ArticleThe Journal of biological chemistry2013
RNA binding of T-cell intracellular antigen-1 (TIA-1) C-terminal RNA recognition motif is modified by pH conditions.
Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 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
11 citing papers in PubMed, 17 citations in OpenAlex.
- Regulation of TIA-1 Condensates: ZnFrontiers in molecular biosciences · 2022Article
- Post-translational Control of RNA-Binding Proteins and Disease-Related Dysregulation.Frontiers in molecular biosciences · 2021Review
- AU-rich element-binding proteins in colorectal cancer.World journal of gastrointestinal oncology · 2019Review
- Structural characterization of a novel KH-domain containing plant chloroplast endonuclease.Scientific reports · 2018Article
- A putative RNA binding protein fromFEBS open bio · 2018Article
- TIA-1 RRM23 binding and recognition of target oligonucleotides.Nucleic acids research · 2017Article
- RNA Binding Protein Regulation and Cross-Talk in the Control of AU-rich mRNA Fate.Frontiers in molecular biosciences · 2017Review
- RNA recognition and stress granule formation by TIA proteins.International journal of molecular sciences · 2014Review
- Structure, dynamics and RNA binding of the multi-domain splicing factor TIA-1.Nucleic acids research · 2014Article
- The C-terminal RNA binding motif of HuR is a multi-functional domain leading to HuR oligomerization and binding to U-rich RNA targets.RNA biology · 2014Article
- The binding of TIA-1 to RNA C-rich sequences is driven by its C-terminal RRM domain.RNA biology · 2014Article
Corrections and comments
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Authors and funding
5 authors at 4 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
T-cell intracellular antigen-1 (TIA-1) is a DNA/RNA-binding protein that regulates critical events in cell physiology by the regulation of pre-mRNA splicing and mRNA translation. TIA-1 is composed of three RNA recognition motifs (RRMs) and a glutamine-rich domain and binds to uridine-rich RNA sequences through its C-terminal RRM2 and RRM3 domains. Here, we show that RNA binding mediated by either isolated RRM3 or the RRM23 construct is controlled by slight environmental pH changes due to the protonation/deprotonation of TIA-1 RRM3 histidine residues. The auxiliary role of the C-terminal RRM3 domain in TIA-1 RNA recognition is poorly understood, and this work provides insight into its binding mechanisms.
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What OpenQuestion holds
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.