🖼

Figure 1: The vicious cycle of TDP-43-mediated proteostatic collapse. TDP-43 aggregates ac...

active
paper figure Created: 2026-04-11T11:51:04 By: paper_figures_pipeline Quality: 95% 🔗 External ID: paper-fig-41900026-1
Figure 1: The vicious cycle of TDP-43-mediated proteostatic collapse. TDP-43 aggregates ac...
Figure 1Figure 1
The vicious cycle of TDP-43-mediated proteostatic collapse. TDP-43 aggregates actively contribute to pathology rather than merely serving as passive metabolic waste. They sequester essential components of the UPS, such as ubiquitin and E2/E3 ligases, and disrupt the ALP by depleting related components (e.g., dynactin-1), which are essential for autophagosome-lysosomal fusion. This leads to a self-perpetuating “vicious cycle” in which TDP-43 disrupts the very complexes responsible for its clearance, thereby impairing autophagic flux. Created in BioRender. Angelo Jamerlan. (2025) https://BioRender.com/ .
PubMed: 41900026
Metadata
doi10.3390/molecules31060924
pmid41900026
pmcidPMC13028736
_origin{'url': 'https://www.ebi.ac.uk/europepmc/articles/PMC13028736/bin/molecules-31-00924-g001.jpg', 'type': 'external', 'tracked_at': '2026-04-11T18:51:04.268953'}
captionThe vicious cycle of TDP-43-mediated proteostatic collapse. TDP-43 aggregates actively contribute to pathology rather than merely serving as passive metabolic waste. They sequester essential component
image_urlhttps://www.ebi.ac.uk/europepmc/articles/PMC13028736/bin/molecules-31-00924-g001.jpg
image_path
description
figure_labelFigure 1
figure_number1
_schema_version1
source_strategypmc_api
entities_mentioned
📊 Evidence Profile
Evidence Balance
+0%
Certainty
0%
Debates
0
Incoming
0
Outgoing
1
0 supporting 0 contradicting 0 neutral
View full evidence profile →
Public annotations (0)Annotate on Hypothes.is →
No public annotations yet.