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Relevant bibliographies by topics / Prion-like disorder

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Academic literature on the topic 'Prion-like disorder'

Author: Grafiati

Published: 11 March 2023

Last updated: 31 July 2025

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Journal articles on the topic "Prion-like disorder"

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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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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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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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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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Dissertations / Theses on the topic "Prion-like disorder"

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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 th

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Books on the topic "Prion-like disorder"

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Cummings, Jeffrey L., and 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 asy

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Book chapters on the topic "Prion-like disorder"

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

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Ross, Eric D., and Sean M. Cascarina. "The roles of prion-like domains in amyloid formation, phase separation, and solubility." In Structure and Intrinsic Disorder in Enzymology. 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." In Mayo Clinic Neurology Board Review, edited by Kelly D. Flemming. 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 orga

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Rundo, Jessica Vensel, Hillor Mehta, and Reena Mehra. "Dying to Fall Asleep." In Sleep Disorders. 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 c

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

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Kamper, Joel E., Emily N. VanDerBleek, and Erin K. Bailey. "Rare and Rapidly Progressive Dementias." In Dementia, edited by Robin C. Hilsabeck and Gayle Y. Ayers. Oxford University PressNew York, 2024. http://dx.doi.org/10.1093/med/9780197690024.003.0013.

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Abstract Aging is a risk factor for acquired neurocognitive dysfunction, with older adults at a relatively higher risk of developing delirium, dementia, and other common syndromes. While knowledge of high-base rate etiologies like Alzheimer’s disease is certainly critical, practitioners working with older adults should also have familiarity with a number of rare and rapidly progressing neurobehavioral syndromes. This chapter highlights the clinical presentation, management, and prognosis of several of these disease processes. These include prion diseases, neuroinvasive infections and their seq

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Pandey, Mukesh, Jahangir Nabi, Nahida Tabassum, Faheem Hyder Pottoo, Renuka Khatik, and Niyaz Ahmad. "Molecular Chaperones in Neurodegeneration." In Quality Control of Cellular Protein in Neurodegenerative Disorders. 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), Pa

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Mamun, Abdullah Al, and Md Farhad Hossain. "Post-Translational Modifications in Neurodegeneration." In Quality Control of Cellular Protein in Neurodegenerative Disorders. 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 sp

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Biney, Robert Peter, Thabisile Mpofana, and Ella Anle Kasanga. "Free Radicals in Oxidative Stress, Aging, and Neurodegenerative Disorders." In Advances in Medical Diagnosis, Treatment, and Care. 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. Di

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

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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. Di

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