ArticleThe Journal of biological chemistry2012
Polyalanine-independent conformational conversion of nuclear poly(A)-binding protein 1 (PABPN1).
Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
What it found
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Who cites it
9 citing papers in PubMed, 12 citations in OpenAlex.
- mRNA alternative polyadenylation (APA) in regulation of gene expression and diseases.Genes & diseases · 2023Review
- Multi-omic analyses in Abyssinian cats with primary renal amyloid deposits.Scientific reports · 2021Article
- Post-transcriptional regulation of Pabpn1 by the RNA binding protein HuR.Nucleic acids research · 2018Article
- Polyalanine expansions drive a shift into α-helical clusters without amyloid-fibril formation.Nature structural & molecular biology · 2015Article
- Q&A: repeat-containing proteins.Nature structural & molecular biology · 2015Article
- Conformational stability of the RNP domain controls fibril formation of PABPN1.Protein science : a publication of the Protein Society · 2015Article
- Association of polyalanine and polyglutamine coiled coils mediates expansion disease-related protein aggregation and dysfunction.Human molecular genetics · 2014Article
- RNA-binding protein misregulation in microsatellite expansion disorders.Advances in experimental medicine and biology · 2014Review
- PABPN1: molecular function and muscle disease.The FEBS journal · 2013Review
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Oculopharyngeal muscular dystrophy is a late-onset disease caused by an elongation of a natural 10-alanine segment within the N-terminal domain of the nuclear poly(A)-binding protein 1 (PABPN1) to maximally 17 alanines. The disease is characterized by intranuclear deposits consisting primarily of PABPN1. In previous studies, we could show that the N-terminal domain of PABPN1 forms amyloid-like fibrils. Here, we analyze fibril formation of full-length PABPN1. Unexpectedly, fibril formation was independent of the presence of the alanine segment. With regard to fibril formation kinetics and resistance against denaturants, fibrils formed by full-length PABPN1 had completely different properties from those formed by the N-terminal domain. Fourier transformed infrared spectroscopy and limited proteolysis showed that fibrillar PABPN1 has a structure that differs from native PABPN1. Circumstantial evidence is presented that the C-terminal domain is involved in fibril formation.
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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.