ArticleNucleic acids research2014
Poly(A) RNA and Paip2 act as allosteric regulators of poly(A)-binding protein.
Article in Nucleic acids research, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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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
12 citing papers in PubMed, 19 citations in OpenAlex.
- RNA-binding proteins in the mouse lens: Functional classifications, expression profiling, and interaction studies of Carhsp1 with crystallin mRNAs.Developmental biology · 2026Article
- smDeepFLUOR: single-molecule deep learning fluorescence classification.Nature communications · 2026Article
- Messenger RNA therapy in bone and joint diseases: Rationale, delivery systems, and applications.Biomaterials translational · 2026Article
- DNA Hanger: Surface-Minimized Single-Molecule Immunoassay Platform.Small (Weinheim an der Bergstrasse, Germany) · 2025Article
- dCas13-mediated translational repression for accurate gene silencing in mammalian cells.Nature communications · 2024Article
- Single-molecule visualization of mRNA circularization during translation.Experimental & molecular medicine · 2023Review
- The flip-flop configuration of the PABP-dimer leads to switching of the translation function.Nucleic acids research · 2022Article
- Molecular Basis for poly(A) RNP Architecture and Recognition by the Pan2-Pan3 Deadenylase.Cell · 2019Article
- Polyadenylate-binding protein-interacting proteins PAIP1 and PAIP2 affect translation termination.The Journal of biological chemistry · 2019Article
- Proteomic and Phosphoproteomic Changes Induced by Prolonged Activation of Human Eosinophils with IL-3.Journal of proteome research · 2018Article
- The bent conformation of poly(A)-binding protein induced by RNA-binding is required for its translational activation function.RNA biology · 2017Article
- CRISPR/Cpf1-mediated DNA-free plant genome editing.Nature communications · 2017Article
Corrections and comments
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Authors and funding
7 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
When bound to the 3' poly(A) tail of mRNA, poly(A)-binding protein (PABP) modulates mRNA translation and stability through its association with various proteins. By visualizing individual PABP molecules in real time, we found that PABP, containing four RNA recognition motifs (RRMs), adopts a conformation on poly(A) binding in which RRM1 is in proximity to RRM4. This conformational change is due to the bending of the region between RRM2 and RRM3. PABP-interacting protein 2 actively disrupts the bent structure of PABP to the extended structure, resulting in the inhibition of PABP-poly(A) binding. These results suggest that the changes in the configuration of PABP induced by interactions with various effector molecules, such as poly(A) and PABP-interacting protein 2, play pivotal roles in its function.
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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.