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Literatura académica sobre el tema "Prion-like disorder"

Autor: Grafiati

Publicado: 11 de marzo de 2023

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Artículos de revistas sobre el tema "Prion-like disorder"

Monzón, Marta. "Morphological Changes of Glia in Prion and a Prion-Like Disorder". Alzheimer’s & Neurodegenerative Diseases 2, n.º 1 (5 de mayo de 2016): 1–4. http://dx.doi.org/10.24966/and-9608/100005.

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Jellinger, Kurt A., Gregor K. Wenning y Nadia Stefanova. "Is Multiple System Atrophy a Prion-like Disorder?" International Journal of Molecular Sciences 22, n.º 18 (18 de septiembre de 2021): 10093. http://dx.doi.org/10.3390/ijms221810093.

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Multiple system atrophy (MSA) is a rapidly progressive, fatal neurodegenerative disease of uncertain aetiology that belongs to the family of α-synucleinopathies. It clinically presents with parkinsonism, cerebellar, autonomic, and motor impairment in variable combinations. Pathological hallmarks are fibrillary α-synuclein (αSyn)-rich glial cytoplasmic inclusions (GCIs) mainly involving oligodendroglia and to a lesser extent neurons, inducing a multisystem neurodegeneration, glial activation, and widespread demyelinization. The neuronal αSyn pathology of MSA has molecular properties different from Lewy bodies in Parkinson’s disease (PD), both of which could serve as a pool of αSyn (prion) seeds that could initiate and drive the pathogenesis of synucleinopathies. The molecular cascade leading to the “prion-like” transfer of “strains” of aggregated αSyn contributing to the progression of the disease is poorly understood, while some presented evidence that MSA is a prion disease. However, this hypothesis is difficult to reconcile with postmortem analysis of human brains and the fact that MSA-like pathology was induced by intracerebral inoculation of human MSA brain homogenates only in homozygous mutant 53T mice, without production of disease-specific GCIs, or with replication of MSA prions in primary astrocyte cultures from transgenic mice expressing human αSyn. Whereas recent intrastriatal injection of Lewy body-derived or synthetic human αSyn fibrils induced PD-like pathology including neuronal αSyn aggregates in macaques, no such transmission of αSyn pathology in non-human primates by MSA brain lysate has been reported until now. Given the similarities between αSyn and prions, there is a considerable debate whether they should be referred to as “prions”, “prion-like”, “prionoids”, or something else. Here, the findings supporting the proposed nature of αSyn as a prion and its self-propagation through seeding as well as the transmissibility of neurodegenerative disorders are discussed. The proof of disease causation rests on the concordance of scientific evidence, none of which has provided convincing evidence for the classification of MSA as a prion disease or its human transmission until now.

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Murakami, Tomoaki, Yasuo Inoshima y Naotaka Ishiguro. "Systemic AA amyloidosis as a prion-like disorder". Virus Research 207 (septiembre de 2015): 76–81. http://dx.doi.org/10.1016/j.virusres.2014.12.019.

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Garcés, Moisés, M. Isabel Guijarro, Antonia Vargas, Juan J. Badiola y Marta Monzón. "Neuroglial patterns are shared by cerebella from prion and prion-like disorder affected patients". Mechanisms of Ageing and Development 184 (diciembre de 2019): 111176. http://dx.doi.org/10.1016/j.mad.2019.111176.

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Ma, Jiyan, Jingjing Zhang y Runchuan Yan. "Recombinant Mammalian Prions: The “Correctly” Misfolded Prion Protein Conformers". Viruses 14, n.º 9 (31 de agosto de 2022): 1940. http://dx.doi.org/10.3390/v14091940.

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Generating a prion with exogenously produced recombinant prion protein is widely accepted as the ultimate proof of the prion hypothesis. Over the years, a plethora of misfolded recPrP conformers have been generated, but despite their seeding capability, many of them have failed to elicit a fatal neurodegenerative disorder in wild-type animals like a naturally occurring prion. The application of the protein misfolding cyclic amplification technique and the inclusion of non-protein cofactors in the reaction mixture have led to the generation of authentic recombinant prions that fully recapitulate the characteristics of native prions. Together, these studies reveal that recPrP can stably exist in a variety of misfolded conformations and when inoculated into wild-type animals, misfolded recPrP conformers cause a wide range of outcomes, from being completely innocuous to lethal. Since all these recPrP conformers possess seeding capabilities, these results clearly suggest that seeding activity alone is not equivalent to prion activity. Instead, authentic prions are those PrP conformers that are not only heritable (the ability to seed the conversion of normal PrP) but also pathogenic (the ability to cause fatal neurodegeneration). The knowledge gained from the studies of the recombinant prion is important for us to understand the pathogenesis of prion disease and the roles of misfolded proteins in other neurodegenerative disorders.

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Harrison, Paul M. "Variable absorption of mutational trends by prion-forming domains during Saccharomycetes evolution". PeerJ 8 (6 de agosto de 2020): e9669. http://dx.doi.org/10.7717/peerj.9669.

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Prions are self-propagating alternative states of protein domains. They are linked to both diseases and functional protein roles in eukaryotes. Prion-forming domains in Saccharomyces cerevisiae are typically domains with high intrinsic protein disorder (i.e., that remain unfolded in the cell during at least some part of their functioning), that are converted to self-replicating amyloid forms. S. cerevisiae is a member of the fungal class Saccharomycetes, during the evolution of which a large population of prion-like domains has appeared. It is still unclear what principles might govern the molecular evolution of prion-forming domains, and intrinsically disordered domains generally. Here, it is discovered that in a set of such prion-forming domains some evolve in the fungal class Saccharomycetes in such a way as to absorb general mutation biases across millions of years, whereas others do not, indicating a spectrum of selection pressures on composition and sequence. Thus, if the bias-absorbing prion formers are conserving a prion-forming capability, then this capability is not interfered with by the absorption of bias changes over the duration of evolutionary epochs. Evidence is discovered for selective constraint against the occurrence of lysine residues (which likely disrupt prion formation) in S. cerevisiae prion-forming domains as they evolve across Saccharomycetes. These results provide a case study of the absorption of mutational trends by compositionally biased domains, and suggest methodology for assessing selection pressures on the composition of intrinsically disordered regions.

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Marciniuk, Kristen, Ryan Taschuk y Scott Napper. "Evidence for Prion-Like Mechanisms in Several Neurodegenerative Diseases: Potential Implications for Immunotherapy". Clinical and Developmental Immunology 2013 (2013): 1–20. http://dx.doi.org/10.1155/2013/473706.

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Transmissible spongiform encephalopathies (TSEs) are fatal, untreatable neurodegenerative diseases. While the impact of TSEs on human health is relatively minor, these diseases are having a major influence on how we view, and potentially treat, other more common neurodegenerative disorders. Until recently, TSEs encapsulated a distinct category of neurodegenerative disorder, exclusive in their defining characteristic of infectivity. It now appears that similar mechanisms of self-propagation may underlie other proteinopathies such as Alzheimer’s disease, Parkinson’s disease, Amyotrophic lateral sclerosis, and Huntington’s disease. This link is of scientific interest and potential therapeutic importance as this route of self-propagation offers conceptual support and guidance for vaccine development efforts. Specifically, the existence of a pathological, self-promoting isoform offers a rational vaccine target. Here, we review the evidence of prion-like mechanisms within a number of common neurodegenerative disorders and speculate on potential implications and opportunities for vaccine development.

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Olanow, C. Warren y Patrik Brundin. "Parkinson's Disease and Alpha Synuclein: Is Parkinson's Disease a Prion-Like Disorder?" Movement Disorders 28, n.º 1 (enero de 2013): 31–40. http://dx.doi.org/10.1002/mds.25373.

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Chauhan, Aneesha y Alexander F. Jeans. "Is Parkinson’s Disease Truly a Prion-Like Disorder? An Appraisal of Current Evidence". Neurology Research International 2015 (2015): 1–8. http://dx.doi.org/10.1155/2015/345285.

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Parkinson’s disease (PD) is the world’s second most common neurodegenerative disease and most common movement disorder. Characterised by a loss of dopaminergic neurons and the development of intraneuronal inclusions known as Lewy bodies, it has classically been thought of as a cell-autonomous disease. However, in 2008, two groups reported the startling observation of Lewy bodies within embryonic neuronal grafts transplanted into PD patients little more than a decade previously, suggesting that PD pathology can be propagated to neighbouring cells and calling basic assumptions of our understanding of the disease into question. Subsequent research has largely served to confirm this interpretation, pointing towards a prion-like intercellular transfer of misfoldedα-synuclein, the main component of Lewy bodies, as central to PD. This shift in thinking offers a revolutionary approach to PD treatment, potentially enabling a transition from purely symptomatic therapy to direct targeting of the pathology that drives disease progression. In this short review, we appraise current experimental support for PD as a prion-like disease, whilst highlighting areas of controversy or inconsistency which must be resolved. We also offer a brief discussion of the therapeutic implications of these discoveries.

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Won, Sae-Young, Yong-Chan Kim, Kyoungtag Do y Byung-Hoon Jeong. "Absence of Strong Genetic Linkage Disequilibrium between Single Nucleotide Polymorphisms (SNPs) in the Prion Protein Gene (PRNP) and the Prion-Like Protein Gene (PRND) in the Horse, a Prion-Resistant Species". Genes 11, n.º 5 (7 de mayo de 2020): 518. http://dx.doi.org/10.3390/genes11050518.

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Prion disease is a fatal neurodegenerative disorder caused by a deleterious prion protein (PrPSc). However, prion disease has not been reported in horses during outbreaks of transmissible spongiform encephalopathies (TSEs) in various animals in the UK. In previous studies, single nucleotide polymorphisms (SNPs) in the prion protein gene (PRNP) have been significantly associated with susceptibility to prion disease, and strong linkage disequilibrium (LD) between PRNP and prion-like protein gene (PRND) SNPs has been identified in prion disease-susceptible species. On the other hand, weak LD values have been reported in dogs, a prion disease-resistant species. In this study, we investigated SNPs in the PRND gene and measured the LD values between the PRNP and PRND SNPs and the impact of a nonsynonymous SNP found in the horse PRND gene. To identify SNPs in the PRND gene, we performed direct sequencing of the PRND gene. In addition, to assess whether the weak LD value between the PRNP and PRND SNPs is a characteristic of prion disease-resistant animals, we measured the LD value between the PRNP and PRND SNPs using D’ and r2 values. Furthermore, we evaluated the impact of a nonsynonymous SNP in the Doppel protein with PolyPhen-2, PROVEAN, and PANTHER. We observed two novel SNPs, c.331G > A (A111T) and c.411G > C. The genotype and allele frequencies of the c.331G > A (A111T) and c.411G > C SNPs were significantly different between Jeju, Halla, and Thoroughbred horses. In addition, we found a total of three haplotypes: GG, AG, and GC. The GG haplotype was the most frequently observed in Jeju and Halla horses. Furthermore, the impact of A111T on the Doppel protein was predicted to be benign by PolyPhen-2, PROVEAN, and PANTHER. Interestingly, a weak LD value between the PRNP and PRND SNPs was found in the horse, a prion disease-resistant animal. To the best of our knowledge, these results suggest that a weak LD value could be one feature of prion disease-resistant animals.

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Más fuentes

Tesis sobre el tema "Prion-like disorder"

Xiang, Fengqing. "Genetic studies of neurological disorders : Rett syndrome and HD-like familial prion disease /". Stockholm, 2001. http://diss.kib.ki.se/2001/91-628-4882-8/.

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Brozzetti, Lorenzo. "Neurodegeneration associated-proteins in human olfactory epithelium: immunocytochemical and biomolecular study in healthy subjects and patients with synucleinopathies". Doctoral thesis, 2020. http://hdl.handle.net/11562/1017250.

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Olfactory impairment is considered an initial disturbance of several neurodegenerative diseases (NDs), including Parkinson’s disease (PD) and Alzheimer’s disease (AD). In addition, smell impairment precedes a decade, or even longer, the onset of motor or cognitive symptoms. Olfactory signals are detected by olfactory receptor proteins (ORPs) expressed in the cilia of olfactory receptor neurons (ONs). ONs are the distinctive cellular components of the peripheral olfactory epithelium (OE) and lie in the nasal vault. ONs axons pass the cribriform plate and reach the olfactory bulb (OB) where the olfactory stimuli are processed and sent to the superior nuclei of the CNS. Previous studies in AD and other neurodegenerative disorders have shown the presence of β-amyloid deposits in the OB, neurofibrillary tangles, as well as Lewy body pathology. OB represents the brain area earlier involved in the neuropathological process, decades before the development of clinical symptoms. Therefore, OB can be considered a target in the study of neurodegenerative diseases in their early molecular processes. Moreover, the OB of healthy subjects presents deposits of aggregated proteins confirming that these aggregates are deposited in a prodromal disease stage. Since the OB is an early accumulation site of aggregated proteins and the synapses derive from the ONs, it is possible that the first event of protein aggregation occurs in OE. ONs are directly exposed to the external environment including chemical/physical toxic injuries and such micro-environment predisposes to abnormal protein processing and folding (Sammeta and McClintock 2010). In addition, ONs and all other mature cell components have a half-life of three months and programmed apoptosis. The neural activity is maintained by a constant cellular turn-over, which is sustained by the basal stem cells. This regeneration process is persistent during the whole life of an individual, albeit with a decreasing rate with aging. Extensive scientific literature indicates the neuronal damage as the consequence of exposure to toxic injuries leading to neurodegeneration and ONs are a natural model of this noxious process (Lema Tomé, Tyson et al. 2013). The hypothesis of this pathological pathway is supported by several studies, in which aggregated forms of α-synuclein, tau and β-amyloid are detected in olfactory mucosa (OM) biopsies as well as in autoptic samples of patients with Parkinson’s disease (PD), Lewy body dementia (LBD), Frontotemporal dementia (FTD) and Alzheimer disease (AD) (Funabe, Takao et al. 2013) (Saito, Shioya et al. 2016) (Tabaton, Cammarata et al. 1991) (Talamo, Rudel et al. 1989) (Crino, Greenberg et al. 1995) (Arnold, Lee et al. 2010). In this study, we investigated for the first-time primary ONs sampled ex vivo using olfactory brushing (OBg) in normal subjects and patients with different neurodegenerative disorders. Because of its convenient location, OE is easily accessible and can be sampled to obtain the ONs in the tissue outer layer. This sampling method is harmless and non-invasive, bypassing potential artifacts due to post mortem specimens as well as avoiding the invasiveness of biopsy procedures. Recently, we showed that OBg procedure in Creutzfeldt-Jakob Disease (CJD) patients allows efficient OM sampling for the Real-Time Quaking-Induced Conversion (RT-QuIC) assay. We specifically amplified pathological prion protein (PrPSc) providing a diagnostic intra vitam test with sensitivity and specificity nearly to 100% (Orrú, Bongianni et al. 2014). For the purpose of our study, we firstly defined the phenotypic characterization of the human olfactory cells sampled with OBg from healthy subjects. Distinct antibodies were selected to analyze the olfactory epithelium cells: olfactory marker protein (OMP), neuron-specific class III β-tubulin (TUJ-1), protein gene product 9.5 (PGP 9.5), Pan-Cytokeratin (PCK). Secondly, we aimed to determine the expression patterns of the major misfolded proteins involved in the main neurodegenerative diseases. In particular, the selected proteins were: α-synuclein, APP/beta-amyloid, tau, and TDP-43. The identification of the expression patterns of these proteins in the ONs might provide information to understand the abnormal molecular mechanisms in the initial misfolding species involved in the pathological process. Moreover, in this study, we speculated on the subcellular locale where the protein aggregation may occur. Furthermore, by demonstrating the constitutive expression of the native NDs-associated proteins in the OE, we could assume that they may represent a potential template for triggering the aggregation process. Based on the immunocytochemistry analysis, we investigated the α-synuclein expression in patients affected by different synucleinopathies. In fact, α-synuclein misfolding and aggregation mechanisms are involved in the pathogenesis of neurodegenerative disorders such as Parkinson's disease (PD), dementia with Lewy bodies (LBD) and multiple system atrophy (MSA), which are all characterized by α-synuclein fibrils deposition (Spillantini, Schmidt et al. 1997). Finally, we analyzed the immunocytochemistry results in OM samples tested by α-synuclein RT-QuIC (α-syn RT-QuIC).

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Libros sobre el tema "Prion-like disorder"

Cummings, Jeffrey L. y Jagan A. Pillai. Neurodegenerative Diseases. Oxford University Press, 2016. http://dx.doi.org/10.1093/med/9780190233563.003.0001.

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Neurodegenerative diseases (NDDs) are growing in frequency and represent a major threat to public health. Advances in scientific progress have made it clear that NDDs share many underlying processes, including shared intracellular mechanisms such as protein misfolding and aggregation, cell-to-cell prion-like spread, growth factor signaling abnormalities, RNA and DNA disturbances, glial cell changes, and neuronal loss. Transmitter deficits are shared across many types of disorders. Means of studying NDDs with human iPS cells and transgenic models are similar. The progression of NDDs through asymptomatic, prodromal, and manifest stages is shared across disorders. Clinical features of NDDs, including cognitive impairment, disease progression, age-related effects, terminal stages, neuropsychiatric manifestations, and functional disorders and disability, have many common elements. Clinical trials, biomarkers, brain imaging, and regulatory aspects of NDD can share information across NDDs. Disease-modifying and transmitter-based therapeutic interventions, clinical trials, and regulatory approaches to treatments for NDDs are also similar.

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Capítulos de libros sobre el tema "Prion-like disorder"

Rey, Nolwen L., Elodie Angot, Christopher Dunning, Jennifer A. Steiner y Patrik Brundin. "Accumulating Evidence Suggests that Parkinson’s Disease Is a Prion-Like Disorder". En Proteopathic Seeds and Neurodegenerative Diseases, 97–113. Berlin, Heidelberg: Springer Berlin Heidelberg, 2013. http://dx.doi.org/10.1007/978-3-642-35491-5_8.

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Ross, Eric D. y Sean M. Cascarina. "The roles of prion-like domains in amyloid formation, phase separation, and solubility". En Structure and Intrinsic Disorder in Enzymology, 397–426. Elsevier, 2023. http://dx.doi.org/10.1016/b978-0-323-99533-7.00014-5.

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Cutsforth-Gregory, Jeremy K. "Prion Disorders: Creutzfeldt-Jakob Disease and Related Disorders". En Mayo Clinic Neurology Board Review, editado por Kelly D. Flemming, 1044–49. Oxford University Press, 2021. http://dx.doi.org/10.1093/med/9780197512166.003.0116.

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Prion disorders, or transmissible spongiform encephalopathies (TSEs), are universally fatal human and animal diseases that cause rapid degeneration of brain neurons by way of a conformational change in the prion protein that autocatalyzes further conformational change and selective neuronal toxicity. TSEs may occur sporadically, be inherited, or, least frequently, spread like an infectious agent. Mounting evidence suggests that degenerative proteinopathies such as Alzheimer disease and Parkinson disease may also involve prionlike spread of abnormal proteins between neurons but not between organisms as in the prion disorders discussed in this chapter.

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Rundo, Jessica Vensel, Hillor Mehta y Reena Mehra. "Dying to Fall Asleep". En Sleep Disorders, 724–42. Oxford University Press, 2019. http://dx.doi.org/10.1093/med/9780190671099.003.0042.

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Fatal familial insomnia (FFI) is a rare autosomal dominant genetic disease characterized by progressive insomnia, autonomic hyperactivity, memory deficits, hallucinations, and myoclonus. Unlike its name, insomnia is not the most common initial presentation in patients with FFI. More common features like autonomic hyperactivity (hypertension and tachycardia) are often missed, delaying the diagnosis of FFI. Genetic analysis of FFI shows a D178N-129M mutation that results in generation of insoluble proteins (prion proteins) that aggregate to form amyloid plaques, leading to deterioration of the central nervous system, particularly in the hypothalamus. This case illustrates the difficulty in determining a definitive diagnosis in patients with FFI. Unfortunately, no treatment or cure is available for FFI. The disease is fatal in all the patients.

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Walker, Lary C. "Prion-like Protein Seeding and the Pathobiology of Alzheimer’s Disease". En Protein Folding Disorders of the Central Nervous System, 57–82. WORLD SCIENTIFIC, 2017. http://dx.doi.org/10.1142/9789813222960_0003.

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Pandey, Mukesh, Jahangir Nabi, Nahida Tabassum, Faheem Hyder Pottoo, Renuka Khatik y Niyaz Ahmad. "Molecular Chaperones in Neurodegeneration". En Quality Control of Cellular Protein in Neurodegenerative Disorders, 354–79. IGI Global, 2020. http://dx.doi.org/10.4018/978-1-7998-1317-0.ch014.

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Cellular chaperones are essential players to this protein quality control network that functions to prevent protein misfolding, refold misfolded proteins, or degrade them, thereby maintaining neuronal proteostasis. Moreover, overexpression of cellular chaperones is considered to inhibit protein aggregation and apoptosis in various experimental models of neurodegeneration. Alterations or downregulation of chaperone machinery by age-related decline, molecular crowding, or genetic mutations are regarded as key pathological hallmarks of neurodegenerative disorders like Alzheimer's disease (AD), Parkinson's disease (PD), amyotrophic lateral sclerosis (ALS), Huntington's disease (HD), and Prion diseases. Therefore, chaperones may serve as potential therapeutic targets in these diseases. This chapter presents a generalized view of misfolding and aggregation of proteins in neurodegeneration and then critically analyses some of the known cellular chaperones and their role in several neurodegenerative disorders.

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Mamun, Abdullah Al y Md Farhad Hossain. "Post-Translational Modifications in Neurodegeneration". En Quality Control of Cellular Protein in Neurodegenerative Disorders, 129–53. IGI Global, 2020. http://dx.doi.org/10.4018/978-1-7998-1317-0.ch005.

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Post-translational modifications (PTMs) increase proteome activity for controlling every feature of normal cell biology. PTMs such as phosphorylation, acetylation, glycosylation, fatty acylation, palmitoylation, myristoylation, ubiquitination, SUMOylation (small ubiquitin-like modifiers), methylation, deamidation, nitrosylation, etc. of proteins can regulate the properties of protein including intracellular distribution, functionality, stability, accumulation, as well as interactions. PTMs take place at any stage of the protein life cycle, regulating protein folding and activity in time and space, subcellular localization of the protein, and their activity. Hence, PTMs play a pivotal role in the regulation of numerous cellular processes. Abnormal PTMs of one or more culprit proteins might contribute to neurodegeneration, which is shown in some neurodegenerative disorders including Alzheimer's, Parkinson's, and prion disease. In this chapter, the authors focus on the most essential PTMs that are observed in neurodegenerative disorders and elucidating the pathogenesis wherein they are involved.

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Biney, Robert Peter, Thabisile Mpofana y Ella Anle Kasanga. "Free Radicals in Oxidative Stress, Aging, and Neurodegenerative Disorders". En Advances in Medical Diagnosis, Treatment, and Care, 48–75. IGI Global, 2019. http://dx.doi.org/10.4018/978-1-5225-5282-6.ch003.

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Free radicals are intricately woven into the fabric of oxidative stress and are significant in the development of neurodegenerative disorders (NDs). This chapter examines free radicals in the context of neurodegeneration and provides overview of the multiple roles they play in the pathophysiology and clinical progression of varying NDs including Pick's disease (PiD), Parkinson's disease (PD), Alzheimer's disease (AD), prion diseases (PrD), traumatic brain injury, and aging. The molecular mechanisms of degeneration in Huntington's disease (HD) are also examined with respect to free radicals. Different antioxidant systems and their mechanisms of action are briefly reviewed in addition to the role of diet in aging. The effectiveness of selected synthetic drugs and natural products used in oxidative stress is also reviewed. Lastly, the chapter examines challenges associated with the use of antioxidants and how promising future directions like the endocannabinoid system is being pursued in the race to effectively manage NDs.

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Biney, Robert Peter, Thabisile Mpofana y Ella Anle Kasanga. "Free Radicals in Oxidative Stress, Aging, and Neurodegenerative Disorders". En Research Anthology on Supporting Healthy Aging in a Digital Society, 225–52. IGI Global, 2022. http://dx.doi.org/10.4018/978-1-6684-5295-0.ch015.

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Galzitskaya, Oxana V. "Search for functions of intrinsically disordered prion-like domains for FET proteins involved in amyotrophic lateral sclerosis and frontotemporal dementia". En TDP-43 and Neurodegeneration, 117–33. Elsevier, 2022. http://dx.doi.org/10.1016/b978-0-12-820066-7.00003-5.

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