ArticleNucleic acids research2013
Cross-talk between prion protein and quadruplex-forming nucleic acids: a dynamic complex formation.
Article in Nucleic acids research, 2013. 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, 37 citations in OpenAlex.
- Discovery of a G-rich ultra stable human ncRNA G-quadruplex that binds ATP.Non-coding RNA research · 2026Article
- Therapeutic Oligonucleotides for Neurodegenerative Diseases: Aptamer Strategies and Clay Nanoparticle-Based Delivery.Chemical record (New York, N.Y.) · 2025Review
- Down-Regulation of OncogeneInternational journal of molecular sciences · 2025Article
- Selective Up-Regulation of Tumor Suppressor Gene Retinoblastoma by Bisacridine Derivative Through Gene Promoter Quadruplex Structures for Cancer Treatment.International journal of molecular sciences · 2025Article
- Expanding the Functions of KHSRP Protein: Insights into DNA G-Quadruplex Binding.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025Article
- (Dys)functional insights into nucleic acids and RNA-binding proteins modulation of the prion protein and α-synuclein phase separation.Biophysical reviews · 2023Review
- Aptamer Applications in Neuroscience.Pharmaceuticals (Basel, Switzerland) · 2021Review
- Rabbit PrP Is Partially Resistant toFrontiers in neuroscience · 2021Article
- Recognition and Unfolding of c-MYC and Telomeric G-Quadruplex DNAs by the RecQ C-Terminal Domain of Human Bloom Syndrome Helicase.ACS omega · 2020Article
- Unraveling Prion Protein Interactions with Aptamers and Other PrP-Binding Nucleic Acids.International journal of molecular sciences · 2017Review
- The "Jekyll and Hyde" Actions of Nucleic Acids on the Prion-like Aggregation of Proteins.The Journal of biological chemistry · 2016Review
- Biophysical and morphological studies on the dual interaction of non-octarepeat prion protein peptides with copper and nucleic acids.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2014Article
- G-quadruplexes within prion mRNA: the missing link in prion disease?Nucleic acids research · 2014Article
- Pathological implications of nucleic acid interactions with proteins associated with neurodegenerative diseases.Biophysical reviews · 2014Review
Corrections and comments
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Authors and funding
7 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Prion protein (PrP) is involved in lethal neurodegenerative diseases, and many issues remain unclear about its physio-pathological role. Quadruplex-forming nucleic acids (NAs) have been found to specifically bind to both PrP cellular and pathological isoforms. To clarify the relevance of these interactions, thermodynamic, kinetic and structural studies have been performed, using isothermal titration calorimetry, surface plasmon resonance and circular dichroism methodologies. Three quadruplex-forming sequences, d(TGGGGT), r(GGAGGAGGAGGA), d(GGAGGAGGAGGA), and various forms of PrP were selected for this study. Our results showed that these quadruplexes exhibit a high affinity and specificity toward PrP, with K(D) values within the range 62÷630 nM, and a weaker affinity toward a PrP-β oligomer, which mimics the pathological isoform. We demonstrated that the NA quadruplex architecture is the structural determinant for the recognition by both PrP isoforms. Furthermore, we spotted both PrP N-terminal and C-terminal domains as the binding regions involved in the interaction with DNA/RNAs, using several PrP truncated forms. Interestingly, a reciprocally induced structure loss was observed upon PrP-NA interaction. Our results allowed to surmise a quadruplex unwinding-activity of PrP, that may have a feedback in vivo.
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Registered trials
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