ArticleBiochemistry2009
The domains of polypyrimidine tract binding protein have distinct RNA structural preferences.
Article in Biochemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 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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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
31 citing papers in PubMed, 42 citations in OpenAlex.
- PTBP1 at the host-virus interface: mechanistic roles in viral RNA translation, replication, and immune modulation.Molecular biology reports · 2026Review
- Proteins that recognize unique features of U7 snRNA and may substitute for Gemin5 in the assembly of U7-specific Sm ring.RNA (New York, N.Y.) · 2025Article
- Article
- RNA binding proteins PTBP1 and HNRNPL regulateHeliyon · 2023Article
- Reviewing PTBP1 Domain Modularity in the Pre-Genomic Era: A Foundation to Guide the Next Generation of Exploring PTBP1 Structure-Function Relationships.International journal of molecular sciences · 2023Review
- Polypyrimidine-Tract-Binding Protein Isoforms Differentially Regulate the Hepatitis C Virus Internal Ribosome Entry Site.Viruses · 2022Article
- PRIESSTESS: interpretable, high-performing models of the sequence and structure preferences of RNA-binding proteins.Nucleic acids research · 2022Article
- Identification of the role of mono-ADP-ribosylation in colorectal cancer by integrated transcriptome analysis.Medical oncology (Northwood, London, England) · 2021Article
- A transient α-helix in the N-terminal RNA recognition motif of polypyrimidine tract binding protein senses RNA secondary structure.Nucleic acids research · 2020Article
- Post-Translational Modifications in Polypyrimidine Tract Binding Proteins PTBP1 and PTBP2.Biochemistry · 2018Article
- Global spatial analysis of Arabidopsis natural variants implicates 5'UTR splicing of LATE ELONGATED HYPOCOTYL in responses to temperature.Plant, cell & environment · 2018Article
- Article
- RNA and Proteins: Mutual Respect.F1000Research · 2017Review
- Human polypyrimidine tract-binding protein interacts with mitochondrial tRNA(Thr) in the cytosol.Nucleic acids research · 2016Article
- Article
- Polypyrimidine tract-binding proteins of potato mediate tuberization through an interaction with StBEL5 RNA.Journal of experimental botany · 2015Article
- Review
- PTBP1 is required for glucose-stimulated cap-independent translation of insulin granule proteins and Coxsackieviruses in beta cells.Molecular metabolism · 2014Article
- New insights into functional roles of the polypyrimidine tract-binding protein.International journal of molecular sciences · 2013Review
- Update on the Development of Anti-Viral Agents Against Hepatitis C.Journal of clinical and translational hepatology · 2013Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
PTB (polypyrimidine tract binding protein) participates in cellular regulatory functions in the nucleus and the cytoplasm. It binds to internal ribosome entry sites to facilitate their use in cap-independent translation. It binds to polypyrimidine tracts in pre-mRNA introns to repress inclusion of exons. It binds to the 3' untranslated regions of mRNAs to stabilize the message. These RNAs have various structures, yet PTB binds to all of them. Here, RNAs with structured or unstructured polypyrimidine tracts are bound to the full-length PTB1 protein and two protein subdomains, each containing two RNA recognition motifs. Hairpin loops from c-src and GABAA gamma2 pre-mRNAs and from the 3' terminus of hepatitis C virus (HCV) were compared to a single-stranded polypyrimidine tract from GABAA gamma2 pre-mRNA. We conclude that PTB1 RNA binding function is modular: the N-terminal RRMs preferentially bind to short (U/C) tracts displayed in loops, while the RRM3-RRM4 complex preferentially binds to longer flexible RNA sequences. Since it can bind to short and long polypyrimidine tracts, structured or single-stranded, PTB takes on the role of a versatile adaptor protein that facilitates formation of RNA-protein regulatory complexes.
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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.