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2022, Number 3

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Rev Neurol Neurocir Psiquiat 2022; 50 (3)

Prion diseases and prion-like diseases

Castillo-Juárez JC, Batres-Godoy SS, Calderón MJ, Solís-Aguilar R, Palencia AE, Silva-Arévalo G

Language: Spanish
References: 97
Page: 94-105
PDF size: 244.01 Kb.


ABSTRACT

Prion diseases are a group of neurodegenerative diseases with a global impact of 1 to 2 cases per million, mostly ignored by the physician. Even though these diseases affect primarily the central nervous system, recently, alterations in diverse systems of the organism have been found. On the other hand, it has been shown that neuro-degenerative diseases like Parkinson and Alzheimer disease, possess similar mechanisms in their physiopathology to those found in prion disease. The objective of this review is to contribute knowledge and comprehension about epidemiology, etiology, clinical manifestations, diagnosis and the current state of researches for possible treatments on prion disease. This was done through researching information from PubMed, Science Direct, Europe PMC, Google Scholar, Scielo y Redalyc. It was pinpointed that amongst the most promising technologies for the diagnosis of prion disease is the Real-Time Quaking-Induced Conversion; there are research for the treatment of prion disease that are in initial stages; and that the knowledge of the similar mechanisms to prions on chronic-degenerative disease can contribute to a better understanding of them.


REFERENCES

  1. Lewin S, Perna A, Salamano R, Ketzoian C, Salinas D, Rodríguez MM, et al. Enfermedades priónicas en el ser humano en Uruguay: registro de los últimos 25 años. Rev Médica del Uruguay. 2012; 28 (1): 35-42.

  2. Atkinson CJ, Zhang K, Munn AL, Wiegmans A. Prion protein scrapie and the normal cellular prion protein. Prion. 2016; 10: 63-82. doi: 10.1080/19336896.2015.1110293.

  3. Castle AR, Gill AC. Physiological functions of the cellular prion protein. Front Mol Biosci. 2017; 4: 19. doi: 10.3389/fmolb.2017.00019.

  4. Franceschini A, Baiardi S, Hughson AG, McKenzie N, Moda F, Rossi M et al. High diagnostic value of second generation CSF RT-QuIC across the wide spectrum of CJD prions. Sci Rep. 2017; 7 (1): 10655. Available in: https://pubmed.ncbi.nlm.nih.gov/28878311

  5. Vallabh SM, Minikel EV, Schreiber SL, Lander ES. Personal view towards a treatment for genetic prion disease: trials and biomarkers. Lancet Neurol. 2020; 19 (4): 361-368. Available in: http://dx.doi.org/10.1016/S1474-4422(19)30403-X

  6. Alibhai JD, Casalone C, Andreoletti O, Cashman NR, Appleby BS, Castl AR et al. Handbook of Clinical Neurology [Internet]. 3rd ed. Pocchiari M, Manson J, editors. Elseriver; 2018. 2-498 p. Available in: https://www.sciencedirect.com/handbook/handbook-of-clinical-neurology/vol/153/suppl/C

  7. Sarnataro D, Pepe A, Zurzolo C. Cell Biology of Prion Protein. In: Legname G, Vanni S, editors. Progress in Molecular Biology and Translational Science [Internet]. [cited 2020 Apr 1] Academic Press; 2017, pp. 57-82; 182-196. doi: 10.1016/bs.pmbts.2017.06.018.

  8. Chen C, Dong XP. Epidemiological characteristics of human prion diseases. Infect Dis Poverty. 2016; 5 (1): 1-10. doi: 10.1186/s40249-016-0143-8.

  9. Maddox RA, Person MK, Blevins JE, Abrams JY, Appleby BS, Schonberger LB, et al. Prion disease incidence in the United States: 2003-2015. Neurology. 2020; 94 (2): e153-157. doi: 10.1212/WNL.0000000000008680.

  10. González-Duarte A, Medina Z, Balaguer RR, Calleja JH.. Can prion disease suspicion be supported earlier? Clinical, radiological and laboratory findings in a series of cases. Prion. 2011; 5 (3): 201-207. doi: https://doi.org/10.4161/pri.5.3.16187.

  11. Prasad KN, Bondy SC. Oxidative and inflammatory events in prion diseases: can they be therapeutic targets? Curr Aging Sci. 2018; 11 (4): 216-225. doi: 10.2174/187460981266619011110020.

  12. Uttley L, Carroll C, Wong R, Hilton DA, Stevenson M. Review Creutzfeldt-Jakob disease : a systematic review of global incidence, prevalence, infectivity, and incubation. Lancet Infect Dis. 2020; 20 (1): e2-10. doi: 10.1016/S1473-3099(19)30615-2.

  13. Begué C, Martinetto H, Schultz M, Rojas E, Romero C, D'Giano C et al. Creutzfeldt-Jakob disease surveillance in Argentina, 1997-2008. Neuroepidemiology. 2011; 37 (3-4): 193-202. doi: 10.1159/000331907.

  14. Ramírez M, Gallardo A, Vidal A, Cornejo S, Ramírez D, Medinas D et al. Desafíos en el diagnóstico de enfermedad de Creutzfeldt-Jakob: caso clínico. Rev Med Chil. 2016; 144 (6): 796-806. doi: 10.4067/s0034-98872016000600016.

  15. Cartier LR, Quiroz GZ, Leiva MH, Vergara CR. Identificación clínica y patológica de las diversas formas de la enfermedad de Creutzfeldt Jakob en Chile. Rev Med Chil. 2012; 140 (2): 161-168. doi: 10.4067/S0034-98872012000200003.

  16. Mercado FM, Taboada BJ, González PM, Flores RJ. Hallazgos por resonancia magnética en demencia rápidamente progresiva, probable enfermedad de priones tipo Creutzfeldt-Jakob forma esporádica. An Radiol México. 2015; 14 (3): 292-298. Available in https://www.medigraphic.com/pdfs/anaradmex/arm-2015/arm153g.pdf

  17. Escandón-Vargas K, Zorrilla-Vaca A, Corral-Prado RH. Positive 14-3-3 and tau proteins in a sporadic Creutzfeldt-Jakob disease case and a brief perspective of prion diseases in Colombia. Biomedica. 2016; 36: 29-36. doi: 10.7705/biomedica.v36i3.2729.

  18. Hernández A, Céspedes G, Guerrero A. Enfermedad de Creutzfeldt-Jakob Esporádica en Venezuela: A propósito de un nuevo caso. VITAE. 2017; 69: 1-12. Disponible en: https://vitae.ucv.ve/pdfs/VITAE_5460.pdf

  19. Alem JM, Jos P, Guill F. Rapidly progressive dementia in sporadic prion disease: report of unprecedented event in Ecuador and update. Acta Neurol Colomb. 2016; 32 (2): 169-178.

  20. Herrán GET, Heredia ADO, Burbano BM, Serrano-Dueñas M, Yepez MAO, Madera RAB et al. Correction to: case series of Creutzfeldt-Jakob disease in a third-level hospital in Quito. BMC Neurol. 2018; 18 (1): 84. doi: 10.1186/s12883-018-1088-2.

  21. Torres-Ramírez L, Ramírez-Quiñones J, Cosentino-Esquerre C, Vélez-Rojas M, Flores-Mendoza M, Rivas-Franchini D et al. Enfermedad de Creutzfeldt-Jakob en el Perú: reporte de once casos. Rev Peru Med Exp Salud Publica. 2014; 31 (2): 364-369. doi: 10.17843/rpmesp.2014.312.60.

  22. Cardoso CA de O, Navarro MBM de A, Correa Soares BE, Cardoso TA de O. Avaliacao epidemiológica dos óbitos por doencas prionicas no Brasil sob o enfoque da biosseguranca. Cad Saúde Coletiva. 2015; 23 (1): 2-10. doi: 10.1590/1414-462X201500010002.

  23. Smid J, Studart Neto A, Landemberger MC, Machado CF, Nóbrega PR, Canedo NHS, et al. High phenotypic variability in Gerstmann-Straussler-Scheinker disease. Arq Neuropsiquiatr. 2017; 75 (6): 331-338. doi: 10.1590/0004-282x20170049.

  24. Mead S, Rudge P. CJD mimics and chameleons. Pract Neurol. 2017; 17 (2): 113-121. doi: 10.1136/practneurol-2017-001629.

  25. Ritchie DL, Ironside JW. Variant Creutzfeldt-Jakob disease. Curated Ref Collect Neurosci Biobehav Psychol. 2016: 25-32. doi: 10.1016/B978-0-12-809324-5.01941-6.

  26. Qi C, Zhang JT, Zhao W, Xing XW, Yu SY. Sporadic creutzfeldt-jakob disease: a retrospective analysis of 104 cases. Eur Neurol. 2020; 83 (1): 65-72. DOI: 10.1159/000507189.

  27. Geschwind MD. Prion diseases. Continuum (Minneap Minn). 2015; 21 (6 Neuroinfectious Disease):1612-1638. doi: 10.1212/CON.0000000000000251.

  28. Brown P, Brandel J-P, Sato T, Nakamura Y, MacKenzie J, Will RG, et al. Iatrogenic Creutzfeldt-Jakob disease, final assessment. Emerg Infect Dis. 2012; 18 (6): 901-907. doi: 10.3201/eid1806.120116.

  29. Kang MJ, Suh J, An SS, Kim S, Park YH. Pearls & Oy-sters: Challenging diagnosis of Gerstmann-Straussler-Scheinker disease Clinical and imaging findings. Neurology [Internet]. 2019; 92 (2): 101-103. doi: 10.1212/WNL.0000000000006730.

  30. Llorens F, Zarranz J, Fischer A, Zerr I, Ferrer I. Fatal familial insomnia: clinical aspects and molecular alterations. Curr Neurol Neurosci Rep. 2017; 17 (30): 1-7. doi: 10.1007/s11910-017-0743-0.

  31. Shi Q, Xiao K, Zhou W, Wang J, Chen C, Gao C et al. Fatal familial insomnia: insight of the most common genetic prion disease in china based on the analysis of 40 patients. Neuropsychiatry (London). 2018; 8 (6): 1806-1814. doi: 10.4172/Neuropsychiatry.1000522.

  32. Liberski PP, Gajos A, Sikorska B, Lindenbaum S. Kuru, the first human prion disease. Viruses. 2019; 11 (3): 232. doi: 10.3390/v11030232.

  33. Shintaku M, Yutani C, Doh-ura K. Brain stem lesions in sporadic Creutzfeldt-Jakob disease: a histopathological and immunohistochemical study. Neuropathology. 2006; 26 (1): 43-49. doi: 10.1111/j.1440-1789.2006.00654.x.

  34. Ironside JW, Mccardle L, Horsburgh A, Lim Z, Head MW. Pathological diagnosis of variant Creutzfeldt-Jakob disease. APMIS. 2002; 110: 79-87. doi: 10.1034/j.1600-0463.2002.100110.x.

  35. Ishizawa K, Mitsufuji T, Shioda K, Kobayashi A, Komori T, Nakazato Y, et al. An autopsy report of three kindred in a Gerstmann–Sträussler-Scheinker disease P105L family with a special reference to prion protein, tau, and beta-amyloid. Brain Behav. 2018; 8 (10): 1-14. doi: 10.1002/brb3.1117.

  36. Simpson M, Johanssen V, Boyd A, Klug G, Masters CL, Li Q-X, et al. Unusual Clinical and Molecular-Pathological Profile of Gerstmann-Straussler-Scheinker Disease Associated With a Novel PRNP Mutation (V176G). JAMA Neurol. 2013; 70 (9): 1180-1185. doi: 10.1001/jamaneurol.2013.165.

  37. Baldelli L, Provini F. Autonomic neuroscience: basic and clinical fatal familial insomnia and Agrypnia excitata: autonomic dysfunctions and pathophysiological implications. Auton Neurosci Basic Clin. 2019; 218: 68-86. doi: 10.1016/j.autneu.2019.02.007.

  38. Llorens F, Thüne K, Schmitz M, Ansoleaga B, Frau-Méndez MA, Cramm M et al. Identification of new molecular alterations in fatal familial insomnia. Hum Mol Genet. 2016; 25 (12): 2417-2436. doi: 10.1093/hmg/ddw108.

  39. Liberski PP, Sikorska B, Lindenbaum S, Goldfarb LG, McLean C, Hainfellner JA et al. Kuru: genes, cannibals and neuropathology. J Neuropathol Exp Neurol. 2012; 71 (2): 92-103. doi: 10.1097/NEN.0b013e3182444efd.

  40. Carroll JA, Chesebro B. Neuroinflammation, microglia, and cell-association during prion disease. Viruses. 2019; 11 (1): 1-20. doi: 10.3390/v11010065.

  41. Saá P, Harris DA, Cervenakova L. Mechanisms of prion-induced neurodegeneration. Expert Rev Mol Med. 2020; 18 (5): 1-18. doi: 10.1017/erm.2016.8.

  42. Fang C, Imberdis T, Garza MC, Wille H, Harris DA. A neuronal culture system to detect prion synaptotoxicity. PLoS Pathog. 2016; 12 (5): 1-17. doi: 10.1371/journal.ppat.1005623.

  43. Garcés M, Guijarro MI, Vargas A, Badiola JJ, Monzón M. Neuroglial patterns are shared by cerebella from prion and prion-like disorder affected patients. Mech Ageing Dev. 2019; 184: 111176. doi: 10.1016/j.mad.2019.111176.

  44. Aguzzi A, Zhu C. Microglia in prion diseases. J Clin Invest. 2017; 127 (9): 3230-3239. doi: 10.1172/JCI90605.

  45. Victoria GS, Arkhipenko A, Zhu S, Syan S, Zurzolo C. Astrocyte-to-neuron intercellular prion transfer is mediated by cell-cell contact. Sci Rep. 2016; 6: 25-28. doi: 10.1038/srep20762.

  46. Hartmann K, Sepulveda-Falla D, Rose IVL, Madore C, Muth C, Matschke J et al. Complement 3+-astrocytes are highly abundant in prion diseases, but their abolishment led to an accelerated disease course and early dysregulation of microglia. Acta Neuropathol Commun. 2019; 7 (1): 83. doi: 10.1186/s40478-019-0735-1.

  47. Carroll JA, Race B, Williams K, Striebel J, Chesebro B. Microglia are critical in host defense against prion disease. J Virol. 2018; 92 (15): 1-17. doi: 10.1128/jvi.00549-18.

  48. Ferrer I. Oligodendrogliopathy in neurodegenerative diseases with abnormal protein aggregates: The forgotten partner. Prog Neurobiol. 2018; 169: 24-54. doi: 10.1016/j.pneurobio.2018.07.004.

  49. Küffer A, Lakkaraju AK, Mogha A, Petersen SC, Airich K, Doucerain C et al. The prion protein is an agonistic ligand of the G protein-coupled receptor Adgrg6. Nature. 2016; 536: 464-468. doi: 10.1038/nature19312.

  50. Baiardi S, Redaelli V, Ripellino P, Rossi M, Franceschini A, Moggio M et al. Prion-related peripheral neuropathy in sporadic Creutzfeldt-Jakob disease. J Neurol Neurosurg Psychiatry. 2018; 90: 1-4. doi: 10.1136/jnnp-2018-319221.

  51. Rudge P, Jaunmuktane Z, Hyare H, Ellis M, Koltzenburg M, Collinge J et al. Early neurophysiological biomarkers and spinal cord pathology in inherited prion disease. Brain. 2019; 142 (3): 760-770. doi: 10.1093/brain/awy358.

  52. Satoh K, Fuse T, Nonaka T, Dong T, Takao M. Postmortem quantitative analysis of prion seeding. Molecules. 2019; 24 (24): 1-7. doi: doi:10.3390/molecules24244601.

  53. Ano Y, Sakudo A, Uraki R, Kono J, Yukawa M, Onodera T. Intestinal transmission of prions and role of exosomes in enterocytes. Food Saf. 2013; 1 (1): 43-48. doi: 10.14252/foodsafetyfscj.2013005.

  54. D'Argenio V, Sarnataro D. Microbiome influence in the pathogenesis of prion and Alzheimer's diseases. Int J Mol Sci. 2019; 20 (19): 4604-4620. doi: 10.3390/ijms20194704.

  55. Urayama A, Concha-Marambio L, Khan U, Bravo-Alegria J, Kharat V, Soto C. Prions efficiently cross the intestinal barrier after oral administration: study of the bioavailability, and cellular and tissue distribution in vivo. Sci Rep. 2016; 6: 1-12. doi: 10.1038/srep32338

  56. Herbst A, Banser P, Velasquez CD, Mays CE, Sim VL, Westaway D et al. Infectious prions accumulate to high levels in non proliferative C2C12 myotubes. PLoS Pathog. 2013; 9 (11): 1-11. doi: 10.1371/journal.ppat.1003755.

  57. Neumann M, Krasemann S, Schrock K, Steinbach K, Glatzel M. Myositis facilitates preclinical accumulation of pathological prion protein in muscle. Acta Neuropathol Commun. 2013; 1 (78): 1-13. doi: 10.1186/2051-5960-1-78.

  58. Joshi-Barr S, Bett C, Chiang W-C, Trejo M, Goebel HH, Sikorska B et al. De novo prion aggregates trigger autophagy in skeletal muscle. J Virol. 2014; 88 (4): 2071-2082. doi: 10.1128/JVI.02279-13.

  59. World Health Organization. Global surveillance, diagnosis and therapy of human transmissible spongiform encephalopathies: report of a WHO Consultation [Internet]. [Cited Oct 13 2020] Geneva, Suiza; 1998. Available in: https://apps.who.int/iris/bitstream/handle/10665/65516/WHO_EMC_ZDI_98.9.pdf?sequence=1&isAllowed=y

  60. Number FR, Government S, Unit S, Building BM, Hospital WG, Road C. Surveillance of CJD in the UK [Internet] [cited Oct 13 2020]. 2017. p. 1-85. Available in: https://www.cdc.gov/prions/cjd/diagnostic-criteria.html

  61. Gregor H, Schindler K, Zumsteg D. EEG in Creutzfeldt-Jakob disease. Clin Neurophysiol. 2006; 117: 935-951. doi: 10.1016/j.clinph.2005.12.007.

  62. Fragoso DC, Goncalves Filho AL da M, Pacheco FT, Barros BR, Aguiar Littig I, Nunes RH et al. Imaging of Creutzfeldt-Jakob disease: imaging patterns and their differential diagnosis. Radiographics. 2017; 37 (1): 234-257. doi: 10.1148/rg.2017160075.

  63. Manix M, Kalakoti P, Henry M, Thakur J, Menger R, Guthikonda B et al. Creutzfeldt-Jakob disease: updated diagnostic criteria, treatment algorithm, and the utility of brain biopsy. Neurosurg Focus. 2015; 39: 1-11. doi: 10.3171/2015.8.FOCUS15328.

  64. Gaudino S, Gangemi E, Colantonio R, Botto A, Ruberto E, Calandrelli R et al. Neuroradiology of human prion diseases, diagnosis and differential diagnosis. Radiol Medica. 2017; 122 (5): 369-385. doi: 10.1007/s11547-017-0725-y.

  65. Wu L-Y, Zhan S-Q, Huang Z-Y, Zhang B, Wang T, Liu C-F et al. Expert consensus on clinical diagnostic criteria for fatal familial insomnia. Chin Med J (Engl). 2018;131(13):1613–7. doi: 10.4103/0366-6999.235115.

  66. Jiang AA, Longardner K, Dickson D, Sell R. Gerstmann-Straussler-Scheinker syndrome misdiagnosed as conversion disorder. BMJ Case Rep. 2019; l: 12-15. doi: 10.1136/bcr-2019-229729.

  67. Wang J, Xiao K, Zhou W, Shi Q, Dong X-P. Analysis of 12 chinese patients with proline-to-leucine mutation at codon 102-associated gerstmann-straussler-scheinker disease. J Clin Neurol. 2019; 15 (2): 184-190. doi: 10.3988/jcn.2019.15.2.184.

  68. Hermann P, Laux M, Glatzel M, Matschke J, Knipper T, Goebel S et al. Validation and utilization of amended diagnostic criteria in Creutzfeldt-Jakob disease surveillance. Neurology. 2018; 91 (4): e331-338. doi: 10.1212/WNL.0000000000005860.

  69. Sano K, Satoh K, Atarashi R, Takashima H, Iwasaki Y, Yoshida M et al. Early detection of abnormal prion protein in genetic human prion diseases now possible using real-time QUIC assay. PLoS One. 2013; 8 (1): 8-11. doi: 10.1371/journal.pone.0054915.

  70. Green AJE. RT-QuIC: a new test for sporadic CJD. Pract Neurol. 2019; 19 (1): 49-55. doi: 10.1136/practneurol-2018-001935.

  71. Burchell JT, Panegyres PK. Prion diseases: immunotargets and therapy. ImmunoTargets and Therapy. 2016; 5: 57-68. doi: 10.2147/ITT.S64795.

  72. Teruya K, Doh-ura K. Insights from Therapeutic Studies for PrP. Cold Spring Harb Perspect Med. 2017; 7 (3): 1-18. doi: 10.1101/cshperspect.a024430.

  73. Yamaguchi K, Kamatari YO, Ono F, Shibata H, Fuse T, Elhelaly AE et al. A designer molecular chaperone against transmissible spongiform encephalopathy slows disease progression in mice and macaques. Nat Biomed Eng. 2019; 3 (3): 206-219. doi: 10.1038/s41551-019-0349-8.

  74. Schwartz M, Brandel JP, Babonneau ML, Boucher C, Schaerer E, Haik S et al. Genetic testing in prion disease: psychological consequences of the decisions to know or not to know. Front Genet. 2019; 10: 1-8. doi: 10.3389/fgene.2019.00895.

  75. Mead S, Reilly MM. REVIEWS A new prion disease: relationship with central and peripheral amyloidoses. Nat Publ Gr. 2015; 11: 90-97. doi: 10.1038/nrneurol.2014.263.

  76. Brandel JP, Vlaicu MB, Culeux A, Belondrade M, Bougard D, Grznarova K et al. Variant Creutzfeldt-Jakob disease diagnosed 7.5 years after occupational exposure. N Engl J Med. 2020; 383 (1): 83-85. doi: 10.1056/NEJMc2000687.

  77. Xavier EA. Prions: the danger of biochemical weapons. Food Sci Technol. 2014; 34 (3): 433-440. doi: 10.1590/1678-457x.6342.

  78. Ma J, Gao J, Wang J, Xie A. Prion-Like Mechanisms in Parkinson's Disease. Front Neurosci. 2019; 13: 552. doi: 10.3389/fnins.2019.00552.

  79. Peters C, Espinoza MP, Gallegos S, Opazo C, Aguayo LG. Alzheimer's Aβ interacts with cellular prion protein inducing neuronal membrane damage and synaptotoxicity. Neurobiol Aging. 2015; 36 (3): 1369-1377. doi: 10.1016/j.neurobiolaging.2014.11.019.

  80. Zamponi E, Pigino GF. Protein misfolding, signaling abnormalities and altered fast axonal transport: implications for Alzheimer and prion diseases. Front Cell Neurosci. 2019; 13: 350. doi: 10.3389/fncel.2019.00350.

  81. Melki R. Alpha-synuclein and the prion hypothesis in Parkinson's disease. Rev Neurol (Paris). 2018; 174 (9): 644-652. doi: 10.1016/j.neurol.2018.08.002.

  82. Mukherjee A, Soto C. Prion-like protein aggregates and type 2 diabetes. Cold Spring Harb Perspect Med. 2017; 7 (5): a024315. doi: 10.1101/cshperspect.a024315.

  83. Arunagiri A, Haataja L, Cunningham CN, Shrestha N, Tsai B, Qi L et al. Misfolded proinsulin in the endoplasmic reticulum during development of beta cell failure in diabetes. Ann N Y Acad Sci. 2018; 1418 (1): 5-19. doi: 10.1111/nyas.13531.

  84. McAlary L, Plotkin SS, Yerbury JJ, Cashman NR. Prion-Like propagation of protein misfolding and aggregation in amyotrophic lateral sclerosis. Front Mol Neurosci. 2019; 12: 262. doi: 10.3389/fnmol.2019.00262.

  85. Weickenmeier J, Jucker M, Goriely A, Kuhl E. A physics-based model explains the prion-like features of neurodegeneration in Alzheimer's disease, Parkinson's disease, and amyotrophic lateral sclerosis. J Mech Phys Solids. 2019; 124: 264-281. doi: 10.1016/j.jmps.2018.10.013.

  86. Srinageshwar B, Petersen RB, Dunbar GL, Rossignol J. Prion-like mechanisms in neurodegenerative disease: implications for Huntington's disease therapy. Stem Cells Transl Med. 2020; 9 (5): 559-566. doi: 10.1002/sctm.19-0248.

  87. Aoyagi A, Condello C, Stohr J, Yue W, Rivera BM, Lee JC et al. AB and tau prion-like activities decline with longevity in the Alzheimer's disease human brain. Sci Transl Med. 2019; 8462: 1-14. doi: 10.1126/scitranslmed.aat8462.

  88. Iglesias V, Paladin L, Juan-Blanco T, Pallarès I, Aloy P, Tosatto SCE et al. In silico characterization of human prion-like proteins: beyond neurological diseases. Front Physiol. 2019; 10: 314. doi: 10.3389/fphys.2019.00314.

  89. Yang X, Zhang Y, Zhang L, He T, Zhang J, Li C. Prion protein and cancers. Acta Biochim Biophys Sin (Shanghai). 2014; 46 (6): 431-440. doi: 10.1093/abbs/gmu019.

  90. Thellung S, Corsaro A, Bosio AG, Zambito M, Barbieri F, Mazzanti M, et al. Emerging role of cellular prion protein in the maintenance and expansion of glioma stem cells. Cells. 2019; 8 (11): 1458: 1-23. doi: 10.3390/cells8111458.

  91. Gil M, Kim YK, Kim KE, Kim W, Park CS, Lee KJ. Cellular prion protein regulates invasion and migration of breast cancer cells through MMP-9 activity. Biochem Biophys Res Commun. 2016; 470 (1): 213-219. doi: 10.1016/j.bbrc.2016.01.038.

  92. Mehrpour M, Codogno P. Prion protein: From physiology to cancer biology. Cancer Lett. 2010; 290 (1): 1-23. doi: 10.1016/j.canlet.2009.07.009.

  93. Navalkar A, Ghosh S, Pandey S, Paul A, Datta D, Maji SK. Prion-like p53 amyloids in cancer. Biochemistry. 2020; 59 (2): 146-155. doi: 10.1021/acs.biochem.9b00796.

  94. Silva JL, De Moura Gallo CV, Costa DC, Rangel LP. Prion-like aggregation of mutant p53 in cancer. Trends Biochem Sci. 2014; 39 (6): 260-267. doi: 10.1016/j.tibs.2014.04.001.

  95. De Oliveira GAP, Petronilho EC, Pedrote MM, Marques MA, Vieira TCRG, Cino EA et al. The status of p53 oligomeric and aggregation states in cancer. Biomolecules. 2020; 10: 548-561. doi: 10.3390/biom10040548.

  96. Wickner RB. Anti-prion systems in yeast. J Biol Chem. 2019; 294 (5): 1729-1738. doi: 10.1074/jbc.TM118.004168.

  97. Du Z, Valtierra S, Cardona LR, Dunne SF, Luan C. Identifying anti-prion chemical compounds using a newly established yeast high-throughput screening system. Cell Chem Biol. 2019; 26: 1-17. doi: 10.1016/j.chembiol.2019.10.004.




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