Relevant bibliographies by topics / Prion protein

Academic literature on the topic 'Prion protein'

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Published: 4 June 2021
Last updated: 14 March 2023

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Journal articles on the topic "Prion protein"

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Requena, Jesús R. "The protean prion protein." PLOS Biology 18, no. 6 (June 25, 2020): e3000754. http://dx.doi.org/10.1371/journal.pbio.3000754.

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Ma, Jiyan, Jingjing Zhang, and Runchuan Yan. "Recombinant Mammalian Prions: The “Correctly” Misfolded Prion Protein Conformers." Viruses 14, no. 9 (August 31, 2022): 1940. http://dx.doi.org/10.3390/v14091940.

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Generating a prion with exogenously produced recombinant prion protein is widely accepted as the ultimate proof of the prion hypothesis. Over the years, a plethora of misfolded recPrP conformers have been generated, but despite their seeding capability, many of them have failed to elicit a fatal neurodegenerative disorder in wild-type animals like a naturally occurring prion. The application of the protein misfolding cyclic amplification technique and the inclusion of non-protein cofactors in the reaction mixture have led to the generation of authentic recombinant prions that fully recapitulate the characteristics of native prions. Together, these studies reveal that recPrP can stably exist in a variety of misfolded conformations and when inoculated into wild-type animals, misfolded recPrP conformers cause a wide range of outcomes, from being completely innocuous to lethal. Since all these recPrP conformers possess seeding capabilities, these results clearly suggest that seeding activity alone is not equivalent to prion activity. Instead, authentic prions are those PrP conformers that are not only heritable (the ability to seed the conversion of normal PrP) but also pathogenic (the ability to cause fatal neurodegeneration). The knowledge gained from the studies of the recombinant prion is important for us to understand the pathogenesis of prion disease and the roles of misfolded proteins in other neurodegenerative disorders.
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Atkinson, Caroline J., Kai Zhang, Alan L. Munn, Adrian Wiegmans, and Ming Q. Wei. "Prion protein scrapie and the normal cellular prion protein." Prion 10, no. 1 (December 8, 2015): 63–82. http://dx.doi.org/10.1080/19336896.2015.1110293.

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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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Dimcheff, Derek E., John L. Portis, and Byron Caughey. "Prion proteins meet protein quality control." Trends in Cell Biology 13, no. 7 (July 2003): 337–40. http://dx.doi.org/10.1016/s0962-8924(03)00125-9.

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Kupfer, L., W. Hinrichs, and M. Groschup. "Prion Protein Misfolding." Current Molecular Medicine 9, no. 7 (September 1, 2009): 826–35. http://dx.doi.org/10.2174/156652409789105543.

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Rezaei, H. "Prion Protein Oligomerization." Current Alzheimer Research 5, no. 6 (December 1, 2008): 572–78. http://dx.doi.org/10.2174/156720508786898497.

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Lawson, Victoria A., Steven J. Collins, Colin L. Masters, and Andrew F. Hill. "Prion protein glycosylation." Journal of Neurochemistry 93, no. 4 (May 2005): 793–801. http://dx.doi.org/10.1111/j.1471-4159.2005.03104.x.

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Gough, N. R. "Prion Protein Protection." Science Signaling 1, no. 19 (May 13, 2008): ec174-ec174. http://dx.doi.org/10.1126/stke.119ec174.

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Prusiner, Stanley B., Michael R. Scott, Stephen J. DeArmond, and Fred E. Cohen. "Prion Protein Biology." Cell 93, no. 3 (May 1998): 337–48. http://dx.doi.org/10.1016/s0092-8674(00)81163-0.

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Dissertations / Theses on the topic "Prion protein"

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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 susceptibility/disposition to prion diseases and their phenotypes.¶The normal function of PRNP is elusive. The Prnp knock-out mice with disrupted ORF show only very subtle phenotype. A number of hypotheses were proposed on the function of mammalian PRNP. The extracellular, GPI-anchored, glycosylated mammalian PrP^C expressed in a heterogenous set of cells could: transport copper from extracellular to intracellular milieu, buffer copper from synapse, contribute to redox signalling, act neuroprotectively, mediate cell-cell contacts, affect lymphocyte activation, participate in nucleic acid metabolism, be a memory molecule, and be a signal-transduction protein.¶ Experimental evidence demonstrated a redundancy between the PRNP and another, unknown gene. The critical issue therefore is to discover new genes homologous with PRNP, candidates for this redundancy. Using unpublished data, a sequence of zebrafish cDNA sequenced by Prof. Tatjana Simonic’s group (University of Milan, Italy), I discovered a new paralogue of PRNP. By searching manually, and in a targeted fashion, data deposited in public biological databases, I compiled support for the new human gene Shadow of prion protein (SPRN) including the direct evidence, homology-based evidence and ab initio gene prediction. The protein product called Shadoo (shadow in Japanese) is an extracellular, potentially glycosylated and GPI-anchored protein of a mature size of 100-odd amino acids. It is conserved from fish (zebrafish, Fugu, Tetraodon) to mammals (human, mouse, rat), and exhibits similarity of overall protein features with PrP. Most remarkably, the Sho is the first human/mammalian protein apart from PrP that contains the middle hydrophobic region that is essential for both normal and pathogenic properties of PrP. As this region is critical for heterodimerization of PrP, Sho may have potential to interact with PrP and is a likely candidate for the Protein X. Mammalian SPRN could be predominantly expressed in brain (Tatjana Simonic Lab, University of Milan, Italy).¶ Using the same approach to search public databases, I found, in addition, a fish duplicate of SPRN called SPRNB, and defined a new vertebrate SPRN gene family. Further, I also expanded a number of known fish genes from the PRNP gene family. The total number of the new genes that I discovered is 11. With the representatives of two vertebrate gene family datasets in hand, I conducted comparative genomic analysis in order to determine evolutionary trajectories of the SPRN and PRNP genes. This analysis, complemented with phylogenetic studies (Dr. Lars Jermiin, University of Sydney, Australia), demonstrated conservative evolution of the mammalian SPRN gene, and more relaxed evolutionary constraints acting on the mammalian PRNP gene. This evolutionary dialectic challenges widely adopted view on the “highly conserved vertebrate” PRNP and indicates that the SPRN gene may have more prominent function. More conserved Sprn could therefore substitute for the loss of less conserved, dispensable Prnp in the Prnp knock-out mice. Furthermore, the pathogenic potential of PRNP may be a consequence of relaxed evolutionary constraints.¶ Depth of comparative genomic analysis, strategy to understand biological function, depends on the number of species in comparison and their relative evolutionary distance. To understand better evolution and function of mammalian PRNP, I isolated and characterized the PRNP gene from Australian model marsupial tammar wallaby (Macropus eugenii). Marsupials are mammals separated from their eutherian relatives by roughly 180 million years. Comparison of the tammar wallaby and Brazilian opossum PrP with other vertebrate PrPs indicated patterns of evolution of the PrP regions. Whereas the repeat region is conserved within lineages but differs between lineages, the hydrophobic region is invariably conserved in all the PrPs. Conservation of PrP between marsupials and eutherians suggests that marsupial PrP could have the same pathogenic potential as eutherian PrPs. Using the marsupial PRNP gene in comparison with the PRNP genes from eutherian species in which prion diseases occur naturally (human, bovine, ovine) or experimentally (mouse), I defined gene regions that are conserved mammalian-wide and showed the utility of the marsupial genomic sequence for cross-species comparisons. These regions are potential regulatory elements that could govern gene expression and posttranscriptional control of mRNA activity. These findings shed new light on the normal function of mammalian PRNP supporting best the signal-transduction hypothesis. The normal function of PRNP may be triggering of signalling cascades which contribute to cell-cell interactions and may act anti-apoptotically. Yet, in the heterogenous set of cells expressing PrP^C these pathways will contribute to a number of cell-specific phenotypes, such as the synaptic plasticity and activation of lymphoid cells.
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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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Apetri, Constantin Adrian. "Folding of the Prion Protein." Case Western Reserve University School of Graduate Studies / OhioLINK, 2004. http://rave.ohiolink.edu/etdc/view?acc_num=case1080747299.

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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 sequence specificity) and prion strains (conformational specificity) by unknown mechanisms. Even though the ability of prions to cross a species barrier has been recognized, the precise mechanisms of interspecies prion transmission remain unclear. This dissertation research was conducted in order to learn more about the molecular mechanisms of conversion, propagation and transmission of PrPSc; about determinants of genetic susceptibility to infection in prion diseases; and about understanding those mechanisms, which might govern the zoonotic potential of prion diseases. First, we investigated the transmissibility risk of multiple strains of Chronic Wasting Disease, which is a cervid TSE, with humanized transgenic mice and showed that the transmission barriers between cervid and the humanized mice are high. Next, the structural factors underlying the species barrier of prion diseases were studied using cell culture systems by systematically introducing amino acid substitutions in the regions of PrP, where the most divergences of different PrP species are recognized. Thirdly, we investigated the effects of the genetic susceptibility to prions as well as conversion kinetics and properties of PrPSc using Tg mice expressing ovine PrP polymorphism (OvPrP) at codon 136 either alanine (A) or valine (V). The templating characteristics of OvPrPSc-V136 were dominant over OvPrPSc-A136 under co-expressions of OvPrPC-A136 and OvPrPC-V136. Finally, the function of PrP was studied in relation to the pathogenesis of Alzheimer’s disease. These studies demonstrated that the conformational compatibility between PrPC and PrPSc contributed to the conversion kinetics and species barrier. We concluded that the conformational compatibility of PrPC to PrPSc is controlled not only by the PrP sequence specificity but also by the tertiary structure of PrPC.
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Resenberger, Ulrike. "Das zelluläre Prion-Protein als Mediator der Scrapie-Prion-Protein- und Amyloid Beta-induzierten Neurotoxizität." Diss., lmu, 2012. http://nbn-resolving.de/urn:nbn:de:bvb:19-153987.

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Papadopoulos, Maria. "The prion protein interacts with Bcl-2 and Bax proteins." Thesis, National Library of Canada = Bibliothèque nationale du Canada, 1998. http://www.collectionscanada.ca/obj/s4/f2/dsk1/tape10/PQDD_0026/MQ50849.pdf.

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Hart, Tanya Clare. "Mutational studies of prion protein folding." Thesis, Imperial College London, 2005. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.418318.

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Davies, Paul. "The metallochemistry of the prion protein." Thesis, University of Bath, 2009. https://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.512372.

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The Prion protein (PrP) is a cell surface glycoprotein that has been directly implicated in the pathogenesis of a range of neurological disorders referred to as the transmissible spongiform encephalopathies (TSE’s). The protein has been shown to bind copper within its unstructured N-terminus but the affinity and stoichiometry of the association is a matter of some debate. In addition, the functional significance of this copper binding has yet to be elucidated. This study aimed to determine accurate metal binding parameters for PrP through the use of calorimetry and to provide insight into the potential redox implications of metal once bound. A method of analysis for complex binding to proteins is thoroughly assessed and found to be suitable. The study also aimed to qualify the involvement of metals in the proteins remarkable ability to survive in the environment. This study confirms that PrP binds copper with an affinity relative to the amount of copper available to the protein. A high nanomolar affinity is reported within two regions on the protein, the octarepeat and the 5th site. Binding within the octarepeat region is found to be highest at low copper concentrations, reducing to micromolar affinity when copper levels exceed equivalents of 1. There is also strong evidence of a complex and cooperative binding mechanism. The 5th site also displays high nanomolar affinity for a single atom of copper. These two regions on the protein also interact in the coordination of copper (II). The copper bound protein is highly redox active and is capable of fully reversible cycling of electrons that are dependent mainly on the octarepeat. The protein does bind other divalent cations but none appear to be physiologically relevant considering the amount of these free metal ions in the body. When adsorbed to model clays, PrP is able to survive for long periods at room temperature. This longevity is increased significantly by the presence of metals in the soil, especially manganese. These data provide confirmation of the precise parameters of divalent cation binding to PrP. It also confirms that the copper bound protein is capable of a physiological redox role.
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Steele, Andrew D. Ph D. Massachusetts Institute of Technology. "Prion protein in health and disease." Thesis, Massachusetts Institute of Technology, 2008. http://hdl.handle.net/1721.1/42396.

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Thesis (Ph. D.)--Massachusetts Institute of Technology, Dept. of Biology, 2008.
Includes bibliographical references.
The prion protein (PrP) is a conserved glycoprotein tethered to cell membranes by a glycosylphosphatidylinositol anchor. In mammals, PrP is expressed in many tissues, most abundantly in brain, heart, and muscle. Importantly, PrP is required for prion diseases, which are neurodegenerative diseases associated with misfolding and aggregation of PrP. PrP can adopt a self-perpetuating conformation that templates the misfolding of normal PrP molecules into its pathogenic conformation, termed PrPsC. The role of PrPSC in the pathogenesis of prion diseases, or transmissible spongiform encephalopathies, has been studied intensively yet the mechanism by which PrP misfolding in neurons leads to injury and death remains enigmatic. Much less attention has been focused on the role of PrP in normal physiology despite the possibility that deciphering PrP's normal function could help to understand prion diseases. My thesis work has spanned both the study of the normal function of PrP and the neurotoxic pathways that are involved in prion pathogenesis. Because prion disease and other neurodegenerative diseases share protein misfolding as the primary etiology, I aimed to determine whether PrP contributed to other neurodegenerative diseases apart from prion diseases. We deleted PrP from several well established transgenic mouse models of neurodegenerative disease, including Tauopathy, Parkinson's and Huntington's diseases. Deleting PrP did not substantially alter the disease phenotypes of the models that we tested, suggesting that PrP is not a major contributor to or protector against these disorders. In addition, in collaborative efforts we determined that PrP knockout mice have defects in hematopoiesis and neurogenesis.
(cont.) Hematopoietic stem cells from PrP knockout mice have defects in self-renewal, as manifested during serial bone marrow transplantation or during the aging process. PrP knockout mice also display a slight reduction in cellular proliferation and/or neurogenesis in the adult brain. I also participated in the development of a video based behavior recognition system. We used this system to quantify the home cage behavioral changes in two mouse models of neurodegeneration, Huntington's disease and prion disease. Because studies of prion disease have been focused primary on the pathological level, I have attempted to elucidate the molecular pathways responsible for mediating neurotoxicity in a mouse model of infectious prion disease. In the first series of studies we tested whether apoptotoic cell death pathways are activated in prion disease. We inoculated mice deficient for Caspase-12 and Bax, both of which have been implicated in mediating prion toxicity, but did not observe any protection against disease in these mice. Also, neuronal overexpression of Bcl-2 did not protect against prion toxicity and instead, inhibition of apoptosis may have enhanced several aspects of disease (as did deletion of Bax). In a second attempt at determining pathways involved in prion toxicity, I determined that deletion of heat shock factor 1 (Hsfl), a stress responsive transcription factor, protects against prion toxicity. Mice that are deficient for Hsfl succumb to prion disease faster than controls, despite similar pathological and behavioral onset.
by Andrew D. Steele.
Ph.D.
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Young, Duncan Scott. "Post-translational modifications of prion protein." Thesis, University of Cambridge, 2005. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.615154.

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Books on the topic "Prion protein"

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Hill, Andrew F., ed. Prion Protein Protocols. Totowa, NJ: Humana Press, 2008. http://dx.doi.org/10.1007/978-1-59745-234-2.

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Zhang, Jiapu. Molecular Dynamics Analyses of Prion Protein Structures. Singapore: Springer Singapore, 2018. http://dx.doi.org/10.1007/978-981-10-8815-5.

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Fatal flaws: How a misfolded protein baffled scientists and changed the way we look at the brain. New Haven: Yale University Press, 2013.

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Fatal flaws: How a misfolded protein baffled scientists and changed the way we look at the brain. Toronto, Ont: HarperCollins, 2012.

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Ridley, Rosalind M. Fatal protein: The story of CJD, BSE, and other prion diseases. Oxford: Oxford University Press, 1998.

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Silverman, Gregory Lindsay. Identification and characterization of proteins binding to the amino-terminus of the human prion protein. Ottawa: National Library of Canada, 1999.

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The pathological protein: Mad Cow, Chronic Wasting, and other deadly prion diseases. New York: Copernicus, 2003.

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Loftus, Brendan. Analysis of the prion protein (PrP) and PrP genes from Ovis aries and Oryctalagus cuniculus. Dublin: University College Dublin, 1996.

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Dr, Soto Claudio, ed. Prions: The new biology of proteins. Boca Raton, FL: CRC/Taylor & Francis, 2006.

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Tatzelt, Jörg, ed. Prion Proteins. Berlin, Heidelberg: Springer Berlin Heidelberg, 2011. http://dx.doi.org/10.1007/978-3-642-24067-6.

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Book chapters on the topic "Prion protein"

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Donato, Dominique M., Steven K. Hanks, Kenneth A. Jacobson, M. P. Suresh Jayasekara, Zhan-Guo Gao, Francesca Deflorian, John Papaconstantinou, et al. "Prion Protein." In Encyclopedia of Signaling Molecules, 1462. New York, NY: Springer New York, 2012. http://dx.doi.org/10.1007/978-1-4419-0461-4_101083.

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Donato, Dominique M., Steven K. Hanks, Kenneth A. Jacobson, M. P. Suresh Jayasekara, Zhan-Guo Gao, Francesca Deflorian, John Papaconstantinou, et al. "Prion Protein (PRNP)." In Encyclopedia of Signaling Molecules, 1462–77. New York, NY: Springer New York, 2012. http://dx.doi.org/10.1007/978-1-4419-0461-4_390.

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Rigter, Alan, Jan Priem, Drophatie Timmers-Parohi, Jan Pm Langeveld, and Alex Bossers. "Mapping Functional Prion–Prion Protein Interaction Sites Using Prion Protein Based Peptide-Arrays." In Peptide Microarrays, 257–71. Totowa, NJ: Humana Press, 2009. http://dx.doi.org/10.1007/978-1-60327-394-7_12.

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Zou, Wen-Quan. "Insoluble Cellular Prion Protein." In Prions and Diseases, 67–82. New York, NY: Springer New York, 2012. http://dx.doi.org/10.1007/978-1-4614-5305-5_5.

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Sim, Valerie L., and Byron Caughey. "Prion Disease Therapy: Trials and Tribulations." In Protein Misfolding Diseases, 259–303. Hoboken, NJ, USA: John Wiley & Sons, Inc., 2010. http://dx.doi.org/10.1002/9780470572702.ch13.

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Kitamoto, T., and J. Tateishi. "Human Prion Disease and Human Prion Protein Disease." In Current Topics in Microbiology and Immunology, 27–34. Berlin, Heidelberg: Springer Berlin Heidelberg, 1996. http://dx.doi.org/10.1007/978-3-642-60983-1_3.

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Kretzschmar, H. A., T. Tings, A. Madlung, A. Giese, and J. Herms. "Function of PrPC as a copper-binding protein at the synapse." In Prion Diseases, 239–49. Vienna: Springer Vienna, 2000. http://dx.doi.org/10.1007/978-3-7091-6308-5_23.

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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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Caughey, Byron, and Gregory J. Raymond. "Protease-Resistant Prion Protein Formation." In Prions and Brain Diseases in Animals and Humans, 217–24. Boston, MA: Springer US, 1998. http://dx.doi.org/10.1007/978-1-4899-1896-3_22.

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Bonomo, R. P., D. Grasso, G. Grasso, V. Guantieri, G. Impellizzeri, C. Rosa, D. Milardi, G. Pappalardo, G. Tabbì, and E. Rizzarelli. "Metal Binding to Prion Protein." In Metal-Ligand Interactions, 21–39. Dordrecht: Springer Netherlands, 2003. http://dx.doi.org/10.1007/978-94-010-0191-5_2.

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Conference papers on the topic "Prion protein"

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Zou, Wen-Quan, and Jue Yuan. "Prion protein and human cognition." In 2010 9th IEEE International Conference on Cognitive Informatics (ICCI). IEEE, 2010. http://dx.doi.org/10.1109/coginf.2010.5599805.

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Zawada, Zbigniew, Martin Šafařík, Jaroslav Šebestík, Ivan Stibor, and Petr Bouř. "Reaction of prion protein with quinacrine." In XIIth Conference Biologically Active Peptides. Prague: Institute of Organic Chemistry and Biochemistry, Academy of Sciences of the Czech Republic, 2011. http://dx.doi.org/10.1135/css201113163.

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Han, Yipeng, and Guangjie Chen. "A Method of Analyzing the Structures of Misfolding Proteins like Prion Protein." In 2008 2nd International Conference on Bioinformatics and Biomedical Engineering (ICBBE '08). IEEE, 2008. http://dx.doi.org/10.1109/icbbe.2008.66.

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Frankiewicz, Lukasz P., Wiktor Banachewicz, and Aleksandra Misicka. "Aggregation studies of β-amyloid and prion protein fragments." In IXth Conference Biologically Active Peptides. Prague: Institute of Organic Chemistry and Biochemistry, Academy of Sciences of the Czech Republic, 2005. http://dx.doi.org/10.1135/css200508023.

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Šebestík, Jaroslav, Alexandr Pavlíček, Martin Šafařík, Karel Holada, Jan Hlaváček, and Ivan Stibor. "Acridine nucleophilic displacement – possible culprit of acridine interaction with prion protein." In Xth Conference Biologically Active Peptides. Prague: Institute of Organic Chemistry and Biochemistry, Academy of Sciences of the Czech Republic, 2007. http://dx.doi.org/10.1135/css200709093.

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PICCARDO, PEDRO, BERNARDINO GHETTI, FABRIZIO TAGLIAVINI, and ORSO BUGIANI. "STRUCTURAL VARIATIONS OF ABNORMAL PRION PROTEIN IN GERSTMANN-STRÄUSSLER-SCHEINKER DISEASE." In Proceedings of the International Seminar on Nuclear War and Planetary Emergencies — 26th Session. WORLD SCIENTIFIC, 2002. http://dx.doi.org/10.1142/9789812776945_0048.

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Zhai, Ying, Na Li, Dachuan Zhang, Qi Li, Guoping Zhou, Rui Li, and Zhiguo Liu. "A Unique Functional Feature of the Recombinant Bovine Prion Protein Fragment." In International Conference on Medical Engineering and Bioinformatics. Southampton, UK: WIT Press, 2014. http://dx.doi.org/10.2495/meb140421.

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Wang, Ye. "The Molecular Dynamics Study on the stability of Elk Prion Protein." In ICBBE '20: 2020 7th International Conference on Biomedical and Bioinformatics Engineering. New York, NY, USA: ACM, 2020. http://dx.doi.org/10.1145/3444884.3444904.

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Wang, Yiwei, Lan Zhou, and Wei Xin. "Abstract 5207: Targeting prion protein as a potential oncogene in pancreatic cancer." In Proceedings: AACR 104th Annual Meeting 2013; Apr 6-10, 2013; Washington, DC. American Association for Cancer Research, 2013. http://dx.doi.org/10.1158/1538-7445.am2013-5207.

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Xia, Kui, Xinpeng Li, Jingjing Xue, Damao Xun, and Rongri Tan. "The Effect of Ethanol on Mutant Human Prion Protein using Molecular Dynamics Simulations." In BIC 2022: 2022 2nd International Conference on Bioinformatics and Intelligent Computing. New York, NY, USA: ACM, 2022. http://dx.doi.org/10.1145/3523286.3524536.

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Reports on the topic "Prion protein"

1

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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Chen, Shu G. Characterization of Antibody Specific for Disease Associated Prion Protein. Fort Belvoir, VA: Defense Technical Information Center, July 2004. http://dx.doi.org/10.21236/ada432993.

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Constantine, Niel T. Ultra-Sensitive Detection of Prion Protein in Blood Using Isothermal Amplification Technology. Fort Belvoir, VA: Defense Technical Information Center, December 2005. http://dx.doi.org/10.21236/ada455290.

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McGuirl, Michele A. Elucidation of Prion Protein Conformational Changes Associated With Infectivity by Fluorescence Spectroscopy. Fort Belvoir, VA: Defense Technical Information Center, June 2004. http://dx.doi.org/10.21236/ada426340.

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McGuirl, Michele A., and Jessica Gilbert. Elucidation of Prion Protein Conformational Changes Associated with Infectivity by Fluorescence Spectroscopy. Fort Belvoir, VA: Defense Technical Information Center, June 2007. http://dx.doi.org/10.21236/ada575958.

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McGuirl, Michele. Elucidation of Prion Protein Conformational Changes Associated with Infectivity by Fluorescence Spectroscopy. Fort Belvoir, VA: Defense Technical Information Center, June 2006. http://dx.doi.org/10.21236/ada462868.

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Wemmer, David E. New Structural Approaches to Understand the Disease Related Forms of the Prion Protein. Fort Belvoir, VA: Defense Technical Information Center, July 2005. http://dx.doi.org/10.21236/ada446341.

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