ReviewBiophysical reviews2014
Pathological implications of nucleic acid interactions with proteins associated with neurodegenerative diseases.
Review in Biophysical reviews, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
19 citing papers in PubMed, 38 citations in OpenAlex.
- RNA-seq analyses reveal the relevance of RNAs involved in ribosomal complex to induce mammalian prion protein aggregation and phase separationRNA biology · 2025Article
- Modeling genotype-protein interaction and correlation for Alzheimer's disease: a multi-omics imaging genetics study.Briefings in bioinformatics · 2024Article
- (Dys)functional insights into nucleic acids and RNA-binding proteins modulation of the prion protein and α-synuclein phase separation.Biophysical reviews · 2023Review
- The dynamics of extracellular DNA associates with treatment response in patients with rheumatoid arthritis.Scientific reports · 2022Article
- Epigenetic Changes in Prion and Prion-like Neurodegenerative Diseases: Recent Advances, Potential as Biomarkers, and Future Perspectives.International journal of molecular sciences · 2022Review
- Nuclear alpha-synuclein is present in the human brain and is modified in dementia with Lewy bodies.Acta neuropathologica communications · 2022Article
- Probing TDP-43 condensation using an in silico designed aptamer.Nature communications · 2022Article
- Modulation of the Conformational Space of SARS-CoV-2 RNA Quadruplex RG-1 by Cellular Components and the Amyloidogenic Peptides α-Synuclein and hIAPP.Chemistry (Weinheim an der Bergstrasse, Germany) · 2022Article
- ProNAB: database for binding affinities of protein-nucleic acid complexes and their mutants.Nucleic acids research · 2022Article
- The Amyloid Region of Hfq Riboregulator Promotes DsrA:Biology · 2021Article
- "Protein aggregates" contain RNA and DNA, entrapped by misfolded proteins but largely rescued by slowing translational elongation.Aging cell · 2021Article
- Identification and characterization of the Hfq bacterial amyloid region DNA interactions.BBA advances · 2021Article
- Phase Separation and Disorder-to-Order Transition of Human Brain Expressed X-Linked 3 (hBEX3) in the Presence of Small Fragments of tRNA.Journal of molecular biology · 2020Article
- Bacterial DNA promotes Tau aggregation.Scientific reports · 2020Article
- Effect of the micro-environment on α-synuclein conversion and implication in seeded conversion assays.Translational neurodegeneration · 2020Review
- RNA as a key factor in driving or preventing self-assembly of the TAR DNA-binding protein 43.Journal of molecular biology · 2019Article
- Distinct modulatory role of RNA in the aggregation of the tumor suppressor protein p53 core domain.The Journal of biological chemistry · 2017Article
- 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
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Protein misfolding disorders (PMDs) refer to a group of diseases related to the misfolding of particular proteins that aggregate and deposit in the cells and tissues of humans and other mammals. The mechanisms that trigger protein misfolding and aggregation are still not fully understood. Increasing experimental evidence indicates that abnormal interactions between PMD-related proteins and nucleic acids (NAs) can induce conformational changes. Here, we discuss these protein-NA interactions and address the role of deoxyribonucleic (DNA) and ribonucleic (RNA) acid molecules in the conformational conversion of different proteins that aggregate in PMDs, such as Alzheimer's, Parkinson's, and prion diseases. Studies on the affinity, stability, and specificity of proteins involved in neurodegenerative diseases and NAs are specifically addressed. A landscape of reciprocal effects resulting from the binding of prion proteins, amyloid-β peptides, tau proteins, huntingtin, and α-synuclein are presented here to clarify the possible role of NAs, not only as encoders of genetic information but also in triggering PMDs.
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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.