{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,25]],"date-time":"2026-09-25T10:08:27Z","timestamp":1790330907805,"version":"4.1.0"},"reference-count":60,"publisher":"The Company of Biologists","issue":"18","license":[{"start":{"date-parts":[[2026,9,25]],"date-time":"2026-09-25T00:00:00Z","timestamp":1790294400000},"content-version":"vor","delay-in-days":10,"URL":"http:\/\/creativecommons.org\/licenses\/by\/4.0"}],"funder":[{"name":"National Institutes of Health"},{"name":"National Institute of Allergy and Infectious Diseases","award":["ZIA AI000752-31"],"award-info":[{"award-number":["ZIA AI000752-31"]}],"id":[{"id":"https:\/\/ror.org\/043z4tv69","id-type":"ROR","asserted-by":"crossref"}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"published-print":{"date-parts":[[2026,9,15]]},"abstract":"<jats:title>ABSTRACT<\/jats:title>\n                  <jats:p>Prion diseases are transmissible, neurodegenerative diseases caused by misfolded, protease-resistant and infectious aggregates of the mammalian prion protein (PrPSc) that replicate by converting properly folded prion protein (PrPC, encoded by PRNP in humans) into PrPSc. Spongiform change and cellular loss in the brain are hallmarks of prion disease, but our understanding of how prions alter cellular fitness remains incomplete. Here, we characterized changes in mitochondrial redox state and respiration in mouse neural cells following uptake of two different PrPSc strains: 22L and 87V. Only 22L PrPSc induced changes in cellular respiration and mitochondrial redox state, even in cells that did not produce PrPC. These effects were disrupted by treatment with detergent and dependent upon endolysosomal acidification, suggesting that both PrPSc membrane association and lysosomal degradation are involved. Interestingly, cells chronically infected with 22L appeared to adapt to infection, showing no signs of mitochondrial dysfunction, but were more susceptible to oxidative stress even though mitochondrial respiration was normal. Thus, during initial prion infection, PrPSc drives mitochondrial dysfunction in a manner that is both strain dependent and independent of PrPC expression, whereas persistent prion infection increases mitochondrial sensitivity to cellular stress.<\/jats:p>","DOI":"10.1242\/jcs.264762","type":"journal-article","created":{"date-parts":[[2026,9,1]],"date-time":"2026-09-01T08:49:41Z","timestamp":1788252581000},"source":"Crossref","is-referenced-by-count":0,"title":["Exposure of cells to prions induces prion strain-dependent changes in mitochondrial redox state and respiration"],"prefix":"10.1242","volume":"139","author":[{"ORCID":"https:\/\/orcid.org\/0009-0004-5773-2920","authenticated-orcid":false,"given":"Daniel","family":"Shoup","sequence":"first","affiliation":[{"name":"National Institute of Allergy and Infectious Diseases, National Institutes of Health Rocky Mountain Laboratories, Laboratory of Neurological Infections and Immunity , , 903 S. 4th St, Hamilton, MT 59840 ,","place":["USA"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Leah R.","family":"Varner","sequence":"additional","affiliation":[{"name":"National Institute of Allergy and Infectious Diseases, National Institutes of Health Rocky Mountain Laboratories, Laboratory of Neurological Infections and Immunity , , 903 S. 4th St, Hamilton, MT 59840 ,","place":["USA"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Brent","family":"Race","sequence":"additional","affiliation":[{"name":"National Institute of Allergy and Infectious Diseases, National Institutes of Health Rocky Mountain Laboratories, Laboratory of Neurological Infections and Immunity , , 903 S. 4th St, Hamilton, MT 59840 ,","place":["USA"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Elyssa","family":"Hawk","sequence":"additional","affiliation":[{"name":"National Institute of Allergy and Infectious Diseases, National Institutes of Health Rocky Mountain Laboratories, Laboratory of Neurological Infections and Immunity , , 903 S. 4th St, Hamilton, MT 59840 ,","place":["USA"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Suzette A.","family":"Priola","sequence":"additional","affiliation":[{"name":"National Institute of Allergy and Infectious Diseases, National Institutes of Health Rocky Mountain Laboratories, Laboratory of Neurological Infections and Immunity , , 903 S. 4th St, Hamilton, MT 59840 ,","place":["USA"]}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"237","published-online":{"date-parts":[[2026,9,25]]},"reference":[{"key":"2026092505450686300_JCS264762C1","doi-asserted-by":"publisher","first-page":"403","DOI":"10.1002\/path.1711760412","article-title":"The abnormal isoform of the prion protein accumulates in late-endosome-like organelles in scrapie-infected mouse brain","volume":"176","author":"Arnold","year":"1995","journal-title":"J. Pathol."},{"key":"2026092505450686300_JCS264762C2","doi-asserted-by":"publisher","first-page":"6556","DOI":"10.1038\/s41598-018-24786-1","article-title":"Prion protein modulates glucose homeostasis by altering intracellular iron","volume":"8","author":"Ashok","year":"2018","journal-title":"Sci. Rep."},{"key":"2026092505450686300_JCS264762C3","doi-asserted-by":"publisher","first-page":"7854","DOI":"10.1128\/JVI.00424-06","article-title":"Prion strain-dependent differences in conversion of mutant prion proteins in cell culture","volume":"80","author":"Atarashi","year":"2006","journal-title":"J. Virol."},{"key":"2026092505450686300_JCS264762C4","doi-asserted-by":"publisher","first-page":"23815","DOI":"10.1073\/pnas.2007406117","article-title":"Highly infectious prions are not directly neurotoxic","volume":"117","author":"Benilova","year":"2020","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"2026092505450686300_JCS264762C5","doi-asserted-by":"publisher","first-page":"329","DOI":"10.1099\/0022-1317-73-2-329","article-title":"Identification of two biologically distinct strains of transmissible mink encephalopathy in hamsters","volume":"73","author":"Bessen","year":"1992","journal-title":"J. Gen. Virol."},{"key":"2026092505450686300_JCS264762C6","doi-asserted-by":"publisher","first-page":"698","DOI":"10.1038\/375698a0","article-title":"Non-genetic propagation of strain-specific properties of scrapie prion protein","volume":"375","author":"Bessen","year":"1995","journal-title":"Nature"},{"key":"2026092505450686300_JCS264762C60","doi-asserted-by":"publisher","first-page":"5404","DOI":"10.1073\/pnas.85.15.5404","article-title":"Overcoming interference to retroviral superinfection results in amplified expression and transmission of cloned genes","volume":"85","author":"Bestwick","year":"1988","journal-title":"Proc. Natl Acad. Sci. USA"},{"key":"2026092505450686300_JCS264762C7","doi-asserted-by":"publisher","first-page":"e1002522","DOI":"10.1371\/journal.ppat.1002522","article-title":"Biochemical properties of highly neuroinvasive prion strains","volume":"8","author":"Bett","year":"2012","journal-title":"PLoS Pathog."},{"key":"2026092505450686300_JCS264762C8","doi-asserted-by":"publisher","first-page":"684","DOI":"10.1038\/37783","article-title":"The cellular prion protein binds copper in vivo","volume":"390","author":"Brown","year":"1997","journal-title":"Nature"},{"key":"2026092505450686300_JCS264762C9","doi-asserted-by":"publisher","first-page":"1339","DOI":"10.1016\/0092-8674(93)90360-3","article-title":"Mice devoid of PrP are resistant to scrapie","volume":"73","author":"B\u00fceler","year":"1993","journal-title":"Cell"},{"key":"2026092505450686300_JCS264762C10","doi-asserted-by":"publisher","first-page":"6597","DOI":"10.1128\/jvi.65.12.6597-6603.1991","article-title":"N-terminal truncation of the scrapie-associated form of PrP by lysosomal protease (s): implications regarding the site of conversion of PrP to the protease-resistant state","volume":"65","author":"Caughey","year":"1991","journal-title":"J. Virol."},{"key":"2026092505450686300_JCS264762C11","doi-asserted-by":"publisher","first-page":"11552","DOI":"10.1128\/JVI.01484-13","article-title":"A specific population of abnormal prion protein aggregates is preferentially taken up by cells and disaggregated in a strain-dependent manner","volume":"87","author":"Choi","year":"2013","journal-title":"J. Virol."},{"key":"2026092505450686300_JCS264762C12","doi-asserted-by":"publisher","first-page":"157","DOI":"10.1016\/j.bbrc.2014.04.069","article-title":"Dysfunction of mitochondrial dynamics in the brains of scrapie-infected mice","volume":"448","author":"Choi","year":"2014","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"2026092505450686300_JCS264762C13","doi-asserted-by":"publisher","first-page":"a006833","DOI":"10.1101\/cshperspect.a006833","article-title":"Prions","volume":"3","author":"Colby","year":"2011","journal-title":"Cold Spring Harbor Perspect. Biol."},{"key":"2026092505450686300_JCS264762C14","doi-asserted-by":"publisher","first-page":"6","DOI":"10.1186\/1750-1326-5-6","article-title":"PrPSc accumulation in neuronal plasma membranes links Notch-1 activation to dendritic degeneration in prion diseases","volume":"5","author":"Dearmond","year":"2010","journal-title":"Mol. Neurodegener."},{"key":"2026092505450686300_JCS264762C15","doi-asserted-by":"publisher","first-page":"41556","DOI":"10.1038\/srep41556","article-title":"Cellular prion protein is present in mitochondria of healthy mice","volume":"7","author":"Faris","year":"2017","journal-title":"Sci. Rep."},{"key":"2026092505450686300_JCS264762C16","doi-asserted-by":"publisher","first-page":"e00524-17","DOI":"10.1128\/jvi.00524-17","article-title":"Mitochondrial respiration is impaired during late-stage hamster prion infection","volume":"91","author":"Faris","year":"2017","journal-title":"J. Virol."},{"key":"2026092505450686300_JCS264762C17","doi-asserted-by":"publisher","first-page":"6923","DOI":"10.1038\/s41598-017-07260-2","article-title":"Prion strains depend on different endocytic routes for productive infection","volume":"7","author":"Fehlinger","year":"2017","journal-title":"Sci. Rep."},{"key":"2026092505450686300_JCS264762C18","doi-asserted-by":"publisher","first-page":"9683","DOI":"10.1073\/pnas.0308413101","article-title":"Cells release prions in association with exosomes","volume":"101","author":"Fevrier","year":"2004","journal-title":"Proc. Natl Acad. Sci. USA"},{"key":"2026092505450686300_JCS264762C19","doi-asserted-by":"publisher","first-page":"102733","DOI":"10.1016\/j.redox.2023.102733","article-title":"Temporary alteration of neuronal network communication is a protective response to redox imbalance that requires GPI-anchored prion protein","volume":"63","author":"Foliaki","year":"2023","journal-title":"Redox Biol."},{"key":"2026092505450686300_JCS264762C20","doi-asserted-by":"publisher","first-page":"e62143","DOI":"10.1371\/journal.pone.0062143","article-title":"Alpha-synuclein induces lysosomal rupture and cathepsin dependent reactive oxygen species following endocytosis","volume":"8","author":"Freeman","year":"2013","journal-title":"PLoS ONE"},{"key":"2026092505450686300_JCS264762C21","doi-asserted-by":"publisher","first-page":"21","DOI":"10.1016\/B978-0-444-63945-5.00002-7","article-title":"The cellular and pathologic prion protein","author":"Gill","year":"2018","journal-title":"Handbook of Clinical Neurology"},{"key":"2026092505450686300_JCS264762C22","doi-asserted-by":"publisher","first-page":"12","DOI":"10.1016\/j.mcn.2014.12.009","article-title":"Prion degradation pathways: potential for therapeutic intervention","volume":"66","author":"Goold","year":"2015","journal-title":"Mol. Cell. Neurosci."},{"key":"2026092505450686300_JCS264762C23","doi-asserted-by":"publisher","first-page":"E2634","DOI":"10.1073\/pnas.1713849115","article-title":"Identification of a highly neurotoxic \u03b1-synuclein species inducing mitochondrial damage and mitophagy in Parkinson's disease","volume":"115","author":"Grassi","year":"2018","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"2026092505450686300_JCS264762C24","doi-asserted-by":"publisher","first-page":"284","DOI":"10.1016\/j.virol.2008.07.006","article-title":"Acute cellular uptake of abnormal prion protein is cell type and scrapie-strain independent","volume":"379","author":"Greil","year":"2008","journal-title":"Virology"},{"key":"2026092505450686300_JCS264762C25","doi-asserted-by":"publisher","first-page":"594","DOI":"10.1016\/j.freeradbiomed.2011.03.035","article-title":"Acute exposure to prion infection induces transient oxidative stress progressing to be cumulatively deleterious with chronic propagation in vitro","volume":"51","author":"Haigh","year":"2011","journal-title":"Free Radic. Biol. Med."},{"key":"2026092505450686300_JCS264762C26","doi-asserted-by":"publisher","first-page":"13044","DOI":"10.1074\/jbc.M312846200","article-title":"Investigating mitochondrial redox potential with redox-sensitive green fluorescent protein indicators","volume":"279","author":"Hanson","year":"2004","journal-title":"J. Biol. Chem."},{"key":"2026092505450686300_JCS264762C27","doi-asserted-by":"publisher","first-page":"4504","DOI":"10.1038\/srep04504","article-title":"Increased expression of p62\/SQSTM1 in prion diseases and its association with pathogenic prion protein","volume":"4","author":"Homma","year":"2014","journal-title":"Sci. Rep."},{"key":"2026092505450686300_JCS264762C28","doi-asserted-by":"publisher","first-page":"200","DOI":"10.1016\/j.virol.2009.08.025","article-title":"Generation of monoclonal antibody that distinguishes PrPSc from PrPC and neutralizes prion infectivity","volume":"394","author":"Horiuchi","year":"2009","journal-title":"Virology"},{"key":"2026092505450686300_JCS264762C29","doi-asserted-by":"publisher","first-page":"e1010947","DOI":"10.1371\/journal.ppat.1010947","article-title":"Cryo-EM of prion strains from the same genotype of host identifies conformational determinants","volume":"18","author":"Hoyt","year":"2022","journal-title":"PLoS Pathog."},{"key":"2026092505450686300_JCS264762C30","doi-asserted-by":"publisher","first-page":"10800","DOI":"10.1038\/s41598-020-67505-5","article-title":"Global analysis of protein degradation in prion infected cells","volume":"10","author":"Hutti","year":"2020","journal-title":"Sci. Rep."},{"key":"2026092505450686300_JCS264762C31","doi-asserted-by":"publisher","first-page":"57","DOI":"10.1016\/j.nbd.2018.11.003","article-title":"Mitochondrial dysfunction in preclinical genetic prion disease: a target for preventive treatment?","volume":"124","author":"Keller","year":"2019","journal-title":"Neurobiol. Dis."},{"key":"2026092505450686300_JCS264762C32","doi-asserted-by":"publisher","first-page":"2744","DOI":"10.3390\/cells11172744","article-title":"Impairment of neuronal mitochondrial quality control in prion-induced neurodegeneration","volume":"11","author":"Kim","year":"2022","journal-title":"Cells"},{"key":"2026092505450686300_JCS264762C33","doi-asserted-by":"publisher","first-page":"1484","DOI":"10.1128\/JVI.02167-10","article-title":"Crucial role for prion protein membrane anchoring in the neuroinvasion and neural spread of prion infection","volume":"85","author":"Klingeborn","year":"2011","journal-title":"J. Virol."},{"key":"2026092505450686300_JCS264762C34","doi-asserted-by":"publisher","first-page":"4540","DOI":"10.1016\/j.molcel.2021.08.011","article-title":"High-resolution structure and strain comparison of infectious mammalian prions","volume":"81","author":"Kraus","year":"2021","journal-title":"Mol. Cell"},{"key":"2026092505450686300_JCS264762C35","doi-asserted-by":"publisher","first-page":"19105","DOI":"10.1073\/pnas.0608970103","article-title":"Continuum of prion protein structures enciphers a multitude of prion isolate-specified phenotypes","volume":"103","author":"Legname","year":"2006","journal-title":"Proc. Natl Acad. Sci. USA"},{"key":"2026092505450686300_JCS264762C36","doi-asserted-by":"publisher","first-page":"1005","DOI":"10.1007\/s10571-008-9274-1","article-title":"Chemically induced accumulation of GAGs delays PrP Sc clearance but prolongs prion disease incubation time","volume":"28","author":"Mayer-Sonnenfeld","year":"2008","journal-title":"Cell. Mol. Neurobiol."},{"key":"2026092505450686300_JCS264762C37","doi-asserted-by":"publisher","first-page":"4469","DOI":"10.1128\/JVI.02412-08","article-title":"Cells expressing anchorless prion protein are resistant to scrapie infection","volume":"83","author":"McNally","year":"2009","journal-title":"J. Virol."},{"key":"2026092505450686300_JCS264762C38","doi-asserted-by":"publisher","first-page":"365","DOI":"10.1038\/s41594-021-00565-x","article-title":"Scaling analysis reveals the mechanism and rates of prion replication in vivo","volume":"28","author":"Meisl","year":"2021","journal-title":"Nat. Struct. Mol. Biol."},{"key":"2026092505450686300_JCS264762C39","doi-asserted-by":"publisher","first-page":"13937","DOI":"10.1073\/pnas.250289197","article-title":"Prion infection impairs the cellular response to oxidative stress","volume":"97","author":"Milhavet","year":"2000","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"2026092505450686300_JCS264762C40","doi-asserted-by":"publisher","first-page":"99","DOI":"10.4161\/pri.3.2.9059","article-title":"Comparative prion disease gene expression profiling using the prion disease mimetic, cuprizone","volume":"3","author":"Moody","year":"2009","journal-title":"Prion"},{"key":"2026092505450686300_JCS264762C41","doi-asserted-by":"publisher","first-page":"681","DOI":"10.1016\/j.bbadis.2006.12.006","article-title":"The prion strain phenomenon: molecular basis and unprecedented features","volume":"1772","author":"Morales","year":"2007","journal-title":"Biochim. Biophys. Acta"},{"key":"2026092505450686300_JCS264762C42","doi-asserted-by":"publisher","first-page":"118928","DOI":"10.1016\/j.bbamcr.2020.118928","article-title":"Cathepsin B is an executioner of ferroptosis","volume":"1868","author":"Nagakannan","year":"2021","journal-title":"Biochim. Biophys. Acta Mol. Cell. Res."},{"key":"2026092505450686300_JCS264762C43","doi-asserted-by":"publisher","first-page":"e0139330","DOI":"10.1371\/journal.pone.0139330","article-title":"Endocytosed 2-microglobulin amyloid fibrils induce necrosis and apoptosis of rabbit synovial fibroblasts by disrupting endosomal\/lysosomal membranes: a novel mechanism on the cytotoxicity of amyloid fibrils","volume":"10","author":"Okoshi","year":"2015","journal-title":"PLoS ONE"},{"key":"2026092505450686300_JCS264762C44","doi-asserted-by":"publisher","first-page":"45","DOI":"10.1016\/B978-0-444-63945-5.00003-9","article-title":"Cell biology of prion infection","volume-title":"Handbook of Clinical Neurology","author":"Priola","year":"2018"},{"key":"2026092505450686300_JCS264762C45","doi-asserted-by":"publisher","first-page":"4673","DOI":"10.1128\/JVI.75.10.4673-4680.2001","article-title":"Efficient conversion of normal prion protein (PrP) by abnormal hamster PrP is determined by homology at amino acid residue 155","volume":"75","author":"Priola","year":"2001","journal-title":"J. Virol."},{"key":"2026092505450686300_JCS264762C46","doi-asserted-by":"publisher","first-page":"e2315690121","DOI":"10.1073\/pnas.2315690121","article-title":"Tau fibrils induce nanoscale membrane damage and nucleate cytosolic tau at lysosomes","volume":"121","author":"Rose","year":"2024","journal-title":"Proc. Natl Acad. Sci. USA"},{"key":"2026092505450686300_JCS264762C47","doi-asserted-by":"publisher","first-page":"398","DOI":"10.1080\/19336896.2017.1391435","article-title":"Novel amplification mechanism of prions through disrupting sortilin-mediated trafficking","volume":"11","author":"Sakaguchi","year":"2017","journal-title":"Prion"},{"key":"2026092505450686300_JCS264762C48","doi-asserted-by":"publisher","first-page":"921908","DOI":"10.3389\/fnmol.2022.921908","article-title":"Mitophagy: an emergence of new player in Alzheimer's disease","volume":"15","author":"Sharma","year":"2022","journal-title":"Front. Mol. Neurosci."},{"key":"2026092505450686300_JCS264762C49","doi-asserted-by":"publisher","first-page":"398","DOI":"10.1021\/acs.biochem.0c00923","article-title":"The size and stability of infectious prion aggregates fluctuate dynamically during cellular uptake and disaggregation","volume":"60","author":"Shoup","year":"2021","journal-title":"Biochemistry"},{"key":"2026092505450686300_JCS264762C50","doi-asserted-by":"publisher","first-page":"165","DOI":"10.1093\/jb\/mvad032","article-title":"Full-length prion protein incorporated into prion aggregates is a marker for prion strain-specific destabilization of aggregate structure following cellular uptake","volume":"174","author":"Shoup","year":"2023","journal-title":"J. Biochem."},{"key":"2026092505450686300_JCS264762C51","doi-asserted-by":"publisher","first-page":"107346","DOI":"10.1016\/j.jbc.2024.107346","article-title":"Grp78 destabilization of infectious prions is strain-specific and modified by multiple factors including accessory chaperones and pH","volume":"300","author":"Shoup","year":"2024","journal-title":"J. Biol. Chem."},{"key":"2026092505450686300_JCS264762C52","doi-asserted-by":"publisher","first-page":"e1008653","DOI":"10.1371\/journal.ppat.1008653","article-title":"Genome-wide transcriptomics identifies an early preclinical signature of prion infection","volume":"16","author":"Sorce","year":"2020","journal-title":"PLoS Pathog."},{"key":"2026092505450686300_JCS264762C53","doi-asserted-by":"publisher","first-page":"541","DOI":"10.1016\/j.molcel.2004.05.012","article-title":"Propagating prions in fungi and mammals","volume":"14","author":"Tuite","year":"2004","journal-title":"Mol. Cell"},{"key":"2026092505450686300_JCS264762C54","doi-asserted-by":"publisher","first-page":"e1006470","DOI":"10.1371\/journal.ppat.1006470","article-title":"Prions amplify through degradation of the VPS10P sorting receptor sortilin","volume":"13","author":"Uchiyama","year":"2017","journal-title":"PLoS Pathog."},{"key":"2026092505450686300_JCS264762C55","doi-asserted-by":"publisher","first-page":"1031","DOI":"10.1002\/jnr.22640","article-title":"Intraneuronal amyloid \u03b2 oligomers cause cell death via endoplasmic reticulum stress, endosomal\/lysosomal leakage, and mitochondrial dysfunction in vivo","volume":"89","author":"Umeda","year":"2011","journal-title":"J. Neurosci. Res."},{"key":"2026092505450686300_JCS264762C56","doi-asserted-by":"publisher","first-page":"14945","DOI":"10.1073\/pnas.93.25.14945","article-title":"Subcellular colocalization of the cellular and scrapie prion proteins in caveolae-like membranous domains","volume":"93","author":"Vey","year":"1996","journal-title":"Proc. Natl Acad. Sci. USA"},{"key":"2026092505450686300_JCS264762C57","doi-asserted-by":"publisher","first-page":"41","DOI":"10.1089\/ars.2015.6587","article-title":"Redox indicator mice stably expressing genetically encoded neuronal roGFP: versatile tools to decipher subcellular redox dynamics in neuropathophysiology","volume":"25","author":"Wagener","year":"2016","journal-title":"Antioxid Redox Signal."},{"key":"2026092505450686300_JCS264762C58","doi-asserted-by":"publisher","first-page":"e0267720","DOI":"10.1371\/journal.pone.0267720","article-title":"Lack of the immune adaptor molecule SARM1 accelerates disease in prion infected mice and is associated with increased mitochondrial respiration and decreased expression of NRF2","volume":"17","author":"Ward","year":"2022","journal-title":"PLoS ONE"},{"key":"2026092505450686300_JCS264762C59","doi-asserted-by":"publisher","first-page":"35914","DOI":"10.1074\/jbc.M507327200","article-title":"Reactive oxygen species-mediated \u03b2-cleavage of the prion protein in the cellular response to oxidative stress","volume":"280","author":"Watt","year":"2005","journal-title":"J. Biol. Chem."}],"container-title":["Journal of Cell Science"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/journals.biologists.com\/jcs\/article-pdf\/doi\/10.1242\/jcs.264762\/3715225\/jcs264762.pdf","content-type":"application\/pdf","content-version":"am","intended-application":"syndication"},{"URL":"https:\/\/journals.biologists.com\/jcs\/article-pdf\/doi\/10.1242\/jcs.264762\/3719291\/jcs264762.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"syndication"},{"URL":"https:\/\/journals.biologists.com\/jcs\/article-pdf\/doi\/10.1242\/jcs.264762\/3719291\/jcs264762.pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2026,9,25]],"date-time":"2026-09-25T09:45:52Z","timestamp":1790329552000},"score":1,"resource":{"primary":{"URL":"https:\/\/journals.biologists.com\/jcs\/article\/139\/18\/jcs264762\/373006\/Exposure-of-cells-to-prions-induces-prion-strain"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2026,9,15]]},"references-count":60,"journal-issue":{"issue":"18","published-print":{"date-parts":[[2026,9,15]]}},"URL":"https:\/\/doi.org\/10.1242\/jcs.264762","relation":{},"ISSN":["0021-9533","1477-9137"],"issn-type":[{"value":"0021-9533","type":"print"},{"value":"1477-9137","type":"electronic"}],"subject":[],"published":{"date-parts":[[2026,9,15]]},"article-number":"jcs264762"}}