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Figure 1: The vicious cycle of TDP-43-mediated proteostatic collapse. TDP-43 aggregates ac...
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Created: 2026-04-11T11:51:04
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ID: paper-fig-41900026-1
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/ .
▸Metadata
| doi | 10.3390/molecules31060924 |
| pmid | 41900026 |
| pmcid | PMC13028736 |
| _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'} |
| caption | 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 component |
| image_url | https://www.ebi.ac.uk/europepmc/articles/PMC13028736/bin/molecules-31-00924-g001.jpg |
| image_path | |
| description | |
| figure_label | Figure 1 |
| figure_number | 1 |
| _schema_version | 1 |
| source_strategy | pmc_api |
| entities_mentioned |
📊 Evidence Profile
Evidence Balance
+0%
Certainty
0%
Debates
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Incoming
0
Outgoing
1
0 supporting
0 contradicting
0 neutral
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