{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,26]],"date-time":"2026-10-26T19:17:44Z","timestamp":1793042264785,"version":"4.5.0"},"reference-count":156,"publisher":"Elsevier BV","license":[{"start":{"date-parts":[[2015,9,1]],"date-time":"2015-09-01T00:00:00Z","timestamp":1441065600000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2015,2,17]],"date-time":"2015-02-17T00:00:00Z","timestamp":1424131200000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"DOI":"10.13039\/501100004963","name":"FP7","doi-asserted-by":"publisher","award":["222887"],"award-info":[{"award-number":["222887"]}],"id":[{"id":"10.13039\/501100004963","id-type":"DOI","asserted-by":"publisher"}]},{"name":"Alberta Prion Research Institute","award":["2011000111"],"award-info":[{"award-number":["2011000111"]}]},{"DOI":"10.13039\/501100002715","name":"Alberta Livestock and Meat Agency","doi-asserted-by":"publisher","award":["2012A001R"],"award-info":[{"award-number":["2012A001R"]}],"id":[{"id":"10.13039\/501100002715","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Virus Research"],"published-print":{"date-parts":[[2015,9]]},"DOI":"10.1016\/j.virusres.2015.02.004","type":"journal-article","created":{"date-parts":[[2015,2,12]],"date-time":"2015-02-12T19:14:53Z","timestamp":1423768493000},"page":"136-145","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":23,"special_numbering":"C","title":["Subcellular distribution of the prion protein in sickness and in health"],"prefix":"10.1016","volume":"207","author":[{"ORCID":"https:\/\/orcid.org\/0000-0002-3359-6483","authenticated-orcid":false,"given":"Susan F.","family":"Godsave","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Peter J.","family":"Peters","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-5102-8706","authenticated-orcid":false,"given":"Holger","family":"Wille","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"key":"10.1016\/j.virusres.2015.02.004_bib0005","doi-asserted-by":"crossref","first-page":"2409","DOI":"10.1016\/j.febslet.2010.04.040","article-title":"Cellular factors implicated in prion replication","volume":"584","author":"Abid","year":"2010","journal-title":"FEBS Lett."},{"key":"10.1016\/j.virusres.2015.02.004_bib0010","doi-asserted-by":"crossref","first-page":"994","DOI":"10.1111\/his.12097","article-title":"Localization of A11-reactive oligomeric species in prion diseases","volume":"62","author":"Aidt","year":"2013","journal-title":"Histopathology"},{"key":"10.1016\/j.virusres.2015.02.004_bib0015","first-page":"15","article-title":"Proteolytic processing of the prion protein in health and disease","volume":"1","author":"Altmeppen","year":"2012","journal-title":"Am. J. Neurodegener. Dis."},{"key":"10.1016\/j.virusres.2015.02.004_bib0020","doi-asserted-by":"crossref","first-page":"1530","DOI":"10.1016\/j.freeradbiomed.2008.08.028","article-title":"Opposing roles of prion protein in oxidative stress- and ER stress-induced apoptotic signaling","volume":"45","author":"Anantharam","year":"2008","journal-title":"Free Radic. Biol. Med."},{"key":"10.1016\/j.virusres.2015.02.004_bib0025","doi-asserted-by":"crossref","first-page":"693","DOI":"10.1002\/mc.20642","article-title":"Prion protein expression and the M129V polymorphism of the PRNP gene in patients with colorectal cancer","volume":"49","author":"Antonacopoulou","year":"2010","journal-title":"Mol. Carcinog."},{"key":"10.1016\/j.virusres.2015.02.004_bib0030","doi-asserted-by":"crossref","first-page":"18008","DOI":"10.1074\/jbc.M313581200","article-title":"The effect of disease-associated mutations on the folding pathway of human prion protein","volume":"279","author":"Apetri","year":"2004","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.virusres.2015.02.004_bib0035","doi-asserted-by":"crossref","first-page":"e1003643","DOI":"10.1371\/journal.ppat.1003643","article-title":"Inherited prion disease A117V is not simply a proteinopathy but produces prions transmissible to transgenic mice expressing homologous prion protein","volume":"9","author":"Asante","year":"2013","journal-title":"PLoS Pathog."},{"key":"10.1016\/j.virusres.2015.02.004_bib0040","doi-asserted-by":"crossref","first-page":"3463","DOI":"10.1091\/mbc.E08-01-0087","article-title":"Retrotranslocation of prion proteins from the endoplasmic reticulum by preventing GPI signal transamidation","volume":"19","author":"Ashok","year":"2008","journal-title":"Mol. Biol. Cell"},{"key":"10.1016\/j.virusres.2015.02.004_bib0045","doi-asserted-by":"crossref","first-page":"e1001317","DOI":"10.1371\/journal.ppat.1001317","article-title":"The strain-encoded relationship between PrP replication, stability and processing in neurons is predictive of the incubation period of disease","volume":"7","author":"Ayers","year":"2011","journal-title":"PLoS Pathog."},{"key":"10.1016\/j.virusres.2015.02.004_bib0050","doi-asserted-by":"crossref","first-page":"692","DOI":"10.1016\/j.bbadis.2006.07.007","article-title":"Converting the prion protein: what makes the protein infectious","volume":"1772","author":"Baskakov","year":"2007","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/j.virusres.2015.02.004_bib0055","doi-asserted-by":"crossref","first-page":"7935","DOI":"10.1074\/jbc.M111.275743","article-title":"Neurodegeneration induced by clustering of sialylated glycosylphosphatidylinositols of prion proteins","volume":"287","author":"Bate","year":"2012","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.virusres.2015.02.004_bib0060","doi-asserted-by":"crossref","first-page":"354","DOI":"10.1212\/WNL.57.2.354","article-title":"Two-octapeptide repeat deletion of prion protein associated with rapidly progressive dementia","volume":"57","author":"Beck","year":"2001","journal-title":"Neurology"},{"key":"10.1016\/j.virusres.2015.02.004_bib0065","doi-asserted-by":"crossref","first-page":"472","DOI":"10.1126\/science.1215659","article-title":"Facilitated cross-species transmission of prions in extraneural tissue","volume":"335","author":"Beringue","year":"2012","journal-title":"Science"},{"key":"10.1016\/j.virusres.2015.02.004_bib0070","doi-asserted-by":"crossref","first-page":"47","DOI":"10.1051\/vetres:2008024","article-title":"Prion agent diversity and species barrier","volume":"39","author":"Beringue","year":"2008","journal-title":"Vet. Res."},{"key":"10.1016\/j.virusres.2015.02.004_bib0075","doi-asserted-by":"crossref","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":"10.1016\/j.virusres.2015.02.004_bib0080","doi-asserted-by":"crossref","first-page":"319","DOI":"10.1093\/glycob\/3.4.319","article-title":"Release of the cellular prion protein from cultured cells after loss of its glycoinositol phospholipid anchor","volume":"3","author":"Borchelt","year":"1993","journal-title":"Glycobiology"},{"key":"10.1016\/j.virusres.2015.02.004_bib0085","doi-asserted-by":"crossref","first-page":"339","DOI":"10.1038\/379339a0","article-title":"Normal host prion protein necessary for scrapie-induced neurotoxicity","volume":"379","author":"Brandner","year":"1996","journal-title":"Nature"},{"key":"10.1016\/j.virusres.2015.02.004_bib0090","doi-asserted-by":"crossref","first-page":"684","DOI":"10.1038\/37733","article-title":"The cellular prion protein binds copper in vivo","volume":"390","author":"Brown","year":"1997","journal-title":"Nature"},{"key":"10.1016\/j.virusres.2015.02.004_bib0095","doi-asserted-by":"crossref","first-page":"1339","DOI":"10.1016\/0092-8674(93)90360-3","article-title":"Mice devoid of PrP are resistant to scrapie","volume":"73","author":"Bueler","year":"1993","journal-title":"Cell"},{"key":"10.1016\/j.virusres.2015.02.004_bib0100","doi-asserted-by":"crossref","first-page":"102","DOI":"10.1016\/j.tcb.2004.12.002","article-title":"The highways and byways of prion protein trafficking","volume":"15","author":"Campana","year":"2005","journal-title":"Trends Cell Biol."},{"key":"10.1016\/j.virusres.2015.02.004_bib0105","doi-asserted-by":"crossref","first-page":"1628","DOI":"10.1212\/01.WNL.0000035533.86833.28","article-title":"Creutzfeldt-Jakob disease associated with a deletion of two repeats in the prion protein gene","volume":"59","author":"Capellari","year":"2002","journal-title":"Neurology"},{"key":"10.1016\/j.virusres.2015.02.004_bib0110","doi-asserted-by":"crossref","first-page":"21","DOI":"10.1007\/s00401-010-0760-4","article-title":"Genetic Creutzfeldt-Jakob disease and fatal familial insomnia: insights into phenotypic variability and disease pathogenesis","volume":"121","author":"Capellari","year":"2011","journal-title":"Acta Neuropathol."},{"key":"10.1016\/j.virusres.2015.02.004_bib0115","doi-asserted-by":"crossref","first-page":"2135","DOI":"10.1128\/JVI.68.4.2135-2141.1994","article-title":"Binding of the protease-sensitive form of PrP (prion protein) to sulfated glycosaminoglycan and congo red [corrected]","volume":"68","author":"Caughey","year":"1994","journal-title":"J. Virol."},{"key":"10.1016\/j.virusres.2015.02.004_bib0120","doi-asserted-by":"crossref","first-page":"267","DOI":"10.1146\/annurev.neuro.26.010302.081142","article-title":"Protofibrils, pores, fibrils, and neurodegeneration: separating the responsible protein aggregates from the innocent bystanders","volume":"26","author":"Caughey","year":"2003","journal-title":"Annu. Rev. Neurosci."},{"key":"10.1016\/j.virusres.2015.02.004_bib0125","doi-asserted-by":"crossref","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":"10.1016\/j.virusres.2015.02.004_bib0130","doi-asserted-by":"crossref","first-page":"19173","DOI":"10.1074\/jbc.270.32.19173","article-title":"Truncated forms of the human prion protein in normal brain and in prion diseases","volume":"270","author":"Chen","year":"1995","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.virusres.2015.02.004_bib0135","doi-asserted-by":"crossref","first-page":"e1000800","DOI":"10.1371\/journal.ppat.1000800","article-title":"Fatal transmissible amyloid encephalopathy: a new type of prion disease associated with lack of prion protein membrane anchoring","volume":"6","author":"Chesebro","year":"2010","journal-title":"PLoS Pathog."},{"key":"10.1016\/j.virusres.2015.02.004_bib0140","doi-asserted-by":"crossref","first-page":"363","DOI":"10.1016\/j.nbd.2005.12.002","article-title":"An integrated, temporal study of the behavioural, electrophysiological and neuropathological consequences of murine prion disease","volume":"22","author":"Chiti","year":"2006","journal-title":"Neurobiol. Dis."},{"key":"10.1016\/j.virusres.2015.02.004_bib0145","doi-asserted-by":"crossref","first-page":"a006833","DOI":"10.1101\/cshperspect.a006833","article-title":"Prions","volume":"3","author":"Colby","year":"2011","journal-title":"Cold Spring Harb. Perspect. Biol."},{"key":"10.1016\/j.virusres.2015.02.004_bib0150","doi-asserted-by":"crossref","first-page":"1166","DOI":"10.1136\/jnnp.2003.020198","article-title":"Octapeptide repeat insertions in the prion protein gene and early onset dementia","volume":"75","author":"Croes","year":"2004","journal-title":"J. Neurol. Neurosurg. Psychiatr."},{"key":"10.1016\/j.virusres.2015.02.004_bib0155","doi-asserted-by":"crossref","first-page":"2147","DOI":"10.1046\/j.1460-9568.2003.02662.x","article-title":"Synaptic changes characterize early behavioural signs in the ME7 model of murine prion disease","volume":"17","author":"Cunningham","year":"2003","journal-title":"Eur. J. Neurosci."},{"key":"10.1016\/j.virusres.2015.02.004_bib0160","doi-asserted-by":"crossref","first-page":"855","DOI":"10.1136\/gutjnl-2011-300511","article-title":"Cell surface proteomics identifies glucose transporter type 1 and prion protein as candidate biomarkers for colorectal adenoma-to-carcinoma progression","volume":"61","author":"de Wit","year":"2012","journal-title":"Gut"},{"key":"10.1016\/j.virusres.2015.02.004_bib0165","doi-asserted-by":"crossref","first-page":"R22","DOI":"10.1186\/bcr3398","article-title":"Endoplasmic reticulum stress induces PRNP prion protein gene expression in breast cancer","volume":"15","author":"Dery","year":"2013","journal-title":"Breast Cancer Res."},{"key":"10.1016\/j.virusres.2015.02.004_bib0170","doi-asserted-by":"crossref","first-page":"209","DOI":"10.2478\/s11658-013-0085-0","article-title":"Prion protein and its role in signal transduction","volume":"18","author":"Didonna","year":"2013","journal-title":"Cell. Mol. Biol. Lett."},{"key":"10.1016\/j.virusres.2015.02.004_bib0175","doi-asserted-by":"crossref","first-page":"29","DOI":"10.1186\/1750-1326-5-29","article-title":"Aberrant ERK 1\/2 complex activation and localization in scrapie-infected GT1-1 cells","volume":"5","author":"Didonna","year":"2010","journal-title":"Mol. Neurodegener."},{"key":"10.1016\/j.virusres.2015.02.004_bib0180","doi-asserted-by":"crossref","first-page":"21732","DOI":"10.1074\/jbc.M213247200","article-title":"Mutant PrP is delayed in its exit from the endoplasmic reticulum, but neither wild-type nor mutant PrP undergoes retrotranslocation prior to proteasomal degradation","volume":"278","author":"Drisaldi","year":"2003","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.virusres.2015.02.004_bib0185","doi-asserted-by":"crossref","first-page":"213","DOI":"10.1002\/ijc.20570","article-title":"Overexpression and significance of prion protein in gastric cancer and multidrug-resistant gastric carcinoma cell line SGC7901\/ADR","volume":"113","author":"Du","year":"2005","journal-title":"Int. J. Cancer"},{"key":"10.1016\/j.virusres.2015.02.004_bib0190","doi-asserted-by":"crossref","first-page":"259","DOI":"10.1111\/j.1365-2990.2008.00988.x","article-title":"Abnormal prion protein is associated with changes of plasma membranes and endocytosis in bovine spongiform encephalopathy (BSE)-affected cattle brains","volume":"35","author":"Ersdal","year":"2009","journal-title":"Neuropathol. Appl. Neurobiol."},{"key":"10.1016\/j.virusres.2015.02.004_bib0195","doi-asserted-by":"crossref","first-page":"11","DOI":"10.1016\/j.nbd.2013.03.007","article-title":"Targeted mutation of the gene encoding prion protein in zebrafish reveals a conserved role in neuron excitability","volume":"55","author":"Fleisch","year":"2013","journal-title":"Neurobiol. Dis."},{"key":"10.1016\/j.virusres.2015.02.004_bib0200","doi-asserted-by":"crossref","first-page":"189","DOI":"10.1097\/NEN.0b013e3181654386","article-title":"Loss of perineuronal net in ME7 prion disease","volume":"67","author":"Franklin","year":"2008","journal-title":"J. Neuropathol. Exp. Neurol."},{"key":"10.1016\/j.virusres.2015.02.004_bib0205","doi-asserted-by":"crossref","first-page":"5863","DOI":"10.1093\/emboj\/20.21.5863","article-title":"The 37-kDa\/67-kDa laminin receptor acts as the cell-surface receptor for the cellular prion protein","volume":"20","author":"Gauczynski","year":"2001","journal-title":"EMBO J."},{"key":"10.1016\/j.virusres.2015.02.004_bib0210","doi-asserted-by":"crossref","first-page":"744","DOI":"10.1073\/pnas.93.2.744","article-title":"Vascular variant of prion protein cerebral amyloidosis with tau-positive neurofibrillary tangles: the phenotype of the stop codon 145 mutation in PRNP","volume":"93","author":"Ghetti","year":"1996","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.virusres.2015.02.004_bib0215","doi-asserted-by":"crossref","first-page":"12489","DOI":"10.1523\/JNEUROSCI.4474-08.2008","article-title":"Cryo-immunogold electron microscopy for prions: toward identification of a conversion site","volume":"28","author":"Godsave","year":"2008","journal-title":"J. Neurosci."},{"key":"10.1016\/j.virusres.2015.02.004_bib0220","doi-asserted-by":"crossref","first-page":"1621","DOI":"10.1016\/j.neurobiolaging.2012.12.015","article-title":"Plasma membrane invaginations containing clusters of full-length PrP(Sc) are an early form of prion-associated neuropathology in vivo","volume":"34","author":"Godsave","year":"2013","journal-title":"Neurobiol. Aging"},{"key":"10.1016\/j.virusres.2015.02.004_bib0225","doi-asserted-by":"crossref","first-page":"281","DOI":"10.1038\/ncomms1282","article-title":"Rapid cell-surface prion protein conversion revealed using a novel cell system","volume":"2","author":"Goold","year":"2011","journal-title":"Nat. Commun."},{"key":"10.1016\/j.virusres.2015.02.004_bib0230","doi-asserted-by":"crossref","first-page":"85","DOI":"10.1016\/S0169-328X(99)00334-4","article-title":"Cellular prion protein binds laminin and mediates neuritogenesis","volume":"76","author":"Graner","year":"2000","journal-title":"Brain Res. Mol. Brain Res."},{"key":"10.1016\/j.virusres.2015.02.004_bib0235","doi-asserted-by":"crossref","first-page":"63","DOI":"10.1016\/j.nbd.2009.04.001","article-title":"Selective presynaptic degeneration in the synaptopathy associated with ME7-induced hippocampal pathology","volume":"35","author":"Gray","year":"2009","journal-title":"Neurobiol. Dis."},{"key":"10.1016\/j.virusres.2015.02.004_bib0240","doi-asserted-by":"crossref","first-page":"1456","DOI":"10.1111\/j.1471-4159.2006.03837.x","article-title":"Molecular morphology and toxicity of cytoplasmic prion protein aggregates in neuronal and non-neuronal cells","volume":"97","author":"Grenier","year":"2006","journal-title":"J. Neurochem."},{"key":"10.1016\/j.virusres.2015.02.004_bib0245","doi-asserted-by":"crossref","first-page":"35973","DOI":"10.1074\/jbc.M109.051086","article-title":"The alpha-secretase-derived N-terminal product of cellular prion, N1, displays neuroprotective function in vitro and in vivo","volume":"284","author":"Guillot-Sestier","year":"2009","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.virusres.2015.02.004_bib0250","doi-asserted-by":"crossref","first-page":"5021","DOI":"10.1074\/jbc.M111.323626","article-title":"alpha-Secretase-derived fragment of cellular prion, N1, protects against monomeric and oligomeric amyloid beta (Abeta)-associated cell death","volume":"287","author":"Guillot-Sestier","year":"2012","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.virusres.2015.02.004_bib0255","doi-asserted-by":"crossref","first-page":"1915","DOI":"10.1242\/jcs.03459","article-title":"Cellular prion protein interaction with vitronectin supports axonal growth and is compensated by integrins","volume":"120","author":"Hajj","year":"2007","journal-title":"J. Cell Sci."},{"key":"10.1016\/j.virusres.2015.02.004_bib0260","doi-asserted-by":"crossref","first-page":"1009","DOI":"10.1021\/bi00055a003","article-title":"Processing of a cellular prion protein: identification of N- and C-terminal cleavage sites","volume":"32","author":"Harris","year":"1993","journal-title":"Biochemistry"},{"key":"10.1016\/j.virusres.2015.02.004_bib0265","doi-asserted-by":"crossref","first-page":"827","DOI":"10.1126\/science.279.5352.827","article-title":"A transmembrane form of the prion protein in neurodegenerative disease","volume":"279","author":"Hegde","year":"1998","journal-title":"Science"},{"key":"10.1016\/j.virusres.2015.02.004_bib0270","doi-asserted-by":"crossref","first-page":"85","DOI":"10.1016\/S1097-2765(00)80116-1","article-title":"Regulation of protein topology by trans-acting factors at the endoplasmic reticulum","volume":"2","author":"Hegde","year":"1998","journal-title":"Mol. Cell"},{"key":"10.1016\/j.virusres.2015.02.004_bib0275","doi-asserted-by":"crossref","first-page":"12725","DOI":"10.1074\/jbc.M611909200","article-title":"Perturbation of endoplasmic reticulum homeostasis facilitates prion replication","volume":"282","author":"Hetz","year":"2007","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.virusres.2015.02.004_bib0280","doi-asserted-by":"crossref","first-page":"37","DOI":"10.2174\/156652406775574578","article-title":"Stressing out the ER: a role of the unfolded protein response in prion-related disorders","volume":"6","author":"Hetz","year":"2006","journal-title":"Curr. Mol. Med."},{"key":"10.1016\/j.virusres.2015.02.004_bib0285","doi-asserted-by":"crossref","first-page":"886","DOI":"10.1073\/pnas.0408612101","article-title":"Notch-1 activation and dendritic atrophy in prion disease","volume":"102","author":"Ishikura","year":"2005","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.virusres.2015.02.004_bib0290","doi-asserted-by":"crossref","first-page":"781","DOI":"10.1002\/ana.20093","article-title":"Scrapie-specific neuronal lesions are independent of neuronal PrP expression","volume":"55","author":"Jeffrey","year":"2004","journal-title":"Ann. Neurol."},{"key":"10.1016\/j.virusres.2015.02.004_bib0295","doi-asserted-by":"crossref","first-page":"41","DOI":"10.1046\/j.1365-2990.2000.00216.x","article-title":"Synapse loss associated with abnormal PrP precedes neuronal degeneration in the scrapie-infected murine hippocampus","volume":"26","author":"Jeffrey","year":"2000","journal-title":"Neuropathol. Appl. Neurobiol."},{"key":"10.1016\/j.virusres.2015.02.004_bib0300","doi-asserted-by":"crossref","first-page":"113","DOI":"10.1007\/s00401-010-0700-3","article-title":"Cellular and sub-cellular pathology of animal prion diseases: relationship between morphological changes, accumulation of abnormal prion protein and clinical disease","volume":"121","author":"Jeffrey","year":"2011","journal-title":"Acta Neuropathol."},{"key":"10.1016\/j.virusres.2015.02.004_bib0305","doi-asserted-by":"crossref","first-page":"32018","DOI":"10.1074\/jbc.M403467200","article-title":"Preferential Cu2+ coordination by His96 and His111 induces beta-sheet formation in the unstructured amyloidogenic region of the prion protein","volume":"279","author":"Jones","year":"2004","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.virusres.2015.02.004_bib0310","doi-asserted-by":"crossref","first-page":"1829","DOI":"10.1093\/brain\/awr079","article-title":"Inherited prion disease with 4-octapeptide repeat insertion: disease requires the interaction of multiple genetic risk factors","volume":"134","author":"Kaski","year":"2011","journal-title":"Brain"},{"key":"10.1016\/j.virusres.2015.02.004_bib0315","doi-asserted-by":"crossref","first-page":"3671","DOI":"10.1016\/j.febslet.2009.10.049","article-title":"The role of glycophosphatidylinositol anchor in the amplification of the scrapie isoform of prion protein in vitro","volume":"583","author":"Kim","year":"2009","journal-title":"FEBS Lett."},{"key":"10.1016\/j.virusres.2015.02.004_bib0320","doi-asserted-by":"crossref","first-page":"287","DOI":"10.1016\/S0002-9440(10)62252-3","article-title":"Subcellular localization of disease-associated prion protein in the human brain","volume":"166","author":"Kovacs","year":"2005","journal-title":"Am. J. Pathol."},{"key":"10.1016\/j.virusres.2015.02.004_bib0325","doi-asserted-by":"crossref","first-page":"16857","DOI":"10.1523\/JNEUROSCI.1858-12.2012","article-title":"The complex PrP(c)-Fyn couples human oligomeric Abeta with pathological tau changes in Alzheimer's disease","volume":"32","author":"Larson","year":"2012","journal-title":"J. Neurosci."},{"key":"10.1016\/j.virusres.2015.02.004_bib0330","doi-asserted-by":"crossref","DOI":"10.15252\/emmm.201404588","article-title":"Octarepeat region flexibility impacts prion function, endoproteolysis and disease manifestation","volume":"7","author":"Lau","year":"2015","journal-title":"EMBO Mol. Med."},{"key":"10.1016\/j.virusres.2015.02.004_bib0335","doi-asserted-by":"crossref","first-page":"1128","DOI":"10.1038\/nature07761","article-title":"Cellular prion protein mediates impairment of synaptic plasticity by amyloid-beta oligomers","volume":"457","author":"Laur\u00e9n","year":"2009","journal-title":"Nature"},{"key":"10.1016\/j.virusres.2015.02.004_bib0340","doi-asserted-by":"crossref","first-page":"362","DOI":"10.1111\/j.1471-4159.2010.06601.x","article-title":"Treatment with normal prion protein delays differentiation and helps to maintain high proliferation activity in human embryonic stem cells","volume":"114","author":"Lee","year":"2010","journal-title":"J. Neurochem."},{"key":"10.1016\/j.virusres.2015.02.004_bib0345","doi-asserted-by":"crossref","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. U. S. A."},{"key":"10.1016\/j.virusres.2015.02.004_bib0350","doi-asserted-by":"crossref","first-page":"279","DOI":"10.1091\/mbc.E04-06-0508","article-title":"The efficiency of protein compartmentalization into the secretory pathway","volume":"16","author":"Levine","year":"2005","journal-title":"Mol. Biol. Cell"},{"key":"10.1016\/j.virusres.2015.02.004_bib0355","doi-asserted-by":"crossref","first-page":"1125","DOI":"10.1097\/NEN.0b013e3181b96981","article-title":"Increased proportions of C1 truncated prion protein protect against cellular M1000 prion infection","volume":"68","author":"Lewis","year":"2009","journal-title":"J. Neuropathol. Exp. Neurol."},{"key":"10.1016\/j.virusres.2015.02.004_bib0360","doi-asserted-by":"crossref","first-page":"30328","DOI":"10.1074\/jbc.M110.147413","article-title":"Pro-prion binds filamin A, facilitating its interaction with integrin beta1, and contributes to melanomagenesis","volume":"285","author":"Li","year":"2010","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.virusres.2015.02.004_bib0365","doi-asserted-by":"crossref","first-page":"2725","DOI":"10.1172\/JCI39542","article-title":"Binding of pro-prion to filamin A disrupts cytoskeleton and correlates with poor prognosis in pancreatic cancer","volume":"119","author":"Li","year":"2009","journal-title":"J. Clin. Investig."},{"key":"10.1016\/j.virusres.2015.02.004_bib0370","doi-asserted-by":"crossref","first-page":"504","DOI":"10.1007\/s00018-008-8548-6","article-title":"The role of P-glycoprotein\/cellular prion protein interaction in multidrug-resistant breast cancer cells treated with paclitaxel","volume":"66","author":"Li","year":"2009","journal-title":"Cell. Mol. Life Sci."},{"key":"10.1016\/j.virusres.2015.02.004_bib0375","doi-asserted-by":"crossref","first-page":"769","DOI":"10.4161\/cbt.6.5.4001","article-title":"Hypoxia induced overexpression of PrP(C) in gastric cancer cell lines","volume":"6","author":"Liang","year":"2007","journal-title":"Cancer Biol. Ther."},{"key":"10.1016\/j.virusres.2015.02.004_bib0380","doi-asserted-by":"crossref","first-page":"1041","DOI":"10.1534\/genetics.111.137760","article-title":"Prions in yeast","volume":"191","author":"Liebman","year":"2012","journal-title":"Genetics"},{"key":"10.1016\/j.virusres.2015.02.004_bib0385","doi-asserted-by":"crossref","first-page":"2001","DOI":"10.1016\/j.bbamcr.2008.05.022","article-title":"Cytosolic prion protein is the predominant anti-Bax prion protein form: exclusion of transmembrane and secreted prion protein forms in the anti-Bax function","volume":"1783","author":"Lin","year":"2008","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/j.virusres.2015.02.004_bib0390","doi-asserted-by":"crossref","first-page":"1105","DOI":"10.1007\/s00018-011-0847-7","article-title":"Allosteric function and dysfunction of the prion protein","volume":"69","author":"Linden","year":"2012","journal-title":"Cell. Mol. Life Sci."},{"key":"10.1016\/j.virusres.2015.02.004_bib0395","doi-asserted-by":"crossref","first-page":"11330","DOI":"10.1523\/JNEUROSCI.2313-05.2005","article-title":"Interaction of cellular prion and stress-inducible protein 1 promotes neuritogenesis and neuroprotection by distinct signaling pathways","volume":"25","author":"Lopes","year":"2005","journal-title":"J. Neurosci."},{"key":"10.1016\/j.virusres.2015.02.004_bib0400","doi-asserted-by":"crossref","first-page":"8508","DOI":"10.1074\/jbc.M110197200","article-title":"Cellular phenotyping of secretory and nuclear prion proteins associated with inherited prion diseases","volume":"277","author":"Lorenz","year":"2002","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.virusres.2015.02.004_bib0405","doi-asserted-by":"crossref","first-page":"14955","DOI":"10.1073\/pnas.011578098","article-title":"Wild-type PrP and a mutant associated with prion disease are subject to retrograde transport and proteasome degradation","volume":"98","author":"Ma","year":"2001","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.virusres.2015.02.004_bib0410","doi-asserted-by":"crossref","first-page":"1785","DOI":"10.1126\/science.1073619","article-title":"Conversion of PrP to a self-perpetuating PrPSc-like conformation in the cytosol","volume":"298","author":"Ma","year":"2002","journal-title":"Science"},{"key":"10.1016\/j.virusres.2015.02.004_bib0541","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":"10.1016\/j.virusres.2015.02.004_bib0415","doi-asserted-by":"crossref","first-page":"201","DOI":"10.1038\/nrmicro1346","article-title":"Prions and their lethal journey to the brain","volume":"4","author":"Mabbott","year":"2006","journal-title":"Nat. Rev. Microbiol."},{"key":"10.1016\/j.virusres.2015.02.004_bib0420","doi-asserted-by":"crossref","first-page":"328","DOI":"10.1126\/science.1173155","article-title":"Functional amyloids as natural storage of peptide hormones in pituitary secretory granules","volume":"325","author":"Maji","year":"2009","journal-title":"Science"},{"key":"10.1016\/j.virusres.2015.02.004_bib0425","doi-asserted-by":"crossref","first-page":"e55","DOI":"10.1371\/journal.pbio.1000055","article-title":"Regulation of embryonic cell adhesion by the prion protein","volume":"7","author":"Malaga-Trillo","year":"2009","journal-title":"PLoS Biol."},{"key":"10.1016\/j.virusres.2015.02.004_bib0430","doi-asserted-by":"crossref","first-page":"871","DOI":"10.1126\/science.1090187","article-title":"Depleting neuronal PrP in prion infection prevents disease and reverses spongiosis","volume":"302","author":"Mallucci","year":"2003","journal-title":"Science"},{"key":"10.1016\/j.virusres.2015.02.004_bib0435","doi-asserted-by":"crossref","first-page":"195","DOI":"10.4161\/pri.3.4.9981","article-title":"Prion neurodegeneration: starts and stops at the synapse","volume":"3","author":"Mallucci","year":"2009","journal-title":"Prion"},{"key":"10.1016\/j.virusres.2015.02.004_bib0440","doi-asserted-by":"crossref","first-page":"125","DOI":"10.1016\/j.biolcel.2003.11.007","article-title":"Alpha- and beta-cleavages of the amino-terminus of the cellular prion protein","volume":"96","author":"Mange","year":"2004","journal-title":"Biol. Cell\/Under Auspices Eur. Cell Biol. Organ."},{"key":"10.1016\/j.virusres.2015.02.004_bib0445","doi-asserted-by":"crossref","first-page":"e1000426","DOI":"10.1371\/journal.ppat.1000426","article-title":"Identification of an intracellular site of prion conversion","volume":"5","author":"Marijanovic","year":"2009","journal-title":"PLoS Pathog."},{"key":"10.1016\/j.virusres.2015.02.004_bib0450","first-page":"63","article-title":"Prion protein: orchestrating neurotrophic activities","volume":"12","author":"Martins","year":"2010","journal-title":"Curr. Issues Mol. Biol."},{"key":"10.1016\/j.virusres.2015.02.004_bib0455","doi-asserted-by":"crossref","first-page":"141","DOI":"10.1159\/000225243","article-title":"Antibodies to prion protein inhibit human colon cancer cell growth","volume":"30","author":"McEwan","year":"2009","journal-title":"Tumour Biol."},{"key":"10.1016\/j.virusres.2015.02.004_bib0460","doi-asserted-by":"crossref","first-page":"2286","DOI":"10.1074\/jbc.M007243200","article-title":"Cleavage of the amino terminus of the prion protein by reactive oxygen species","volume":"276","author":"McMahon","year":"2001","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.virusres.2015.02.004_bib0465","doi-asserted-by":"crossref","first-page":"7183","DOI":"10.1523\/JNEUROSCI.23-18-07183.2003","article-title":"Cytosolic prion protein in neurons","volume":"23","author":"Mironov","year":"2003","journal-title":"J. Neurosci."},{"key":"10.1016\/j.virusres.2015.02.004_bib0470","doi-asserted-by":"crossref","first-page":"609","DOI":"10.1110\/ps.051822606","article-title":"Octapeptide repeat insertions increase the rate of protease-resistant prion protein formation","volume":"15","author":"Moore","year":"2006","journal-title":"Protein Sci.: Publ. Protein Soc."},{"key":"10.1016\/j.virusres.2015.02.004_bib0475","doi-asserted-by":"crossref","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":"10.1016\/j.virusres.2015.02.004_bib0480","doi-asserted-by":"crossref","first-page":"507","DOI":"10.1038\/nature11058","article-title":"Sustained translational repression by eIF2alpha-P mediates prion neurodegeneration","volume":"485","author":"Moreno","year":"2012","journal-title":"Nature"},{"key":"10.1016\/j.virusres.2015.02.004_bib0485","doi-asserted-by":"crossref","first-page":"613","DOI":"10.1096\/fj.08-115360","article-title":"Opposing effects of ERK and p38-JNK MAP kinase pathways on formation of prions in GT1-1 cells","volume":"23","author":"Nordstrom","year":"2009","journal-title":"FASEB J.: Offi. Publ. Fed. Am. Soc. Exp. Biol."},{"key":"10.1016\/j.virusres.2015.02.004_bib0490","doi-asserted-by":"crossref","first-page":"13828","DOI":"10.1074\/jbc.M511174200","article-title":"Amyloid fibrils of mammalian prion protein are highly toxic to cultured cells and primary neurons","volume":"281","author":"Novitskaya","year":"2006","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.virusres.2015.02.004_bib0495","doi-asserted-by":"crossref","first-page":"30431","DOI":"10.1074\/jbc.M605320200","article-title":"Conditions of endoplasmic reticulum stress favor the accumulation of cytosolic prion protein","volume":"281","author":"Orsi","year":"2006","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.virusres.2015.02.004_bib0500","doi-asserted-by":"crossref","first-page":"612","DOI":"10.1074\/jbc.M310453200","article-title":"Primary cultured neurons devoid of cellular prion display lower responsiveness to staurosporine through the control of p53 at both transcriptional and post-transcriptional levels","volume":"279","author":"Paitel","year":"2004","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.virusres.2015.02.004_bib0505","doi-asserted-by":"crossref","first-page":"81","DOI":"10.1042\/bj20020773","article-title":"Cell-surface prion protein interacts with glycosaminoglycans","volume":"368","author":"Pan","year":"2002","journal-title":"Biochem. J."},{"key":"10.1016\/j.virusres.2015.02.004_bib0510","doi-asserted-by":"crossref","first-page":"2241","DOI":"10.1093\/hmg\/ddi228","article-title":"The prion gene is associated with human long-term memory","volume":"14","author":"Papassotiropoulos","year":"2005","journal-title":"Hum. Mol. Genet."},{"key":"10.1016\/j.virusres.2015.02.004_bib0515","doi-asserted-by":"crossref","first-page":"15710","DOI":"10.1021\/bi0615442","article-title":"Isolation and characterization of a proteinase K-sensitive PrP(Sc) fraction","volume":"45","author":"Pastrana","year":"2006","journal-title":"Biochemistry"},{"key":"10.1016\/j.virusres.2015.02.004_bib0520","doi-asserted-by":"crossref","first-page":"889","DOI":"10.1084\/jem.20120741","article-title":"Prion-like spread of protein aggregates in neurodegeneration","volume":"209","author":"Polymenidou","year":"2012","journal-title":"J. Exp. Med."},{"key":"10.1016\/j.virusres.2015.02.004_bib0525","doi-asserted-by":"crossref","first-page":"1511","DOI":"10.1126\/science.1222951","article-title":"Cell biology. A unifying role for prions in neurodegenerative diseases","volume":"336","author":"Prusiner","year":"2012","journal-title":"Science"},{"key":"10.1016\/j.virusres.2015.02.004_bib0530","doi-asserted-by":"crossref","first-page":"1183","DOI":"10.1016\/0896-6273(95)90105-1","article-title":"Neuron-specific expression of a hamster prion protein minigene in transgenic mice induces susceptibility to hamster scrapie agent","volume":"15","author":"Race","year":"1995","journal-title":"Neuron"},{"key":"10.1016\/j.virusres.2015.02.004_bib0535","doi-asserted-by":"crossref","first-page":"6057","DOI":"10.1093\/emboj\/16.20.6057","article-title":"Astrocyte-specific expression of hamster prion protein (PrP) renders PrP knockout mice susceptible to hamster scrapie","volume":"16","author":"Raeber","year":"1997","journal-title":"EMBO J."},{"key":"10.1016\/j.virusres.2015.02.004_bib0540","doi-asserted-by":"crossref","first-page":"359","DOI":"10.1016\/j.devcel.2008.06.015","article-title":"Reduced translocation of nascent prion protein during ER stress contributes to neurodegeneration","volume":"15","author":"Rane","year":"2008","journal-title":"Dev. Cell"},{"key":"10.1016\/j.virusres.2015.02.004_bib0545","doi-asserted-by":"crossref","first-page":"2057","DOI":"10.1038\/emboj.2011.86","article-title":"The cellular prion protein mediates neurotoxic signalling of beta-sheet-rich conformers independent of prion replication","volume":"30","author":"Resenberger","year":"2011","journal-title":"EMBO J."},{"key":"10.1016\/j.virusres.2015.02.004_bib0550","doi-asserted-by":"crossref","first-page":"11667","DOI":"10.1073\/pnas.95.20.11667","article-title":"Prion protein NMR structure and familial human spongiform encephalopathies","volume":"95","author":"Riek","year":"1998","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.virusres.2015.02.004_bib0555","doi-asserted-by":"crossref","first-page":"153","DOI":"10.1002\/jnr.10864","article-title":"Neuroprotective functions of prion protein","volume":"75","author":"Roucou","year":"2004","journal-title":"J. Neurosci. Res."},{"key":"10.1016\/j.virusres.2015.02.004_bib0560","doi-asserted-by":"crossref","first-page":"783","DOI":"10.1038\/sj.cdd.4401629","article-title":"Cellular prion protein inhibits proapoptotic Bax conformational change in human neurons and in breast carcinoma MCF-7 cells","volume":"12","author":"Roucou","year":"2005","journal-title":"Cell Death Differ."},{"key":"10.1016\/j.virusres.2015.02.004_bib0565","doi-asserted-by":"crossref","first-page":"40877","DOI":"10.1074\/jbc.M306177200","article-title":"Cytosolic prion protein is not toxic and protects against Bax-mediated cell death in human primary neurons","volume":"278","author":"Roucou","year":"2003","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.virusres.2015.02.004_bib0570","doi-asserted-by":"crossref","first-page":"423","DOI":"10.1083\/jcb.201308028","article-title":"Live imaging of prions: nascent PrPSc in cell surface, raft-associated amyloid strings & webs","volume":"204","author":"Rouvinski","year":"2014","journal-title":"J. Cell Biol."},{"key":"10.1016\/j.virusres.2015.02.004_bib0575","doi-asserted-by":"crossref","first-page":"1157","DOI":"10.1038\/2654","article-title":"Eight prion strains have PrP(Sc) molecules with different conformations","volume":"4","author":"Safar","year":"1998","journal-title":"Nat. Med."},{"key":"10.1016\/j.virusres.2015.02.004_bib0580","doi-asserted-by":"crossref","first-page":"108","DOI":"10.4161\/pri.18666","article-title":"Molecular pathogenesis of sporadic prion diseases in man","volume":"6","author":"Safar","year":"2012","journal-title":"Prion"},{"key":"10.1016\/j.virusres.2015.02.004_bib0585","doi-asserted-by":"crossref","first-page":"1126","DOI":"10.1002\/stem.664","article-title":"Enhanced neural progenitor\/stem cells self-renewal via the interaction of stress-inducible protein 1 with the prion protein","volume":"29","author":"Santos","year":"2011","journal-title":"Stem Cells"},{"key":"10.1016\/j.virusres.2015.02.004_bib0590","doi-asserted-by":"crossref","first-page":"341","DOI":"10.1083\/jcb.200409127","article-title":"Prion protein recruits its neuronal receptor NCAM to lipid rafts to activate p59fyn and to enhance neurite outgrowth","volume":"169","author":"Santuccione","year":"2005","journal-title":"J. Cell Biol."},{"key":"10.1016\/j.virusres.2015.02.004_bib0595","doi-asserted-by":"crossref","first-page":"e7208","DOI":"10.1371\/journal.pone.0007208","article-title":"Evolutionary descent of prion genes from the ZIP family of metal ion transporters","volume":"4","author":"Schmitt-Ulms","year":"2009","journal-title":"PLoS ONE"},{"key":"10.1016\/j.virusres.2015.02.004_bib0600","doi-asserted-by":"crossref","first-page":"1209","DOI":"10.1006\/jmbi.2000.5183","article-title":"Binding of neural cell adhesion molecules (N-CAMs) to the cellular prion protein","volume":"314","author":"Schmitt-Ulms","year":"2001","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.virusres.2015.02.004_bib0605","doi-asserted-by":"crossref","first-page":"1177","DOI":"10.1016\/j.neurobiolaging.2004.10.004","article-title":"Prion protein (PrPc) promotes beta-amyloid plaque formation","volume":"26","author":"Schwarze-Eicker","year":"2005","journal-title":"Neurobiol. Aging"},{"key":"10.1016\/j.virusres.2015.02.004_bib0610","doi-asserted-by":"crossref","first-page":"123","DOI":"10.4161\/pri.5.3.16327","article-title":"(Ctm)PrP and ER stress: a neurotoxic mechanism of some special PrP mutants","volume":"5","author":"Shi","year":"2011","journal-title":"Prion"},{"key":"10.1016\/j.virusres.2015.02.004_bib0615","doi-asserted-by":"crossref","first-page":"421","DOI":"10.1016\/j.cell.2010.01.008","article-title":"Aplysia CPEB can form prion-like multimers in sensory neurons that contribute to long-term facilitation","volume":"140","author":"Si","year":"2010","journal-title":"Cell"},{"key":"10.1016\/j.virusres.2015.02.004_bib0620","first-page":"170","article-title":"Neuronal autophagy and aggresomes constitute a consistent part of neurodegeneration in experimental scrapie","volume":"45","author":"Sikorska","year":"2007","journal-title":"Folia Neuropathol.\/Assoc. Pol. Neuropathol. Med. Res. Cent. Pol. Acad. Sci."},{"key":"10.1016\/j.virusres.2015.02.004_bib0625","doi-asserted-by":"crossref","first-page":"257","DOI":"10.1038\/nature03989","article-title":"The most infectious prion protein particles","volume":"437","author":"Silveira","year":"2005","journal-title":"Nature"},{"key":"10.1016\/j.virusres.2015.02.004_bib0630","doi-asserted-by":"crossref","first-page":"e125","DOI":"10.1371\/journal.ppat.0030125","article-title":"In vitro and in vivo neurotoxicity of prion protein oligomers","volume":"3","author":"Simoneau","year":"2007","journal-title":"PLoS Pathog."},{"key":"10.1016\/j.virusres.2015.02.004_bib0635","doi-asserted-by":"crossref","first-page":"1271","DOI":"10.1089\/ars.2009.2628","article-title":"Redox control of prion and disease pathogenesis","volume":"12","author":"Singh","year":"2010","journal-title":"Antioxid. Redox Signal."},{"key":"10.1016\/j.virusres.2015.02.004_bib0640","doi-asserted-by":"crossref","first-page":"1411","DOI":"10.2353\/ajpath.2010.091037","article-title":"Morphological and functional abnormalities in mitochondria associated with synaptic degeneration in prion disease","volume":"177","author":"Siskova","year":"2010","journal-title":"Am. J. Pathol."},{"key":"10.1016\/j.virusres.2015.02.004_bib0645","doi-asserted-by":"crossref","first-page":"99","DOI":"10.4161\/pri.23490","article-title":"A closer look at prion strains: characterization and important implications","volume":"7","author":"Solforosi","year":"2013","journal-title":"Prion"},{"key":"10.1016\/j.virusres.2015.02.004_bib0650","doi-asserted-by":"crossref","first-page":"102","DOI":"10.1038\/nature12402","article-title":"The toxicity of antiprion antibodies is mediated by the flexible tail of the prion protein","volume":"501","author":"Sonati","year":"2013","journal-title":"Nature"},{"key":"10.1016\/j.virusres.2015.02.004_bib0655","doi-asserted-by":"crossref","first-page":"114","DOI":"10.1186\/1471-2164-9-114","article-title":"Comprehensive transcriptional profiling of prion infection in mouse models reveals networks of responsive genes","volume":"9","author":"Sorensen","year":"2008","journal-title":"BMC Genom."},{"key":"10.1016\/j.virusres.2015.02.004_bib0660","doi-asserted-by":"crossref","first-page":"8879","DOI":"10.1021\/bi00490a001","article-title":"Identification of glycoinositol phospholipid linked and truncated forms of the scrapie prion protein","volume":"29","author":"Stahl","year":"1990","journal-title":"Biochemistry"},{"key":"10.1016\/j.virusres.2015.02.004_bib0665","doi-asserted-by":"crossref","first-page":"1991","DOI":"10.1021\/bi00059a016","article-title":"Structural studies of the scrapie prion protein using mass spectrometry and amino acid sequencing","volume":"32","author":"Stahl","year":"1993","journal-title":"Biochemistry"},{"key":"10.1016\/j.virusres.2015.02.004_bib0670","doi-asserted-by":"crossref","first-page":"243","DOI":"10.4161\/pri.1.4.5551","article-title":"Prion pathogenesis is independent of caspase-12","volume":"1","author":"Steele","year":"2007","journal-title":"Prion"},{"key":"10.1016\/j.virusres.2015.02.004_bib0675","doi-asserted-by":"crossref","first-page":"13022","DOI":"10.1523\/JNEUROSCI.3290-07.2007","article-title":"Diminishing apoptosis by deletion of Bax or overexpression of Bcl-2 does not protect against infectious prion toxicity in vivo","volume":"27","author":"Steele","year":"2007","journal-title":"J. Neurosci."},{"key":"10.1016\/j.virusres.2015.02.004_bib0680","doi-asserted-by":"crossref","first-page":"83","DOI":"10.4161\/pri.1.2.4346","article-title":"The prion protein knockout mouse: a phenotype under challenge","volume":"1","author":"Steele","year":"2007","journal-title":"Prion"},{"key":"10.1016\/j.virusres.2015.02.004_bib0685","doi-asserted-by":"crossref","first-page":"2212","DOI":"10.1074\/jbc.M006763200","article-title":"Most pathogenic mutations do not alter the membrane topology of the prion protein","volume":"276","author":"Stewart","year":"2001","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.virusres.2015.02.004_bib0690","doi-asserted-by":"crossref","first-page":"1956","DOI":"10.1074\/jbc.M609663200","article-title":"The C-terminal products of cellular prion protein processing, C1 and C2, exert distinct influence on p53-dependent staurosporine-induced caspase-3 activation","volume":"282","author":"Sunyach","year":"2007","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.virusres.2015.02.004_bib0695","doi-asserted-by":"crossref","first-page":"453","DOI":"10.2217\/bmm.10.14","article-title":"The fatal attraction between pro-prion and filamin A: prion as a marker in human cancers","volume":"4","author":"Sy","year":"2010","journal-title":"Biomark. Med."},{"key":"10.1016\/j.virusres.2015.02.004_bib0700","doi-asserted-by":"crossref","first-page":"15002","DOI":"10.1073\/pnas.0907339106","article-title":"Measuring prions by bioluminescence imaging","volume":"106","author":"Tamg\u00fcney","year":"2009","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.virusres.2015.02.004_bib0705","doi-asserted-by":"crossref","first-page":"21","DOI":"10.1111\/j.1432-1033.1988.tb14246.x","article-title":"Purification and properties of the cellular and scrapie hamster prion proteins","volume":"176","author":"Turk","year":"1988","journal-title":"Eur. J. Biochem.\/FEBS"},{"key":"10.1016\/j.virusres.2015.02.004_bib0710","doi-asserted-by":"crossref","first-page":"12868","DOI":"10.1021\/bi025958g","article-title":"Protease-sensitive scrapie prion protein in aggregates of heterogeneous sizes","volume":"41","author":"Tzaban","year":"2002","journal-title":"Biochemistry"},{"key":"10.1016\/j.virusres.2015.02.004_bib0715","doi-asserted-by":"crossref","first-page":"348","DOI":"10.1097\/01.jnen.0000218445.30535.6f","article-title":"Endoplasmic reticulum stress features are prominent in Alzheimer disease but not in prion diseases in vivo","volume":"65","author":"Unterberger","year":"2006","journal-title":"J. Neuropathol. Exp. Neurol."},{"key":"10.1016\/j.virusres.2015.02.004_bib0720","doi-asserted-by":"crossref","first-page":"461","DOI":"10.1093\/protein\/gzp039","article-title":"The consequences of pathogenic mutations to the human prion protein","volume":"22","author":"van der Kamp","year":"2009","journal-title":"Protein Eng. Des. Sel."},{"key":"10.1016\/j.virusres.2015.02.004_bib0725","doi-asserted-by":"crossref","first-page":"2373","DOI":"10.1096\/fj.10-173815","article-title":"An overlapping reading frame in the PRNP gene encodes a novel polypeptide distinct from the prion protein","volume":"25","author":"Vanderperre","year":"2011","journal-title":"FASEB J."},{"key":"10.1016\/j.virusres.2015.02.004_bib0730","doi-asserted-by":"crossref","first-page":"598","DOI":"10.1016\/j.bbadis.2007.02.010","article-title":"Update on human prion disease","volume":"1772","author":"Wadsworth","year":"2007","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/j.virusres.2015.02.004_bib0735","doi-asserted-by":"crossref","first-page":"35914","DOI":"10.1074\/jbc.M507327200","article-title":"Reactive oxygen species-mediated beta-cleavage of the prion protein in the cellular response to oxidative stress","volume":"280","author":"Watt","year":"2005","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.virusres.2015.02.004_bib0740","doi-asserted-by":"crossref","first-page":"44234","DOI":"10.1074\/jbc.M111.286195","article-title":"A naturally occurring C-terminal fragment of the prion protein (PrP) delays disease and acts as a dominant-negative inhibitor of PrPSc formation","volume":"286","author":"Westergard","year":"2011","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.virusres.2015.02.004_bib0745","doi-asserted-by":"crossref","first-page":"47","DOI":"10.1186\/jbiol148","article-title":"Prion variants, species barriers, generation and propagation","volume":"8","author":"Wickner","year":"2009","journal-title":"J. Biol."},{"key":"10.1016\/j.virusres.2015.02.004_bib0750","doi-asserted-by":"crossref","first-page":"498","DOI":"10.4161\/pri.22588","article-title":"Separate mechanisms act concurrently to shed and release the prion protein from the cell","volume":"6","author":"Wik","year":"2012","journal-title":"Prion"},{"key":"10.1016\/j.virusres.2015.02.004_bib0755","doi-asserted-by":"crossref","first-page":"433","DOI":"10.1006\/exnr.1997.6424","article-title":"PrP deposition, microglial activation, and neuronal apoptosis in murine scrapie","volume":"144","author":"Williams","year":"1997","journal-title":"Exp. Neurol."},{"key":"10.1016\/j.virusres.2015.02.004_bib0760","doi-asserted-by":"crossref","first-page":"5383","DOI":"10.1093\/emboj\/20.19.5383","article-title":"Proteasomes and ubiquitin are involved in the turnover of the wild-type prion protein","volume":"20","author":"Yedidia","year":"2001","journal-title":"EMBO J."},{"key":"10.1016\/j.virusres.2015.02.004_bib0765","doi-asserted-by":"crossref","first-page":"90","DOI":"10.1016\/j.expneurol.2006.03.025","article-title":"Oxidative stress in the brain at early preclinical stages of mouse scrapie","volume":"201","author":"Yun","year":"2006","journal-title":"Exp. Neurol."},{"key":"10.1016\/j.virusres.2015.02.004_bib0770","doi-asserted-by":"crossref","first-page":"3307","DOI":"10.1093\/emboj\/cdf325","article-title":"Stress-inducible protein 1 is a cell surface ligand for cellular prion that triggers neuroprotection","volume":"21","author":"Zanata","year":"2002","journal-title":"EMBO J."},{"key":"10.1016\/j.virusres.2015.02.004_bib0775","doi-asserted-by":"crossref","first-page":"33650","DOI":"10.1074\/jbc.C000483200","article-title":"Solution structure of the E200K variant of human prion protein. Implications for the mechanism of pathogenesis in familial prion diseases","volume":"275","author":"Zhang","year":"2000","journal-title":"J. Biol. Chem."}],"container-title":["Virus Research"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S016817021500057X?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S016817021500057X?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2024,6,7]],"date-time":"2024-06-07T05:31:18Z","timestamp":1717738278000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S016817021500057X"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2015,9]]},"references-count":156,"alternative-id":["S016817021500057X"],"URL":"https:\/\/doi.org\/10.1016\/j.virusres.2015.02.004","relation":{},"ISSN":["0168-1702"],"issn-type":[{"value":"0168-1702","type":"print"}],"subject":[],"published":{"date-parts":[[2015,9]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Subcellular distribution of the prion protein in sickness and in health","name":"articletitle","label":"Article Title"},{"value":"Virus Research","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.virusres.2015.02.004","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"Copyright \u00a9 2015 The Authors. Published by Elsevier B.V.","name":"copyright","label":"Copyright"}]}}