ArticlePNAS nexus2025
Structural basis for T-cell intracellular antigen-1 amyloid fibril formation revealed by cryo-electron microscopy.
Article in PNAS nexus, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.
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.
The trial behind it
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Who cites it
1 citing paper in PubMed.
- Expression Patterns of T-Cell Intracellular Antigen 1 in Neurodegenerative Disorders and Stroke.International journal of molecular sciences · 2026Review
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Authors and funding
14 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
T-cell intracellular antigen-1 (TIA-1) is a key component of stress granules and contains an intrinsically disordered region called the prion-like domain (PLD). TIA-1 PLD can form condensates via phase separation that subsequently convert into amyloid fibrils. However, the structural basis underlying TIA-1 PLD amyloid fibril formation remains unclear, hindering clinical understanding and therapeutic intervention at the molecular level. Using cryo-electron microscopy, we identified structural features that are consistent with a labile architecture, including a kinked backbone conformation, a polar zipper, and a proline-mediated cross-β structure. We also determined the fibril structure containing a G355R missense mutation and found that this mutation disrupts the tight conformation around G355 in the wild-type structure, leading to delayed fibril formation. The amyloid fibril structures of TIA-1 PLD provide an atomic-level framework for mechanistic studies of mutation-driven dysfunction.
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