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Relevant bibliographies by topics / Prion diseases

Academic literature on the topic 'Prion diseases'

Author: Grafiati

Published: 4 June 2021

Last updated: 28 July 2024

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Journal articles on the topic "Prion diseases"

1

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

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

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

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Yokoyama, Takashi, and Shirou Mohri. "Prion Diseases and Emerging Prion Diseases." Current Medicinal Chemistry 15, no. 9 (April 1, 2008): 912–16. http://dx.doi.org/10.2174/092986708783955437.

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Gambetti, P. "Approaches to Prions: Prion Diseases." Science 273, no. 5278 (August 23, 1996): 1052b—1053b. http://dx.doi.org/10.1126/science.273.5278.1052b.

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SKRIPCHENKO, E. YU, K. V. MARKOVA, N. V. SKRIPCHENKO, and A. V. GOLUBEVA. "Prions and prion diseases: myths and reality." Practical medicine 22, no. 1 (2024): 8–13. http://dx.doi.org/10.32000/2072-1757-2024-1-8-13.

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The article contains modern data about prions and the main prion-associated diseases. The authors describe the main conditions that provide prion-associated infectious diseases, primarily the conformation changes of protein PrPС expressed in healthy tissues of humans and animals and forming the pathogenic PrPSc protein. All prion-caused diseases are considered to be neurodegenerative with fatal outcomes due to a specific spongy brain damage. Information on some aspects of pathogenesis and therapeutic options for prion diseases is presented. The data on the prion safety of biological preparations widely used in healthcare are also presented.

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Belay, Ermias D. "Prions and Prion Diseases: Current Perspectives." Emerging Infectious Diseases 10, no. 12 (December 2004): 2265–66. http://dx.doi.org/10.3201/eid1012.3040847.

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Gamage, R. "Prion diseases." Ceylon Medical Journal 45, no. 1 (January 20, 2015): 3. http://dx.doi.org/10.4038/cmj.v45i1.7941.

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Sánchez-Valle, Raquel. "Prion diseases." European Neuropsychopharmacology 55 (February 2022): 1–3. http://dx.doi.org/10.1016/j.euroneuro.2021.09.008.

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Caramelli, Maria, Giuseppe Ru, Pierluigi Acutis, and Gianluigi Forloni. "Prion Diseases." CNS Drugs 20, no. 1 (2006): 15–28. http://dx.doi.org/10.2165/00023210-200620010-00002.

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Dissertations / Theses on the topic "Prion diseases"

1

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

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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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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.
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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Pennington, Catherine Margaret. "Genetic aspects of human prion diseases." Thesis, University of Edinburgh, 2013. http://hdl.handle.net/1842/24216.

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Introduction: Human prion diseases are progressive, fatal neurological conditions linked to conformational changes in the structure of the prion protein. Prion diseases may be sporadic (sporadic Creutzfeldt-Jakob disease or sCJD, Sporadic Fatal Insomnia), acquired (variant CJD, iatrogenic CJD, kuru) or genetic (genetic prion disease, gPD). gPD is due to a disease-specific point or octapeptide repeat insertion (OPRI) mutation in the prion protein gene (PRNP). Numerous different PRNP mutations have been described. In some cases of gPD the phenotype may closely resemble that of sCJD, and it can be impossible to distinguish sporadic from genetic cases without genetic screening. The clinico-pathological phenotype of gPD is highly variable, both between different mutations and even within families carrying the same mutation. This variability can be partly explained by a polymorphism at codon 129 of PRNP. Codon 129 encodes either methionine or valine, and the status of both the mutated and wild-type alleles may influence disease susceptibility and phenotype. Codon 129 may also affect the manifestations of sporadic and acquired prion disease. Homozygosity for methionine at codon 129 is over-represented in both sporadic CJD (sCJD) and variant CJD (vCJD); indeed all definite or probable clinical cases of vCJD seen to date have been homozygous for methionine. Other polymorphisms of PRNP have been found in a small number of patients with sporadic and variant CJD. The significance of these polymorphisms has not been fully investigated. It is likely that other, as yet unidentified, genetic factors also play a role in influencing susceptibility to prion diseases and the clinico-pathological phenotype. A recent genome wide association study of vCJD patients found codon 129 to be the main genetic risk factor for vCJD, but did identify other candidate loci that may contribute to disease susceptibility. Work is in progress to carry out genomic screens for other, novel polymorphisms in 309 patients with sCJD and 118 patients with vCJD. Aims: The aims of the work described in this MD thesis are: 1) To review all cases of gPD on the database of the National Creutzfeldt-Jakob Disease Research and Surveillance Unit. The clinico-pathological phenotype, investigative findings and family history will be reviewed in detail. The findings will be compared with those cases of gPD previously described, in particular with cases seen in other European countries. The incidence and prevalence of these diseases in the UK will also be assessed. 2) To review cases of sCJD and vCJD with novel PRNP polymorphisms of uncertain significance. The clinico-pathological phenotype will be reviewed in detail to attempt to establish if these novel polymorphisms exert any influence over disease susceptibility or phenotype. Results: 159 cases of gPD were identified between 1970 and 2009, representing 7.8% of the prion disease (of any type) cases referred to the NCJDRSU over this time period. 17 different PRNP haplotypes were identified: P102L-129M, P105L-129V, A117V-129V, S132I-129M, Y163X, D167G-129M, D178N-129M, D178N-129V, E200K-129M, D202N-129V, V210I-129M, Q212P-129M, 2-OPRI, 4-OPRI, 5- OPRI, 6-OPRI, 7-OPRI. The clinicopathological phenotypes were highly variable and often difficult to distinguish from sCJD. The highest number of cases was caused by the 6-OPRI, most of which belonged to a single kindred. Several cases in the 4-OPRI group were found to share an additional risk allele, rsl029273C. In may be that this mutation is not pathogenic unless this risk allele is also present. This raises the possibility that other as yet unidentified genetic risk factors exist which influence gPD susceptibility and clinicopathological phenotype. Overall 61.4% of cases tested had a positive cerebrospinal fluid (CSF) 14-3-3, 90.0% an elevated SI00b, 23.1% had Magnetic Resonance Imaging (MRI) of the brain showing basal ganglia or cortical high signal, and 18.1% had an electroencephalogram (EEG) showing triphasic periodic complexes. A positive family history of prion disease was present in 57.9% of cases. Discussion: The range of point mutations and OPRI seen in the UK is considerable, but the majority of cases were due to 6-OPRI, E200K, or PI 02L. The UK differs from the rest of the world in that E200K is not the commonest mutation, due to the presence of a large British kindred with the 6-OPRI. Even within the larger kindreds, the clinicopathological phenotype remained very variable. Some distinctive features which may act as pointers towards gPD were found, such as a linear pattern of PrPSc deposition in the cerebellum seen in E200K-129M cases. Analysing the data in the smaller groups should be done with caution, and further large international studies are needed in order to truly determine the influence of factors such as codon 129 status. As with other forms of prion disease, there is an excess of individuals with methionine homozygosity at codon 129. It is unclear whether or not PRNP mutations in cis with valine at codon 129 will result in prion disease at an older age or with a different phenotype, or if these are not actually pathogenic in this genetic context. In the case of 4-OPRI, it appears that an additional risk allele is required for the development of disease, and it remains to be seen if other additional genetic factors will be found to influence disease susceptibility and phenotype. A relatively small percentage of cases had EEGs showing periodic triphasic waves, or basal ganglia or cortical high signal on MRI. CSF SI00b was more sensitive than 14-3-3, the reverse of the pattern seen in sCJD. A pattern of a negative 14-3-3 and a very high SI00b should lead to suspicions of gPD. The current diagnostic criteria for gPD are relatively strict, and may exclude some individuals who have neuropathologically confirmed prion disease (without PRNP genotyping) and several second degree relatives with gPD. This is a potential problem, especially as the neuropathological appearances cannot be relied upon to distinguish sporadic from genetic disease. Particular attention should be paid to the family history and any subtle unusual neuropathological appearances to try and reduce the risk of gPD cases being missed. In conclusion, gPD remains a difficult condition to diagnose and study. Large systematic collaborative studies are essential to increase our understanding of these rare conditions.

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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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Glatzel, Markus. "Epidemiology and molecular pathology of prion diseases /." Zürich, 2003. http://opac.nebis.ch/cgi-bin/showAbstract.pl?sys=000253382.

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Jones, Daryl Rhys. "Treatment of prion diseases with camelid antibodies." Thesis, Royal Veterinary College (University of London), 2013. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.618290.

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Spagnolli, Giovanni. "Folding, Misfolding and Therapeutics in Prion Diseases." Doctoral thesis, Università degli studi di Trento, 2021. http://hdl.handle.net/11572/308935.

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Prion diseases are rare neurodegenerative disorders affecting humans and other animals, caused by a proteinaceous infectious agent named prion. The pivotal event in these pathologies is the conversion of PrPC, a physiologically expressed protein of poorly characterized function, into a misfolded conformer, named PrPSc, which is capable of replicating its conformationally-encoded information by inducing the conversion of its physiological counterpart. The aggregates resulting from this misfolding process accumulate in the central nervous system of affected organisms leading to neuronal death. Prion diseases are always fatal and no therapy is currently available. The lack of an effective therapeutic strategy to tackle such conditions is the result of the poor available information regarding many aspects of PrPSc, such as its structure, pathogenicity, and its replication mechanism. To complicate things further, PrPSc can appear as a set of distinct conformers, named strains, characterized by the capacity to evolve through modification and selection of their conformations, promoting resistance to treatments. In this work, we focus on two main aspects of prion biology, the elucidation of prion structure and propagation, and the development of a novel pharmacological strategy to tackle prion diseases. In both projects, we exploited the potential of integrative schemes combining computational methods and experimental data. Such approaches allowed us to build a plausible atomistic model of PrPSc and to propose a propagation mechanism describing the series of events underlying prion propagation. Moreover, the application of advanced computational schemes enabled us to identify a PrP folding intermediate displaying unique druggability properties. By exploiting the structural information of this protein conformer we identified a compound capable of acting as a pharmacological degrader for PrP by interfering with its folding pathway. Overall, this work highlights how the integration of computational and experimental methods is an extremely valuable scheme to answer complex biological questions, such as unraveling the mechanisms of protein misfolding and providing the tools to design pharmacological strategies for untreatable diseases.

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Spagnolli, Giovanni. "Folding, Misfolding and Therapeutics in Prion Diseases." Doctoral thesis, Università degli studi di Trento, 2021. http://hdl.handle.net/11572/308935.

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Prion diseases are rare neurodegenerative disorders affecting humans and other animals, caused by a proteinaceous infectious agent named prion. The pivotal event in these pathologies is the conversion of PrPC, a physiologically expressed protein of poorly characterized function, into a misfolded conformer, named PrPSc, which is capable of replicating its conformationally-encoded information by inducing the conversion of its physiological counterpart. The aggregates resulting from this misfolding process accumulate in the central nervous system of affected organisms leading to neuronal death. Prion diseases are always fatal and no therapy is currently available. The lack of an effective therapeutic strategy to tackle such conditions is the result of the poor available information regarding many aspects of PrPSc, such as its structure, pathogenicity, and its replication mechanism. To complicate things further, PrPSc can appear as a set of distinct conformers, named strains, characterized by the capacity to evolve through modification and selection of their conformations, promoting resistance to treatments. In this work, we focus on two main aspects of prion biology, the elucidation of prion structure and propagation, and the development of a novel pharmacological strategy to tackle prion diseases. In both projects, we exploited the potential of integrative schemes combining computational methods and experimental data. Such approaches allowed us to build a plausible atomistic model of PrPSc and to propose a propagation mechanism describing the series of events underlying prion propagation. Moreover, the application of advanced computational schemes enabled us to identify a PrP folding intermediate displaying unique druggability properties. By exploiting the structural information of this protein conformer we identified a compound capable of acting as a pharmacological degrader for PrP by interfering with its folding pathway. Overall, this work highlights how the integration of computational and experimental methods is an extremely valuable scheme to answer complex biological questions, such as unraveling the mechanisms of protein misfolding and providing the tools to design pharmacological strategies for untreatable diseases.

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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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Books on the topic "Prion diseases"

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1942-, Prusiner Stanley B., and Ridley Rosalind M, eds. Prion biology and diseases. Cold Spring Harbor, New York: Cold Spring Harbor Laboratory Press, 1999.

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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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Groschup, Martin H., and Hans A. Kretzschmar, eds. Prion Diseases. Vienna: Springer Vienna, 2000. http://dx.doi.org/10.1007/978-3-7091-6308-5.

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Liberski, Pawel P., ed. Prion Diseases. New York, NY: Springer New York, 2017. http://dx.doi.org/10.1007/978-1-4939-7211-1.

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F, Baker Harry, and Ridley Rosalind M, eds. Prion diseases. Totowa, N.J: Humana Press, 1996.

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MD, Collinge John, and Palmer Mark S, eds. Prion diseases. Oxford: Oxford University Press, 1997.

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

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O, Morrison Douglas R., North Atlantic Treaty Organization. Scientific Affairs Division., and NATO Advanced Research Workshop on Prions and Brain Diseases in Animals and Humans (1996 : Erice, Italy), eds. Prions and brain diseases in animals and humans. New York: Plenum Press, in cooperation with NATO Scientific Affairs Division, 1998.

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Prion biology: Research and advances. Toronto: Apple Academic Press, 2013.

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F, Baker Harry, ed. Molecular and cellular pathology in prion disease. Totowa, N.J: Humana Press, 2001.

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Book chapters on the topic "Prion diseases"

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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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Whitechurch, Benjamin C., Jeremy M. Welton, Steven J. Collins, and Victoria A. Lawson. "Prion Diseases." In Advances in Neurobiology, 335–64. Cham: Springer International Publishing, 2017. http://dx.doi.org/10.1007/978-3-319-57193-5_13.

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Belay, Ermias D., and Jason C. Bartz. "Prion Diseases." In Viral Infections of Humans, 1165–86. Boston, MA: Springer US, 2014. http://dx.doi.org/10.1007/978-1-4899-7448-8_47.

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Gelpi, Ellen, and Herbert Budka. "Prion Diseases." In International Neurology, 336–39. Oxford, UK: Wiley-Blackwell, 2010. http://dx.doi.org/10.1002/9781444317008.ch91.

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Nasralla, Salam, Daniel D. Rhoads, and Brian S. Appleby. "Prion Diseases." In Current Clinical Neurology, 365–80. Cham: Springer International Publishing, 2020. http://dx.doi.org/10.1007/978-3-030-56084-3_18.

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Mead, Simon, and Peter Rudge. "Prion Diseases." In Neurodegenerative Disorders, 213–31. Cham: Springer International Publishing, 2016. http://dx.doi.org/10.1007/978-3-319-23309-3_12.

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Mead, Simon, and Peter Rudge. "Prion Diseases." In Neurodegenerative Disorders, 197–224. London: Springer London, 2011. http://dx.doi.org/10.1007/978-1-84996-011-3_10.

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Beckerman, Martin. "Prion Diseases." In Biological and Medical Physics, Biomedical Engineering, 191–222. Cham: Springer International Publishing, 2015. http://dx.doi.org/10.1007/978-3-319-22117-5_7.

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Gelpi, Ellen, and Herbert Budka. "Prion diseases." In International Neurology, 296–99. Chichester, UK: John Wiley & Sons, Ltd, 2016. http://dx.doi.org/10.1002/9781118777329.ch78.

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Kong, Qingzhong, and Richard A. Bessen. "Prion Diseases." In Neuroimmune Pharmacology, 517–31. Cham: Springer International Publishing, 2016. http://dx.doi.org/10.1007/978-3-319-44022-4_34.

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Conference papers on the topic "Prion diseases"

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Borovečki, Fran. "Prion associated dementia." In Rijeka Forum on Neurodegenerative Diseases (2 ; 2018 ; Rijeka). Hrvatska akademija znanosti i umjetnosti, 2019. http://dx.doi.org/10.21857/9e31lhne3m.

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Dzagakhova, Agunda Vladimirovna, and Laura Paatovna Dzhabieva. "Pharmacology relevance of prion diseases." In International Research-to-practice Conference for students. TSNS Interaktiv Plus, 2016. http://dx.doi.org/10.21661/r-115103.

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Shamsir, Mohd Shahir, Zeti Azura Hussein, and Johan Sharif. "Unravelling Prion Diseases Using Molecular Dynamics Simulations." In 2008 Second Asia International Conference on Modelling & Simulation (AMS). IEEE, 2008. http://dx.doi.org/10.1109/ams.2008.31.

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"Study of the diagnosis and treatment of prion diseases." In International Conference on Medicine, Public Health and Biological Sciences. CASRP Publishing Company, Ltd. Uk, 2016. http://dx.doi.org/10.18869/mphbs.2016.05.

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Smid, Jerusa, Ricardo Nitrini, Vilma Martins, Michele Landemberger, Helio Gomes, Nathalie Canedo Canedo, and Leila Chimelli. "THE BRAZILIAN SURVEILLANCE FOR PRION DISEASE: CURRENT DATA." In XIII Meeting of Researchers on Alzheimer's Disease and Related Disorders. Zeppelini Editorial e Comunicação, 2021. http://dx.doi.org/10.5327/1980-5764.rpda014.

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Background: The Brazilian Surveillance for Prion Disease began in 2005 with compulsory notification of suspected cases. Objective: To determine the diagnosis of reported patients to the Brazilian Surveillance for Prion Disease and evaluate the clinical and genetic data. Methods: Data from the notification sheet were collected and patients were classified according to current clinical and pathological criteria. Results: 757 cases were notified from 2005 to 2019. 51 cases were defined DCJ, 295 probable DCJ, 172 possible DCJ and 38 genetic DCJ. 55 patients had other diagnosis and 146 were unclassified (missing data). The most frequent mutations were E200K, D178N, P102L and V180I. Among defined and probable DCJ: 55% were female, mean age was 62 y.o. and median age was 61.9 y.o.; 51.8% were M129M and 23.2% V129V. CSF 14.3.3 was positive in 69.2%, disease-typical EEG findings were observed in 42.3% and MRI revealed typical findings in 76.9%. No variant CJD were diagnosed. Discussion: considering the Brazilian population and the prevalence of CJD worldwilde, we expected more cases of CJD than were notified. Methionine and valine homozygotes are overrepresented, in agreement with international data. MRI were the more useful subsidiary test for clinical classification.. Conclusion: besides the undernotification, the Brazilian surveillance for prion diseases evaluated 757 suspected cases in the last 15 years. 50.7% were probable, defined CJD or genetic prion disease.

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Guelli, Mariana Sandoval Terra Campos, Daniela Bastos de Almeida Zampier, Lorena Araújo Silva Dias, and Marina de Oliveira Nunes Ibrahim. "Creutzfeldt-Jakob Disease - a literature review." In XIII Congresso Paulista de Neurologia. Zeppelini Editorial e Comunicação, 2021. http://dx.doi.org/10.5327/1516-3180.126.

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Background: Creutzfeldt-Jakob disease (CJD) is a progressive, rare, fatal and rapid human neurodegenerative disease that occurs in the etiologies: sporadic (CJD), familial, iatrogenic (CJD) and CJD variant (CJV) in which cell prion protein (PrP) can be transmitted through animals. Objectives: Literature review about Creutzfeldt-Jakob diseaseDesign and setting: Literature review development in the Centro Universitário de Volta Redonda, Rio de Janeiro, Brazil. Methods: The Creutzfeldt-Jakob disease, infectious diseases and neuroinfection indexes were used in the PUBMED and Scielo databases. Results:CJD has different etiologies with different clinical and pathological phenotypes. CJDV shows psychiatric behaviors and symptoms followed by abnormalities, ataxia and dementia. The sporadic form is the most common, with a progressive clinical course with generalized brain deposition of abnormal prion protein aggregates (PrPTSE) that leads to spongiform change, gliosis and neuronal loss. CJD progresses to dementia and two or more symptoms: cerebellar or visual impairments; pyramidal or extrapyramidal signs; myoclonus; and akinetic mutism. Complex periods of acute wave in the electroencephalogram (EEG) are strongly suggestive of prionic diseases. Rapidly evolving field neuroimmune disorders have shown an increasing in autoantibody testing; attempt to diagnose a range of immune-mediated conditions. Evidence indicates that diffusion-weighted magnetic resonance imaging (DWI) is more sensitive for detecting signal abnormalities. Conclusion: The disease progresses to dementia, accompanied by myoclonus, pyramidal signs and characteristic EEG. It is a complex pathology, which has only symptomatic treatment and requires strict control of reservoirs and risk of contamination.

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Athamneh, Ahmad, and Justin Barone. "Enzyme-Mediated Self-Assembly of Highly Ordered Structures From Disordered Proteins." In ASME 2008 Conference on Smart Materials, Adaptive Structures and Intelligent Systems. ASMEDC, 2008. http://dx.doi.org/10.1115/smasis2008-540.

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Trypsin hydrolysis of wheat gluten produced glutamine-rich short peptides with a tendency to self-assemble into supermolecular structures extrinsic to native wheat gluten. Fourier transform infrared and X-ray diffraction data suggested that the new structures formed resembled that of cross-β amyloid fibrils found in some insect silk and implicated in prion diseases. The superstructures were about 10 μm in diameter with clear right-handed helical configuration and appeared to be bundles of smaller fibrils of about 63 nm in diameter. Results demonstrate the potential for utilizing cheap protein sources and natural mechanisms of protein self-assembly to design advanced nanomaterials that can provide a wide range of structural and chemical functionality.

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Ourselin, Sébastien, Simon Mead, Marc Modat, Liane Canas, Benjamin Yvernault, Carole Sudre, Enrico De Vita, M. Jorge Cardoso, John Thornton, and Frederik Barkhof. "Imaging biomarkers for the diagnosis of Prion disease." In Image Processing, edited by Elsa D. Angelini and Bennett A. Landman. SPIE, 2018. http://dx.doi.org/10.1117/12.2293676.

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Pham, L. H. L., and C. Landeen. "New Onset Refractory Status Epilepticus in Prion Disease." In American Thoracic Society 2024 International Conference, May 17-22, 2024 - San Diego, CA. American Thoracic Society, 2024. http://dx.doi.org/10.1164/ajrccm-conference.2024.209.1_meetingabstracts.a5614.

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Barannyk, Oleksandr, Satya Karri, and Peter Oshkai. "In Vitro Study of the Influence of the Aortic Root Geometry on Flow Characteristics of a Prosthetic Heart Valve." In ASME 2013 Pressure Vessels and Piping Conference. American Society of Mechanical Engineers, 2013. http://dx.doi.org/10.1115/pvp2013-97105.

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In this paper, performance of aortic heart valve prosthesis in different geometries of the aortic root is investigated experimentally. The objective of this investigation is to establish a set of parameters, which are associated with abnormal flow patterns due to the flow through a prosthetic heart valve implanted to the patients that had certain types of valve diseases prior to the valve replacement. Specific valve diseases, classified into two clinical categories, were correlated with the corresponding changes of aortic root geometry. These categories correspond to aortic valve stenosis and aortic valve insufficiency. The control case that corresponds to the aortic root of a patient without valve disease was used as a reference. Experiments were performed at test conditions corresponding to 70 beats/min, 5.5 L/min target cardiac output and a mean aortic pressure of 100 mmHg. By varying the aortic root geometry, it was possible to investigate corresponding changes in the levels of Reynolds shear stress and establish the possibility of platelet activation and, as a result of that, the formation of blood clots.

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Reports on the topic "Prion diseases"

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Cox, Daniel L., and Rajiv R. Singh. Theoretical Modeling of Molecular Mechanisms, Time Scales, and Strains in Prion Diseases. Fort Belvoir, VA: Defense Technical Information Center, July 2006. http://dx.doi.org/10.21236/ada462946.

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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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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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Sonia Vallabh & Eric Minikel, Sonia Vallabh &. Eric Minikel. Can anle138b delay the onset of genetic prion disease? Experiment, May 2013. http://dx.doi.org/10.18258/0558.

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Young, Alan J. Migratory Leukocytes in the Pathogenesis and Diagnosis of Prion Disease. Fort Belvoir, VA: Defense Technical Information Center, June 2004. http://dx.doi.org/10.21236/ada426355.

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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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Zuckermann, Ronald. Molecular Recognition of Protein Nanofibers as a Basis for Prior Disease Diagnostics. Office of Scientific and Technical Information (OSTI), February 2012. http://dx.doi.org/10.2172/1331981.

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