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2019 3
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2023 14
2024 6

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Downregulation of apoptotic repressor AVEN exacerbates cardiac injury after myocardial infarction.
Yu P, Song S, Zhang X, Cui S, Wei G, Huang Z, Zeng L, Ni T, Sun A. Yu P, et al. Proc Natl Acad Sci U S A. 2023 Oct 17;120(42):e2302482120. doi: 10.1073/pnas.2302482120. Epub 2023 Oct 10. Proc Natl Acad Sci U S A. 2023. PMID: 37816050 Free PMC article.
Mechanistically, AVEN 3' UTR lengthening provides additional binding sites for miR-30b-5p and miR-30c-5p, thus reducing AVEN expression. Additionally, PABPN1 (poly(A)-binding protein 1) was identified as a potential regulator of AVEN 3' UTR lengthening after MI. ...
Mechanistically, AVEN 3' UTR lengthening provides additional binding sites for miR-30b-5p and miR-30c-5p, thus reducing AVEN expression. Add …
The polyA tail facilitates splicing of last introns with weak 3' splice sites via PABPN1.
Huang L, Li G, Du C, Jia Y, Yang J, Fan W, Xu YZ, Cheng H, Zhou Y. Huang L, et al. EMBO Rep. 2023 Oct 9;24(10):e57128. doi: 10.15252/embr.202357128. Epub 2023 Sep 4. EMBO Rep. 2023. PMID: 37661812 Free PMC article.
The polyA tail is essential for PABPN1-enhanced last intron splicing and functions in a length-dependent manner. Tethering PABPN1 to nonpolyadenylated transcripts also promotes splicing, suggesting a direct role for PABPN1 in splicing regulation. ...PABPN1
The polyA tail is essential for PABPN1-enhanced last intron splicing and functions in a length-dependent manner. Tethering PABPN1
Novel read-through fusion transcript Bcl2l2-Pabpn1 in glioblastoma cells.
Zhang L, Wang D, Han X, Guo X, Cao Y, Xia Y, Gao D. Zhang L, et al. J Cell Mol Med. 2022 Sep;26(17):4686-4697. doi: 10.1111/jcmm.17481. Epub 2022 Jul 27. J Cell Mol Med. 2022. PMID: 35894779 Free PMC article.
We performed paired-end RNA-seq of rat C6 glioma cells and normal cells and discovered a read-through fusion transcript Bcl2l2-Pabpn1 in which exon 3 of Bcl-2-like protein 2 (Bcl2l2) fused to exon 2 of Polyadenylate-binding protein 1 (Pabpn1). ...Unlike other fusion …
We performed paired-end RNA-seq of rat C6 glioma cells and normal cells and discovered a read-through fusion transcript Bcl2l2-Pabpn1
Oculopharyngeal muscular dystrophy mutations link the RNA-binding protein HNRNPQ to autophagosome biogenesis.
Ishtayeh H, Galves M, Barnatan TT, Berdichevsky Y, Amer-Sarsour F, Pasmanik-Chor M, Braverman I, Blumen SC, Ashkenazi A. Ishtayeh H, et al. Aging Cell. 2023 Oct;22(10):e13949. doi: 10.1111/acel.13949. Epub 2023 Aug 9. Aging Cell. 2023. PMID: 37559347 Free PMC article.
The RBPs HNRNPQ and poly(A) binding protein nuclear 1 (PABPN1) form a regulatory network that controls the turnover of distinct autophagy-related (ATG) proteins. ...Our data reveal a regulatory mechanism of autophagy induction that is compromised by PABPN1 disease m …
The RBPs HNRNPQ and poly(A) binding protein nuclear 1 (PABPN1) form a regulatory network that controls the turnover of distinct autop …
Cytoskeletal disorganization underlies PABPN1-mediated myogenic disability.
Olie CS, van der Wal E, Cikes D, Maton L, de Greef JC, Lin IH, Chen YF, Kareem E, Penninger JM, Kessler BM, Raz V. Olie CS, et al. Sci Rep. 2020 Oct 19;10(1):17621. doi: 10.1038/s41598-020-74676-8. Sci Rep. 2020. PMID: 33077830 Free PMC article.
Reduced levels of the polyadenylation binding protein nucleus 1 (PABPN1), a multifactorial regulator of mRNA processing, cause muscle atrophy. A proteomic study in muscles with reduced PABPN1 levels suggested dysregulation of sarcomeric and cytoskeletal proteins. He …
Reduced levels of the polyadenylation binding protein nucleus 1 (PABPN1), a multifactorial regulator of mRNA processing, cause muscle …
PABPN1 functions as a predictive biomarker in colorectal carcinoma.
Wang QH, Yan PC, Shi LZ, Teng YJ, Gao XJ, Yao LQ, Liang ZW, Zhou MH, Han W, Li R. Wang QH, et al. Mol Biol Rep. 2023 Dec 29;51(1):40. doi: 10.1007/s11033-023-08936-x. Mol Biol Rep. 2023. PMID: 38158471
PURPOSE: PABPN1 acts as a modulator of poly(A) tail length and alternative polyadenylation. This research was aimed to explore the role of PABPN1 in colorectal cancer (CRC). ...In addition, in vitro experiments were then carried out to identify the role of PABPN1
PURPOSE: PABPN1 acts as a modulator of poly(A) tail length and alternative polyadenylation. This research was aimed to explore the ro …
Assessment of PABPN1 nuclear inclusions on a large cohort of patients and in a human xenograft model of oculopharyngeal muscular dystrophy.
Roth F, Dhiab J, Boulinguiez A, Mouigni HR, Lassche S, Negroni E, Muraine L, Marhic A, Oliver A, Lainé J, Rouche A, O'Ferrall EK, van Engelen B, Ottenheijm C, Greif H, Blumen S, Lacau St Guily J, Perie S, Butler-Browne G, Mouly V, Trollet C. Roth F, et al. Acta Neuropathol. 2022 Dec;144(6):1157-1170. doi: 10.1007/s00401-022-02503-7. Epub 2022 Oct 5. Acta Neuropathol. 2022. PMID: 36197469 Free PMC article.
Here we demonstrate that age and genotype influence PABPN1 aggregates: the percentage of myonuclei containing PABPN1 aggregates increases with age and the chaperone HSP70 co-localize more frequently with PABPN1 aggregates with a larger polyalanine tract. ...O …
Here we demonstrate that age and genotype influence PABPN1 aggregates: the percentage of myonuclei containing PABPN1 aggregate …
Mitochondrial localization of PABPN1 in oculopharyngeal muscular dystrophy.
Doki T, Yamashita S, Wei FY, Hara K, Yamamoto T, Zhang Z, Zhang X, Tawara N, Hino H, Uyama E, Kurashige T, Maruyama H, Tomizawa K, Ando Y. Doki T, et al. Lab Invest. 2019 Nov;99(11):1728-1740. doi: 10.1038/s41374-019-0243-8. Epub 2019 Mar 20. Lab Invest. 2019. PMID: 30894671 Free article.
We also investigated the mechanism by which expanded PABPN1 would cause mitochondrial dysfunction in the mouse and cell models of OPMD. Mitochondrial localization of PABPN1 was observed in the muscle fibers of patients with OPMD. ...In cells expressing PABPN1
We also investigated the mechanism by which expanded PABPN1 would cause mitochondrial dysfunction in the mouse and cell models of OPM …
PABPN1 aggregation is driven by Ala expansion and poly(A)-RNA binding, leading to CFIm25 sequestration that impairs alternative polyadenylation.
Guan WL, Jiang LL, Yin XF, Hu HY. Guan WL, et al. J Biol Chem. 2023 Aug;299(8):105019. doi: 10.1016/j.jbc.2023.105019. Epub 2023 Jul 7. J Biol Chem. 2023. PMID: 37422193 Free PMC article.
The factors that drive PABPN1 aggregation and its cellular consequences remain largely unknown. Here, we investigated the roles of Ala stretch and poly(A) RNA in the phase transition of PABPN1 using biochemical and molecular cell biology methods. ...In conclusion, o …
The factors that drive PABPN1 aggregation and its cellular consequences remain largely unknown. Here, we investigated the roles of Al …
PABPN1 prevents the nuclear export of an unspliced RNA with a constitutive transport element and controls human gene expression via intron retention.
Kwiatek L, Landry-Voyer AM, Latour M, Yague-Sanz C, Bachand F. Kwiatek L, et al. RNA. 2023 May;29(5):644-662. doi: 10.1261/rna.079294.122. Epub 2023 Feb 8. RNA. 2023. PMID: 36754576 Free PMC article.
Here, we provide evidence that the human nuclear poly(A)-binding protein, PABPN1, functions in such restrictions. Using a reporter construct in which nuclear export of an incompletely spliced mRNA is enhanced by a viral constitutive transport element (CTE), we show that …
Here, we provide evidence that the human nuclear poly(A)-binding protein, PABPN1, functions in such restrictions. Using a reporter co …
43 results