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Journal articles on the topic 'Prion-like disorder'

Author: Grafiati

Published: 11 March 2023

Last updated: 31 July 2025

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1

Monzón, Marta. "Morphological Changes of Glia in Prion and a Prion-Like Disorder." Alzheimer’s & Neurodegenerative Diseases 2, no. 1 (2016): 1–4. http://dx.doi.org/10.24966/and-9608/100005.

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Jellinger, Kurt A., Gregor K. Wenning, and Nadia Stefanova. "Is Multiple System Atrophy a Prion-like Disorder?" International Journal of Molecular Sciences 22, no. 18 (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 f

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3

Murakami, Tomoaki, Yasuo Inoshima, and Naotaka Ishiguro. "Systemic AA amyloidosis as a prion-like disorder." Virus Research 207 (September 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, and Marta Monzón. "Neuroglial patterns are shared by cerebella from prion and prion-like disorder affected patients." Mechanisms of Ageing and Development 184 (December 2019): 111176. http://dx.doi.org/10.1016/j.mad.2019.111176.

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Ma, Jiyan, Jingjing Zhang, and Runchuan Yan. "Recombinant Mammalian Prions: The “Correctly” Misfolded Prion Protein Conformers." Viruses 14, no. 9 (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 recapitulat

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Marciniuk, Kristen, Ryan Taschuk, and 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

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7

Olanow, C. Warren, and Patrik Brundin. "Parkinson's Disease and Alpha Synuclein: Is Parkinson's Disease a Prion-Like Disorder?" Movement Disorders 28, no. 1 (2013): 31–40. http://dx.doi.org/10.1002/mds.25373.

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Chauhan, Aneesha, and 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 understandi

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Harrison, Paul M. "Variable absorption of mutational trends by prion-forming domains during Saccharomycetes evolution." PeerJ 8 (August 6, 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 mol

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10

Won, Sae-Young, Yong-Chan Kim, Kyoungtag Do, and 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, no. 5 (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 valu

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11

Pradnya D Jadhav, Vaibhav V Kakade, and Aniket E Indrale. "The review on: “Creutzfeldt-Jakob disease”." International Journal of Research in Pharmaceutical Sciences 13, no. 1 (2022): 50–56. http://dx.doi.org/10.26452/ijrps.v13i1.19.

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This review will explore the information about Creutzfeldt -Jakob disease (CJD), which is the human prion disease. CJD is a rare brain disorder and rapidly progressive. CJD belongs to the family of human prion disease, which is caused by misfolded, transmissible infections particles, or prions. Transmissible spongiform encephalopathy (TSEs), also known as prion disease. Spongiform refers to the characteristic appearance of infected brains. CJD affects about one person in every one million people per year worldwide. CJD is a fatal neurodegenerative disorder which is having a higher mortality ra

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12

Chen, Merry, Julie Vincent, Alexis Ezeanii, Saurabh Wakade, Shobha Yerigenahally та Danielle E. Mor. "Heparan sulfate proteoglycans mediate prion-like α-synuclein toxicity in Parkinson’s in vivo models". Life Science Alliance 5, № 11 (2022): e202201366. http://dx.doi.org/10.26508/lsa.202201366.

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Parkinson’s disease (PD) is a debilitating neurodegenerative disorder characterized by progressive motor decline and the aggregation of α-synuclein protein. Growing evidence suggests that α-synuclein aggregates may spread from neurons of the digestive tract to the central nervous system in a prion-like manner, yet the mechanisms of α-synuclein transmission and neurotoxicity remain poorly understood. Animal models that are amenable to high-throughput investigations are needed to facilitate the discovery of disease mechanisms. Here we describe the first Caenorhabditis elegans models in which fee

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Kujawska, Małgorzata, and Jadwiga Jodynis-Liebert. "What Is the Evidence that Parkinson’s Disease Is a Prion Disorder, Which Originates in the Gut?" International Journal of Molecular Sciences 19, no. 11 (2018): 3573. http://dx.doi.org/10.3390/ijms19113573.

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Parkinson’s disease (PD) is a neurodegenerative disorder resulting from degeneration of dopaminergic neurons in the substantia nigra pars compacta (SNpc). PD is characterized by motor dysfunctions as well as gastrointestinal symptoms and mental impairment. The pathological hallmark of PD is an accumulation of misfolded α-synuclein aggregates within the brain. The etiology of PD and related synucleinopathy is poorly understood, but recently, the hypothesis that α-synuclein pathology spreads in a prion-like fashion originating in the gut has gained much scientific attention. A crucial clue was t

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Chen, Merry, та Danielle E. Mor. "Gut-to-Brain α-Synuclein Transmission in Parkinson’s Disease: Evidence for Prion-like Mechanisms". International Journal of Molecular Sciences 24, № 8 (2023): 7205. http://dx.doi.org/10.3390/ijms24087205.

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Parkinson’s disease (PD) is a multifactorial disorder involving both motor and non-motor symptoms caused by the progressive death of distinct neuronal populations, including dopaminergic neurons in the substantia nigra. The deposition of aggregated α-synuclein protein into Lewy body inclusions is a hallmark of the disorder, and α-synuclein pathology has been found in the enteric nervous system (ENS) of PD patients up to two decades prior to diagnosis. In combination with the high occurrence of gastrointestinal dysfunction in early stages of PD, current evidence strongly suggests that some form

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15

Chiesa, Roberto, Pedro Piccardo, Elena Quaglio, et al. "Molecular Distinction between Pathogenic and Infectious Properties of the Prion Protein." Journal of Virology 77, no. 13 (2003): 7611–22. http://dx.doi.org/10.1128/jvi.77.13.7611-7622.2003.

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ABSTRACT Tg(PG14) mice express a prion protein (PrP) with a nine-octapeptide insertion associated with a human familial prion disease. These animals spontaneously develop a fatal neurodegenerative disorder characterized by ataxia, neuronal apoptosis, and accumulation in the brain of an aggregated and weakly protease-resistant form of mutant PrP (designated PG14spon). Brain homogenates from Tg(PG14) mice fail to transmit disease after intracerebral inoculation into recipient mice, indicating that PG14spon, although pathogenic, is distinct from PrPSc, the infectious form of PrP. In contrast, ino

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Tarnacka, Beata, Anna Jopowicz, and Maria Maślińska. "Copper, Iron, and Manganese Toxicity in Neuropsychiatric Conditions." International Journal of Molecular Sciences 22, no. 15 (2021): 7820. http://dx.doi.org/10.3390/ijms22157820.

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Copper, manganese, and iron are vital elements required for the appropriate development and the general preservation of good health. Additionally, these essential metals play key roles in ensuring proper brain development and function. They also play vital roles in the central nervous system as significant cofactors for several enzymes, including the antioxidant enzyme superoxide dismutase (SOD) and other enzymes that take part in the creation and breakdown of neurotransmitters in the brain. An imbalance in the levels of these metals weakens the structural, regulatory, and catalytic roles of d

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Jones, David T., Ryan A. Townley, Jonathan Graff-Radford, et al. "Amyloid- and tau-PET imaging in a familial prion kindred." Neurology Genetics 4, no. 6 (2018): e290. http://dx.doi.org/10.1212/nxg.0000000000000290.

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ObjectiveTo study the in vivo binding properties of 18F-AV-1451 (tau-PET) and Pittsburgh compound B (PiB-PET) in a unique kindred with a familial prion disorder known to produce amyloid plaques composed of prion protein alongside Alzheimer disease (AD)–like tau tangles.MethodsA case series of 4 symptomatic family members with the 12-octapeptide repeat insertion in the PRNP gene were imaged with 3T MRI, PiB-PET, and tau-PET in their fourth decade of life.ResultsThere was significant neocortical uptake of the tau-PET tracer in all 4 familial prion cases. However, PiB-PET images did not demonstra

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18

Hennig, Sven, Geraldine Kong, Taro Mannen, et al. "Prion-like domains in RNA binding proteins are essential for building subnuclear paraspeckles." Journal of Cell Biology 210, no. 4 (2015): 529–39. http://dx.doi.org/10.1083/jcb.201504117.

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Prion-like domains (PLDs) are low complexity sequences found in RNA binding proteins associated with the neurodegenerative disorder amyotrophic lateral sclerosis. Recently, PLDs have been implicated in mediating gene regulation via liquid-phase transitions that drive ribonucleoprotein granule assembly. In this paper, we report many PLDs in proteins associated with paraspeckles, subnuclear bodies that form around long noncoding RNA. We mapped the interactome network of paraspeckle proteins, finding enrichment of PLDs. We show that one protein, RBM14, connects key paraspeckle subcomplexes via in

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19

Westermark, Per, and Gunilla T. Westermark. "Reflections on amyloidosis in Papua New Guinea." Philosophical Transactions of the Royal Society B: Biological Sciences 363, no. 1510 (2008): 3701–5. http://dx.doi.org/10.1098/rstb.2008.0073.

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The amyloidoses comprise a heterogeneous group of diseases in which 1 out of more than 25 human proteins aggregates into characteristic beta-sheet fibrils with some unique properties. Aggregation is nucleation dependent. Among the known amyloid-forming constituents is the prion protein, well known for its ability to transmit misfolding and disease from one individual to another. There is increasing evidence that other amyloid forms also may be transmissible but only if certain prerequisites are fulfilled. One of these forms is systemic AA-amyloidosis in which an acute-phase reactant, serum AA,

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20

Abhay, Kamble Nakul Kathar Gajanan Sanap. "Novel Drug Delivery System for Treating Neuropsychological Disorder." International Journal in Pharmaceutical Sciences 1, no. 12 (2023): 317–29. https://doi.org/10.5281/zenodo.10370141.

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One of the main health issues in the world today is acknowledged to be neurological diseases (NDs). The World Health Organisation (WHO) lists neurological illnesses as one of the leading causes of death globally. Alzheimer's disease, Parkinson's disease, Huntington's disease, frontotemporal dementia, amyotrophic lateral sclerosis, Prion disease, brain tumours, spinal cord injuries, and strokes are examples of neurological illnesses.  Since there are no particular treatments that can penetrate the blood-brain barrier (BBB) and significantly enter the brain to have a pharmacological effect,

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21

Harrison, Paul M. "Robust phylogenetic profile clustering for Saccharomyces cerevisiae proteins." PeerJ 13 (April 28, 2025): e19370. https://doi.org/10.7717/peerj.19370.

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Background Genes are continually formed and lost as a genome evolves. However, new genes may tend to appear during specific evolutionary epochs rather than others, or disappear together in a more recent organismal clade. Methods to identify gene origination might simply use the last common ancestor to contain an ortholog as the putative gene origination point, or use a heuristic threshold that allows for a certain amount of missing orthologs in the cohort of species examined. Here, to avoid such issues, an alternative approach based on the clustering of phylogenetic profiles is applied, and th

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Longhena, Francesca, Gaia Faustini, Cristina Missale, Marina Pizzi, PierFranco Spano та Arianna Bellucci. "The Contribution ofα-Synuclein Spreading to Parkinson’s Disease Synaptopathy". Neural Plasticity 2017 (2017): 1–15. http://dx.doi.org/10.1155/2017/5012129.

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Synaptopathies are diseases with synapse defects as shared pathogenic features, encompassing neurodegenerative disorders such as Parkinson’s disease (PD). In sporadic PD, the most common age-related neurodegenerative movement disorder, nigrostriatal dopaminergic deficits are responsible for the onset of motor symptoms that have been related toα-synuclein deposition at synaptic sites. Indeed,α-synuclein accumulation can impair synaptic dopamine release and induces the death of nigrostriatal neurons. While in physiological conditions the protein can interact with and modulate synaptic vesicle pr

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Chmielarz, Piotr, and Mart Saarma. "Neurotrophic factors for disease-modifying treatments of Parkinson's disease: gaps between basic science and clinical studies." Pharmacological Reports 72, no. 5 (2020): 1195–217. http://dx.doi.org/10.1007/s43440-020-00120-3.

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Abstract Background Neurotrophic factors are endogenous proteins promoting the survival of different neural cells. Therefore, they elicited great interest as a possible treatment for neurodegenerative disorders, including Parkinson’s Disease (PD). PD is the second most common neurodegenerative disorder, scientifically characterized more than 200 years ago and initially linked with motor abnormalities. Currently, the disease is viewed as a highly heterogeneous, progressive disorder with a long presymptomatic phase, and both motor and non-motor symptoms. Presently only symptomatic treatments for

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Tamaki, Yoshitaka, Jay P. Ross, Paria Alipour, et al. "Spinal cord extracts of amyotrophic lateral sclerosis spread TDP-43 pathology in cerebral organoids." PLOS Genetics 19, no. 2 (2023): e1010606. http://dx.doi.org/10.1371/journal.pgen.1010606.

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Amyotrophic lateral sclerosis (ALS) is a fatal neurodegenerative disorder caused by progressive loss of motor neurons and there is currently no effective therapy. Cytoplasmic mislocalization and aggregation of TAR DNA-binding protein 43 kDa (TDP-43) within the CNS is a pathological hallmark in sporadic ALS and prion-like propagation of pathogenic TDP-43 is thought to be implicated in disease progression. However, cell-to-cell transmission of pathogenic TDP-43 in the human CNS has not been confirmed experimentally. Here we used induced pluripotent stem cells (iPSCs)-derived cerebral organoids a

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Galbatsov, D. F., M. B. Borisenko, N. N. Soloviev, A. M. Emelin, and R. V. Deev. "Autopsy observations of sporadic Creutzfeldt-Jakob disease." CLINICAL AND EXPERIMENTAL MORPHOLOGY 14, no. 3 (2025): 80–85. https://doi.org/10.31088/cem2025.14.3.80-85.

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Introduction. Creutzfeldt-Jakob disease is a fatal neurodegenerative disorder caused by deposited prion protein in neurons, which is resistant to human cell proteases. This disease manifests as polymorphic neurological symptoms, progressive dementia, and impaired breathing and swallowing. The fatal outcome is observed within 6–12 months. Postmortem morphological examination reveals spongiform degeneration of brain tissue, neuronophagia, and amyloid-like protein conglomerates. This paper describescharacteristic changes identified on histological examination of brain tissue of a patient with Cre

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Bagnoli, Enrico, and Una FitzGerald. "Mitral cells and the glucagon-like peptide 1 receptor: The sweet smell of success?" European Journal of Neuroscience, May (August 3, 2018): 1–18. https://doi.org/10.1111/ejn.14115.

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The olfactory bulb (OB) is often affected at very early stages of neurodegenerative disorders, in the so-called 'prodromal' phase. In Parkinson's disease (PD), olfactory disturbances appear years before motor symptoms arise. Additionally, pathological alpha-synuclein aggregates are found in olfactory regions before spreading to other areas of the brain. Being positioned at the frontier between the brain and a potentially hostile environment, could explain the particular vulnerability of the OB. Mitral cells (MCs), the principal projecting neurons of the olfactory system, are involv

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Pintado-Grima, Carlos, Oriol Bárcenas, Andrea Bartolomé-Nafría, et al. "A Review of Fifteen Years Developing Computational Tools to Study Protein Aggregation." Biophysica 3, no. 1 (2023): 1–20. http://dx.doi.org/10.3390/biophysica3010001.

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The presence of insoluble protein deposits in tissues and organs is a hallmark of many human pathologies. In addition, the formation of protein aggregates is considered one of the main bottlenecks to producing protein-based therapeutics. Thus, there is a high interest in rationalizing and predicting protein aggregation. For almost two decades, our laboratory has been working to provide solutions for these needs. We have traditionally combined the core tenets of both bioinformatics and wet lab biophysics to develop algorithms and databases to study protein aggregation and its functional implica

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Zhu, Seng, Saïda Abounit, Carsten Korth, and Chiara Zurzolo. "Transfer of disrupted-in-schizophrenia 1 aggregates between neuronal-like cells occurs in tunnelling nanotubes and is promoted by dopamine." Open Biology 7, no. 3 (2017): 160328. http://dx.doi.org/10.1098/rsob.160328.

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The disrupted-in-schizophrenia 1 ( DISC1 ) gene was identified as a genetic risk factor for chronic mental illnesses (CMI) such as schizophrenia, bipolar disorder and severe recurrent depression. Insoluble aggregated DISC1 variants were found in the cingular cortex of sporadic, i.e. non-genetic, CMI patients. This suggests protein pathology as a novel, additional pathogenic mechanism, further corroborated in a recent transgenic rat model presenting DISC1 aggregates. Since the potential role of aggregation of DISC1 in sporadic CMI is unknown, we investigated whether DISC1 undergoes aggregation

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Biswas, Subhadip, and Davit A. Potoyan. "Decoding biomolecular condensate dynamics: an energy landscape approach." PLOS Computational Biology 21, no. 2 (2025): e1012826. https://doi.org/10.1371/journal.pcbi.1012826.

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Many eukaryotic proteins and RNAs contain low-complexity domains (LCDs) with a strong propensity for binding and driving phase separation into biomolecular condensates. Mutations in LCDs frequently disrupt condensate dynamics, resulting in pathological transitions to solid-like states. Understanding how the molecular sequence grammar of LCDs governs condensate dynamics is essential for uncovering their biological functions and the evolutionary forces that shape these sequences. To this end, we present an energy landscape framework that operates on a continuous ‘stickiness’ energy scale rather

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Meducator, The, Morgan Puusaari, and David Shen. "An Evaluation of a Novel Method for the Detection of Parkinson's Disease." Meducator 1, no. 45 (2025): 26–29. https://doi.org/10.15173/m.v1i45.3687.

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Parkinson’s Disease (PD) is a neurodegenerative disorder affecting millions of individuals worldwide. However, current diagnostic tools are limited to the clinical assessment of overt symptoms, after PD has already progressed into the clinical stage. A novel PD testing method, α-synuclein seed amplification assay (αsyn-SAA), may revolutionize the testing by allowing clinicians to detect PD before symptoms arise. The α-synuclein protein abundant in pre-synapse is typically involved in the release of dopamine. However, in the development of PD, αsyn proteins become misfolded and infect their pat

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Weiß, Alexander, Andreu Matamoros-Angles, Fanni Annamária Boros, Philipp Arnold, and Friederike Zunke. "Extracellular vesicles – upcoming biomarkers in Parkinson's disease's biofluids." Novel methods and insights: A profound look at the function of extracellular vesicles 4, no. 1 (2022): 45–51. http://dx.doi.org/10.47184/tev.2022.01.06.

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The search of a biomarker for an early detection of neurodegenerative diseases is one of the biggest challenges of our times. The second most common neurodegenerative disorder Parkinson's disease (PD) is characterized by misfolded alpha-synuclein (a-syn) aggregates within the central nervous system (CNS). Currently, definitive PD diagnosis still requires post-mortem brain examination. As a result, the misdiagnosis of PD based only on clinical symptoms and delayed diagnosis in advanced stages cannot be excluded. Since a-syn aggregates abnormally, it might be an interesting candidate for a bioma

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Bhopatkar, Anukool A., Vladimir N. Uversky, and Vijayaraghavan Rangachari. "Granulins modulate liquid–liquid phase separation and aggregation of the prion-like C-terminal domain of the neurodegeneration-associated protein TDP-43." Journal of Biological Chemistry 295, no. 8 (2020): 2506–19. http://dx.doi.org/10.1074/jbc.ra119.011501.

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TAR DNA-binding protein 43 (TDP-43) has emerged as a key player in many neurodegenerative pathologies, including frontotemporal lobar degeneration (FTLD) and amyotrophic lateral sclerosis (ALS). Hallmarks of both FTLD and ALS are the toxic cytoplasmic inclusions of the prion-like C-terminal fragments of TDP-43 CTD (TDP-43 C-terminal domain), formed upon proteolytic cleavage of full-length TDP-43 in the nucleus and subsequent transport to the cytoplasm. Both full-length TDP-43 and its CTD are also known to form stress granules by coacervating with RNA in the cytoplasm during stress and may be i

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Cuevas, Eva P., Alberto Rodríguez-Fernández, Valle Palomo, Ana Martínez, and Ángeles Martín-Requero. "TDP-43 Pathology and Prionic Behavior in Human Cellular Models of Alzheimer’s Disease Patients." Biomedicines 10, no. 2 (2022): 385. http://dx.doi.org/10.3390/biomedicines10020385.

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Alzheimer’s disease (AD) is a neurodegenerative disorder for which there is currently no effective treatment. Despite advances in the molecular pathology of the characteristic histopathological markers of the disease (tau protein and β-amyloid), their translation to the clinic has not provided the expected results. Increasing evidences have demonstrated the presence of aggregates of TDP-43 (TAR DNA binding protein 43) in the postmortem brains of patients diagnosed with AD. The present research is focused on of the study of the pathological role of TDP-43 in AD. For this purpose, immortalized l

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Perna, Alessia, Massimo Santoro, and Elisa Colaizzo. "Understanding the Best Nutritional Management for Creutzfeldt–Jakob Disease Patients: A Comparison Between East Asian and Western Experiences." Life 14, no. 11 (2024): 1496. http://dx.doi.org/10.3390/life14111496.

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(1) Background: Creutzfeldt–Jakob disease (CJD) is a rare and fatal neurodegenerative disorder caused by the accumulation of an altered prion protein, which usually leads to death within one year after clinical onset. CJD patients usually present with rapid cognitive impairment associated with declines in cerebellar, motor, visual, behavioral, and swallowing functions. Moreover, CJD patients lose their ability to eat and take medications orally very early on in treatment; nevertheless, there are no specific nutritional guidelines for this disease shared worldwide. (2) Methods: This review aims

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Angot, Elodie, Jennifer A. Steiner, Christian Hansen, Jia-Yi Li, and Patrik Brundin. "Are synucleinopathies prion-like disorders?" Lancet Neurology 9, no. 11 (2010): 1128–38. http://dx.doi.org/10.1016/s1474-4422(10)70213-1.

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Chapman, A. H., and Djalma Vieira e. Silva. "Creutzfeldt-Jakob disease a case report, with special attention to the electroencephalogram in this disorder and to its possible relationships to kuru, scrapie and «mad cow disease»." Arquivos de Neuro-Psiquiatria 51, no. 2 (1993): 258–66. http://dx.doi.org/10.1590/s0004-282x1993000200020.

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A case of Creutzfeldt-Jakob disease in a 58-year-old Brazillian cattle rancher and businessman is presented. The EEG was normal, which is consistent with the fact that it was made during the first half of his illness; in a later stage suppression of normal rhythms by slow moderate voltage waves would be expected. The resemblances of kuru, scrapie and "mad cow disease» to C-J disease are discussed. In each of these 4 illnesses the patient or affected animal (scrapie and «mad cow disease") (a) has a widespread spongiform encephalopathy and consequent dementia, myoclonic epilepsy and cerebellar a

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Cherry, Pearl, and Sabine Gilch. "The Role of Vesicle Trafficking Defects in the Pathogenesis of Prion and Prion-Like Disorders." International Journal of Molecular Sciences 21, no. 19 (2020): 7016. http://dx.doi.org/10.3390/ijms21197016.

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Prion diseases are fatal and transmissible neurodegenerative diseases in which the cellular form of the prion protein ‘PrPc’, misfolds into an infectious and aggregation prone isoform termed PrPSc, which is the primary component of prions. Many neurodegenerative diseases, like Alzheimer’s disease, Parkinson’s disease, and polyglutamine diseases, such as Huntington’s disease, are considered prion-like disorders because of the common characteristics in the propagation and spreading of misfolded proteins that they share with the prion diseases. Unlike prion diseases, these are non-infectious outs

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Ali, Addison, Kristeen Pareja, and Tara Tracy. "Acetylation of Tau Induces Alzheimer's Disease-Associated Tau in Transgenic Mice." Innovation in Aging 5, Supplement_1 (2021): 958. http://dx.doi.org/10.1093/geroni/igab046.3457.

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Abstract Alzheimer’s disease (AD) is a neurodegenerative disorder that is characterized by neurofibrillary tangles (NFTs) and amyloid beta plaques. These NFTs are made up of aggregated tau proteins. Tau is involved in stabilizing microtubules and does not usually display aggregation. Acetylation of tau protein causes an increase in tau aggregation but its role in AD progression is still not well understood. I hypothesized that enhanced acetylated tau results in an increase in AD-like tau pathology. To test this, a murine prion promoter-tauKQ transgene was injected into the mouse fertilized ooc

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Wilson, Rona, Declan King, Nora Hunter, Wilfred Goldmann, and Rona M. Barron. "Characterization of an unusual transmissible spongiform encephalopathy in goat by transmission in knock-in transgenic mice." Journal of General Virology 94, no. 8 (2013): 1922–32. http://dx.doi.org/10.1099/vir.0.051706-0.

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Bovine spongiform encephalopathy (BSE) is a fatal neurodegenerative disorder of cattle, and its transmission to humans through contaminated food is thought to be the cause of the variant form of Creutzfeldt–Jakob disease. BSE is believed to have spread from the recycling in cattle of ruminant tissue in meat and bone meal (MBM). However, during this time, sheep and goats were also exposed to BSE-contaminated MBM. Both sheep and goats are experimentally susceptible to BSE, and while there have been no reported natural BSE cases in sheep, two goat BSE field cases have been documented. While cases

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Pineau, Hailey, and Valerie Sim. "POSCAbilities: The Application of the Prion Organotypic Slice Culture Assay to Neurodegenerative Disease Research." Biomolecules 10, no. 7 (2020): 1079. http://dx.doi.org/10.3390/biom10071079.

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Prion diseases are fatal, transmissible neurodegenerative disorders whose pathogenesis is driven by the misfolding, self-templating and cell-to-cell spread of the prion protein. Other neurodegenerative diseases such as Alzheimer’s disease, Parkinson’s disease, amyotrophic lateral sclerosis and Huntington’s disease, share some of these prion-like features, with different aggregation-prone proteins. Consequently, researchers have begun to apply prion-specific techniques, like the prion organotypic slice culture assay (POSCA), to these disorders. In this review we explore the ways in which the pr

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Heng, Yang, Yan-Yan Li, Lu Wen, Jia-Qing Yan, Nai-Hong Chen, and Yu-He Yuan. "Gastric Enteric Glial Cells: A New Contributor to the Synucleinopathies in the MPTP-Induced Parkinsonism Mouse." Molecules 27, no. 21 (2022): 7414. http://dx.doi.org/10.3390/molecules27217414.

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Accumulating evidence has shown that Parkinson’s disease (PD) is a systemic disease other than a mere central nervous system (CNS) disorder. One of the most important peripheral symptoms is gastrointestinal dysfunction. The enteric nervous system (ENS) is regarded as an essential gateway to the environment. The discovery of the prion-like behavior of α-synuclein makes it possible for the neurodegenerative process to start in the ENS and spread via the gut-brain axis to the CNS. We first confirmed that synucleinopathies existed in the stomachs of chronic 1-methyl-4-phenyl-1,2,3,6-tetrahydropyri

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González-Sánchez, María, María Jesús Ramírez-Expósito, and José Manuel Martínez-Martos. "Pathophysiology, Clinical Heterogeneity, and Therapeutic Advances in Amyotrophic Lateral Sclerosis: A Comprehensive Review of Molecular Mechanisms, Diagnostic Challenges, and Multidisciplinary Management Strategies." Life 15, no. 4 (2025): 647. https://doi.org/10.3390/life15040647.

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Amyotrophic lateral sclerosis (ALS) is a progressive neurodegenerative disorder characterized by the progressive degeneration of upper and lower motor neurons, leading to muscle atrophy, paralysis, and respiratory failure. This comprehensive review synthesizes the current knowledge on ALS pathophysiology, clinical heterogeneity, diagnostic frameworks, and evolving therapeutic strategies. Mechanistically, ALS arises from complex interactions between genetic mutations (e.g., in C9orf72, SOD1, TARDBP (TDP-43), and FUS) and dysregulated cellular pathways, including impaired RNA metabolism, protein

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Sarnataro, Daniela. "Attempt to Untangle the Prion-Like Misfolding Mechanism for Neurodegenerative Diseases." International Journal of Molecular Sciences 19, no. 10 (2018): 3081. http://dx.doi.org/10.3390/ijms19103081.

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The misfolding and aggregation of proteins is the neuropathological hallmark for numerous diseases including Alzheimer’s disease, Parkinson’s disease, and prion diseases. It is believed that misfolded and abnormal β-sheets forms of wild-type proteins are the vectors of these diseases by acting as seeds for the aggregation of endogenous proteins. Cellular prion protein (PrPC) is a glycosyl-phosphatidyl-inositol (GPI) anchored glycoprotein that is able to misfold to a pathogenic isoform PrPSc, the causative agent of prion diseases which present as sporadic, dominantly inherited and transmissible

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Acquatella-Tran Van Ba, Isabelle, Thibaut Imberdis, and Véronique Perrier. "From Prion Diseases to Prion-Like Propagation Mechanisms of Neurodegenerative Diseases." International Journal of Cell Biology 2013 (2013): 1–8. http://dx.doi.org/10.1155/2013/975832.

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Prion diseases are fatal neurodegenerative sporadic, inherited, or acquired disorders. In humans, Creutzfeldt-Jakob disease is the most studied prion disease. In animals, the most frequent prion diseases are scrapie in sheep and goat, bovine spongiform encephalopathy in cattle, and the emerging chronic wasting disease in wild and captive deer in North America. The hallmark of prion diseases is the deposition in the brain of PrPSc, an abnormalβ-sheet-rich form of the cellular prion protein (PrPC) (Prusiner 1982). According to the prion hypothesis, PrPSccan trigger the autocatalytic conversion o

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Peggion, Caterina, Maria Sorgato, and Alessandro Bertoli. "Prions and Prion-Like Pathogens in Neurodegenerative Disorders." Pathogens 3, no. 1 (2014): 149–63. http://dx.doi.org/10.3390/pathogens3010149.

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Mastrianni, James A. "The Prion Diseases: Creutzfeldt-Jakob, Gerstmann-Sträussler-Scheinker, and Related Disorders." Journal of Geriatric Psychiatry and Neurology 11, no. 2 (1998): 78–97. http://dx.doi.org/10.1177/089198879801100206.

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The prion diseases are an interesting group of neurodegenerative disorders for a variety of reasons. The most obvious is their property of transmissibility, but beyond that they constitute a fascinating example of the diversity of disease expression possible from a common etiologic factor. Thought of as “strains” in animals and phenotypes in humans, these varied expressions of prion disease are most likely due to subtle conformational changes in the pathogenic form of the prion protein. These strain-like characteristics are best exemplified in the genetic varieties of human prion disease in wh

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Contiliani, Danyel Fernandes, Yasmin de Araújo Ribeiro, Vitor Nolasco de Moraes, and Tiago Campos Pereira. "MicroRNAs in Prion Diseases—From Molecular Mechanisms to Insights in Translational Medicine." Cells 10, no. 7 (2021): 1620. http://dx.doi.org/10.3390/cells10071620.

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MicroRNAs (miRNAs) are small non-coding RNA molecules able to post-transcriptionally regulate gene expression via base-pairing with partially complementary sequences of target transcripts. Prion diseases comprise a singular group of neurodegenerative conditions caused by endogenous, misfolded pathogenic (prion) proteins, associated with molecular aggregates. In humans, classical prion diseases include Creutzfeldt–Jakob disease, fatal familial insomnia, Gerstmann–Sträussler–Scheinker syndrome, and kuru. The aim of this review is to present the connections between miRNAs and prions, exploring ho

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Costanzo, Maddalena, and Chiara Zurzolo. "The cell biology of prion-like spread of protein aggregates: mechanisms and implication in neurodegeneration." Biochemical Journal 452, no. 1 (2013): 1–17. http://dx.doi.org/10.1042/bj20121898.

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The misfolding and aggregation of specific proteins is a common hallmark of many neurodegenerative disorders, including highly prevalent illnesses such as Alzheimer's and Parkinson's diseases, as well as rarer disorders such as Huntington's and prion diseases. Among these, only prion diseases are ‘infectious’. By seeding misfolding of the PrPC (normal conformer prion protein) into PrPSc (abnormal disease-specific conformation of prion protein), prions spread from the periphery of the body to the central nervous system and can also be transmitted between individuals of the same or different spe

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Scialò, Carlo, Elena De Cecco, Paolo Manganotti, and Giuseppe Legname. "Prion and Prion-Like Protein Strains: Deciphering the Molecular Basis of Heterogeneity in Neurodegeneration." Viruses 11, no. 3 (2019): 261. http://dx.doi.org/10.3390/v11030261.

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Increasing evidence suggests that neurodegenerative disorders share a common pathogenic feature: the presence of deposits of misfolded proteins with altered physicochemical properties in the Central Nervous System. Despite a lack of infectivity, experimental data show that the replication and propagation of neurodegenerative disease-related proteins including amyloid-β (Aβ), tau, α-synuclein and the transactive response DNA-binding protein of 43 kDa (TDP-43) share a similar pathological mechanism with prions. These observations have led to the terminology of “prion-like” to distinguish between

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Herva, Maria Eugenia, and Maria Grazia Spillantini. "Parkinson's disease as a member of Prion-like disorders." Virus Research 207 (September 2015): 38–46. http://dx.doi.org/10.1016/j.virusres.2014.10.016.

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