ArticleProtein science : a publication of the Protein Society2025
Identifying interactions between TDP-43's N-terminal and RNA-binding domains.
Article in Protein science : a publication of the Protein Society, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
4 citing papers in PubMed.
- TDP-43 controls RNA structure through high affinity lattice interactions.Nature communications · 2026Article
- Maintenance and disruption of the physiological dimer structure of TDP-43 in amyotrophic lateral sclerosis and frontotemporal lobar degeneration.BMC medicine · 2026Review
- TDP-43 controls RNA structure through high affinity lattice interactions.bioRxiv : the preprint server for biology · 2025Article
- Identifying interactions between TDP-43's N-terminal and RNA-binding domains.Protein science : a publication of the Protein Society · 2025Article
Corrections and comments
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Authors and funding
8 authors.
Funding
Abstract
TAR DNA-binding Protein 43 kilodaltons (TDP-43) plays a crucial role in the pathophysiology and progression of amyotrophic lateral sclerosis, affecting familial and sporadic cases. TDP-43 is an intrinsically disordered multidomain protein that consists of an N-terminal domain (NTD
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Registered trials
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