAT 4) enriches in cytoplasmic stress granules (SGs). Upon pharmacological inhibition SUMO2/3-ylation or depletion, enrichment SGs accompanied irreversible aggregation. In cells are unable to assemble SGs,...
Abstract Amyloids are β-sheets-rich protein fibrils that cause neurodegenerative and other incurable human diseases affecting millions of people worldwide. However, a number proteins is functional in the amyloid state various organisms from bacteria to humans. Using an original proteomic approach, we identified set forming amyloid-like aggregates brain young healthy rats. One them FXR1 protein, which known regulate memory emotions. We showed clearly colocalizes cortical neurons with...
Cytosolic aggregation of the nuclear protein TAR DNA-binding 43 (TDP-43) is associated with many neurodegenerative diseases, but triggers for TDP-43 are still debated. Here, we demonstrate that requires a double event. One up-concentration in stress granules beyond threshold, and other oxidative stress. These two events collectively induce intra-condensate demixing, giving rise to dynamic TDP-43-enriched phase within granules, which subsequently transition into pathological aggregates....
Amyloids are non-branching fibrils that composed of stacked monomers stabilized by intermolecular β-sheets. Some amyloids associated with incurable diseases, whereas others, functional amyloids, regulate different vital processes. The prevalence and significance in wildlife still poorly understood. In recent years, applying new approach large-scale proteome screening, a number novel candidate were identified the yeast Saccharomyces cerevisiae, many which localized cell wall. this work, we...
ABSTRACT Prions are proteins that can exist in several structurally and functionally distinct states, one or more of which is transmissible. Yeast Sup35 Rnq1 prion state ([PSI+] [PIN+], respectively) form oligomers aggregates, transmitted from parents to offspring a series generations. Several pieces indirect evidence indicate these aggregates also possess amyloid properties, but their binding amyloid-specific dyes has not been shown vivo. Meanwhile, it the specific Congo Red dye...
Abstract Functional amyloids regulate vital processes in a variety of organisms from bacteria to higher eukaryotes. The development methods enabling large-scale screening for opens up opportunity systemic analysis the prevalence nature. Using an original proteomic approach, we identified several proteins forming amyloid-like detergent-resistant aggregates rat brain. One them is FXR1 protein, which known memory and emotions (1, 2). We demonstrated that brain forms amyloid oligomers insoluble...