ArticleBiophysical journal2012
Solution model of the intrinsically disordered polyglutamine tract-binding protein-1.
Article in Biophysical journal, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed, 21 citations in OpenAlex.
- Single-molecule fluorescence and cross-linking reveal ligand-gated Toc34 oligomerization dynamics.Biophysical journal · 2026Article
- PQBP3 prevents senescence by suppressing PSME3-mediated proteasomal Lamin B1 degradation.The EMBO journal · 2024Article
- Review
- Molecular Determinants of PQBP1 Binding to the HIV-1 Capsid Lattice.Journal of molecular biology · 2024Article
- Identification of a DNA methylation signature for Renpenning syndrome (RENS1), a spliceopathy.European journal of human genetics : EJHG · 2023Article
- PQBP1: The Key to Intellectual Disability, Neurodegenerative Diseases, and Innate Immunity.International journal of molecular sciences · 2022Review
- Tau activates microglia via the PQBP1-cGAS-STING pathway to promote brain inflammation.Nature communications · 2021Article
- Fatal Attraction: The Case of Toxic Soluble Dimers of Truncated PQBP-1 Mutants in X-Linked Intellectual Disability.International journal of molecular sciences · 2021Review
- Predicting Conformational Properties of Intrinsically Disordered Proteins from Sequence.Methods in molecular biology (Clifton, N.J.) · 2020Article
- Polyglutamine Repeats in Viruses.Molecular neurobiology · 2019Review
- Ultra-Early Phase pathologies of Alzheimer's disease and other neurodegenerative diseases.Proceedings of the Japan Academy. Series B, Physical and biological sciences · 2017Review
- Selection pressure on human STR loci and its relevance in repeat expansion disease.Molecular genetics and genomics : MGG · 2016Article
- The importance of intrinsic order in a disordered protein ligand.Biophysical journal · 2014Article
- Conformations of intrinsically disordered proteins are influenced by linear sequence distributions of oppositely charged residues.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
Corrections and comments
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Authors and funding
10 authors at 4 institutions in 3 countries.
Funding
Abstract
Polyglutamine tract-binding protein-1 (PQBP-1) is a 265-residue nuclear protein that is involved in transcriptional regulation. In addition to its role in the molecular pathology of the polyglutamine expansion diseases, mutations of the protein are associated with X-linked mental retardation. PQBP-1 binds specifically to glutamine repeat sequences and proline-rich regions, and interacts with RNA polymerase II and the spliceosomal protein U5-15kD. In this work, we obtained a biophysical characterization of this protein by employing complementary structural methods. PQBP-1 is shown to be a moderately compact but largely disordered molecule with an elongated shape, having a Stokes radius of 3.7 nm and a maximum molecular dimension of 13 nm. The protein is monomeric in solution, has residual β-structure, and is in a premolten globule state that is unaffected by natural osmolytes. Using small-angle x-ray scattering data, we were able to generate a low-resolution, three-dimensional model of PQBP-1.
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