Relevant bibliographies by topics / Prione

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Academic literature on the topic 'Prione'

Author: Grafiati
Published: 9 March 2023
Last updated: 11 March 2023

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Journal articles on the topic "Prione"

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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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Son, Moonil, and Reed B. Wickner. "Anti-Prion Systems in Saccharomyces cerevisiae Turn an Avalanche of Prions into a Flurry." Viruses 14, no. 9 (September 1, 2022): 1945. http://dx.doi.org/10.3390/v14091945.

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Prions are infectious proteins, mostly having a self-propagating amyloid (filamentous protein polymer) structure consisting of an abnormal form of a normally soluble protein. These prions arise spontaneously in the cell without known reason, and their effects were generally considered to be fatal based on prion diseases in humans or mammals. However, the wide array of prion studies in yeast including filamentous fungi revealed that their effects can range widely, from lethal to very mild (even cryptic) or functional, depending on the nature of the prion protein and the specific prion variant (or strain) made by the same prion protein but with a different conformation. This prion biology is affected by an array of molecular chaperone systems, such as Hsp40, Hsp70, Hsp104, and combinations of them. In parallel with the systems required for prion propagation, yeast has multiple anti-prion systems, constantly working in the normal cell without overproduction of or a deficiency in any protein, which have negative effects on prions by blocking their formation, curing many prions after they arise, preventing prion infections, and reducing the cytotoxicity produced by prions. From the protectors of nascent polypeptides (Ssb1/2p, Zuo1p, and Ssz1p) to the protein sequesterase (Btn2p), the disaggregator (Hsp104), and the mysterious Cur1p, normal levels of each can cure the prion variants arising in its absence. The controllers of mRNA quality, nonsense-mediated mRNA decay proteins (Upf1, 2, 3), can cure newly formed prion variants by association with a prion-forming protein. The regulator of the inositol pyrophosphate metabolic pathway (Siw14p) cures certain prion variants by lowering the levels of certain organic compounds. Some of these proteins have other cellular functions (e.g., Btn2), while others produce an anti-prion effect through their primary role in the normal cell (e.g., ribosomal chaperones). Thus, these anti-prion actions are the innate defense strategy against prions. Here, we outline the anti-prion systems in yeast that produce innate immunity to prions by a multi-layered operation targeting each step of prion development.
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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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Miller, Sarah C., Andrea K. Wegrzynowicz, Sierra J. Cole, Rachel E. Hayward, Samantha J. Ganser, and Justin K. Hines. "Hsp40/JDP Requirements for the Propagation of Synthetic Yeast Prions." Viruses 14, no. 10 (September 30, 2022): 2160. http://dx.doi.org/10.3390/v14102160.

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Yeast prions are protein-based transmissible elements, most of which are amyloids. The chaperone protein network in yeast is inexorably linked to the spreading of prions during cell division by fragmentation of amyloid prion aggregates. Specifically, the core “prion fragmentation machinery” includes the proteins Hsp104, Hsp70 and the Hsp40/J-domain protein (JDP) Sis1. Numerous novel amyloid-forming proteins have been created and examined in the yeast system and occasionally these amyloids are also capable of continuous Hsp104-dependent propagation in cell populations, forming synthetic prions. However, additional chaperone requirements, if any, have not been determined. Here, we report the first instances of a JDP-Hsp70 system requirement for the propagation of synthetic prions. We utilized constructs from a system of engineered prions with prion-forming domains (PrDs) consisting of a polyQ stretch interrupted by a single heterologous amino acid interspersed every fifth residue. These “polyQX” PrDs are fused to the MC domains of Sup35, creating chimeric proteins of which a subset forms synthetic prions in yeast. For four of these prions, we show that SIS1 repression causes prion loss in a manner consistent with Sis1′s known role in prion fragmentation. PolyQX prions were sensitive to Sis1 expression levels to differing degrees, congruent with the variability observed among native prions. Our results expand the scope known Sis1 functionality, demonstrating that Sis1 acts on amyloids broadly, rather than through specific protein–protein interactions with individual yeast prion-forming proteins.
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Krauss, Sybille, and Ina Vorberg. "PrionsEx Vivo: What Cell Culture Models Tell Us about Infectious Proteins." International Journal of Cell Biology 2013 (2013): 1–14. http://dx.doi.org/10.1155/2013/704546.

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Prions are unconventional infectious agents that are composed of misfolded aggregated prion protein. Prions replicate their conformation by template-assisted conversion of the endogenous prion protein PrP. Templated conversion of soluble proteins into protein aggregates is also a hallmark of other neurodegenerative diseases. Alzheimer’s disease or Parkinson’s disease are not considered infectious diseases, although aggregate pathology appears to progress in a stereotypical fashion reminiscent of the spreading behavior ofmammalian prions. While basic principles of prion formation have been studied extensively, it is still unclear what exactly drives PrP molecules into an infectious, self-templating conformation. In this review, we discuss crucial steps in the life cycle of prions that have been revealed inex vivomodels. Importantly, the persistent propagation of prions in mitotically active cells argues that cellular processes are in place that not only allow recruitment of cellular PrP into growing prion aggregates but also enable the multiplication of infectious seeds that are transmitted to daughter cells. Comparison of prions with other protein aggregates demonstrates that not all the characteristics of prions are equally shared by prion-like aggregates. Future experiments may reveal to which extent aggregation-prone proteins associated with other neurodegenerative diseases can copy the replication strategies of prions.
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Krejciova, Zuzana, James Alibhai, Chen Zhao, Robert Krencik, Nina M. Rzechorzek, Erik M. Ullian, Jean Manson, James W. Ironside, Mark W. Head, and Siddharthan Chandran. "Human stem cell–derived astrocytes replicate human prions in a PRNP genotype–dependent manner." Journal of Experimental Medicine 214, no. 12 (November 15, 2017): 3481–95. http://dx.doi.org/10.1084/jem.20161547.

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Prions are infectious agents that cause neurodegenerative diseases such as Creutzfeldt–Jakob disease (CJD). The absence of a human cell culture model that replicates human prions has hampered prion disease research for decades. In this paper, we show that astrocytes derived from human induced pluripotent stem cells (iPSCs) support the replication of prions from brain samples of CJD patients. For experimental exposure of astrocytes to variant CJD (vCJD), the kinetics of prion replication occur in a prion protein codon 129 genotype–dependent manner, reflecting the genotype-dependent susceptibility to clinical vCJD found in patients. Furthermore, iPSC-derived astrocytes can replicate prions associated with the major sporadic CJD strains found in human patients. Lastly, we demonstrate the subpassage of prions from infected to naive astrocyte cultures, indicating the generation of prion infectivity in vitro. Our study addresses a long-standing gap in the repertoire of human prion disease research, providing a new in vitro system for accelerated mechanistic studies and drug discovery.
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Tahir, Waqas, Basant Abdulrahman, Dalia H. Abdelaziz, Simrika Thapa, Rupali Walia, and Hermann M. Schätzl. "An astrocyte cell line that differentially propagates murine prions." Journal of Biological Chemistry 295, no. 33 (June 19, 2020): 11572–83. http://dx.doi.org/10.1074/jbc.ra120.012596.

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Prion diseases are fatal infectious neurodegenerative disorders in human and animals caused by misfolding of the cellular prion protein (PrPC) into the pathological isoform PrPSc. Elucidating the molecular and cellular mechanisms underlying prion propagation may help to develop disease interventions. Cell culture systems for prion propagation have greatly advanced molecular insights into prion biology, but translation of in vitro to in vivo findings is often disappointing. A wider range of cell culture systems might help overcome these shortcomings. Here, we describe an immortalized mouse neuronal astrocyte cell line (C8D1A) that can be infected with murine prions. Both PrPC protein and mRNA levels in astrocytes were comparable with those in neuronal and non-neuronal cell lines permitting persistent prion infection. We challenged astrocytes with three mouse-adapted prion strains (22L, RML, and ME7) and cultured them for six passages. Immunoblotting results revealed that the astrocytes propagated 22L prions well over all six passages, whereas ME7 prions did not replicate, and RML prions replicated only very weakly after five passages. Immunofluorescence analysis indicated similar results for PrPSc. Interestingly, when we used prion conversion activity as a readout in real-time quaking-induced conversion assays with RML-infected cell lysates, we observed a strong signal over all six passages, comparable with that for 22L-infected cells. These data indicate that the C8D1A cell line is permissive to prion infection. Moreover, the propagated prions differed in conversion and proteinase K–resistance levels in these astrocytes. We propose that the C8D1A cell line could be used to decipher prion strain biology.
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Safar, Jiri G., Klaus Kellings, Ana Serban, Darlene Groth, James E. Cleaver, Stanley B. Prusiner, and Detlev Riesner. "Search for a Prion-Specific Nucleic Acid." Journal of Virology 79, no. 16 (August 15, 2005): 10796–806. http://dx.doi.org/10.1128/jvi.79.16.10796-10806.2005.

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ABSTRACT Diversity of prion strains was attributed to an elusive nucleic acid, yet a search spanning nearly two decades has failed to identify a prion-specific polynucleotide. In our search for a prion-specific nucleic acid, we analyzed nucleic acids in purified fractions from the brains of Syrian hamsters infected with Sc237 prions. Purification of Sc237 prions removed nucleic acids larger than 50 nucleotides as measured by return refocusing electrophoresis (RRGE). To determine the size of the largest polynucleotide present in purified fractions at an abundance of one molecule per infectious (ID50) unit, we measured prions present after inoculation. In order to account for the rapid clearance of prions after intracerebral inoculation, we determined the number of PrPSc molecules and ID50 units of prions that were retained in brain. Factoring in clearance after inoculation, we estimate that the largest polynucleotide present in our purified fractions at one molecule per ID50 unit is ≈25 nucleotides in length. In the same fractions, there were ≈3,000 protease-resistant PrPSc molecules per ID50 unit after accounting for clearance of PrPSc following inoculation. We compared the resistance of Sc237 and 139H prions to inactivation by UV irradiation at 254 nm. Irradiation of homogenates and microsomes diminished prion infectivity by a factor of ≈1,000 but did not alter the strain-specified properties of the Sc237 and 139H prions. The data reported here combined with the production of synthetic prions argue that the 25-mer polynucleotides found in purified prion preparations are likely to be host encoded and of variable sequence; additionally, these 25-mers are unlikely to be prion specific.
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Evarts, Jacob, and Mikala Capage. "Hunting for Prions: Propagating Putative Prion States in Budding Yeast." Oregon Undergraduate Research Journal 18, no. 1 (2021): 26–34. http://dx.doi.org/10.5399/uo/ourj/18.1.4.

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Prions have been closely associated with fatal neurodegenerative diseases. Recent evidence, however, suggests that prions also represent an additional class of epigenetic mechanism that is biologically beneficial. From an evolutionary standpoint, the ability to change phenotypes without requiring changes to the genome, as prions do, would be hugely beneficial in fluctuating environments. Through overexpressing proteins and introducing environmental stressors, two techniques known to increase de novo prion formation, we performed a large-scale screen of many RNA-modifying enzymes in budding yeast to test if they harbor beneficial prionogenic behavior. From this screen, six induced prion-like states were found to be mitotically stable and infectious. We show that many of these putative prions are dominant and are dependent on chaperone proteins, which is consistent with a prion-based epigenetic mechanism. Prion-based inheritance is expanding on the central dogma of biology, contributing to the belief that prions work as an epigenetic mechanism for passing on heritable traits.
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Terry, Cassandra, Adam Wenborn, Nathalie Gros, Jessica Sells, Susan Joiner, Laszlo L. P. Hosszu, M. Howard Tattum, et al. "Ex vivo mammalian prions are formed of paired double helical prion protein fibrils." Open Biology 6, no. 5 (May 2016): 160035. http://dx.doi.org/10.1098/rsob.160035.

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Mammalian prions are hypothesized to be fibrillar or amyloid forms of prion protein (PrP), but structures observed to date have not been definitively correlated with infectivity and the three-dimensional structure of infectious prions has remained obscure. Recently, we developed novel methods to obtain exceptionally pure preparations of prions from mouse brain and showed that pathogenic PrP in these high-titre preparations is assembled into rod-like assemblies. Here, we have used precise cell culture-based prion infectivity assays to define the physical relationship between the PrP rods and prion infectivity and have used electron tomography to define their architecture. We show that infectious PrP rods isolated from multiple prion strains have a common hierarchical assembly comprising twisted pairs of short fibres with repeating substructure. The architecture of the PrP rods provides a new structural basis for understanding prion infectivity and can explain the inability to systematically generate high-titre synthetic prions from recombinant PrP.
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Dissertations / Theses on the topic "Prione"

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CUNATI, DIANA. "Ruolo dei lipid raft nel metabolismo della proteina prionica." Doctoral thesis, Università degli Studi di Milano-Bicocca, 2011. http://hdl.handle.net/10281/27001.

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The prion protein (PrP) is a GPI-anchored protein primarily concentrated in neuronal cells. Under certain conditions, the innocuous cellular form of this protein, PrPC, can convert into the lethal scrapie isoform, PrPSc, which can aggregate with other PrP molecules and exert its neurotoxic activity. The structure of PrPC consists of two domains: an N-terminal, glycosylated, flexible disordered domain which is capable of binding copper and a C-terminal α-helical domain. In contrast, PrPSc is enriched in β-sheet structures and characterized by its poor solubility in non-denaturing detergents, propensity for aggregation, partial resistance to proteinase K digestion. The conversion of PrPC into PrPSc occurs in particular regions of the cell membrane, enriched with cholesterol and glycosphingolipid, called lipid rafts; these microdomains are thought to play a crucial role both in physiological functions and in the alternative folding of the prion protein. In addition, it’s known that: -PrPC can be cleaved at the 110/111 peptidyl bond to produce a C-terminal fragment, C1, which remains membrane bound and a N-terminal fragment, N1, released in the extracellular space. C1 fragments can’t be converted to the scrapie isoform; - in cell cultures, ADAM10 and ADAM17 were shown to be responsible for this processing and their activation seems PKC-dependent. The aim of our project is to establish if the alteration of cell lipid composition can modify the membrane distribution of the prion protein within rafts or non-raft regions and promote the activity of disintegrins such as ADAM10/17 upon the prion protein. For this reason, granule cells, from the cerebella of 8-day-old rats, were incubated after 8 days in culture with GM1 or GD1a or GT1b for 4 hours at 37°C or with GM1 for 4 hours at 4°C. Detergent resistant fractions, containing lipid rafts, were isolated and proteins in all gradient fractions were separated and analyzed by EF/WB with specific antibodies. After cell treatments with exogenous gangliosides, a good percentage of them was found in lipid rafts; immunoblotting analysis with specific antibodies showed a significant reduction in the amount of proteins, normally localized in lipid rafts, after incubation with GT1b. The incorporation of this ganglioside, characterized by a remarkable steric encumbrance, might be responsible for lipid rafts destabilization and proteins redistribution toward non-raft regions. Another possibility is that GT1b incorporation reduces the number of lipid rafts on the cell membrane. Immunoblotting analysis with three different anti-PrP antibodies showed that this protein is not selectively located in lipid rafts but it is also distributed in several intracellular compartments. Cell treatments with GM1 or GD1a at 37°C for 4 hours were not able to promote PrPC cleavage at the 110/111 peptidyl bond; cell incubation with GM1 seemed able to induce a conformational change of the prion protein toward a “simil-scrapie” isoform, partially resistant to classical denaturation protocols. Further studies are in progress to fully demonstrate that GM1-PrP interaction results in this conformational change.
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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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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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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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Bhamra, S. K. "Systematic mutagenesis of the mouse prion protein to identify critical regions for the efficient propagation of prions." Thesis, University College London (University of London), 2014. http://discovery.ucl.ac.uk/1443249/.

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The aim of this study was to systematically investigate the contributions of various amino acids within the prion protein, on prion propagation. To test this in a cellular system, we used a sub-cloned population of N2a cells (PK1) that are highly susceptible to RML mouse prions. A library of stable PK1 cells was generated, which expressed the full length mouse prion protein (moPrP) bearing either point, double, or triple alanine replacements. The effects these changes in the prion protein sequence had on the ability of PK1 cells to propagate RML was tested using a previously established cell based assay. We found that: (i) in the unstructured region of the protein, alanine replacements in CC2 region 90-111 of the prion protein severely diminish, but do not abrogate the ability of cells to propagate prions whilst substitutions K23A.K24A.R25A and Q41A exerted a moderate inhibitory effect on propagation; (ii) alanine replacements in CC2 displayed a dominant negative effect by imposing their propagation inhibition phenotype in the presence of the wild-type protein; (iii) the diminished propagation abilities of cells expressing CC2 alanine mutants were a result of these cells being less susceptible to infection than their wild-type counterparts (iv) all alanine replacements tested in the structured region of the protein appeared to hamper prion propagation, regardless of their positioning within this globular domain. Taken together, these results suggest that integrity of the structured region is vital for successful prion propagation, and that although the flexible region of the prion protein alone (residues 23-111), does not exclusively confer infectivity and/or propagative capacity, charge interactions in this region govern the efficacy with which propagation ensues.
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Wang, Weiqiang. "Prion inspired nanomaterials and their biomedical applications." Doctoral thesis, Universitat Autònoma de Barcelona, 2020. http://hdl.handle.net/10803/670982.

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Els amiloides presenten una estructura fibril·lar molt ordenada. Molts d’aquests conjunts de proteïnes apareixen associats a malalties humanes. No obstant això, es pot aprofitar la naturalesa controlable, estable, ajustable i robusta de les fibres amiloides per crear nanomaterials amb una àmplia gamma d’aplicacions. Els prions funcionals constitueixen una classe particular d’amiloides. Aquestes proteïnes transmissibles presenten una arquitectura modular, amb un domini prió desordenat responsable del assemblatge i d’un o més dominis globulars que proporcionen l’activitat. És important destacar que la proteïna globular original es pot substituir per qualsevol proteïna d’interès, sense comprometre el potencial de fibril·lació. Aquestes fusions genètiques formen fibres en les quals el domini global roman plegat, formant nanoestructures funcionals. Tot i això, en molts casos, els impediments estèrics poden restringir l’activitat d’aquestes fibres. Aquesta limitació es pot solucionar disseccionant els dominis priònics en seqüències més curtes que mantenen les seves propietats d’auto-assemblatge alhora que permeten un millor accés a la proteïna en estat fibril·lar. En aquesta tesi doctoral, vam aprofitar el “soft amyloid core” (SAC) del prió de llevat Sup35p com una unitat de muntatge modular, que recapitula la propensió a l’agregació del domini priònic complet. Vam fusionar el SAC amb diferents proteïnes globulars d’interès que difereixen en la conformació i la mida, creant un mètode genètic general i senzill per generar nanofibres dotades de les funcionalitats desitjades. El modelatge computacional ens va permetre conèixer la relació entre la mida dels dominis globulars i la longitud del enllaç que els connecta al SAC, proporcionant les bases per al disseny de nanomaterials amb diferents propietats mesoscòpiques, ja siguin nanofibres o nanopartícules. Sobre aquesta base, hem dissenyat i produït, per primera vegada, nanopartícules amiloides esfèriques altament actives, no tòxiques, de mida definida, i s’han produït nanoestructures bifuncionals amb aplicació en el subministrament específic de fàrmacs. Les lliçons apreses en aquests exercicis van donar lloc a la construcció d’una nanofibrilla similar a un anticòs biespecífic amb potencial per la immunoteràpia. En resum, els nanomaterials funcionals de tipus priònic descrits aquí aprofiten l’enfocament de la fusió genètica per crear un nou conjunt d’estructures amb aplicacions en biomedicina i biotecnologia.
Los amiloides muestran una estructura fibrilar altamente ordenada. Muchos de estos ensamblajes aparecen asociados a enfermedades humanas. No obstante, la naturaleza controlable, estable, modulable y robusta de las fibras amiloides se puede emplear para construir nanomateriales notables con una amplia gama de aplicaciones. Los priones funcionales constituyen una clase particular de amiloides. Estas proteínas transmisibles exhiben una arquitectura modular, con un dominio priónico desordenado responsable del ensamblaje y uno o más dominios globulares que dan cuenta de la actividad. Cabe destacar que la proteína globular original se puede reemplazar con cualquier proteína de interés sin comprometer el potencial de fibrilación. Estas fusiones genéticas forman fibrillas en las que el dominio globular permanece plegado, lo que genera nanoestructuras funcionales. Sin embargo, en muchos casos, el impedimento estérico restringe la actividad de estas fibrillas. Esta limitación puede resolverse diseccionando los dominios de priones en secuencias más cortas que mantengan sus propiedades de autoensamblado mientras permiten un mejor acceso a la proteína en el estado fibrilar. En esta tesis doctoral, exploramos el "soft amyloid core" (SAC) del prion de levadura Sup35p como una unidad modular de autoensamblaje, que recapitula la propensión a la agregación del dominio priónico completo. Fusionamos el SAC con diferentes proteínas globulares de interés que difieren en conformación y tamaños, creando un enfoque genético general y directo para generar nanofibrillas dotadas de las funcionalidades deseadas. El modelado computacional nos permitió obtener información sobre la relación entre el tamaño de los dominios globulares y la longitud del conector que los une con el SAC, proporcionando la base para el diseño de nanomateriales con diferentes propiedades mesoscópicas, ya sean nanofibrillas o nanopartículas. Sobre esta base, diseñamos y producimos, por primera vez, nanopartículas amiloides esféricas, altamente activas, no tóxicas, de tamaño definido, y diseñamos nanoestructuras bifuncionales con aplicación en la administración dirigida de fármacos. Las lecciones aprendidas en estos ejercicios permitieron la construcción de una nanofibrilla similar a un anticuerpo biespecífico con potencial para su uso en inmunoterapia. En resumen, los nanomateriales funcionales similares a los priones descritos aquí aprovechan la metodología de fusión genética para generar un nuevo conjunto de estructuras con aplicación en biomedicina y biotecnología.
Amyloids display a highly ordered fibrillar structure. Many of these assemblies appear associated with human disease. However, the controllable, stable, tunable, and robust nature of amyloid fibrils can be exploited to build up remarkable nanomaterials with a wide range of applications. Functional prions constitute a particular class of amyloids. These transmissible proteins exhibit a modular architecture, with a disordered prion domain responsible for the assembly and one or more globular domains that account for the activity. Importantly, the original globular protein can be replaced with any protein of interest, without compromising the fibrillation potential. These genetic fusions form fibrils in which the globular domain remains folded, rendering functional nanostructures. However, in many cases, steric hindrance restricts the activity of these fibrils. This limitation can be solved by dissecting prion domains into shorter sequences that keep their self-assembling properties while allowing better access to the protein in the fibrillar state. In this PhD thesis, we exploited the "soft amyloid core (SAC)" of the Sup35p yeast prion as a modular self-assembling unit, which recapitulates the aggregation propensity of the complete prion domain. We fused the SAC to different globular proteins of interest differing in conformation and sizes, building up a general and straightforward genetic approach to generate nanofibrils endowed with desired functionalities. Computational modeling allowed us to gain insights into the relationship between the size of the globular domains and the length of the linker that connects them to the SAC, providing the basis for the design of nanomaterials with different mesoscopic properties, either nanofibrils or nanoparticles. On this basis, we designed and produced, for the first time, highly active, non-toxic, spherical amyloid nanoparticles of defined size and engineered bifunctional nanostructures with application in targeted drug delivery. The lessons learned in these exercises resulted in the construction of a bispecific antibody-like nanofibril, showing potential in immunotherapy. In summary, the prion-like functional nanomaterials described here take profit of the genetic fusion approach to render a novel set of structures with application in biomedicine and biotechnology.
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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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Howlin, Robert. "Decontamination of prions, prion-associated amyloid and infectivity from surgical stainless steel : implications for the risk of iatrogenic transmission of CJD." Thesis, University of Southampton, 2009. https://eprints.soton.ac.uk/150533/.

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The physicochemical nature of the infectious agent in prion diseases creates a significant challenge for decontamination services. It has been shown to be both resistant to standard methods of decontamination, used to inactivate viruses and bacteria, and to associate avidly with surgical stainless steel. Moreover, the pathophysiology of the variant, iatrogenic and sporadic forms of Creutzfeldt-Jakob Disease (CJD) suggests deposition of the infectious agent across a wide range of extraneural, lymphoid tissues, as well as in the skeletal muscle and blood. Coupled with the potential for asymptomatic carriers, there is a significant risk of iatrogenic transmission of CJD through both neurosurgical procedures and standard surgery. This PhD study was undertaken in order to improve methods of instrument decontamination and to evaluate prion detection techniques and their applicability for the assessment of prion inactivation and removal. The project has provided relevant, critical assessment of hospital decontamination procedures, in addition to guidance on how working protocols should be improved to provide a cleaner and safer end product for the patient. Moreover, laboratory studies have been performed to evaluate current methods of prion decontamination in the context of hospital procedures for instrument reprocessing. Challenges faced by sterile service departments, such as soil drying and surface degradation, have been addressed and their impact on the risk of iatrogenic transmission of prions has been investigated. Critically, the use of a fluorescent amyloid fluorophore for the detection of prionassociated amyloid as a marker for disease permitted the investigation of the role of amyloid in infectious disease under denaturing conditions. Correlation of this detection technique with the identification of PrPres by Western blot and infectious disease suggested that, whilst fluorescent detection of prion-associated amyloid was more sensitive than Western blot, PrPres detection was more specific relative to infectivity. Improved fluorophores, with greater sensitivity, have been evaluated which will enhance in situ detection of prions in the future.
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Sun, Meng. "Development of the new yeast-based assays for prion properties." Diss., Georgia Institute of Technology, 2011. http://hdl.handle.net/1853/45831.

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Prion is an infectious isoform of a normal cellular protein which is capable of converting the non-prion form of the same protein into the alternative prion form. Mammalian prion protein PrP is responsible for prion formation in mammals, causing a series of fatal and incurable prion diseases. (1) We constructed, for the first time, a two-component system to phenotypically monitor the conformational status of PrP in the yeast cells. In this system, the prion domain of Sup35 (Sup35N) was fused to PrP90-230, and the initial formation of the PrPSc-like conformation stimulated prion formation of Sup35N, which in turn converted soluble Sup35 into the prion isoform, leading to a detectable phenotype. Prion-like properties of PrP were studied in this novel yeast model system. Additionally, we employed this system to study amyloidogenic protein Aβ42 aggregation in the yeast model. It has been suggested that the ability to form transmissible amyloids (prions) is widespread among yeast proteins and is likely intrinsic to proteins from other organisms. However, the distribution of yeast prions in natural conditions is not yet clear, which prevents us from understanding the relationship between prions and their adaptive roles in various environmental conditions. (2) We modified and developed sequence and phenotype-independent approaches for prion detection and monitoring. We employed these approaches for prion-profiling among yeast strains of various origins. (3) Lastly, we found a prion-like state [MCS+] causing nonsense suppression in the absence of the Sup35 prion domain. Our results suggested that [MCS+] is determined by both a prion factor and a nuclear factor. The prion-related properties of [MCS+] were studied by genetic and biochemical approaches.
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Dakowski, Caroline. "Rôle de la protéine prion cellulaire (PRPC) dans la différenciation neuronale : Infection par les prions (PRPSC) et bases moléculaires de la neurodégénérescence." Thesis, Paris 5, 2012. http://www.theses.fr/2012PA05T032.

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Books on the topic "Prione"

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

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Zhang, Jiapu. Molecular Structures and Structural Dynamics of Prion Proteins and Prions. Dordrecht: Springer Netherlands, 2015. http://dx.doi.org/10.1007/978-94-017-7318-8.

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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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Kleopatra, Ferla, ed. Priene. Cambridge, Mass: Harvard University Press, 2004.

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Kleopatra, Ferla, ed. Priene. 2nd ed. Athens, Greece: Foundation of the Hellenic World, 2005.

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

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Baker, Harry F., and Rosalind M. Ridley. Prion Diseases. New Jersey: Humana Press, 1996. http://dx.doi.org/10.1385/0896033422.

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Book chapters on the topic "Prione"

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Schröder, Bjürn. "Prione." In Lexikon der Infektionskrankheiten des Menschen, 668–74. Berlin, Heidelberg: Springer Berlin Heidelberg, 2009. http://dx.doi.org/10.1007/978-3-540-39026-8_888.

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Gries, Oliver, and Thomas Ly. "Prione (Allgemein)." In Infektologie - Kompendium humanpathogener Infektionskrankheiten und Erreger, 591–94. Berlin, Heidelberg: Springer Berlin Heidelberg, 2019. http://dx.doi.org/10.1007/978-3-662-58219-0_89.

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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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Legname, Giuseppe, Gabriele Giachin, and Federico Benetti. "Structural Studies of Prion Proteins and Prions." In Non-fibrillar Amyloidogenic Protein Assemblies - Common Cytotoxins Underlying Degenerative Diseases, 289–317. Dordrecht: Springer Netherlands, 2011. http://dx.doi.org/10.1007/978-94-007-2774-8_9.

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Knight, Richard. "Overview on Treatment of Prion Diseases and Decontamination of Prions." In Prions and Diseases, 257–67. New York, NY: Springer New York, 2012. http://dx.doi.org/10.1007/978-1-4614-5338-3_16.

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Knight, Richard. "Overview on Treatment of Prion Diseases and Decontamination of Prions." In Prions and Diseases, 727–43. Cham: Springer International Publishing, 2023. http://dx.doi.org/10.1007/978-3-031-20565-1_35.

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Buselmaier, Werner. "Prionen." In Biologie für Mediziner, 292–93. Berlin, Heidelberg: Springer Berlin Heidelberg, 2009. http://dx.doi.org/10.1007/978-3-642-00452-0_21.

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Buselmaier, Werner. "Prionen." In Biologie für Mediziner, 373–75. Berlin, Heidelberg: Springer Berlin Heidelberg, 2015. http://dx.doi.org/10.1007/978-3-662-46178-5_23.

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Schmitt, Corinna. "Prionen." In Medizinische Mikrobiologie und Infektiologie, 781–85. Berlin, Heidelberg: Springer Berlin Heidelberg, 2020. http://dx.doi.org/10.1007/978-3-662-61385-6_73.

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Buselmaier, Werner. "Prionen." In Biologie für Mediziner, 295–96. Berlin, Heidelberg: Springer Berlin Heidelberg, 2012. http://dx.doi.org/10.1007/978-3-642-27175-5_21.

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Conference papers on the topic "Prione"

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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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Dugalic, Marijana, Ljiljana Boškovic Rakočevic, Vera Rajicic, and Dragan Terzic. "UTICAJ NAČINA PRIMENE MINERALNIH ĐUBRIVA NA PRINOS KROMPIRA." In SAVETOVANJE o biotehnologiji sa međunarodnim učešćem. University of Kragujeva, Faculty of Agronomy, 2021. http://dx.doi.org/10.46793/sbt26.079d.

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This study showed the effect of different methods of application of mineral fertiliser rates on the yield of two potato cultivars grown under the agroenvironmental conditions of the Radočelo Mountain massif on a luvisol exhibiting rather favourable agrophysical and some what poorer agrochemical properties. In 2018 and 2019, a trial with potato cvs. ‘Arizona’ and ‘Esmee’ was established. Planned rates of mineral fertilisers (N200, P150, K150) were applied as two treatments: treatment 1 – fertiliser rates were ploughed in during autumn, and treatment 2 – one half of the planned rates was applied during seedbed preparation and the other half in-furrow at planting. The results showed that the treatment involving the application of one half of the fertiliser rate before planting, and the other half at planting resulted in higher total yields of both potato cultivars compared with the placement of the whole rate of fertilisers during deep ploughing in autumn.
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Raghavan, Santhi. "Between the Ivory Towers and the Prison Walls: Prison Inmates’ Decision to Pursue Tertiary Education in Open University Malaysia." In Tenth Pan-Commonwealth Forum on Open Learning. Commonwealth of Learning, 2022. http://dx.doi.org/10.56059/pcf10.6370.

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Being a correctional entity, the Malaysian Prison Department through its vision and mission is responsible to provide a safe detention and rehabilitation. One of its objectives is to ensure suitable and effective correctional programmes for all categories of inmates. One of the programmes set up by Malaysian Prison Department is to have a collaboration with higher education providers to offer tertiary education for inmates in order to equip them with knowledge and skills to pursue work after release. One of such engagement is the provision of the undergraduate and postgraduate programmes for inmates in selected Malaysian prisons by Open University Malaysia (OUM). OUM conducts undergraduate and postgraduate degree programmes for prison inmates. This study aims to determine the factors influencing prison inmates’ decision to pursue higher education in the prisons. 37 respondents from a total of 68 prisoners-students are involved in this study. The Stakeholder Theory and the Theory of Planned Behaviour were adopted as the underpining theories as they are related to attitude and planned behaviour. The Stakeholder Theory enables us to comprehend how a diverse range of stakeholders impact prisoner learning and comprehend the expectations and duties of distinct stakeholders regarding prisoner learning. Whereas, the Theory of Planned Behaviour postulates that an individual’s behaviour is determined by their intention to engage in such behaviour. Factor analysis was utilised to identify if these three factors (student attribute, social influence and financial aid) influenced prison inmates’ decision to pursue Open University Malaysia’s programmes in prisons. Results of the multiple linear regression indicated that there was a significant effect between student attribute and decision to study, which means that inmates' own characteristics will motivate them to continue learning which can lead to future success in their pursuit for excellence in tertiary education.
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Đukic, Vojin, Jegor Miladinovic, Zlatica Miladinov Mamlic, Gordana Dozet, Marija Bajagic, Marijana Jovanovic Todorovic, and Vojin Cvijanovic. "PRINOS SOJE U ZAVISNOSTI OD VREMENA PRIMENE NPK ĐUBRIVA." In SAVETOVANJE o biotehnologiji sa međunarodnim učešćem. University of Kragujeva, Faculty of Agronomy, 2021. http://dx.doi.org/10.46793/sbt26.043dj.

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Soybean yield depends on the variety, soil, cultural practices, as well as the weather conditions in certain years. The aim of this research is to examine the impact of NPK fertilizer application in the autumn and spring period on the level of soybean yield. The highest soybean yields were achieved by applying NPK fertilizer in autumn, before the basic tillage with spring application of nitrogen fertilizer AN. Spring application of NPK fertilizers and AN increases the yield, but the effect of fertilizers is significantly less compared to autumn application. The application of nitrogen fertilizer AN increases the soybean yield, and in order for this fertilizer to show its full effect, it is necessary for the soil to be optimally provided with macroelements.
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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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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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Serra Castilhos, Daniela, and Marco Ribeiro Henriques. "FEMALE PRISONER AND PRISONS FOR WOMEN. A FEMINIST LEGAL CRITICAL VIEW ACCORDING TO AN EMPIRICAL-LEGAL DESCRIPTIVE ANALYSIS OF THE RIGHT TO FORMAL EDUCATION IN PRISON." In 11th International Conference on Education and New Learning Technologies. IATED, 2019. http://dx.doi.org/10.21125/edulearn.2019.0103.

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Nikola, Thomas, Steve K. Choi, Cody J. Duell, Rodrigo G. Freundt, Zachary B. Huber, Yaqiong Li, Kshama Malavalli, et al. "CCAT-prime: the epoch reionization spectrometer for primce-cam on FYST." In Millimeter, Submillimeter, and Far-Infrared Detectors and Instrumentation for Astronomy XI, edited by Jonas Zmuidzinas and Jian-Rong Gao. SPIE, 2022. http://dx.doi.org/10.1117/12.2629338.

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Dozet, Gordana, Vojin Đukić, Jegor Miladinović, Zlatica Mamlić, Gorica Cvijanović, Snežana Jakšić, and Olga Kandelinskaja. "UTICAJ FOLIJARNE PRIMENE NPK ĐUBRIVA SA MIKROELEMENTIMA I EFEKTIVNIH MIKROORGANIZAMA NA PRINOS SOJE." In XXVII savetovanje o biotehnologiji. University of Kragujevac, Faculty of Agronomy, 2022. http://dx.doi.org/10.46793/sbt27.111d.

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High yields and stable soybean production are under direct influence of plant nutrient quantity and availability. The aim of this research was to examine the effect of NPK fertilizer with trace elements and effective microorganisms on the yields of three soybean varieties which belong to different maturation groups. Effective microorganisms and NPK fertilizer with trace elements statistically very significantly increase soybean yield. Effective microorganisms increased the yield by 7.28%, NPK fertilizer with trace elements by 11.20%, while the combination of effective microorganisms and NPK fertilizer with trace elements increase soybean yield by 14.86%.
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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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Reports on the topic "Prione"

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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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McCulloch, Neil, Davide Natalini, Naomi Hossain, and Patricia Justino. An Exploration of the Association Between Fuel Subsidies and Fuel Riots. Institute of Development Studies, October 2021. http://dx.doi.org/10.19088/ids.2021.058.

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Between 2005 and 2018, 41 countries had at least one riot directly associated with popular demand for fuel. We make use of a new international data set on fuel riots to explore the effects of fuel prices and price regimes on fuel riots. In line with prior expectations, we find that large domestic fuel price shocks – often linked to international price shocks – are a key driver of riots. In addition, we report a novel result: fuel riots are closely associated with domestic price regimes. Countries that maintain fixed price regimes – notably net energy exporters – tend to have large fuel subsidies. When such subsidies become unsustainable, domestic price adjustments are large, often leading to riots.
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4

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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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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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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Stewart, Richard S. The Role of a Novel Topological Form of the Prion Protein in Prion Disease. Fort Belvoir, VA: Defense Technical Information Center, July 2008. http://dx.doi.org/10.21236/ada494937.

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Stewart, Richard S. The Role of a Novel Topological Form of a Prion Protein in Prion Disease. Fort Belvoir, VA: Defense Technical Information Center, July 2004. http://dx.doi.org/10.21236/ada430363.

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Stewart, Richard S. The Role of a Novel Topological Form of the Prion Protein in Prion Disease. Fort Belvoir, VA: Defense Technical Information Center, July 2005. http://dx.doi.org/10.21236/ada462482.

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Stewart, Richard S. The Role of a Novel Topological Form of the Prion Protein in Prion Disease. Fort Belvoir, VA: Defense Technical Information Center, July 2006. http://dx.doi.org/10.21236/ada470272.

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