{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,4,28]],"date-time":"2026-04-28T16:56:00Z","timestamp":1777395360295,"version":"3.51.4"},"reference-count":55,"publisher":"SAGE Publications","issue":"2","license":[{"start":{"date-parts":[[2021,5,18]],"date-time":"2021-05-18T00:00:00Z","timestamp":1621296000000},"content-version":"unspecified","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by-nc\/4.0\/"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["JAD"],"published-print":{"date-parts":[[2021,5,18]]},"abstract":"<jats:p>Background: Transmissible spongiform encephalopathies (TSEs) are rare neurodegenerative disorders that affect animals and humans. Bovine spongiform encephalopathy (BSE) in cattle, and Creutzfeld-Jakob Disease (CJD) in humans belong to this group. The causative agent of TSEs is called \u201cprion\u201d, which corresponds to a pathological form (PrPSc) of a normal cellular protein (PrPC) expressed in nerve cells. PrPSc is resistant to degradation and can induce abnormal folding of PrPC, and TSEs are characterized by extensive spongiosis and gliosis and the presence of PrPSc amyloid plaques. CJD presents initially with clinical symptoms similar to Alzheimer\u2019s disease (AD). In AD, tau aggregates and amyloid-\u03b2 protein plaques are associated with memory loss and cognitive impairment in patients. Objective: In this work, we study the role of tau and its relationship with PrPSc plaques in CJD. Methods: Multiple immunostainings with specific antibodies were carried out and analyzed by confocal microscopy. Results: We found increased expression of the glial fibrillary acidic protein (GFAP) and matrix metalloproteinase (MMP-9), and an exacerbated apoptosis in the granular layer in cases with prion disease. In these cases, tau protein phosphorylated at Thr-231 was overexpressed in the axons and dendrites of Purkinje cells and the extensions of parallel fibers in the cerebellum. Conclusion: We conclude that phosphorylation of tau may be a response to a toxic and inflammatory environment generated by the pathological form of prion.<\/jats:p>","DOI":"10.3233\/jad-201308","type":"journal-article","created":{"date-parts":[[2021,4,2]],"date-time":"2021-04-02T14:38:44Z","timestamp":1617374324000},"page":"769-785","source":"Crossref","is-referenced-by-count":3,"title":["Tau Protein Phosphorylated at Threonine-231 is Expressed Abundantly in the Cerebellum in Prion Encephalopathies"],"prefix":"10.1177","volume":"81","author":[{"given":"V\u0131ctor Manuel","family":"G\u00f3mez-L\u00f3pez","sequence":"first","affiliation":[{"name":"National Dementia BioBank. Ciencias Biol\u00f3gicas, Facultad de Estudios Superiores, Cuautitl\u00e1n, UNAM, Estado de M\u00e9xico, M\u00e9xico"},{"name":"Physiology, Biophysics and Neuroscience, CINVESTAV, CDMX, M\u00e9xico"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Amparo","family":"Viramontes-Pintos","sequence":"additional","affiliation":[{"name":"National Dementia BioBank. Ciencias Biol\u00f3gicas, Facultad de Estudios Superiores, Cuautitl\u00e1n, UNAM, Estado de M\u00e9xico, M\u00e9xico"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Miguel \u00c1ngel","family":"Ontiveros-Torres","sequence":"additional","affiliation":[{"name":"School of Engineering and Science, Tecnologico de Monterrey, Toluca, M\u00e9xico"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Linda","family":"Garc\u00e9s-Ram\u00edrez","sequence":"additional","affiliation":[{"name":"Escuela Nacional de Ciencias Biol\u00f3gicas, Departamento Fisiolog\u00eda, Instituto Polit\u00e9cnico Nacional, CDMX, M\u00e9xico"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Fidel","family":"de la Cruz","sequence":"additional","affiliation":[{"name":"Escuela Nacional de Ciencias Biol\u00f3gicas, Departamento Fisiolog\u00eda, Instituto Polit\u00e9cnico Nacional, CDMX, M\u00e9xico"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Ignacio","family":"Villanueva-Fierro","sequence":"additional","affiliation":[{"name":"CIIDIR, Durango, Instituto Polit\u00e9cnico Nacional, Durango, Becario COFAA, M\u00e9xico"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Marely","family":"Bravo-Mu\u00f1oz","sequence":"additional","affiliation":[{"name":"National Dementia BioBank. Ciencias Biol\u00f3gicas, Facultad de Estudios Superiores, Cuautitl\u00e1n, UNAM, Estado de M\u00e9xico, M\u00e9xico"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Charles R.","family":"Harrington","sequence":"additional","affiliation":[{"name":"School of Medicine, Medical Sciences and Nutrition, University of Aberdeen, Aberdeen, UK"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Sandra","family":"Mart\u00ednez-Robles","sequence":"additional","affiliation":[{"name":"National Dementia BioBank. Ciencias Biol\u00f3gicas, Facultad de Estudios Superiores, Cuautitl\u00e1n, UNAM, Estado de M\u00e9xico, M\u00e9xico"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Petra","family":"Yescas","sequence":"additional","affiliation":[{"name":"Gen\u00e9tica, Instituto Nacional de Neurolog\u00eda y Neurocirug\u00eda, \u201cManuel Velazco Suerez\u201d CDMX, M\u00e9xico"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Parm\u00e9nides","family":"Guadarrama-Ort\u00edz","sequence":"additional","affiliation":[{"name":"Departamento de Neurocirug\u00eda, Centro Especializado en Neurocirug\u00eda y Neurociencias, M\u00e9xico, (CENNM), CDMX, M\u00e9xico"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Mario","family":"Hernandes-Alejandro","sequence":"additional","affiliation":[{"name":"Departamento de Bioingenier\u00eda, Unidad Profesional Interdisciplinaria de Biotecnolog\u00eda del Instituto Polit\u00e9cnico Nacional, Gustavo A. Madero, M\u00e9xico"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Francisco","family":"Montiel-Sosa","sequence":"additional","affiliation":[{"name":"National Dementia BioBank. Ciencias Biol\u00f3gicas, Facultad de Estudios Superiores, Cuautitl\u00e1n, UNAM, Estado de M\u00e9xico, M\u00e9xico"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Mar","family":"Pacheco-Herrero","sequence":"additional","affiliation":[{"name":"Neuroscience Research Laboratory, Faculty of Health Sciences, Pontificia Universidad Catolica Madre y Maestra, Santiago de los Caballeros, Dominican Republic"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Jos\u00e9","family":"Luna-Mu\u00f1oz","sequence":"additional","affiliation":[{"name":"National Dementia BioBank. Ciencias Biol\u00f3gicas, Facultad de Estudios Superiores, Cuautitl\u00e1n, UNAM, Estado de M\u00e9xico, M\u00e9xico"},{"name":"National Brain Bank. Universidad Nacional Pedro Henr\u00edquez Ure\u00f1a, Santo Domingo, Dominican Republic"}],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"179","reference":[{"key":"10.3233\/JAD-201308_ref1","doi-asserted-by":"crossref","first-page":"163","DOI":"10.1016\/j.nic.2007.12.003","article-title":"Prion protein disease and neuropathology of prion disease","volume":"18","author":"du Plessis","year":"2008","journal-title":"Neuroimaging Clin N Am"},{"key":"10.3233\/JAD-201308_ref2","doi-asserted-by":"crossref","first-page":"264","DOI":"10.1111\/j.1440-1819.2008.01792.x","article-title":"Prion disease causes less severe lesions in human hippocampus than other parts of brain","volume":"62","author":"Kaneko","year":"2008","journal-title":"Psychiatry Clin Neurosci"},{"key":"10.3233\/JAD-201308_ref3","doi-asserted-by":"crossref","first-page":"302","DOI":"10.1097\/WCO.0000000000000197","article-title":"Clinical update of Jakob-Creutzfeldt disease","volume":"28","author":"Kim","year":"2015","journal-title":"Curr Opin Neurol"},{"key":"10.3233\/JAD-201308_ref4","doi-asserted-by":"crossref","first-page":"493","DOI":"10.1186\/1743-422X-8-493","article-title":"An overview of animal prion diseases","volume":"8","author":"Imran","year":"2011","journal-title":"Virol J"},{"key":"10.3233\/JAD-201308_ref5","doi-asserted-by":"crossref","first-page":"187","DOI":"10.1097\/GIM.0b013e3181cd7374","article-title":"The genetics of prion diseases","volume":"12","author":"Mastrianni","year":"2010","journal-title":"Genet Med"},{"key":"10.3233\/JAD-201308_ref6","doi-asserted-by":"crossref","first-page":"19","DOI":"10.3389\/fmolb.2017.00019","article-title":"Physiological functions of the cellular prion protein","volume":"4","author":"Castle","year":"2017","journal-title":"Front Mol Biosci"},{"key":"10.3233\/JAD-201308_ref7","doi-asserted-by":"crossref","first-page":"237","DOI":"10.1016\/S1471-4914(03)00069-8","article-title":"Is loss of function of the prion protein the cause of prion disorders?","volume":"9","author":"Hetz","year":"2003","journal-title":"Trends Mol Med"},{"key":"10.3233\/JAD-201308_ref8","doi-asserted-by":"crossref","first-page":"92","DOI":"10.1016\/j.tins.2011.10.002","article-title":"Prion protein at the crossroads of physiology and disease","volume":"35","author":"Biasini","year":"2012","journal-title":"Trends Neurosci"},{"key":"10.3233\/JAD-201308_ref9","doi-asserted-by":"crossref","first-page":"136","DOI":"10.1126\/science.6801762","article-title":"Novel proteinaceous infectious particles cause scrapie","volume":"216","author":"Prusiner","year":"1982","journal-title":"Science"},{"key":"10.3233\/JAD-201308_ref10","doi-asserted-by":"crossref","first-page":"373","DOI":"10.1111\/j.1365-2990.2007.00868.x","article-title":"Classical sheep transmissible spongiform encephalopathies: Pathogenesis, pathological phenotypes and clinical disease","volume":"33","author":"Jeffrey","year":"2007","journal-title":"Neuropathol Appl Neurobiol"},{"key":"10.3233\/JAD-201308_ref11","doi-asserted-by":"crossref","first-page":"79","DOI":"10.1007\/s00401-010-0761-3","article-title":"Molecular biology and pathology of prion strains in sporadic human prion diseases","volume":"121","author":"Gambetti","year":"2011","journal-title":"Acta Neuropathol"},{"key":"10.3233\/JAD-201308_ref12","doi-asserted-by":"crossref","first-page":"e153","DOI":"10.1212\/WNL.0000000000008680","article-title":"Prion disease incidence in the United States: 2003-2015","volume":"94","author":"Maddox","year":"2020","journal-title":"Neurology"},{"key":"10.3233\/JAD-201308_ref13","doi-asserted-by":"crossref","first-page":"238","DOI":"10.1016\/j.brainresbull.2016.08.018","article-title":"Tau and tauopathies","volume":"126","author":"Arendt","year":"2016","journal-title":"Brain Res Bull"},{"key":"10.3233\/JAD-201308_ref14","doi-asserted-by":"crossref","first-page":"88","DOI":"10.1016\/j.neurobiolaging.2019.06.009","article-title":"The neuritic plaque in Alzheimer\u2019s disease: Perivascular degeneration of neuronal processes","volume":"82","author":"Hansra","year":"2019","journal-title":"Neurobiol Aging"},{"key":"10.3233\/JAD-201308_ref15","doi-asserted-by":"crossref","first-page":"458","DOI":"10.1016\/j.neuint.2010.12.023","article-title":"Post-translational modifications of tau protein: Implications for Alzheimer\u2019s disease","volume":"58","author":"Martin","year":"2011","journal-title":"Neurochem Int"},{"key":"10.3233\/JAD-201308_ref16","doi-asserted-by":"crossref","first-page":"191","DOI":"10.1007\/s00415-009-5290-4","article-title":"Transmissible spongiform encephalopathies with P102L mutation of PRNP manifesting different phenotypes: Clinical, neuroimaging, and electrophysiological studies in Chinese kindred in Taiwan","volume":"257","author":"Chi","year":"2010","journal-title":"J Neurol"},{"key":"10.3233\/JAD-201308_ref17","doi-asserted-by":"crossref","first-page":"712","DOI":"10.1002\/ana.22264","article-title":"Familial prion disease with Alzheimer disease-like tau pathology and clinical phenotype","volume":"69","author":"Jayadev","year":"2011","journal-title":"Ann Neurol"},{"key":"10.3233\/JAD-201308_ref18","doi-asserted-by":"crossref","first-page":"549","DOI":"10.1111\/j.1365-2990.2010.01126.x","article-title":"The first case of fatal familial insomnia (FFI) in the Netherlands: A patient from Egyptian descent with concurrent four repeat tau deposits","volume":"37","author":"Jansen","year":"2011","journal-title":"Neuropathol Appl Neurobiol"},{"key":"10.3233\/JAD-201308_ref19","doi-asserted-by":"crossref","first-page":"5","DOI":"10.1007\/s00401-010-0691-0","article-title":"Tau, prions and A\u03b2: The triad of neurodegeneration","volume":"121","author":"Reiniger","year":"2011","journal-title":"Acta Neuropathol"},{"key":"10.3233\/JAD-201308_ref20","doi-asserted-by":"crossref","first-page":"240","DOI":"10.1136\/jnnp.63.2.240","article-title":"Neurofibrillary tangles in Gerstmann-Straussler-Scheinker syndrome with the A117V prion gene mutation","volume":"63","author":"Tranchant","year":"1997","journal-title":"J Neurol Neurosurg Psychiatry"},{"key":"10.3233\/JAD-201308_ref21","doi-asserted-by":"crossref","first-page":"545","DOI":"10.1042\/BST0380545","article-title":"Change in tau phosphorylation associated with neurodegeneration in the ME7 model of prion disease","volume":"38","author":"Asuni","year":"2010","journal-title":"Biochem Soc Trans"},{"key":"10.3233\/JAD-201308_ref22","doi-asserted-by":"crossref","first-page":"2087","DOI":"10.1046\/j.1471-4159.1997.69052087.x","article-title":"A conformation- and phosphorylation-dependent antibody recognizing the paired helical filaments of Alzheimer\u2019s disease","volume":"69","author":"Jicha","year":"1997","journal-title":"J Neurochem"},{"key":"10.3233\/JAD-201308_ref23","doi-asserted-by":"crossref","first-page":"10032","DOI":"10.1073\/pnas.1630428100","article-title":"Caspase cleavage of tau: Linking amyloid and neurofibrillary tangles in Alzheimer\u2019s disease","volume":"100","author":"Gamblin","year":"2003","journal-title":"Proc Natl Acad Sci U S A"},{"key":"10.3233\/JAD-201308_ref24","first-page":"755","article-title":"Characterisation of the first monoclonal antibody against the pronase resistant core of the Alzheimer PHF","volume":"317","author":"Novak","year":"1989","journal-title":"Prog Clin Biol Res"},{"key":"10.3233\/JAD-201308_ref25","doi-asserted-by":"crossref","first-page":"179","DOI":"10.1016\/j.nbd.2014.06.021","article-title":"Neuroprotective role of MMP-9 overexpression in the brain of Alzheimer\u2019s 5xFAD mice","volume":"70","author":"Fragkouli","year":"2014","journal-title":"Neurobiol Dis"},{"key":"10.3233\/JAD-201308_ref26","first-page":"908636","article-title":"Matrix metalloproteinases and their multiple roles in Alzheimer\u2019s disease","volume":"2014","author":"Wang","year":"2014","journal-title":"Biomed Res Int"},{"key":"10.3233\/JAD-201308_ref27","doi-asserted-by":"crossref","first-page":"433","DOI":"10.1007\/s12311-014-0556-5","article-title":"Torpedo formation and Purkinje cell loss: Modeling their relationship in cerebellar disease","volume":"13","author":"Louis","year":"2014","journal-title":"Cerebellum"},{"key":"10.3233\/JAD-201308_ref28","doi-asserted-by":"crossref","first-page":"38972","DOI":"10.1074\/jbc.M205110200","article-title":"Stimulation of PrPC retrograde transport toward the endoplasmic reticulum increases accumulation of PrPSc in prion-infected cells","volume":"277","author":"Beranger","year":"2002","journal-title":"J Biol Chem"},{"key":"10.3233\/JAD-201308_ref29","doi-asserted-by":"crossref","first-page":"1781","DOI":"10.1126\/science.1073725","article-title":"Neurotoxicity and neurodegeneration when PrP accumulates in the cytosol","volume":"298","author":"Ma","year":"2002","journal-title":"Science"},{"key":"10.3233\/JAD-201308_ref30","doi-asserted-by":"crossref","first-page":"1684","DOI":"10.1002\/glia.21215","article-title":"Increased excitatory amino acid transport into murine prion protein knockout astrocytes cultured in vitro","volume":"59","author":"Pathmajeyan","year":"2011","journal-title":"Glia"},{"key":"10.3233\/JAD-201308_ref31","doi-asserted-by":"crossref","first-page":"278","DOI":"10.3389\/fncel.2015.00278","article-title":"Elusive roles for reactive astrocytes in neurodegenerative diseases","volume":"9","author":"Ben Haim","year":"2015","journal-title":"Front Cell Neurosci"},{"key":"10.3233\/JAD-201308_ref32","first-page":"005","article-title":"Morphological change of glia in prion and a prion-like disorder","volume":"2","author":"Garces","year":"2016","journal-title":"J Alzheimers Neurodegener Dis"},{"key":"10.3233\/JAD-201308_ref33","doi-asserted-by":"crossref","first-page":"e0320","DOI":"10.1097\/MD.0000000000010320","article-title":"Glial alterations in human prion diseases: A correlative study of astroglia, reactive microglia, protein deposition, and neuropathological lesions","volume":"97","author":"Monzon","year":"2018","journal-title":"Medicine (Baltimore)"},{"key":"10.3233\/JAD-201308_ref34","doi-asserted-by":"crossref","first-page":"4138","DOI":"10.1007\/s12035-016-9918-y","article-title":"Hereditary human prion diseases: An update","volume":"54","author":"Schmitz","year":"2017","journal-title":"Mol Neurobiol"},{"key":"10.3233\/JAD-201308_ref35","doi-asserted-by":"crossref","first-page":"393","DOI":"10.1002\/j.1460-2075.1989.tb03390.x","article-title":"Cloning and sequencing of the cDNA encoding an isoform of microtubule-associated protein tau containing four tandem repeats: Differential expression of tau protein mRNAs in human brain","volume":"8","author":"Goedert","year":"1989","journal-title":"EMBO J"},{"key":"10.3233\/JAD-201308_ref36","doi-asserted-by":"crossref","first-page":"353","DOI":"10.1091\/mbc.8.2.353","article-title":"Functional interactions between the proline-rich and repeat regions of tau enhance microtubule binding and assembly","volume":"8","author":"Goode","year":"1997","journal-title":"Mol Biol Cell"},{"key":"10.3233\/JAD-201308_ref37","first-page":"341","article-title":"From tangles to tau protein","volume":"107","author":"Iqbal","year":"2006","journal-title":"Bratisl Lek Listy"},{"key":"10.3233\/JAD-201308_ref38","doi-asserted-by":"crossref","first-page":"2725","DOI":"10.1002\/j.1460-2075.1991.tb07820.x","article-title":"Identification of 3- and 4-repeat tau isoforms within the PHF in Alzheimer\u2019s disease","volume":"10","author":"Jakes","year":"1991","journal-title":"EMBO J"},{"key":"10.3233\/JAD-201308_ref39","doi-asserted-by":"crossref","first-page":"46","DOI":"10.1111\/j.1365-2990.2008.00959.x","article-title":"Ultrastructural study of florid plaques in variant Creutzfeldt-Jakob disease: A comparison with amyloid plaques in kuru, sporadic Creutzfeldt-Jakob disease and Gerstmann-Straussler-Scheinker disease","volume":"35","author":"Sikorska","year":"2009","journal-title":"Neuropathol Appl Neurobiol"},{"key":"10.3233\/JAD-201308_ref40","doi-asserted-by":"crossref","first-page":"50","DOI":"10.1007\/BF00294259","article-title":"Monitoring pathological assembly of tau and \u03b2-amyloid proteins in Alzheimer\u2019s disease","volume":"89","author":"Mena","year":"1995","journal-title":"Acta Neuropathol"},{"key":"10.3233\/JAD-201308_ref41","doi-asserted-by":"crossref","first-page":"293","DOI":"10.1016\/j.vetmic.2006.02.017","article-title":"BSE infection in bovine PrP transgenic mice leads to hyperphosphorylation of tau-protein","volume":"115","author":"Bautista","year":"2006","journal-title":"Vet Microbiol"},{"key":"10.3233\/JAD-201308_ref42","doi-asserted-by":"crossref","first-page":"1845","DOI":"10.1016\/j.bbamcr.2011.06.016","article-title":"Tau inhibits tubulin oligomerization induced by prion protein","volume":"1813","author":"Osiecka","year":"2011","journal-title":"Biochim Biophys Acta"},{"key":"10.3233\/JAD-201308_ref43","doi-asserted-by":"crossref","first-page":"28","DOI":"10.4161\/pri.22512","article-title":"Astrocyte signaling and neurodegeneration: New insights into CNS disorders","volume":"7","author":"Brambilla","year":"2013","journal-title":"Prion"},{"key":"10.3233\/JAD-201308_ref44","doi-asserted-by":"crossref","first-page":"3257","DOI":"10.1242\/jcs.104729","article-title":"Neurofilaments at a glance","volume":"125","author":"Yuan","year":"2012","journal-title":"J Cell Sci"},{"key":"10.3233\/JAD-201308_ref45","doi-asserted-by":"crossref","first-page":"3875","DOI":"10.3390\/v6103875","article-title":"The structure of human prions: From biology to structural models-considerations and pitfalls","volume":"6","author":"Acevedo-Morantes","year":"2014","journal-title":"Viruses"},{"key":"10.3233\/JAD-201308_ref46","doi-asserted-by":"crossref","first-page":"111176","DOI":"10.1016\/j.mad.2019.111176","article-title":"Neuroglial patterns are shared by cerebella from prion and prion-like disorder affected patients","volume":"184","author":"Garces","year":"2019","journal-title":"Mech Ageing Dev"},{"key":"10.3233\/JAD-201308_ref47","first-page":"e124","article-title":"The role of matrix meta-lloproteinase-9 in pro-inflammatory factors-induced brain inflammation and neurodegenerative diseases","volume":"1","author":"Hsi-Lung","year":"2014","journal-title":"Inflamm Cell Signal"},{"key":"10.3233\/JAD-201308_ref48","doi-asserted-by":"crossref","first-page":"2004","DOI":"10.3892\/mmr.2014.2467","article-title":"Differential expression profiling of matrix metalloproteinases and tissue inhibitors of metalloproteinases in females with or without pelvic organ prolapse","volume":"10","author":"Wang","year":"2014","journal-title":"Mol Med Rep"},{"key":"10.3233\/JAD-201308_ref49","doi-asserted-by":"crossref","first-page":"888","DOI":"10.1038\/nri3553","article-title":"The immunobiology of prion diseases","volume":"13","author":"Aguzzi","year":"2013","journal-title":"Nat Rev Immunol"},{"key":"10.3233\/JAD-201308_ref50","doi-asserted-by":"crossref","first-page":"555","DOI":"10.2353\/ajpath.2008.070442","article-title":"Prion diseases: From protein to cell pathology","volume":"172","author":"Kovacs","year":"2008","journal-title":"Am J Pathol"},{"key":"10.3233\/JAD-201308_ref51","doi-asserted-by":"crossref","first-page":"203","DOI":"10.4161\/pri.24503","article-title":"Neuronal zinc regulation and the prion protein","volume":"7","author":"Watt","year":"2013","journal-title":"Prion"},{"key":"10.3233\/JAD-201308_ref52","doi-asserted-by":"crossref","first-page":"35","DOI":"10.1186\/s40478-017-0431-y","article-title":"Altered Ca2+ homeostasis induces Calpain-Cathepsin axis activation in sporadic Creutzfeldt-Jakob disease","volume":"5","author":"Llorens","year":"2017","journal-title":"Acta Neuropathol Commun"},{"key":"10.3233\/JAD-201308_ref53","doi-asserted-by":"crossref","first-page":"1666","DOI":"10.1212\/01.wnl.0000184513.95290.80","article-title":"Increased incidence of genetic human prion disease in Hungary","volume":"65","author":"Kovacs","year":"2005","journal-title":"Neurology"},{"key":"10.3233\/JAD-201308_ref54","doi-asserted-by":"crossref","first-page":"e6647","DOI":"10.1371\/journal.pone.0006647","article-title":"Loss of anti-Bax function in Gerstmann-Straussler-Scheinker syndrome-associated prion protein mutants","volume":"4","author":"Jodoin","journal-title":"PLoS One"},{"key":"10.3233\/JAD-201308_ref55","doi-asserted-by":"crossref","first-page":"3107","DOI":"10.1096\/fj.06-7827com","article-title":"Bcl-2 overexpression delays caspase-3 activation and rescues cerebellar degeneration in prion-deficient mice that overexpress amino-terminally truncated prion","volume":"21","author":"Nicolas","year":"2007","journal-title":"FASEB J"}],"container-title":["Journal of Alzheimer's Disease"],"original-title":[],"link":[{"URL":"https:\/\/content.iospress.com\/download?id=10.3233\/JAD-201308","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2026,4,28]],"date-time":"2026-04-28T10:05:33Z","timestamp":1777370733000},"score":1,"resource":{"primary":{"URL":"https:\/\/journals.sagepub.com\/doi\/full\/10.3233\/JAD-201308"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2021,5,18]]},"references-count":55,"journal-issue":{"issue":"2"},"URL":"https:\/\/doi.org\/10.3233\/jad-201308","relation":{},"ISSN":["1387-2877","1875-8908"],"issn-type":[{"value":"1387-2877","type":"print"},{"value":"1875-8908","type":"electronic"}],"subject":[],"published":{"date-parts":[[2021,5,18]]}}}