Aleksandra Sergeeva

ORCID: 0000-0003-0117-9076
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About
Contact & Profiles
Research Areas
  • 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...

10.1101/2024.01.23.576837 preprint EN cc-by bioRxiv (Cold Spring Harbor Laboratory) 2024-01-23

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,...

10.1126/sciadv.adq2475 article EN cc-by-nc Science Advances 2025-02-21

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...

10.1038/s41598-019-55528-6 article EN cc-by Scientific Reports 2019-12-12

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....

10.1016/j.cell.2025.04.039 article EN cc-by Cell 2025-05-01

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...

10.1080/19336896.2018.1558763 article EN Prion 2018-12-18

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...

10.1093/femsyr/foab046 article EN FEMS Yeast Research 2021-08-31

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...

10.1101/544650 preprint EN bioRxiv (Cold Spring Harbor Laboratory) 2019-02-08
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