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PubMed Journals Articles About "RNAs Play Role Protein Aggregation Neurodegenerative Disease" RSS

23:18 EDT 26th March 2019 | BioPortfolio

RNAs Play Role Protein Aggregation Neurodegenerative Disease PubMed articles on BioPortfolio. Our PubMed references draw on over 21 million records from the medical literature. Here you can see the latest RNAs Play Role Protein Aggregation Neurodegenerative Disease articles that have been published worldwide.

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Showing "RNAs Play Role Protein Aggregation Neurodegenerative Disease" PubMed Articles 1–25 of 52,000+

Modulation of p53 and prion protein aggregation by RNA.

Several RNA-binding proteins undergo reversible liquid-liquid phase transitions, which, in pathological conditions, might evolve into transitions to solid-state phases, giving rise to amyloid structures. Amyloidogenic and prion-like proteins, such as the tumor suppressor protein p53 and the mammalian prion protein (PrP), bind RNAs specifically or nonspecifically, resulting in changes in their propensity to undergo aggregation. Mutant p53 aggregation seems to play a crucial role in cancer through loss of fun...


Imaging individual protein aggregates to follow aggregation and determine the role of aggregates in neurodegenerative disease.

Protein aggregates play a key role in the initiation and spreading of neurodegenerative disease but have been difficult to study due to their low abundance and heterogeneity, in both size and structure. Fluorescence based methods capable of detecting and characterising single aggregates have recently been developed and can be used to measure many important aggregate properties, and can be combined with sensitive assays to measure aggregate toxicity. Here we review these methods and discuss recent examples o...

Protein misfolding and aggregation in neurodegenerative diseases: a review of pathogeneses, novel detection strategies, and potential therapeutics.

Protein folding is a complex, multisystem process characterized by heavy molecular and cellular footprints. Chaperone machinery enables proper protein folding and stable conformation. Other pathways concomitant with the protein folding process include transcription, translation, post-translational modifications, degradation through the ubiquitin-proteasome system, and autophagy. As such, the folding process can go awry in several different ways. The pathogenic basis behind most neurodegenerative diseases is...


Astrocytic expression of the chaperone DNAJB6 results in non-cell autonomous protection in Huntington's disease.

Several neurodegenerative diseases like Huntington's, a polyglutamine (PolyQ) disease, are initiated by protein aggregation in neurons. Furthermore, these diseases are also associated with a multitude of responses in non-neuronal cells in the brain, in particular glial cells, like astrocytes. These non-neuronal responses have repeatedly been suggested to play a disease-modulating role, but how these may be exploited to delay the progression of neurodegeneration has remained unclear. Interestingly, one of th...

Emerging roles of long non-coding RNAs in the pathogenesis of Alzheimer's disease.

Alzheimer's disease (AD) is a heterogeneous neurodegenerative disorder and represents the most common form of senile dementia. The pathogenesis of AD is not yet completely understood and no curative treatment is currently available. With the recent advancement in transcriptome-wide profiling approach, several non-coding RNAs (ncRNAs) have been identified. Among them, long non-coding RNAs (lncRNAs), which are long transcripts without apparent protein-coding capacity, have received increasing interest for the...

Upregulation of miR-200a and miR-204 in MPP -treated differentiated PC12 cells as a model of Parkinson's disease.

Parkinson's disease (PD) is ranked as the second most common neurodegenerative disorder caused by loss of dopaminergic neurons in the substantia nigra. Micro(mi)RNAs are a class of small noncoding RNAs that regulate gene expression and aberrant expression of them is closely correlated with many neurodegenerative conditions including PD. Silent information regulator 1 (SIRT1) as a known deacetylase and B-cell lymphoma-2 (BCL2) as an antiapoptotic factor play vital roles in neural protection and survival.

Proteolytic cleavage of Beclin 1 exacerbates neurodegeneration.

Neuronal cell loss contributes to the pathology of acute and chronic neurodegenerative diseases, including Alzheimer's disease (AD). It remains crucial to identify molecular mechanisms sensitizing neurons to various insults and cell death. To date, the multifunctional, autophagy-related protein Beclin 1 has been shown to be both necessary and sufficient for neuronal integrity in neurodegenerative models associated with protein aggregation. Interestingly, besides its role in cellular homeostasis, Beclin 1 ha...

Modulation of Alpha-Synuclein Aggregation by Cytochrome c Binding and Hetero-di-Tyrosine Adduct Formation.

The aggregation of α-synuclein (A-syn) has been implicated strongly in Parkinson's disease (PD). Intrinsically disordered nature of A-syn makes this protein prone to self-association with itself, or hetero-association with another protein and/or lipid. While the role of conformational fluctuation and free radical chemistry have been shown to play important roles in its ability towards self and hetero association, any systematic understanding of their contributions is missing. Here, we report an in-vitro in...

Upregulated levels and pathological aggregation of abnormally phosphorylated Tau-Protein in children with neurodevelopmental disorders.

The tubulin-associated unit (Tau) protein is an intrinsically disordered protein that plays a well-established role in promoting microtubule assembly and stabilization in neuronal axons at all stages of development. Identification of new interacting partners and different sub-cellular localizations of Tau in recent years led to the discovery of novel physiological functions in regulation of neuronal activity, neurogenesis, long-term depression, iron export and genomic integrity. In addition, Tau gene mutati...

Extending the functional characteristics of naturally occurring autoantibodies against β-Amyloid, Prion Protein and α-Synuclein.

Abnormal aggregation of proteins induces neuronal cell loss in neurodegenerative disorders such as Alzheimer's Disease, Creutzfeldt-Jakob Disease and Parkinson's Disease. Specific stimuli initialize conformational changes in physiological proteins, causing intra- or extracellular protein aggregation. We and other groups have identified naturally occurring autoantibodies (nAbs) as part of the human antibody pool that are able to prevent peptide fibrillation. These nAbs show a rescue effect following exposure...

Protein Aggregation - Mechanisms, Detection, and Control.

Protein aggregation has been recognized as one of the major challenges in the development and commercialization of successful protein-based drug products because of the inherent and high aggregation tendency during various manufacturing processes, storage, and administration. Protein aggregates may impact significantly the product quality, safety and/or efficacy. This review is intended to summarize four major aspects of protein aggregation - (1) aggregation mechanisms,(2) aggregation-influencing factors,(3...

The Role of microRNAs in Spinocerebellar Ataxia Type 3.

More than 90 % of the human genome are transcribed as non-coding RNAs. While it is still under debate if all these non-coding transcripts are functional, there is emerging evidence that RNA has several important functions in addition to coding for proteins. For example, microRNAs (miRNAs) are important regulatory RNAs that control gene expression in various biological processes and human diseases. In spinocerebellar ataxia type 3 (SCA3), a devastating neurodegenerative disease, miRNAs are involved in the di...

Interaction of metal ions with tau protein. The case for a metal-mediated tau aggregation.

Tau protein aggregation and its hyperphosphorylation play an important role in the pathogenesis of Alzheimer's disease. There is also considerable evidence for the accumulation of Fe, Cu, and Zn in the brain of Alzheimer's patients, although their involvement in the etiology of the disease remains unknown. Here, interactions of the 3d metal ions Fe, Cu, and Zn with the longest isoform of the human tau protein (htau40) are studied in detail. Electrospray mass spectrometry and ion mobility mass spectrometry a...

Interactions between the Intrinsically Disordered Proteins β-Synuclein and α-Synuclein.

Several intrinsically disordered proteins (IDPs) have been implicated in the process of amyloid fibril formation in neurodegenerative disease, and developing approaches to inhibit the aggregation of these IDPs is critical for establishing effective therapies against disease progression. The aggregation pathway of the IDP alpha-synuclein (αS), is implicated in several neurodegenerative diseases known as synucleinopathies and has been extensively characterized. Less attention has been leveraged on beta-synuc...

Computational insights into the role of α-strand/sheet in aggregation of α-synuclein.

The α-synuclein is a major component of amyloid fibrils found in Lewy bodies, the characteristic intracellular proteinaceous deposits which are pathological hallmarks of neurodegenerative diseases such as Parkinson's disease (PD) and dementia. It is an intrinsically disordered protein that may undergo dramatic structural changes to form amyloid fibrils. Aggregation process from α-synuclein monomers to amyloid fibrils through oligomeric intermediates is considered as the disease-causative toxic mechanism. ...

Mitochondrial dynamics, a key executioner in neurodegenerative diseases.

Neurodegenerative diseases (NDs) are the group of disorder that includes brain, peripheral nerves, spinal cord and results in sensory and motor neuron dysfunction. Several studies have shown that mitochondrial dynamics and their axonal transport play a central role in most common NDs such as Alzheimer's disease (AD), Parkinson's disease (PD), Huntington's disease (HD) and Amyotrophic Lateral Sclerosis (ALS) etc. In normal physiological condition, there is a balance between mitochondrial fission and fusion p...

Pivotal role of carnosine in the modulation of brain cells activity: multimodal mechanism of action and therapeutic potential in neurodegenerative disorders.

Carnosine (β-alanyl-L-histidine), a dipeptide, is an endogenous antioxidant widely distributed in excitable tissues like muscles and the brain. Although discovered more than a hundred years ago and having been extensively studied in the periphery, the role of carnosine in the brain remains mysterious. Carnosinemia, a rare metabolic disorder with increased levels of carnosine in urine and low levels or absence of carnosinase in the blood, is associated with severe neurological symptoms in humans. This revie...

In silico method for identification of novel copper and iron metabolism proteins in various neurodegenerative disorders.

Copper (Cu) and Iron (Fe) has been the subject of intensive research over several decades as numerous seminal studies robustly support the involvement of Cu and Fe metabolism dyshomeostasis as a common denominator in several neurodegenerative disorders (particularly Alzheimer's disease and Parkinson's disease); however, till date, the exact "cause-effect" association has not been elucidated. Thus, there is urgent need to look for newer association/pathways of these redox active elements in different neuropa...

Circular and long non-coding RNAs and their role in ophthalmologic diseases.

Long non-coding RNAs are 200 nucleotide long RNA molecules which lack or have limited protein-coding potential. They can regulate protein formation through several different mechanisms. Similarly, circular RNAs are reported to play a critical role in post-transcriptional gene regulation. Changes in the expression pattern of these molecules are established to underline various diseases, including cancer, cardiovascular, neurological and immunological disorders. Recent studies suggest that they are differenti...

Acetylation as a major determinant to microtubule-dependent autophagy: Relevance to Alzheimer's and Parkinson disease pathology.

Protein post-translational modifications (PTMs) that potentiate protein aggregation have been implicated in several neurological disorders, including Alzheimer's (AD) and Parkinson's disease (PD). In fact, Tau and alpha-synuclein (ASYN) undergo several PTMs potentiating their aggregation and neurotoxicity. Recent data posits a role for acetylation in Tau and ASYN aggregation. Herein we aimed to clarify the role of Sirtuin-2 (SIRT2) and HDAC6 tubulin deacetylases as well as p300 acetyltransferase in AD and P...

Biophysical and Spectroscopic Methods for Monitoring Protein Misfolding and Amyloid Aggregation.

Proteins exhibit a remarkable structural plasticity and may undergo conformational changes resulting in protein misfolding both in a biological context and upon perturbing physiopathological conditions. Such nonfunctional protein conformers, including misfolded states and aggregates, are often associated to protein folding diseases. Understanding the biology of protein folding diseases thus requires tools that allow the structural characterization of nonnative conformations of proteins and their interconver...

Osthole decreases tau protein phosphorylation via PI3K/AKT/GSK-3β signaling pathway in Alzheimer's disease.

Alzheimer's disease (AD), a neurodegenerative disease, was characterized by the loss of memory and progressive cognitive deterioration. Up to now, there has no effective drugs to cure or delay the state of illness. Increasing evidence indicates that hyperphosphorylated tau protein plays a pivotal role in the occurrence and development of AD. Therefore, in present study, we aim to investigate whether osthole (OST) could decrease hyperphosphorylated tau protein in AD and the underlying mechanism.

Unravelling Protein Aggregation as an Ageing Related Process or a Neuropathological Response.

Protein aggregation is normally associated with amyloidosis, namely motor neurone, Alzheimer's, Parkinson's or prion diseases. However, recent results have unveiled a concept of gradual increase of protein aggregation associated with the ageing process, apparently not necessarily associated with pathological conditions. Given that protein aggregation is sufficient to activate stress-response and inflammation, impairing protein synthesis and quality control mechanisms, the former is assumed to negatively aff...

Single-Molecule FRET Detection of Early-Stage Conformations in α-Synuclein Aggregation.

Misfolding and aggregation of α-synuclein are linked to many neurodegenerative disorders, including Parkinson's and Alzheimer's disease. Despite intense research efforts, detailed structural characterization of early conformational transitions that initiate and drive α-synuclein aggregation remains elusive often due to the low sensitivity and ensemble averaging of commonly used techniques. Single-molecule Förster resonance energy transfer (smFRET) provides unique advantages in detecting minor conformatio...

Chaperoning Against Amyloid Aggregation: Monitoring In Vitro and In Vivo.

Protein aggregation and inclusion body formation have been a key causal phenomenon behind a majority of neurodegenerative disorders. Various approaches aimed at preventing the formation/elimination of protein aggregates are being developed to control these diseases. Molecular chaperones are a class of protein that not only direct the functionally relevant fold of the protein but also perform quality control against stress, misfolding/aggregation. Genes that encode molecular chaperones are induced and expres...


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