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Academic literature on the topic 'Prions'

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Published: 4 June 2021
Last updated: 14 March 2023

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Journal articles on the topic "Prions"

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Bostock, Chris. "Prions prions prions." Virus Research 48, no. 1 (April 1997): 107–8. http://dx.doi.org/10.1016/s0168-1702(96)01414-1.

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Livingston, K. "More on Prions: Prions Prions Prions." Science 273, no. 5278 (August 23, 1996): 1053a. http://dx.doi.org/10.1126/science.273.5278.1053a.

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Obi, R. K., and F. C. Nwanebu. "Prions And Prion Diseases." African Journal of Clinical and Experimental Microbiology 9, no. 1 (January 14, 2008): 38. http://dx.doi.org/10.4314/ajcem.v9i1.7481.

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Beekes, Michael. "Prions and prion diseases." FEBS Journal 274, no. 3 (January 8, 2007): 575. http://dx.doi.org/10.1111/j.1742-4658.2006.05629.x.

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Wickner, R. B., K. L. Taylor, H. K. Edskes, and M.-L. Maddelein. "Prions: Portable prion domains." Current Biology 10, no. 9 (May 2000): R335—R337. http://dx.doi.org/10.1016/s0960-9822(00)00460-7.

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Nixon, Randal R. "Prions and Prion Diseases." Laboratory Medicine 30, no. 5 (May 1, 1999): 335–38. http://dx.doi.org/10.1093/labmed/30.5.335.

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Bian, Jifeng, Vadim Khaychuk, Rachel C. Angers, Natalia Fernández-Borges, Enric Vidal, Crystal Meyerett-Reid, Sehun Kim, et al. "Prion replication without host adaptation during interspecies transmissions." Proceedings of the National Academy of Sciences 114, no. 5 (January 17, 2017): 1141–46. http://dx.doi.org/10.1073/pnas.1611891114.

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Adaptation of prions to new species is thought to reflect the capacity of the host-encoded cellular form of the prion protein (PrPC) to selectively propagate optimized prion conformations from larger ensembles generated in the species of origin. Here we describe an alternate replicative process, termed nonadaptive prion amplification (NAPA), in which dominant conformers bypass this requirement during particular interspecies transmissions. To model susceptibility of horses to prions, we produced transgenic (Tg) mice expressing cognate PrPC. Although disease transmission to only a subset of infected TgEq indicated a significant barrier to EqPrPCconversion, the resulting horse prions unexpectedly failed to cause disease upon further passage to TgEq. TgD expressing deer PrPCwas similarly refractory to deer prions from diseased TgD infected with mink prions. In both cases, the resulting prions transmitted to mice expressing PrPCfrom the species of prion origin, demonstrating that transmission barrier eradication of the originating prions was ephemeral and adaptation superficial in TgEq and TgD. Horse prions produced in vitro by protein misfolding cyclic amplification of mouse prions using horse PrPCalso failed to infect TgEq but retained tropism for wild-type mice. Concordant patterns of neuropathology and prion deposition in susceptible mice infected with NAPA prions and the corresponding prion of origin confirmed preservation of strain properties. The comparable responses of both prion types to guanidine hydrochloride denaturation indicated this occurs because NAPA precludes selection of novel prion conformations. Our findings provide insights into mechanisms regulating interspecies prion transmission and a framework to reconcile puzzling epidemiological features of certain prion disorders.
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Watts, Joel C., Kurt Giles, Daniel J. Saltzberg, Brittany N. Dugger, Smita Patel, Abby Oehler, Sumita Bhardwaj, Andrej Sali, and Stanley B. Prusiner. "Guinea Pig Prion Protein Supports Rapid Propagation of Bovine Spongiform Encephalopathy and Variant Creutzfeldt-Jakob Disease Prions." Journal of Virology 90, no. 21 (July 20, 2016): 9558–69. http://dx.doi.org/10.1128/jvi.01106-16.

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ABSTRACTThe biochemical and neuropathological properties of bovine spongiform encephalopathy (BSE) and variant Creutzfeldt-Jakob disease (vCJD) prions are faithfully maintained upon transmission to guinea pigs. However, primary and secondary transmissions of BSE and vCJD in guinea pigs result in long incubation periods of ∼450 and ∼350 days, respectively. To determine if the incubation periods of BSE and vCJD prions could be shortened, we generated transgenic (Tg) mice expressing guinea pig prion protein (GPPrP). Inoculation of Tg(GPPrP) mice with BSE and vCJD prions resulted in mean incubation periods of 210 and 199 days, respectively, which shortened to 137 and 122 days upon serial transmission. In contrast, three different isolates of sporadic CJD prions failed to transmit disease to Tg(GPPrP) mice. Many of the strain-specified biochemical and neuropathological properties of BSE and vCJD prions, including the presence of type 2 protease-resistant PrPSc, were preserved upon propagation in Tg(GPPrP) mice. Structural modeling revealed that two residues near the N-terminal region of α-helix 1 in GPPrP might mediate its susceptibility to BSE and vCJD prions. Our results demonstrate that expression of GPPrP in Tg mice supports the rapid propagation of BSE and vCJD prions and suggest that Tg(GPPrP) mice may serve as a useful paradigm for bioassaying these prion isolates.IMPORTANCEVariant Creutzfeldt-Jakob disease (vCJD) and bovine spongiform encephalopathy (BSE) prions are two of the prion strains most relevant to human health. However, propagating these strains in mice expressing human or bovine prion protein has been difficult because of prolonged incubation periods or inefficient transmission. Here, we show that transgenic mice expressing guinea pig prion protein are fully susceptible to vCJD and BSE prions but not to sporadic CJD prions. Our results suggest that the guinea pig prion protein is a better, more rapid substrate than either bovine or human prion protein for propagating BSE and vCJD prions.
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Gambetti, P. "Approaches to Prions: Prion Diseases." Science 273, no. 5278 (August 23, 1996): 1052b—1053b. http://dx.doi.org/10.1126/science.273.5278.1052b.

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Stahl, Neil, and Stanley B. Prusiner. "Prions and prion proteins 1." FASEB Journal 5, no. 13 (October 1991): 2799–807. http://dx.doi.org/10.1096/fasebj.5.13.1916104.

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Dissertations / Theses on the topic "Prions"

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Sang, Chieh. "Single molecule fluorescence studies of prions and prion-like proteins." Thesis, University of Cambridge, 2019. https://www.repository.cam.ac.uk/handle/1810/287929.

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Prions are infectious agents that cause fatal neurodegenerative diseases in the brain. The wide-accepted protein-only hypothesis states that the misfolded form of prion protein (PrP) is the sole constituent of prions, and the self-propagating process of PrP is considered to play a central role in prion pathogenesis. Prions are believed to propagate when a PrP assembly enters a cell and replicates to produce two or more fibrils, leading to an exponential increase in PrP aggregate number with time. However, the molecular basis of this process has not yet been established in detail. This prion-like replication is also suggested to be the mechanism in the development of other notorious neurodegenerative disorders, such as Alzheimer's and Parkinson's disease. In this thesis, I use single-aggregate imaging to study fibril fragmentation and elongation of individual murine PrP aggregates from seeded aggregation in vitro. From fluorescence imaging of individual PrP aggregates on the coverslip surface, elongation and fragmentation of the PrP assemblies have been directly observed. PrP elongation occurs via a structural conversion from a proteinase K (PK)-sensitive to PK-resistant conformer. Fibril fragmentation was found to be length-dependent and resulted in the formation of PK-sensitive fragments. To gain more insights into the mechanism of the spread of PrP, the quantified kinetic profiles allows the determination of the rate constants for these processes through the use of kinetic modelling. This enables the estimation of a simple framework for aggregate propagation through the brain, assuming that doubling of the aggregate number is rate-limiting. In contrast, the same method was applied to measurement for α-Synuclein (αS) aggregation, which has been suggested to be prion-like and is associated with Parkinson's disease. While αS aggregated by the same mechanism, it showed significantly slower elongation and fragmentation rate constants than PrP, leading to much slower replication rate. Furthermore, the measurements in αS aggregation has been extended to the cellular environment, I use super-resolution imaging to study the amplification of endogenous αS aggregation in cells and the transcellular spread of αS. Endogenous αS showed a clear amplification in number of aggregates with time after seed transduction, and the newly-formed αS aggregates are likely to spread through cell-to-cell transmission. The proteasome was demonstrated to possess a novel disaggregase function for αS fibrils and thus produce more seeds for further replication. It partially explains that αS aggregation in cells was found to replicate at a substantially faster rate than that in vitro. Determining the nature of the oligomers formed during aggregation has been experimentally difficult due to the lack of suitable methods capable of detecting and characterising the low level of oligomers. To address this problem, I have studied the early formation of PrP oligomers formed during aggregation in vitro using various single-molecule methods. The early aggregation of PrP is observed to form a thioflavin T (ThT)-inactive and two ThT-active species of oligomers, which differ in size and temporal evolution. The ThT-active oligomers undergo a structural conversion from a PK-sensitive to PK-resistant conformer, while a fraction of which grow into mature fibrils. These results also enable the establishment of a kinetic framework for elucidating temporal evolution of PrP aggregation and the relationship between oligomers and fibrils. Overall, my research identifies fibril elongation with fragmentation are the key molecular processes leading to PrP and αS aggregate replication, an important concept in prion biology, and provides a simple framework to estimate the rate of prion and prion-like spreading in animals. The results also show that a diverse range of oligomers is formed and co-exist during PrP aggregation which differ both in their structure and properties and provides mechanistic insights into a prion aggregation. The work provides a new quantitative approach to describe the prion-like property in neurodegenerative diseases from a kinetic perspective that can be verified in extending studies in other proteins or in cells.
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Apodaca, Jennifer J. "Regulation of prion protein in yeast and mammalian cells via ubiquitin mediated degradation a dissertation /." San Antonio : UTHSC, 2008. http://proquest.umi.com.libproxy.uthscsa.edu/pqdweb?did=1594496391&sid=6&Fmt=2&clientId=70986&RQT=309&VName=PQD.

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Urrea, Zazurca Laura. "Funciones de la proteína priónica celular, alfa-sinucleína y reelina en enfermedades neurodegenerativas." Doctoral thesis, Universitat de Barcelona, 2018. http://hdl.handle.net/10803/482168.

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Las enfermedades neurodegenerativas son una serie de trastornos del sistema nervioso caracterizadas por la pérdida de grupos neuronales específicos y por la presencia de cuerpos de inclusión proteicos, entre ellas las más frecuentes son la enfermedad de Alzheimer y la enfermedad de Parkinson, ambas asociadas a la edad. Su etiología, en la mayoría de los casos, aún se desconoce y su manifestación clínica es progresiva y crónica. La enfermedad de Parkinson se caracteriza por la pérdida de neuronas dopaminérgicas de la sustancia nigra pars compacta y por la presencia de agregados intracitoplasmáticos, denominados cuerpos de Lewy (LB). Se ha identificado la α-sinucleína como el principal componente de los LB, su forma desplegada está involucrada en el proceso patológico de la EP. La α-sinucleína desplegada, se agrega para formar protofibrillas que finalmente darán lugar a los LB. La acumulación intracelular de proteínas anormales da lugar al concepto de proteinopatías. Se cree que estas proteínas anómalas son capaces de propagarse entre células. Varios mecanismos moleculares se han propuesto para la transmisión de α-sinucleína, en este caso estudiamos la proteína priónica celular (PrPc) como posible receptor de α-sinucleína. PrPc es conocida por su participación en las enfermedades priónicas en su forma patológica, llamada PrPsc. Esta forma PrPsc se agrega y forma placas en el cerebro. Se ha demostrado que la PrPc es capaz de unirse a péptidos amiloides como los oligómeros β-amiloides que se encuentran en la enfermedad de Alzheimer. En esta tesis estudiamos el transporte de α-sinucleína según la dosis genética de PrPc. Después de realizar inoculaciones intracraneales con protofibrillas de α-sinucleína en animales con distintas dosis génica de PrPc, se observa que los animales sobreexpresantes de la PrPc presentan más agregados de α-sinucleína fosforilada que los animales deficientes de PrPc. Además, también identificamos la región de unión entre PrPc y α-sinucleína. Gracias a las construcciones delecionadas de PrPc detectamos que la región del dominio central cargada es esencial para la unión con α-sinucleína. Además, en esta tesis hemos analizado los niveles de Reelina en distintas enfermedades neurodegenerativas. Reelina es una proteína secretable implicada en el neurodesarrollo. En el adulto, Reelina está involucrada en la plasticidad sináptica, aprendizaje y memoria. Se ha detectado que niveles bajos de Reelina da lugar a fallos en la sinapsis y neurodegeneración. Anteriormente, los niveles de Reelina se han analizado en muestras humanas, sobretodo, en la enfermedad de Alzheimer dando lugar a resultados contradictorios. En el presente estudio, determinamos los cambios del mRNA y proteicos de Reelina en la enfermedad de Alzheimer, la demencia por cuerpos de Lewy, la enfermedad de Parkinson y en la enfermedad Creutzfeldt-Jakob (CJD) esporádica. Mientras los niveles proteicos de Reelina descienden en la enfermedad de Alzheimer y en la demencia por cuerpos de Lewy, en la enfermedad de Parkinson se mantienen. Por otro lado, detectamos que los niveles de Reelina en CJD aumentan, sobretodo en los casos tipo 1. Animales sobreexpresantes de PrPc humana inoculados con extracto cerebral de CJD también presentan un aumento de sus niveles de Reelina. In vitro, se observa que la expresión de Reelina aumenta en presencia del prion sintético que imita la secuencia central de la PrPc humana. Además, el aumento de Reelina es dependiente de las especies reactivas de oxígeno (ROS), mediante el uso de inhibidores de ROS detectamos como los niveles de Reelina se mantienen.
Many neurodegenerative diseases are characterized by the loss of neurons and intracellular accumulation of abnormal proteins, with the formation of inclusion bodies. Parkinson’s disease (PD) is the second most common form of neurodegenerative diseases. PD shows an abnormal accumulation of α-synuclein aggregates in neurons, called Lewy bodies (LB). Several groups have reported that abnormal form of α-synuclein can propagate through the cells and, consequently, form inclusions. Thus, it has been suggested different molecular mechanisms involved in α-synuclein propagation. It has been reported that cellular prion protein (PrPc) is a receptor of β-amyloid. In this study, we analyse whether the PrPc is a receptor for α-synuclein. Animals with different PrPc expression were intracranially injected with α-synuclein protofibrils. We observe that PrPc expression is not mandatory for α-synuclein propagation, but PrPc-overexpressing mice show more aggregates than in PrPc absence. Moreover, charge cluster domain of PrPc is essential for α-synuclein binding. In addition, we study Reelin levels in different neurodegenerative diseases. Reelin is a glycoprotein that is crucial for the correct cytoarchitectonic organization of the developing Central Nervous System. Decreased levels of Reelin lead to synaptic dysfunction or neurodegeneration. In the present study, we analyse the changes in Reelin and Reln mRNA in Alzheimer’s disease, Dementia with Lewy Bodies (DLB), Parkinson´s disease (PD) and sporadic Creutzfeldt-Jakob disease (sCJD). Meanwhile, inmunoblot results indicate decreased levels of Reelin in AD and DLB, PD do not show changes. In contrast, it has been detected an increase in sCJD(I). Reelin increased levels depends on reactive oxygen species (ROS). Using inhibitors of ROS production, as DPI and NAC, Reelin levels are maintained.
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Peoc'h, Katell. "La protéine << prion-like >> Doppel humaine : caractérisation et relation avec la protéine prion." Paris 5, 2003. http://www.theses.fr/2003PA05N096.

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Les prions sont des agents infectieux constitués de Prp sc isoforme modifiée de la protéine prion (PrP c), codée par PRNP. La protéine Doppel (Dpl) est codée par le gène PRND adjacent à PNRP. Quatre polymorphismes de PRND sont observés chez l'homme ; aucun n'influence la suceptibilité aux maladies à prions. L'expression de prnd reste inchangée après infection. La surexpression de Dpl ne module pas l'accumulation de PrPsc et l'expression cérébrale de Dpl n'est pas modifiée chez des patients atteints de maladie de Creutzfeld-Jakob. Dpl est retrouvée dans les cellules de Sertoli, le liquide séminal et sur la flagelle des spermatozoides.
Prion are infectious agents accumulating in the central nervous system, constituted of PrPsc the modified isoform of the prion protein (PrPc), encoded by the PRNP gene. The Doppel protein (Dpl) is encoded by the PRND gene nearby PRNP. Four Polymorphisms of PRND are observed in human ; none of them modify the susceptibility to prion diseases. Prnd expression remains unchanged after infection in neuroblastoma cells. Dpl surexpression do not change the PrPsc accumulation in these cells and the cerebral accumulation of Dpl is not modified in patients with Cretzfeld-Jakob disease. Dpl in humans is so expressed both on germinal and somatic cells in the male genital tract, suggesting its implication in fertility. Sperm cells could make a good tool to investigate the interaction between Dpl and PrP wich are both. .
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Peyrin, Jean-Michel. "Implication des cellules microgliales dans la neuropathologie des maladies à prions." Paris 5, 1998. http://www.theses.fr/1998PA05P226.

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Bariar, Bhawana. "Effects of the components of the Get pathway on prion propagation." Thesis, Atlanta, Ga. : Georgia Institute of Technology, 2007. http://hdl.handle.net/1853/26659.

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Thesis (M. S.)--Biology, Georgia Institute of Technology, 2008.
Committee Chair: Chernoff,Yury; Committee Member: Cairney,John; Committee Member: Choi,Jung; Committee Member: Doyle,Donald; Committee Member: Lobachev,Kirill. Part of the SMARTech Electronic Thesis and Dissertation Collection.
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Bamia, Aline. "Identification de nouvelles molécules anti-prions et caractérisation de leurs modes d'action." Thesis, Brest, 2019. http://www.theses.fr/2019BRES0047.

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Le prion est un agent pathogène infectieux de nature protéique responsable de maladies neurodégénératives à la fois chez l’homme et les animaux. Le prion est responsable de la tremblante chez le mouton et la chèvre et de la maladie de Creutzfeldt-Jakob chez l’homme. Les maladies à prions sont fatales et il n’existe aucun traitement efficace de nos jours. C’est la raison pour laquelle dans mon laboratoire nous nous intéressons à l’identification de nouvelles molécules antiprions.La flunarizine a été identifiée comme étant active contre les prions [PSI+] et [URE3] de levure et contre PrPSc de mammifères in vitro, ex vivo et in vivo. L’efficacité de la flunarizine contre les prions sur tous ces modèles fait d’elle une bonne molécule candidate contre les maladies à prions. Une étude des relations structure-activité (RSA) autour de la flunarizine a été effectuée sur 47, dont 31 étaient actives contre PrPSc in vitro.Une étude des relations structure-activité (RSA) autour de la flunarizine a été effectuée sur 47, dont 31 étaient actives contre PrPSc in vitro. Six des molécules les plus actives en culture organotypique ont aussi montré leur efficacité contre PrPSc. L’effet de la flunarizine et de ses analogues contre le prion PrPSc ne dépendait pas de leurs modes d’actions connus.Les molécules les plus actives contre PrPSc inhibent la PFAR (protein folding activity of ribosome) une activité chaperon de protéines qui est impliquée dans la propagation du prion de levure [PSI+]. L’efficacité de ces molécules contre les prions fait d’elles de bons candidats pour un repositionnement thérapeutique pour les maladies à prions. Par ailleurs, nos travaux suggèrent que la PFAR pourrait être utilisée comme cible thérapeutique pour les maladies à prions
Prion is infectious protein responsible of neurodegenerative diseases in human and animal. Scrapie in goat and sheep and Creutzfeldt-Jakob disease in human are prion-related diseases. Prion diseases are fatal and to date there is no efficient treatment against these troubles. This is why in our lab we focus on identification of new compounds efficient against prions. Flunarizine was identified as new anti-prion compound efficient against yeast prion [PSI+] and [URE3], and against mammalian prion PrPSc in vitro, ex vivo and in vivo. Flunarizine may be good drug candidate against prion diseases due to its anti-prion potential in different model. Structure-activity relationship (SAR) around flunarizine hightlights 31 compounds out of 47 which inhibit prion PrPSc propagation in vitro. Six of most efficient compounds cleared prion PrPSc in organotypic slice culture. There were no relationship between flunarizine and related compound activities against prion PrPSc and their known mode of action. The most potent compounds against PrPSc inhibit PFAR (protein folding activity of ribosome). PFAR is a protein chaperon activity which is involved in yeast prion [PSI+] propagation. Many tested compounds are good candidates for drugs repurposing against prion diseases because of their important activity against PrPSc prion.Inhibition of PFAR by all the hightly effective flunarizine related compounds, suggest that PFAR may be consider as cellular target for prion related-diseases treatment
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Heiseke, Andreas. "Prions and autophagy: Effect of lithium on prion infection and role of basal autophagy in primary prion infection." kostenfrei, 2010. https://mediatum2.ub.tum.de/node?id=818228.

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Krejciova, Zuzana. "Exposure and response of human non-neuronal cells to prions in vitro." Thesis, University of Edinburgh, 2012. http://hdl.handle.net/1842/8186.

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Despite intensive research, the cellular and molecular mechanisms involved in human cellular susceptibility to prion infection remain poorly defined, in part due to the continuing lack of cultured human cells that are susceptible to infection with human prions. Such culture models would present distinct advantages including speed and expense compared with animal models, and would provide systems in which to investigate the interaction between PrPC and PrPSc, the basis of cellular susceptibility, the nature of the species barrier and the mechanism of prion propagation in situ. This study sought to examine whether non-neuronal cells might provide opportunities to establish human cell lines replicating human prions. A human follicular dendritic cell-like cell line (termed HK) was obtained, further characterised and then tested for its ability to support human prion replication. The mechanisms of internalisation, intracellular trafficking and the eventual fate of exogenous PrPSc taken up by these cells were also examined. This thesis similarly examined the cellular response of human embryonic stem cells (hESC) to acute exposure to human and animal prions. PrPC was found to be abundantly expressed by HK cells and HK cell extracts were found to support conversion to PrPSc in a cell-free conversion assay. However, HK cells exposed to infectious brain homogenates failed to accumulate PrPSc or become infected in vitro. Exposed HK and hESC did display a readily detectable, time dependent uptake of PrPSc from medium spiked with prion-infected brain homogenates that was independent of the species, disease phenotype and PRNP codon 129 genotype of the human source and the recipient cells. The exposed cells showed intensely labelled intracellular accumulations of PrPSc with coarse granular morphology, largely in the juxtanuclear region of cytoplasm. However, when the brain-spiked medium was withdrawn and cells were given control medium, the intensity and extent of PrPSc immunostaining rapidly diminished. Co-localisation studies implicated caveolae-mediated endocytic uptake of exogenous PrPSc, apparently preceding uptake via clathrin coated pits in HK cells. Evidence suggesting that the endosomal recycling compartment and lysosomes are involved in intracellular trafficking and degradation of exogenous PrPSc was also found. Understanding the cell biology of these processes may help to explain why the majority of cultured cells are refractory to prion infection in vitro. Internalization of misfolded PrP and its subsequent degradation in the lysosomal compartment might function as a self-protective cellular mechanism, serving to eliminate non-native, presumably dysfunctional and potentially dangerous PrP conformers, whether generated endogenously or acquired through exposure to exogenous prion infectivity.
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Chu, Clement SM. "Towards the structure of yeast prions." Diss., Search in ProQuest Dissertations & Theses. UC Only, 2009. http://gateway.proquest.com/openurl?url_ver=Z39.88-2004&rft_val_fmt=info:ofi/fmt:kev:mtx:dissertation&res_dat=xri:pqdiss&rft_dat=xri:pqdiss:3390039.

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Books on the topic "Prions"

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Prusiner, Stanley B., ed. Prions Prions Prions. Berlin, Heidelberg: Springer Berlin Heidelberg, 1996. http://dx.doi.org/10.1007/978-3-642-60983-1.

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Lewis, Patrick A. Prions. Washington, DC, USA: American Chemical Society, 2022. http://dx.doi.org/10.1021/acsinfocus.7e5002.

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Kitamoto, Tetsuyuki, ed. Prions. Tokyo: Springer-Verlag, 2005. http://dx.doi.org/10.1007/4-431-29402-3.

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Lawson, Victoria A., ed. Prions. New York, NY: Springer New York, 2017. http://dx.doi.org/10.1007/978-1-4939-7244-9.

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C, Telling Glenn, ed. Prions and prion diseases: Current perspectives. Norfolk, Eng: Horizon Bioscience, 2004.

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Schweizer, Laurent. Prions: Roman. Paris: Seuil, 2004.

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Zou, Wen-Quan, and Pierluigi Gambetti, eds. Prions and Diseases. New York, NY: Springer New York, 2013. http://dx.doi.org/10.1007/978-1-4614-5305-5.

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Zou, Wen-Quan, and Pierluigi Gambetti, eds. Prions and Diseases. New York, NY: Springer New York, 2013. http://dx.doi.org/10.1007/978-1-4614-5338-3.

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Zou, Wen-Quan, and Pierluigi Gambetti, eds. Prions and Diseases. Cham: Springer International Publishing, 2023. http://dx.doi.org/10.1007/978-3-031-20565-1.

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Zou, Wen-Quan, and Pierluigi Gambetti. Prions and diseases. New York: Springer, 2013.

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Book chapters on the topic "Prions"

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Momcilovic, Dragan. "Prions and Prion Diseases." In Pathogens and Toxins in Foods, 343–56. Washington, DC, USA: ASM Press, 2014. http://dx.doi.org/10.1128/9781555815936.ch22.

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Modrow, Susanne, Dietrich Falke, Uwe Truyen, and Hermann Schätzl. "Prions." In Molecular Virology, 919–47. Berlin, Heidelberg: Springer Berlin Heidelberg, 2013. http://dx.doi.org/10.1007/978-3-642-20718-1_21.

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Mehlhorn, Heinz. "Prions." In Encyclopedia of Parasitology, 1. Berlin, Heidelberg: Springer Berlin Heidelberg, 2015. http://dx.doi.org/10.1007/978-3-642-27769-6_2518-2.

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Mehlhorn, Heinz. "Prions." In Encyclopedia of Parasitology, 2253. Berlin, Heidelberg: Springer Berlin Heidelberg, 2016. http://dx.doi.org/10.1007/978-3-662-43978-4_2518.

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Sakudo, Akikazu. "Prions." In Handbook of Foodborne Diseases, 151–64. Boca Raton : Taylor & Francis, [2019] | Series: Food microbiology series | “A CRC title, part of the Taylor & Francis imprint, a member of the Taylor & Francis Group, the academic division of T&F Informa plc.”: CRC Press, 2018. http://dx.doi.org/10.1201/b22030-14.

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Darcey, Dennis J. "PRIONS." In Physical and Biological Hazards of the Workplace, 553–55. Hoboken, NJ, USA: John Wiley & Sons, Inc., 2016. http://dx.doi.org/10.1002/9781119276531.ch32.

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Sakudo, Akikazu, and Takashi Onodera. "Prions." In Laboratory Models for Foodborne Infections, 117–27. Boca Raton : CRC Press/Taylor & Francis, 2017. | Series: Food microbiology series: CRC Press, 2017. http://dx.doi.org/10.1201/9781315120089-7.

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Makarava, Natallia, Regina Savtchenko, and Ilia V. Baskakov. "Purification and Fibrillation of Full-Length Recombinant PrP." In Prions, 3–22. New York, NY: Springer New York, 2017. http://dx.doi.org/10.1007/978-1-4939-7244-9_1.

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Lewis, Victoria. "Analysis of Cellular Prion Protein Endoproteolytic Processing." In Prions, 119–32. New York, NY: Springer New York, 2017. http://dx.doi.org/10.1007/978-1-4939-7244-9_10.

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Haigh, Cathryn L. "Cellular Analysis of Adult Neural Stem Cells for Investigating Prion Biology." In Prions, 133–45. New York, NY: Springer New York, 2017. http://dx.doi.org/10.1007/978-1-4939-7244-9_11.

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Conference papers on the topic "Prions"

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Miles, Syreeta L., Kazue Takizawa, Charles P. Gerba, and Ian L. Pepper. "Survival of Infectious Prions in Water." In 12th Annual Conference on Water Distribution Systems Analysis (WDSA). Reston, VA: American Society of Civil Engineers, 2011. http://dx.doi.org/10.1061/41203(425)43.

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Kuznetsov, Ivan A., and Andrey V. Kuznetsov. "Modeling Prion Transport in a Tunneling Nanotube." In ASME 2013 International Mechanical Engineering Congress and Exposition. American Society of Mechanical Engineers, 2013. http://dx.doi.org/10.1115/imece2013-62461.

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We develop a model for simulating prion transport in a tunneling nanotube (TNT). We simulate the situation when two cells, one of which is infected, are connected by a TNT. We consider two mechanisms of prion transport: lateral diffusion in the TNT membrane and active actin-dependent transport inside endocytic vesicles. Endocytic vesicles are propelled by myosin Va molecular motors. Since the transit time of prions through a TNT is short (several minutes), the two population model developed here assumes that there is no interchange between the two prion populations, and that partitioning between the prion populations is decided by prion loading at the TNT entrance. The split between the two prion populations at the TNT entrance is decided by the degree of loading, which indicates the portion of prions that enter a TNT in endocytic vesicles. An analytical solution describing prion concentrations and fluxes is obtained.
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Voth, S. B., S. Piechocki, M. S. Gwin, C. M. Francis, and T. Stevens. "Pulmonary Endothelium Generates Antimicrobial Prions as an Innate Defense Mechanism." In American Thoracic Society 2019 International Conference, May 17-22, 2019 - Dallas, TX. American Thoracic Society, 2019. http://dx.doi.org/10.1164/ajrccm-conference.2019.199.1_meetingabstracts.a1984.

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Voth, S. B., M. S. Gwin, M. Crawford, L. Abou Saleh, C. M. Francis, J. F. Pittet, B. Wagener, S. Moser, and T. Stevens. "Clinical Strains of ExoY-Competent Pseudomonas Elicit Cytotoxic Endothelial Amyloid Prions." In American Thoracic Society 2019 International Conference, May 17-22, 2019 - Dallas, TX. American Thoracic Society, 2019. http://dx.doi.org/10.1164/ajrccm-conference.2019.199.1_meetingabstracts.a1986.

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Heinzl, Nicole, Elisabeth Maritschnegg, Katarzyna Koziel, Stuart Wilson, Georg Heinze, Christine Wallisch, Reinhard Horvat, et al. "Abstract AP15: IDENTIFICATION OF P53 PRIONS AS AN INDEPENDENT PROGNOSTIC MARKER FOR SURVIVAL IN HIGH-GRADE SEROUS OVARIAN CANCER." In Abstracts: 12th Biennial Ovarian Cancer Research Symposium; September 13-15, 2018; Seattle, Washington. American Association for Cancer Research, 2019. http://dx.doi.org/10.1158/1557-3265.ovcasymp18-ap15.

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Rok Hacin, Rok Hacin, Chuck Fileds, and Gorazd Meško. "Prison Staff - Prisoners Relations in Slovenian Prisons." In Twelfth Biennial International Conference Criminal Justice and Security in Central and Eastern Europe: From Common Sense to Evidence-based Policy–making. University of Maribor Pres, 2018. http://dx.doi.org/10.18690/978-961-286-174-2.19.

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Wyatt, Michael R., Stephen Herbein, Todd Gamblin, Adam Moody, Dong H. Ahn, and Michela Taufer. "PRIONN." In ICPP 2018: 47th International Conference on Parallel Processing. New York, NY, USA: ACM, 2018. http://dx.doi.org/10.1145/3225058.3225091.

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Mulyadi, Dedi, and M. Aridhayandi. "Policy Guidance for Prisoners in Perspective of Law Number 12 of 1995 concerning Prisons: Comparative Study of Cianjur Prison and Magelang Prison." In Proceedings of the First International Conference on Progressive Civil Society (ICONPROCS 2019). Paris, France: Atlantis Press, 2019. http://dx.doi.org/10.2991/iconprocs-19.2019.31.

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Pekar, Julius, and Michael S. Patterson. "Multispectral Bioluminescence Tomography: Simulations and Phantom Studies with a priori x-ray CT Spatial Priors." In Biomedical Optics. Washington, D.C.: OSA, 2010. http://dx.doi.org/10.1364/biomed.2010.bmb8.

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Nogueira, Pericles A., Regina M. C. D. M. Abrahao, and Vera M. N. Galesi. "TUBERCULOSIS IN PRISON SYSTEM – SURVEY IN TWO PRISONS IN THE STATE OF SÃO PAULO, BRAZIL, 2008." In American Thoracic Society 2010 International Conference, May 14-19, 2010 • New Orleans. American Thoracic Society, 2010. http://dx.doi.org/10.1164/ajrccm-conference.2010.181.1_meetingabstracts.a6829.

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Reports on the topic "Prions"

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Harris, David A. Propagation of Mammalian Prions in Yeast. Fort Belvoir, VA: Defense Technical Information Center, July 2006. http://dx.doi.org/10.21236/ada472675.

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Liebman, Susan W. Understanding Factors Influencing The Propagation of Prions. Fort Belvoir, VA: Defense Technical Information Center, December 2007. http://dx.doi.org/10.21236/ada482382.

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Ghosh, Arijeet, Madhurima Dhanuka, Sai Bourothu, Fernando Lannes Fernandes, Niyati Singh, and Chenthil Kumar. Lost Identity: Transgender Persons Inside Indian Prisons. Commonwealth Human Rights Initiative, 2020. http://dx.doi.org/10.20933/100001185.

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This report sheds light on challenges faced by Transgender persons in Indian prisons. The report analyses the international and legal frameworks in the country which provide the foundation for policy formulations with regard to confinement of LGBT+ persons, with particular reference to the Transgender community. This report also documents the responses received to right to information requests filed to prison headquarters across the country, which in addition to providing the number of Transgender prisoners in Indian prisons between 1st May 2018 to 30th April 2019, also provides relevant information on compliance within prisons with existing legal frameworks relevant to protecting the rights of Transgender persons in prisons, especially in terms of recognition of a third gender, allocation of wards, search procedures, efforts towards capacity building of prison administrators etc. The finalisation of this report has involved an intense consultative process with individuals and experts, including representatives from the community, community-based organisations as well as researcher and academicians working on this issue. This report aims to enhance the understanding of these issues among stakeholders such as prison administrators, judicial officers, lawyers, legal service providers as well as other non-state actors. It is aimed at better informed policy making, and ensuring that decisions made with respect to LGBTI+ persons in prisons recognize and are sensitive of their rights and special needs.
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Kaatrakoski, Heli. Learning in and for work in correctional services in Norway. University of Stavanger, November 2022. http://dx.doi.org/10.31265/usps.251.

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The study explored the views of prison officer students and their supervisors regarding (1) prison officer education, (2) prison officers’ continuing professional development, (3) prison officers’ training needs and opportunities, and 4) the future of prison work. A total of ten interviews were conducted in a prison in Norway in October 2021. The prison officer students who were interviewed expressed satisfaction with their education. Communication was highlighted as the most relevant learning topic. Regarding the continuing professional development of prison officers, learning about communication and mental health issues were expressed as areas of particular significance. Learning about services for female prisoners was also brought up. The issues that impede prison officers’ participation in training were the limited time to arrange training and the lack of financial resources. The importance of collaborating and learning together with mental health professionals was expressed, but borrowing learning resources from the neighbouring disciplines was considered to be problematic because of the specific character of prison work. The future of prison work was discussed from different viewpoints. The numbers of aggressive prisoners, old prisoners and those with mental health issues were expected to increase. The need to continue the development of prisons and concerns over the future role of prison officer were also expressed. The report provided five suggestions for future research concerning correctional services.
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Atwood, C. L. Constrained noninformative priors. Office of Scientific and Technical Information (OSTI), October 1994. http://dx.doi.org/10.2172/43783.

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Baltagi, Badi H., Georges Bresson, Anoop Chaturvedi, and Guy Lacroix. Robust dynamic space-time panel data models using ε-contamination: An application to crop yields and climate change. CIRANO, January 2023. http://dx.doi.org/10.54932/ufyn4045.

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This paper extends the Baltagi et al. (2018, 2021) static and dynamic ε-contamination papers to dynamic space-time models. We investigate the robustness of Bayesian panel data models to possible misspecification of the prior distribution. The proposed robust Bayesian approach departs from the standard Bayesian framework in two ways. First, we consider the ε-contamination class of prior distributions for the model parameters as well as for the individual effects. Second, both the base elicited priors and the ε-contamination priors use Zellner (1986)’s g-priors for the variance-covariance matrices. We propose a general “toolbox” for a wide range of specifications which includes the dynamic space-time panel model with random effects, with cross-correlated effects `a la Chamberlain, for the Hausman-Taylor world and for dynamic panel data models with homogeneous/heterogeneous slopes and cross-sectional dependence. Using an extensive Monte Carlo simulation study, we compare the finite sample properties of our proposed estimator to those of standard classical estimators. We illustrate our robust Bayesian estimator using the same data as in Keane and Neal (2020). We obtain short run as well as long run effects of climate change on corn producers in the United States.
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Frydman, Roman, Søren Johansen, Anders Rahbek, and Morten Nyboe Tabor. Asset Prices Under Knightian Uncertainty. Institute for New Economic Thinking Working Paper Series, December 2021. http://dx.doi.org/10.36687/inetwp172.

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We extend Lucas’s classic asset-price model by opening the stochastic process driving dividends to Knightian uncertainty arising from unforeseeable change. Implementing Muth’s hypothesis, we represent participants’ expectations as being consistent with our model’s predictions and formalize their ambiguity-averse decisions with maximization of intertemporal multiple-priors utility. We characterize the asset-price function with a stochastic Euler equation and derive a novel prediction that the relationship between prices and dividends undergoes unforeseeable change. Our approach accords participants’ expectations, driven by both fundamental and psychological factors, an autonomous role in driving the asset price over time, without presuming that participants are irrational.
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Ramirez, Ignacio, Federico Lecumberry, and Guillermo Sapiro. Universal Priors for Sparse Modeling(PREPRINT). Fort Belvoir, VA: Defense Technical Information Center, August 2009. http://dx.doi.org/10.21236/ada513254.

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Dippel, Christian, and Michael Poyker. Do Private Prisons Affect Criminal Sentencing? Cambridge, MA: National Bureau of Economic Research, March 2019. http://dx.doi.org/10.3386/w25715.

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Sethuraman, Jayaram. A Constructive Definition of Dirichlet Priors. Fort Belvoir, VA: Defense Technical Information Center, May 1991. http://dx.doi.org/10.21236/ada238689.

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