We are analyzing https://link.springer.com/article/10.1007/s12551-013-0132-0.

Title:
Pathological implications of nucleic acid interactions with proteins associated with neurodegenerative diseases | Biophysical Reviews
Description:
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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Keywords {🔍}

pubmed, google, scholar, cas, protein, prion, disease, central, biol, nucleic, cordeiro, dna, silva, aggregation, alzheimers, rna, amyloid, proteins, chem, mol, diseases, acid, binding, tau, res, acids, neurodegenerative, cell, sci, interaction, article, prp, interactions, gomes, misfolding, huntingtin, huntingtons, human, biochem, conversion, brain, usa, rev, cells, alphasynuclein, aggregates, neurosci, proc, natl, acad,

Topics {✒️}

intriguing nucleic-acid-binding features month download article/chapter prp c-terminal domain neuron-specific protein localized dna-induced partial unfolding beta-sheet-rich conformation amino acid-base interactions beta-amyloid precursor protein quadruplex-forming nucleic acids anomalous protein-dna interactions alpha-synuclein occurs physiologically double-stranded dna stimulates metal-triggered structural transformations antagonizing er/golgi snares ano bom ap beta-amyloid peptide aggregation disease amyloid-beta protein cucl2 induced conformational cellular polyamines promote nucleic acid conformation full article pdf 40-amino acid forms nucleic acid interactions tumor suppressor p53 soluble protein oligomers nucleic acid solution privacy choices/manage cookies prion protein leads n-terminal region figueroa-villar jd beta-sheet conformation trigger protein misfolding ovine prion protein prp conversion depends time-dependent solubility di monte da rio de janeiro financiadora de estudos sequence-specific manner mammalian prion protein protein-dna interactions amyloid beta protein prion protein complexed bovine prion protein presynaptic nerve terminal polyglutamine dependent manner maat-schieman ml protein-dna interaction protein-dna recognition nucleocapsid protein ncp7

Questions {❓}

Costa FF (2007) Non-coding RNAs: lost in translation?
What is strain in neurodegenerative diseases?

Schema {🗺️}

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