ReviewCold Spring Harbor perspectives in biology2017
TIA-1 Is a Functional Prion-Like Protein.
Review in Cold Spring Harbor perspectives in biology, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 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
22 citing papers in PubMed, 47 citations in OpenAlex.
- Review
- TIA-1 promotes FUNDC1-mediated mitophagy to protect against stress-induced cellular senescence.Experimental & molecular medicine · 2026Article
- Astrocytic TIA1-Mediated Stress Granules Promote the Demyelination of Optic Neuritis by Sequestering mRNA of Cholesterol Synthesis Genes in an Experimental Autoimmune Encephalomyelitis Model.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026Article
- The oncolytic vesicular stomatitis virus VSV-GP shows profound oncolytic activity in NUT-carcinoma cell lines.Molecular therapy. Oncology · 2026Article
- GLA-3 mediates the heat shock response in Caenorhabditis elegans germ cells: A key role for the tristetraprolin (TTP) family.PloS one · 2026Article
- Transcriptomic Architecture of Weak Versus Strong Contextual Fear Extinction Learning Uncovers Extinction-Suppressive Role of TIA1.Biological psychiatry global open science · 2025Article
- Participation of host cell proteins in inclusion bodies of non-segmented RNA virus infected cells: a molecular insight.Virology journal · 2025Review
- TIA1-Mediated Stress Granules Promote the Neuroinflammation and Demyelination in Experimental Autoimmune Encephalomyelitis through Upregulating IL-31RA Signaling.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025Article
- Divergent evolution of low-complexity regions in the vertebrate CPEB protein family.Frontiers in bioinformatics · 2025Article
- Article
- Stress granule-related genes during embryogenesis of an invertebrate chordate.Frontiers in cell and developmental biology · 2024Article
- RNA-Binding Proteins: A Role in Neurotoxicity?Neurotoxicity research · 2023Review
- Translation dysregulation in neurodegenerative diseases: a focus on ALS.Molecular neurodegeneration · 2023Review
- Liquid Droplet Aging and Seeded Fibril Formation of the Cytotoxic Granule Associated RNA Binding Protein TIA1 Low Complexity Domain.Journal of the American Chemical Society · 2023Article
- Simple models to understand complex disease: 10 years of progress fromFrontiers in neuroscience · 2023Review
- Two predicted α-helices within the prion-like domain of TIAR-1 play a crucial role in its association with stress granules inFrontiers in cell and developmental biology · 2023Article
- Intracellular accumulation of tau inhibits autophagosome formation by activating TIA1-amino acid-mTORC1 signaling.Military Medical Research · 2022Article
- Article
- Stress granule subtypes: an emerging link to neurodegeneration.Cellular and molecular life sciences : CMLS · 2020Review
- Functional Mammalian Amyloids and Amyloid-Like Proteins.Life (Basel, Switzerland) · 2020Review
Corrections and comments
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Authors and funding
2 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Prions are self-propagating protein conformations that are traditionally regarded as agents of neurodegenerative disease in animals. However, it has become evident that prion-like aggregation of endogenous proteins can also occur under normal physiological conditions (e.g., during memory storage or activation of the immune response). In this review, we focus on the functional prion-related protein TIA-1, an RNA-binding protein that is involved in multiple aspects of RNA metabolism but is best understood in terms of its role in stress granule assembly during the cellular stress response. We propose that stress granule formation provides a useful conceptual framework with which to address the positive role of TIA-1 prion-like aggregation. Elucidating the function of TIA-1 prion-like aggregation will advance our understanding of how prion-based molecular switches are used in normal physiological settings.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.