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Dissertations / Theses on the topic 'Prione'

Author: Grafiati
Published: 9 March 2023
Last updated: 31 July 2025

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1

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,
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2

FASOLI, Elisa. "Trasmissione intraspecie di encefalopatia spongiforme bovina e di encefalopatia spongiforme amiloidotica bovina. Caratterizzazione molecolare e ultrastrutturale di un nuovo ceppo di prione nel bovino." Doctoral thesis, Università degli Studi di Verona, 2008. http://hdl.handle.net/11562/337633.

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Le Encefalopatie Spongiformi Trasmissibili (TSE) o Malattie da Prioni, costituiscono un gruppo di malattie neurodegenerative fatali, ad eziologia sporadica, genetica o infettiva che colpiscono l’uomo e diverse specie animali. Il meccanismo patogenetico responsabile delle TSE consiste nella conversione conformazionale della normale proteina prionica cellulare (PrPC), con una struttura prevalentemente ad α-elica, in una forma aberrante, ricca in β-sheet, parzialmente insolubile in detergenti non ionici e resistente alla digestione con proteasi, denominata PrPSc, che rappresenta il marcato
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3

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-li
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4

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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5

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 intracitoplasmá
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6

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 b
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7

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 destac
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8

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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9

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 Su
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10

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 asymptoma
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11

Premzl, Marko, and Premzl@anu edu au premzl@excite com Marko. "Prion Protein Gene and Its Shadow." The Australian National University. The John Curtin School of Medical Research, 2004. http://thesis.anu.edu.au./public/adt-ANU20050328.164529.

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Prion protein (PrP) is best known for its involvement in prion diseases. A normal, dynamic isoform of prion protein (PrP^C) transforms into a pathogenic, compact isoform (PrP^Sc) during prion disease pathogenesis. The PrP^Sc, acting as a template upon which PrP^C molecules are refolded into a likeness of itself, accumulates in the brain neurones and causes disease. It is the only known component of prions, proteinaceous infectious particles. Both prion protein isoforms have the same primary amino acid structure and are encoded by the same prion protein gene (PRNP). PRNP determines susceptibili
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12

Fröhlich, Gallardo Estefanía Paz. "Aplicación de la inmunohistoquímica en óbex de caprinos para la detección de proteínas priónicas." Tesis, Universidad de Chile, 2017. http://repositorio.uchile.cl/handle/2250/151607.

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Memoria para optar al Título Profesional de Médico Veterinario.<br>El Scrapie es una enfermedad neurodegenerativa y fatal que afecta a pequeños rumiantes como ovinos, caprinos y muflones. El causante de esta enfermedad es una partícula proteinácea infecciosa llamada prión, que se origina por un cambio conformacional de una proteína priónica celular del hospedero (PrPC). Los programas de vigilancia consideran a la Histopatología como método diagnóstico y a la Inmunohistoquímica (IHQ) como método confirmatorio para el Scrapie. Esta memoria fue desarrollada en el laboratorio de la Unidad de
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13

Chen, Buxin. "Prion species barrier at the short phylogenetic distances in the yeast model." Diss., Atlanta, Ga. : Georgia Institute of Technology, 2008. http://hdl.handle.net/1853/29762.

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Thesis (Ph.D)--Biology, Georgia Institute of Technology, 2009.<br>Committee Chair: Chernoff, Yury; Committee Member: Bommarius, Andreas; Committee Member: Doyle, Donald; Committee Member: Lobachev, Kirill; Committee Member: Yi, Soojin. Part of the SMARTech Electronic Thesis and Dissertation Collection.
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14

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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15

Chan, Hok-mo. "Medium security prison." Hong Kong : University of Hong Kong, 1996. http://sunzi.lib.hku.hk/hkuto/record.jsp?B2595149x.

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16

Crozet, Carole. "Souris transgéniques pour la protéine prion ovine : transmission d'encéphalopathies subaiguës spongiformes transmissibles naturelles et expérimentales : contribution à la caractérisation des maladies à prions." Lyon 1, 2001. http://www.theses.fr/2001LYO1T036.

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17

Boudet-Devaud, François. "La protéine prion cellulaire : un relai de neurotoxicité commun aux protéines amyloïdes et aux nanoparticules Protective role of cellular prion protein against TNFα-mediated inlammation through TACE α-secretase PrPSc-induced PDK1 overactivation promotes the production of seedable Amyloid-β peptides in prion diseases Corruption of cellular prion protein signaling by titanium dioxide or carbon black nanoparticles promotes the accumulation of amyloid-β peptides". Thesis, Sorbonne Paris Cité, 2018. http://www.theses.fr/2018USPCB127.

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La protéine prion cellulaire (PrPC) est une protéine majoritairement exprimée à la surface des neurones, dont la conversion transconformationnelle en prion pathogène PrPSc, est à l'origine des maladies à prions. Il est clairement établi que la neurodégénérescence induite par la PrPSc dépend de l'expression de la PrPC dans les neurones et résulte d'une déviation de la/des fonction(s) de la PrPC par la PrPSc. Identifier le rôle de la PrPC est donc un pré-requis pour aborder les mécanismes de neurodégénérescence dans les maladies à prions. Une partie de mes travaux de thèse a permis de montrer qu
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18

Coyle, Andrew G. "The organisational development of the Scottish Prison Service, with particular reference to the role and influence of the prison officer." Thesis, University of Edinburgh, 1986. http://hdl.handle.net/1842/7557.

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This thesis argues that the Prison Service, while it has several unique features, is a bureaucratic structure with a typical mix of organisational strengths and weaknesses. The study of the development of the organisation of the Scottish Prison Service is, therefore, as possible and as proper as is the study of any large organisation. The first substantive chapter of the thesis analyses the historical development of the Scottish Prison Service within an organisational context. This has taken place in 3 main phases, the first two of which were sequential, the third less obviously so and more th
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19

Ezpeleta, Juliette. "Du rôle physiologique de la protéine prion cellulaire à l'infection par les prions : régulation/dérégulation du module de signalisation PDK1/TACE α-secrétase Protective role of cellular prion protein against TNFα-mediated inflammation trough TACE α-secretase Cerebellar compartmentation of prion pathogenesis Production of seedable Amyloid-β peptides in prion diseases upon PrPSc-induced PDK1 overactivation". Thesis, Sorbonne Paris Cité, 2019. http://www.theses.fr/2019USPCB004.

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Les maladies à prions sont des maladies neurodégénératives caractérisées par l'accumulation dans le système nerveux central d'une protéine anormalement conformée et neurotoxique, la protéine prion Scrapie (PrPSc). La PrPSc est l'isoforme transconformationnelle d'une protéine normale de l'hôte, la protéine prion cellulaire (PrPC). Il est établi que la toxicité de la PrPSc est restreinte aux neurones et que la neurodégénérescence résulte d'une corruption de la/des fonction(s) physiologique(s) de la PrPC par la PrPSc. Néanmoins, nul ne sait s'il s'agit d'une perte de fonction protectrice ou d'un
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20

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 ma
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21

Schwengler, Franziska. "Prion Diseases." Diss., lmu, 2005. http://nbn-resolving.de/urn:nbn:de:bvb:19-36790.

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22

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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23

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.<br>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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24

Rumscheid, Frank. "Die figürlichen Terrakotten von Priene : Fundkontexte, Ikonographie und Funktion in Wohnhäusern und Heiligtümern im Licht antiker Parallelbefunde." Wiesbaden Reichert, 2006. http://bvbr.bib-bvb.de:8991/F?func=service&docl̲ibrary=BVB01&docn̲umber=015027207&linen̲umber=0001&funcc̲ode=DBR̲ECORDS&servicet̲ype=MEDIA.

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25

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
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26

Saijo, Eri. "INVESTIGATING THE ROLE OF PRION PROTEIN POLYMORPHISMS ON PRION PATHOGENESIS." UKnowledge, 2012. http://uknowledge.uky.edu/microbio_etds/4.

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Transmissible spongiform encephalopathies (TSEs), also known as prion diseases, are lethal and infectious neurodegenerative diseases of humans and animals. The misfolding of the normal, or cellular isoform of the prion protein (PrPC) into the abnormal disease-associated isoform of PrP (PrPSc) could change the properties of PrP, consequently, PrPSc has lethal infectivity to transmit diseases. The proteinaceous infectious particle consisting mainly of PrPSc is called prion. Transmissibility of prions is strongly influenced by multiple factors including PrP polymorphisms, species barriers (PrP se
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27

Mirabile, I. "Prion pathology in the brainstem : clinical target areas in prion disease." Thesis, University College London (University of London), 2012. http://discovery.ucl.ac.uk/1346475/.

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Prion diseases are fatal transmissible neurodegenerative disorders characterized by spongiform changes, neuronal loss, reactive astrocytosis, and deposition of disease associated prion protein (PrP). Our aim was to investigate "clinical target areas" for prion disease, responsible for disease onset, progression, and the clinical phenotype, using PrP overexpressing MloxP and PrP depleted NFH-Cre/MloxP transgenic mouse lines. Upon infection with different prion strains NFH-Cre/MloxP mice have significantly longer survival than MloxP mice (first set of experiments: Me7, ~29 weeks vs. ~17 weeks; M
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28

Carulla, Martí Patricia. "La proteína priónica celular: Análisis de su función neuroprotectora y reguladora del ciclo Celular." Doctoral thesis, Universitat de Barcelona, 2013. http://hdl.handle.net/10803/129157.

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Las encefalopatías espongiformes transmisibles (EETs) son un conjunto de enfermedades neurodegenerativas letales que afectan tanto animales como humanos. Están causadas por unas partículas proteicas denominadas “priones”, resultantes de la transformación de la proteína priónica celular (PrP(C)) a una forma patogénica denominada PrP(SC), que se acumula en el cerebro en forma de agregados e induce la transformación de más moléculas a expensas de la reducción de los niveles de PrP(C). Hasta el día de hoy, el estudio de las prionopatías se ha centrado en la bioquímica, toxicidad y transmisibilid
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29

Smith, Juliana Jamel. "The cultural dynamic of the prison industrial complex a critique of political rhetoric and popular film during the 1980's /." Diss., Connect to a 24 p. preview or request complete full text in PDF format. Access restricted to UC campuses, 2008. http://wwwlib.umi.com/cr/ucsd/fullcit?p1450190.

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Thesis (M.A.)--University of California, San Diego, 2008.<br>Title from first page of PDF file (viewed April 7, 2008). Available via ProQuest Digital Dissertations. Includes bibliographical references (p. 121-129).
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Radreau, Félicie. "Cellules souches embryonnaires et neurales humaines : quand la PrP et l'APP "s'en mêlent" ou "s’emmêlent"." Thesis, Montpellier, 2016. http://www.theses.fr/2016MONTT045/document.

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La Protéine Prion cellulaire (PrPc) est une protéine ubiquitaire mais majoritairement présente dans le système nerveux central. Elle est plus particulièrement connue pour sa conversion conformationnelle en PrPSc dans les maladies à Prions qui sont des Protéinopathies comme la maladie d’Alzheimer (MA). La MA est en partie associée à des dépôts de peptides beta-amyloïdes (Aβ) agrégés de façon extracellulaire et issus des clivages successifs par la β- puis la γ-sécrétase de la protéine précurseur amyloïde (APP) exprimée dans les neurones. La PrPc et l’APP partagent des fonctions et des voies prot
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Kiachopoulos, Sophia. "Biogenese des Prion-Proteins." Diss., lmu, 2005. http://nbn-resolving.de/urn:nbn:de:bvb:19-44118.

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Sarafoff, Nikolaus. "Amplifikation von Prionen in vitro." Diss., lmu, 2006. http://nbn-resolving.de/urn:nbn:de:bvb:19-57072.

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33

Klingeborn, Mikael. "The prion protein in normal cells and disease : studies on the cellular processing of bovine PrPC and molecular characterization of the Nor98 prion /." Uppsala : Department of Molecular Biosciences, Swedish University of Agricultural Sciences, 2006. http://epsilon.slu.se/2006105.pdf.

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Mead, Simon Harvey. "Molecular genetic analysis of the prion protein gene locus in human prion disease." Thesis, Imperial College London, 2003. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.417947.

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Shi, Song. "Screening anti-prion compounds and diagnosing prion diseases by amplifying PrPSc in vitro." Diss., Ludwig-Maximilians-Universität München, 2015. http://nbn-resolving.de/urn:nbn:de:bvb:19-179963.

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Mahmoud, Mohamed Karmi Hussein. "Studies on pathogenic mechanisms of prion diseases and evaluation of prion strains properties." Diss., Munich Verl. Dr. Hut, 2009. http://d-nb.info/992892376/04.

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Lenuzza, Natacha. "Modélisation de la réplications des Prions : Implication de la dépendance en taille des agrégats de PrP et de l'hétérogénéité des populations cellulaires." Phd thesis, Ecole Centrale Paris, 2009. http://tel.archives-ouvertes.fr/tel-00453321.

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Les maladies à Prions sont des maladies neurodégénératives fatales, touchant l'homme et l'animal. Même si le risque de transmission de la maladie de la vache folle à l'homme semble maîtrisé, il persiste actuellement un risque de santé publique lié à la transmission iatrogène de cette forme, notamment par transfusion sanguine. Pour contrôler cette transmission, il est donc essentiel de mieux comprendre les mécanismes moléculaires et cellulaires de réplication et de dissémination des Prions. Ces mécanismes de réplication se produisent à des échelles de temps et de taille difficilement accessible
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Sanghera, Narinder. "The interaction of the prion protein with lipid membranes and implications for prion conversion." Thesis, University of Warwick, 2001. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.247140.

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Mashima, Tsukasa. "The structural analysis of RNA aptamer against prion protein and its anti-prion activity." Kyoto University, 2013. http://hdl.handle.net/2433/170071.

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40

Pacini, Patrizia. "Anatomie de la prison. Aspects politico-sociaux de la condition carcérale en Italie et en France." Thesis, Université Côte d'Azur (ComUE), 2018. http://www.theses.fr/2018AZUR0011.

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La recherche s’insère de façon réflexive et critique, dans le cadre théorique de l’analyse sociologique, législative, politique et institutionnelle de type comparatif, c’est-à-dire une reconstruction du cadre unitaire et organique de l’univers carcéral de deux pays européens qui sont très proche historiquement et culturellement : la France et l’Italie. C’est une représentation de la dimension carcérale quotidienne des détenus, une réalité articulée et variable qui constitue un des thèmes les plus controversés dans les débats politiques et sociaux actuels au niveau européen. Un travail de reche
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Díaz, Caballero Marta. "Prion inspired assemblies to build up functional bionanomaterials." Doctoral thesis, Universitat Autònoma de Barcelona, 2020. http://hdl.handle.net/10803/670481.

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Malgrat l’ensamblatge amiloide ha estat tradicionalment relacionat amb malaltia, en les darreres dues dècades, s’ha ressaltat la seva implicació en importants funcions biològiques. Aquestes troballes han incrementat l’interès per al desenvolupament de nanomaterials inspirats en amiloides en múltiples àrees com la biomedicina, la nanoelectrònica, les ciències mediambientals o la nanotecnologia. La complexitat de la producció i manipulació de proteïnes amiloides complertes ha manifestat la necessitat d’obtenir blocs alternatius que mimetitzin les seves propietats per a l’ensamblatge de nanomater
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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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43

Ragagnin, Audrey. "Mort neuronale et maladies à prions." Thesis, Strasbourg, 2014. http://www.theses.fr/2014STRAJ094/document.

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La conversion conformationnelle de la protéine prion cellulaire PrPC neuroprotectrice en protéine prion PrPSc infectieuse et pathogène caractérise les maladies à prions. Dans le cerveau infecté par les prions, la perte de PrPC, le gain de PrPSc neurotoxique et l’inflammation concourent à la mort neuronale par des mécanismes encore mal connus.Ces travaux valident les cultures organotypiques de cervelet de souris comme système expérimental ex vivo favorable à l’étude de ces mécanismes et montrent que l’absence de PrPC aussi bien que PrPSc activent des mécanismes apoptotiques et autophagiques qui
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Gierusz, Leszek A. "Folding and fibril formation of prions." Thesis, University of Warwick, 2012. http://wrap.warwick.ac.uk/56927/.

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Prions diseases are a group of fatal neurodegenerative disorders called the transmissible spongiform encephalopathies (TSEs), which include bovine spongiform encephalopathy in cattle, scrapie in sheep and Creutzfeldt-Jakob disease (CJD) in humans. TSEs are associated with the conversion of normal cellular form of the prion protein (PrPC) to an altered pathological form (PrPSc). An important phenomenon known as the species barrier affects prion transmission, resulting in longer incubation time and lower incidence of disease upon transfer between species. Another feature of prion diseases is dis
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45

Toupet, Karine. "Stratégies thérapeutiques des maladies à prions." Montpellier 2, 2009. http://www.theses.fr/2009MON20128.

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Les maladies à prions sont des maladies neurodégénératives qui touchent l'homme et l'animal, et dont l'issue est fatale. Ces maladies sont provoquées par l'accumulation dans le cerveau de la PrPSc, l'isoforme mal repliée de la protéine prion cellulaire. L'apparition de nouveaux risques de transmission de ces maladies et l'absence de traitement efficace, nous ont incité à explorer de nouvelles stratégies et cibles thérapeutiques. Nous avons développé deux approches thérapeutiques innovantes. La première à consister à rechercher des molécules capables de piéger les formes préamyloïdes de la PrPS
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46

Ekwa, Robert. "Les maladies à prions : problèmes épistémologiques." Paris 1, 2012. http://docelec.u-bordeaux.fr/login?url=http://www.harmatheque.com/ebook/les-maladies-a-prions--problemes-epistemologiques--volume-2--vache-folle-et-raisonnements-causals-41085.

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Entrée en Europe au XVIIIe siècle, portant des noms différents attachés au contexte de lecture de ses symptômes, la tremblante resta longtemps un mystère. Dès le milieu des années 1960 sous l'impulsion de Carleton Gadjusek, l'analogie étiologique et pathologique entre cette neuropathologie animale et la maladie du kuru aujourd'hui disparue, permit de tester la transmissibilité de plusieurs maladies neuropsychiatriques et d'établir un groupe de maladies nommées Encéphalopathies spongiformes subaiguës transmissibles. Dès 1982, grâce à Stanley Prusiner, les outils conceptuels et techniques de la
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47

Zahn, Ralph. "Prion propagation and molecular chaperones." Zürich : Institut für Molekularbiologie und Biophysik, Eidgenössische Technische Hochschule Zürich, 2002. http://e-collection.ethbib.ethz.ch/show?type=habil&nr=4.

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48

Uelhoff, Armgard. "Polarisierter Transport des Prion-Proteins." Diss., lmu, 2005. http://nbn-resolving.de/urn:nbn:de:bvb:19-40163.

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Rambold, Angelika. "Funktionelle Charakterisierung des Prion-Proteins." Diss., lmu, 2008. http://nbn-resolving.de/urn:nbn:de:bvb:19-91541.

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50

Norton, Jennifer Diane, and Jennifer Diane Norton. "Mechanisms of Prion Variant Competition." Diss., The University of Arizona, 2017. http://hdl.handle.net/10150/625845.

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The assembly of some misfolded proteins into aggregates can cause dramatic changes in cellular phenotypes. In prion diseases, these phenotypes are self-perpetuating because the highly ordered aggregates are capable of templating the conversion of soluble form of the protein into the aggregated form. Interestingly, the aggregated form of the protein can exist as a range of unique self-replicating conformations, referred to as prion "strains" or "variants," conferring distinct phenotypic characteristics to their hosts. The presence of more than one prion variant has been implicated in the altera
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