{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,7,8]],"date-time":"2026-07-08T01:52:42Z","timestamp":1783475562592,"version":"3.55.0"},"reference-count":112,"publisher":"The Company of Biologists","issue":"1","content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"published-print":{"date-parts":[[2014,1,1]]},"abstract":"<jats:p>The mechanisms underlying the selective targeting of specific brain regions by different neurodegenerative diseases is one of the most intriguing mysteries in medicine. For example, it is known that Alzheimer\u2019s disease primarily affects parts of the brain that play a role in memory, whereas Parkinson\u2019s disease predominantly affects parts of the brain that are involved in body movement. However, the reasons that other brain regions remain unaffected in these diseases are unknown. A better understanding of the phenomenon of selective vulnerability is required for the development of targeted therapeutic approaches that specifically protect affected neurons, thereby altering the disease course and preventing its progression. Prion diseases are a fascinating group of neurodegenerative diseases because they exhibit a wide phenotypic spectrum caused by different sequence perturbations in a single protein. The possible ways that mutations affecting this protein can cause several distinct neurodegenerative diseases are explored in this Review to highlight the complexity underlying selective vulnerability. The premise of this article is that selective vulnerability is determined by the interaction of specific protein conformers and region-specific microenvironments harboring unique combinations of subcellular components such as metals, chaperones and protein translation machinery. Given the abundance of potential contributory factors in the neurodegenerative process, a better understanding of how these factors interact will provide invaluable insight into disease mechanisms to guide therapeutic discovery.<\/jats:p>","DOI":"10.1242\/dmm.012146","type":"journal-article","created":{"date-parts":[[2014,1,6]],"date-time":"2014-01-06T16:29:28Z","timestamp":1389025768000},"page":"21-29","source":"Crossref","is-referenced-by-count":85,"title":["Selective vulnerability to neurodegenerative disease: the curious case of Prion Protein"],"prefix":"10.1242","volume":"7","author":[{"given":"Walker S.","family":"Jackson","sequence":"first","affiliation":[{"name":"German Center for Neurodegenerative Diseases (DZNE), Sigmund-Freud-Str. 25, 53127-Bonn, Germany."}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"237","reference":[{"key":"2021042513043057100_b1-0070021","doi-asserted-by":"crossref","first-page":"783","DOI":"10.1016\/j.neuron.2009.12.016","article-title":"The transcellular spread of cytosolic amyloids, prions, and prionoids","volume":"64","author":"Aguzzi","year":"2009","journal-title":"Neuron"},{"key":"2021042513043057100_b2-0070021","doi-asserted-by":"crossref","first-page":"156","DOI":"10.1126\/science.1227901","article-title":"Microglia: scapegoat, saboteur, or something else?","volume":"339","author":"Aguzzi","year":"2013","journal-title":"Science"},{"key":"2021042513043057100_b3-0070021","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":"2021042513043057100_b4-0070021","doi-asserted-by":"crossref","first-page":"603","DOI":"10.1042\/BC20080025","article-title":"Mouse neuroblastoma cells release prion infectivity associated with exosomal vesicles","volume":"100","author":"Alais","year":"2008","journal-title":"Biol. Cell"},{"key":"2021042513043057100_b5-0070021","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":"2021042513043057100_b6-0070021","doi-asserted-by":"crossref","first-page":"27","DOI":"10.1016\/S0361-9230(96)00107-4","article-title":"GABAergic neurons in mammalian thalamus: a marker of thalamic complexity?","volume":"42","author":"Arcelli","year":"1997","journal-title":"Brain Res. Bull."},{"key":"2021042513043057100_b7-0070021","doi-asserted-by":"crossref","first-page":"e1000479","DOI":"10.1371\/journal.ppat.1000479","article-title":"Selective processing and metabolism of disease-causing mutant prion proteins","volume":"5","author":"Ashok","year":"2009","journal-title":"PLoS Pathog."},{"key":"2021042513043057100_b8-0070021","doi-asserted-by":"crossref","first-page":"26","DOI":"10.1016\/j.neulet.2013.01.027","article-title":"Differential molecular chaperone response associated with various mouse adapted scrapie strains","volume":"538","author":"Asuni","year":"2013","journal-title":"Neurosci. Lett."},{"key":"2021042513043057100_b9-0070021","doi-asserted-by":"crossref","first-page":"2012","DOI":"10.2353\/ajpath.2007.070403","article-title":"Induction of tau pathology by intracerebral infusion of amyloid-beta -containing brain extract and by amyloid-beta deposition in APP \u00d7 Tau transgenic mice","volume":"171","author":"Bolmont","year":"2007","journal-title":"Am. J. Pathol."},{"key":"2021042513043057100_b10-0070021","doi-asserted-by":"crossref","first-page":"159","DOI":"10.1016\/S1050-3862(96)00167-2","article-title":"A vector for expressing foreign genes in the brains and hearts of transgenic mice","volume":"13","author":"Borchelt","year":"1996","journal-title":"Genet. Anal."},{"key":"2021042513043057100_b11-0070021","doi-asserted-by":"crossref","first-page":"239","DOI":"10.1007\/BF00308809","article-title":"Neuropathological stageing of Alzheimer-related changes","volume":"82","author":"Braak","year":"1991","journal-title":"Acta Neuropathol."},{"key":"2021042513043057100_b12-0070021","doi-asserted-by":"crossref","first-page":"310","DOI":"10.1038\/nn.2483","article-title":"Axonal prion protein is required for peripheral myelin maintenance","volume":"13","author":"Bremer","year":"2010","journal-title":"Nat. Neurosci."},{"key":"2021042513043057100_b13-0070021","doi-asserted-by":"crossref","first-page":"353","DOI":"10.1046\/j.1471-4159.2003.01996.x","article-title":"Copper and zinc cause delivery of the prion protein from the plasma membrane to a subset of early endosomes and the Golgi","volume":"87","author":"Brown","year":"2003","journal-title":"J. Neurochem."},{"key":"2021042513043057100_b14-0070021","doi-asserted-by":"crossref","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":"2021042513043057100_b15-0070021","doi-asserted-by":"crossref","first-page":"301","DOI":"10.1038\/nrm2873","article-title":"Prion-like transmission of protein aggregates in neurodegenerative diseases","volume":"11","author":"Brundin","year":"2010","journal-title":"Nat. Rev. Mol. Cell Biol."},{"key":"2021042513043057100_b16-0070021","doi-asserted-by":"crossref","first-page":"10","DOI":"10.1002\/1097-0029(20000701)50:1<10::AID-JEMT3>3.0.CO;2-6","article-title":"Neuropathology of Gerstmann-Str\u00e4ussler-Scheinker disease","volume":"50","author":"Bugiani","year":"2000","journal-title":"Microsc. Res. Tech."},{"key":"2021042513043057100_b17-0070021","doi-asserted-by":"crossref","first-page":"306","DOI":"10.1002\/emmm.201000082","article-title":"Prion protein and Abeta-related synaptic toxicity impairment","volume":"2","author":"Calella","year":"2010","journal-title":"EMBO Mol Med"},{"key":"2021042513043057100_b18-0070021","doi-asserted-by":"crossref","first-page":"1010","DOI":"10.1016\/j.nbd.2011.12.020","article-title":"Copper is toxic to PrP-ablated mice and exacerbates disease in a mouse model of E200K genetic prion disease","volume":"45","author":"Canello","year":"2012","journal-title":"Neurobiol. Dis."},{"key":"2021042513043057100_b19-0070021","doi-asserted-by":"crossref","first-page":"613","DOI":"10.1016\/S0002-9440(10)64572-5","article-title":"Effect of the E200K mutation on prion protein metabolism. Comparative study of a cell model and human brain","volume":"157","author":"Capellari","year":"2000","journal-title":"Am. J. Pathol."},{"key":"2021042513043057100_b20-0070021","doi-asserted-by":"crossref","first-page":"27","DOI":"10.3233\/JAD-2000-2104","article-title":"The Thr183Ala Mutation, not the loss of the first glycosylation site, alters the physical properties of the prion protein","volume":"2","author":"Capellari","year":"2000","journal-title":"J. Alzheimers Dis."},{"key":"2021042513043057100_b21-0070021","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":"2021042513043057100_b22-0070021","doi-asserted-by":"crossref","first-page":"1081","DOI":"10.1038\/nature05865","article-title":"\u2018Rejuvenation\u2019 protects neurons in mouse models of Parkinson\u2019s disease","volume":"447","author":"Chan","year":"2007","journal-title":"Nature"},{"key":"2021042513043057100_b23-0070021","doi-asserted-by":"crossref","first-page":"13258","DOI":"10.1523\/JNEUROSCI.3109-08.2008","article-title":"Aggregated, wild-type prion protein causes neurological dysfunction and synaptic abnormalities","volume":"28","author":"Chiesa","year":"2008","journal-title":"J. Neurosci."},{"key":"2021042513043057100_b24-0070021","doi-asserted-by":"crossref","first-page":"3678","DOI":"10.1242\/jcs.126086","article-title":"Transfer of polyglutamine aggregates in neuronal cells occurs in tunneling nanotubes","volume":"126","author":"Costanzo","year":"2013","journal-title":"J. Cell Sci."},{"key":"2021042513043057100_b25-0070021","doi-asserted-by":"crossref","first-page":"1191","DOI":"10.1242\/jcs.051672","article-title":"Prion-like disorders: blurring the divide between transmissibility and infectivity","volume":"123","author":"Cushman","year":"2010","journal-title":"J. Cell Sci."},{"key":"2021042513043057100_b26-0070021","doi-asserted-by":"crossref","first-page":"42","DOI":"10.1186\/1750-1326-7-42","article-title":"Exosomal cell-to-cell transmission of alpha synuclein oligomers","volume":"7","author":"Danzer","year":"2012","journal-title":"Mol. Neurodegener."},{"key":"2021042513043057100_b27-0070021","doi-asserted-by":"crossref","first-page":"598","DOI":"10.1016\/j.neuron.2008.09.008","article-title":"Mutant prion protein expression causes motor and memory deficits and abnormal sleep patterns in a transgenic mouse model","volume":"60","author":"Dossena","year":"2008","journal-title":"Neuron"},{"key":"2021042513043057100_b28-0070021","doi-asserted-by":"crossref","first-page":"6838","DOI":"10.1523\/JNEUROSCI.5699-09.2010","article-title":"Cell-produced alpha-synuclein is secreted in a calcium-dependent manner by exosomes and impacts neuronal survival","volume":"30","author":"Emmanouilidou","year":"2010","journal-title":"J. Neurosci."},{"key":"2021042513043057100_b29-0070021","doi-asserted-by":"crossref","first-page":"2607","DOI":"10.1016\/j.neuroimage.2009.10.009","article-title":"Context-dependent perturbation of neural systems in transgenic mice expressing a cytosolic prion protein","volume":"49","author":"Faas","year":"2010","journal-title":"Neuroimage"},{"key":"2021042513043057100_b30-0070021","doi-asserted-by":"crossref","first-page":"137","DOI":"10.1136\/jnnp.66.2.137","article-title":"The cholinergic hypothesis of Alzheimer\u2019s disease: a review of progress","volume":"66","author":"Francis","year":"1999","journal-title":"J. Neurol. Neurosurg. Psychiatry"},{"key":"2021042513043057100_b31-0070021","doi-asserted-by":"crossref","first-page":"e1002350","DOI":"10.1371\/journal.ppat.1002350","article-title":"Fatal prion disease in a mouse model of genetic E200K Creutzfeldt-Jakob disease","volume":"7","author":"Friedman-Levi","year":"2011","journal-title":"PLoS Pathog."},{"key":"2021042513043057100_b32-0070021","doi-asserted-by":"crossref","first-page":"155","DOI":"10.1038\/nrn2786","article-title":"Prion-like mechanisms in neurodegenerative diseases","volume":"11","author":"Frost","year":"2010","journal-title":"Nat. Rev. Neurosci."},{"key":"2021042513043057100_b33-0070021","doi-asserted-by":"crossref","first-page":"43","DOI":"10.1111\/j.1750-3639.1995.tb00576.x","article-title":"Fatal familial insomnia and familial Creutzfeldt-Jakob disease: clinical, pathological and molecular features","volume":"5","author":"Gambetti","year":"1995","journal-title":"Brain Pathol."},{"key":"2021042513043057100_b34-0070021","doi-asserted-by":"crossref","first-page":"213","DOI":"10.1093\/bmb\/66.1.213","article-title":"Sporadic and familial CJD: classification and characterisation","volume":"66","author":"Gambetti","year":"2003","journal-title":"Br. Med. Bull."},{"key":"2021042513043057100_b35-0070021","doi-asserted-by":"crossref","first-page":"41","DOI":"10.1007\/BF02778006","article-title":"Familial Gerstmann-Str\u00e4ussler-Scheinker disease with neurofibrillary tangles","volume":"8","author":"Ghetti","year":"1994","journal-title":"Mol. Neurobiol."},{"key":"2021042513043057100_b36-0070021","doi-asserted-by":"crossref","first-page":"570","DOI":"10.1016\/j.neurobiolaging.2005.04.017","article-title":"Common mechanisms of amyloid oligomer pathogenesis in degenerative disease","volume":"27","author":"Glabe","year":"2006","journal-title":"Neurobiol. Aging"},{"key":"2021042513043057100_b37-0070021","doi-asserted-by":"crossref","first-page":"841","DOI":"10.1111\/j.1471-4159.2006.04268.x","article-title":"Altered prion protein glycosylation in the aging mouse brain","volume":"100","author":"Goh","year":"2007","journal-title":"J. Neurochem."},{"key":"2021042513043057100_b38-0070021","doi-asserted-by":"crossref","first-page":"94","DOI":"10.4161\/pri.3.2.8917","article-title":"Tunnelling nanotubes: a highway for prion spreading?","volume":"3","author":"Gousset","year":"2009","journal-title":"Prion"},{"key":"2021042513043057100_b39-0070021","doi-asserted-by":"crossref","first-page":"328","DOI":"10.1038\/ncb1841","article-title":"Prions hijack tunnelling nanotubes for intercellular spread","volume":"11","author":"Gousset","year":"2009","journal-title":"Nat. Cell Biol."},{"key":"2021042513043057100_b40-0070021","doi-asserted-by":"crossref","first-page":"16398","DOI":"10.1073\/pnas.1102645108","article-title":"Intermolecular transmission of superoxide dismutase 1 misfolding in living cells","volume":"108","author":"Grad","year":"2011","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"2021042513043057100_b41-0070021","doi-asserted-by":"crossref","first-page":"770","DOI":"10.1126\/science.3155875","article-title":"Evidence for degenerative and regenerative changes in neostriatal spiny neurons in Huntington\u2019s disease","volume":"227","author":"Graveland","year":"1985","journal-title":"Science"},{"key":"2021042513043057100_b42-0070021","doi-asserted-by":"crossref","first-page":"1433","DOI":"10.1080\/15287394.2011.618967","article-title":"Generalization of the prion hypothesis to other neurodegenerative diseases: an imperfect fit","volume":"74","author":"Guest","year":"2011","journal-title":"J. Toxicol. Environ. Health A"},{"key":"2021042513043057100_b43-0070021","doi-asserted-by":"crossref","first-page":"1062","DOI":"10.1038\/cr.2009.86","article-title":"PrPC-related signal transduction is influenced by copper, membrane integrity and the alpha cleavage site","volume":"19","author":"Haigh","year":"2009","journal-title":"Cell Res."},{"key":"2021042513043057100_b44-0070021","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1016\/0003-9861(89)90409-8","article-title":"Asparagine-linked glycosylation of the scrapie and cellular prion proteins","volume":"274","author":"Haraguchi","year":"1989","journal-title":"Arch. Biochem. Biophys."},{"key":"2021042513043057100_b45-0070021","doi-asserted-by":"crossref","first-page":"428","DOI":"10.1016\/j.neuron.2010.10.020","article-title":"Transsynaptic progression of amyloid-\u03b2-induced neuronal dysfunction within the entorhinal-hippocampal network","volume":"68","author":"Harris","year":"2010","journal-title":"Neuron"},{"key":"2021042513043057100_b46-0070021","doi-asserted-by":"crossref","first-page":"590","DOI":"10.1016\/j.mcn.2007.12.008","article-title":"Elevated manganese levels in blood and CNS in human prion disease","volume":"37","author":"Hesketh","year":"2008","journal-title":"Mol. Cell. Neurosci."},{"key":"2021042513043057100_b47-0070021","doi-asserted-by":"crossref","first-page":"5951","DOI":"10.1073\/pnas.1217321110","article-title":"Cell-to-cell propagation of infectious cytosolic protein aggregates","volume":"110","author":"Hofmann","year":"2013","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"2021042513043057100_b48-0070021","doi-asserted-by":"crossref","first-page":"1587","DOI":"10.1126\/science.1980379","article-title":"Spontaneous neurodegeneration in transgenic mice with mutant prion protein","volume":"250","author":"Hsiao","year":"1990","journal-title":"Science"},{"key":"2021042513043057100_b49-0070021","doi-asserted-by":"crossref","first-page":"1168","DOI":"10.1126\/science.6474172","article-title":"Alzheimer\u2019s disease: cell-specific pathology isolates the hippocampal formation","volume":"225","author":"Hyman","year":"1984","journal-title":"Science"},{"key":"2021042513043057100_b50-0070021","doi-asserted-by":"crossref","first-page":"42409","DOI":"10.1074\/jbc.M106928200","article-title":"Mutant prion proteins are partially retained in the endoplasmic reticulum","volume":"276","author":"Ivanova","year":"2001","journal-title":"J. Biol. Chem."},{"key":"2021042513043057100_b51-0070021","doi-asserted-by":"crossref","first-page":"438","DOI":"10.1016\/j.neuron.2009.07.026","article-title":"Spontaneous generation of prion infectivity in fatal familial insomnia knockin mice","volume":"63","author":"Jackson","year":"2009","journal-title":"Neuron"},{"key":"2021042513043057100_b52-0070021","doi-asserted-by":"crossref","first-page":"14759","DOI":"10.1073\/pnas.1312006110","article-title":"Profoundly different prion diseases in knock-in mice carrying single PrP codon substitutions associated with human diseases","volume":"110","author":"Jackson","year":"2013","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"2021042513043057100_b53-0070021","doi-asserted-by":"crossref","first-page":"532","DOI":"10.1002\/ana.22615","article-title":"Pathogenic protein seeding in Alzheimer disease and other neurodegenerative disorders","volume":"70","author":"Jucker","year":"2011","journal-title":"Ann. Neurol."},{"key":"2021042513043057100_b54-0070021","doi-asserted-by":"crossref","first-page":"3606","DOI":"10.1523\/JNEUROSCI.20-10-03606.2000","article-title":"Evidence for seeding of beta -amyloid by intracerebral infusion of Alzheimer brain extracts in beta-amyloid precursor protein-transgenic mice","volume":"20","author":"Kane","year":"2000","journal-title":"J. Neurosci."},{"key":"2021042513043057100_b55-0070021","doi-asserted-by":"crossref","first-page":"e5730","DOI":"10.1371\/journal.pone.0005730","article-title":"Prion strain discrimination based on rapid in vivo amplification and analysis by the cell panel assay","volume":"4","author":"Karapetyan","year":"2009","journal-title":"PLoS ONE"},{"key":"2021042513043057100_b56-0070021","doi-asserted-by":"crossref","first-page":"486","DOI":"10.1126\/science.1079469","article-title":"Common structure of soluble amyloid oligomers implies common mechanism of pathogenesis","volume":"300","author":"Kayed","year":"2003","journal-title":"Science"},{"key":"2021042513043057100_b57-0070021","doi-asserted-by":"crossref","first-page":"551","DOI":"10.1083\/jcb.200711002","article-title":"Prion protein attenuates excitotoxicity by inhibiting NMDA receptors","volume":"181","author":"Khosravani","year":"2008","journal-title":"J. Cell Biol."},{"key":"2021042513043057100_b58-0070021","doi-asserted-by":"crossref","first-page":"383","DOI":"10.1016\/j.cell.2011.03.028","article-title":"Ribosome-mediated specificity in Hox mRNA translation and vertebrate tissue patterning","volume":"145","author":"Kondrashov","year":"2011","journal-title":"Cell"},{"key":"2021042513043057100_b59-0070021","doi-asserted-by":"crossref","first-page":"1567","DOI":"10.1007\/s00415-002-0896-9","article-title":"Mutations of the prion protein gene phenotypic spectrum","volume":"249","author":"Kov\u00e1cs","year":"2002","journal-title":"J. Neurol."},{"key":"2021042513043057100_b60-0070021","doi-asserted-by":"crossref","first-page":"135","DOI":"10.1016\/j.mcn.2009.02.002","article-title":"The effects of prion protein expression on metal metabolism","volume":"41","author":"Kralovicova","year":"2009","journal-title":"Mol. Cell. Neurosci."},{"key":"2021042513043057100_b61-0070021","doi-asserted-by":"crossref","first-page":"2690","DOI":"10.1002\/jcb.24616","article-title":"The effect of copper and zinc binding on the solubility and resistance to proteolysis of physiological prion protein PrP depends on the tissue source and the PrP glycotypes","volume":"114","author":"Kuczius","year":"2013","journal-title":"J. Cell. Biochem."},{"key":"2021042513043057100_b62-0070021","doi-asserted-by":"crossref","first-page":"16857","DOI":"10.1523\/JNEUROSCI.1858-12.2012","article-title":"The complex PrP(c)-Fyn couples human oligomeric A\u03b2 with pathological tau changes in Alzheimer\u2019s disease","volume":"32","author":"Larson","year":"2012","journal-title":"J. Neurosci."},{"key":"2021042513043057100_b63-0070021","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":"2021042513043057100_b64-0070021","first-page":"172837","article-title":"Accumulation of vesicle-associated human tau in distal dendrites drives degeneration and tau secretion in an in situ cellular tauopathy model","volume":"2012","author":"Lee","year":"2012","journal-title":"Int. J. Alzheimers Dis."},{"key":"2021042513043057100_b65-0070021","doi-asserted-by":"crossref","first-page":"501","DOI":"10.1038\/nm1746","article-title":"Lewy bodies in grafted neurons in subjects with Parkinson\u2019s disease suggest host-to-graft disease propagation","volume":"14","author":"Li","year":"2008","journal-title":"Nat. Med."},{"key":"2021042513043057100_b66-0070021","doi-asserted-by":"crossref","first-page":"137","DOI":"10.1093\/hmg\/10.2.137","article-title":"Neurological abnormalities in a knock-in mouse model of Huntington\u2019s disease","volume":"10","author":"Lin","year":"2001","journal-title":"Hum. Mol. Genet."},{"key":"2021042513043057100_b67-0070021","doi-asserted-by":"crossref","first-page":"975","DOI":"10.1084\/jem.20112457","article-title":"Intracerebral inoculation of pathological \u03b1-synuclein initiates a rapidly progressive neurodegenerative \u03b1-synucleinopathy in mice","volume":"209","author":"Luk","year":"2012","journal-title":"J. Exp. Med."},{"key":"2021042513043057100_b68-0070021","doi-asserted-by":"crossref","first-page":"72","DOI":"10.3389\/fphys.2012.00072","article-title":"Multifaceted roles of tunneling nanotubes in intercellular communication","volume":"3","author":"Marzo","year":"2012","journal-title":"Front Physiol"},{"key":"2021042513043057100_b69-0070021","doi-asserted-by":"crossref","first-page":"370","DOI":"10.1038\/nn1022","article-title":"Extracellular amyloid formation and associated pathology in neural grafts","volume":"6","author":"Meyer-Luehmann","year":"2003","journal-title":"Nat. Neurosci."},{"key":"2021042513043057100_b70-0070021","doi-asserted-by":"crossref","first-page":"1781","DOI":"10.1126\/science.1131864","article-title":"Exogenous induction of cerebral beta-amyloidogenesis is governed by agent and host","volume":"313","author":"Meyer-Luehmann","year":"2006","journal-title":"Science"},{"key":"2021042513043057100_b71-0070021","doi-asserted-by":"crossref","first-page":"143","DOI":"10.1016\/j.brainres.2007.07.069","article-title":"The neurochemical nature of PrP(c)-containing cells in the rat brain","volume":"1174","author":"Moleres","year":"2007","journal-title":"Brain Res."},{"key":"2021042513043057100_b72-0070021","doi-asserted-by":"crossref","first-page":"507","DOI":"10.1038\/nature11058","article-title":"Sustained translational repression by eIF2\u03b1-P mediates prion neurodegeneration","volume":"485","author":"Moreno","year":"2012","journal-title":"Nature"},{"key":"2021042513043057100_b73-0070021","doi-asserted-by":"crossref","first-page":"12661","DOI":"10.1074\/jbc.271.21.12661","article-title":"Effect of the D178N mutation and the codon 129 polymorphism on the metabolism of the prion protein","volume":"271","author":"Petersen","year":"1996","journal-title":"J. Biol. Chem."},{"key":"2021042513043057100_b74-0070021","doi-asserted-by":"crossref","first-page":"979","DOI":"10.1097\/00005072-199810000-00010","article-title":"Phenotypic variability of Gerstmann-Str\u00e4ussler-Scheinker disease is associated with prion protein heterogeneity","volume":"57","author":"Piccardo","year":"1998","journal-title":"J. Neuropathol. Exp. Neurol."},{"key":"2021042513043057100_b75-0070021","doi-asserted-by":"crossref","first-page":"4712","DOI":"10.1073\/pnas.0609241104","article-title":"Accumulation of prion protein in the brain that is not associated with transmissible disease","volume":"104","author":"Piccardo","year":"2007","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"2021042513043057100_b76-0070021","doi-asserted-by":"crossref","first-page":"143","DOI":"10.1016\/j.bcmd.2005.06.013","article-title":"Prions and exosomes: from PrPc trafficking to PrPsc propagation","volume":"35","author":"Porto-Carreiro","year":"2005","journal-title":"Blood Cells Mol. Dis."},{"key":"2021042513043057100_b77-0070021","doi-asserted-by":"crossref","first-page":"13363","DOI":"10.1073\/pnas.95.23.13363","article-title":"Prions","volume":"95","author":"Prusiner","year":"1998","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"2021042513043057100_b78-0070021","doi-asserted-by":"crossref","first-page":"206","DOI":"10.1039\/c0mt00037j","article-title":"Prion protein expression level alters regional copper, iron and zinc content in the mouse brain","volume":"3","author":"Pushie","year":"2011","journal-title":"Metallomics"},{"key":"2021042513043057100_b79-0070021","doi-asserted-by":"crossref","first-page":"2057","DOI":"10.1038\/emboj.2011.86","article-title":"The cellular prion protein mediates neurotoxic signalling of \u03b2-sheet-rich conformers independent of prion replication","volume":"30","author":"Resenberger","year":"2011","journal-title":"EMBO J."},{"key":"2021042513043057100_b80-0070021","doi-asserted-by":"crossref","first-page":"180","DOI":"10.1038\/382180a0","article-title":"NMR structure of the mouse prion protein domain PrP (121\u2013231)","volume":"382","author":"Riek","year":"1996","journal-title":"Nature"},{"key":"2021042513043057100_b81-0070021","doi-asserted-by":"crossref","first-page":"282","DOI":"10.1016\/S0014-5793(97)00920-4","article-title":"NMR characterization of the full-length recombinant murine prion protein, mPrP (23\u2013231)","volume":"413","author":"Riek","year":"1997","journal-title":"FEBS Lett."},{"key":"2021042513043057100_b82-0070021","doi-asserted-by":"crossref","first-page":"21","DOI":"10.1093\/bmb\/66.1.21","article-title":"Biochemistry and structure of PrP(C) and PrP(Sc)","volume":"66","author":"Riesner","year":"2003","journal-title":"Br. Med. Bull."},{"key":"2021042513043057100_b83-0070021","doi-asserted-by":"crossref","first-page":"700","DOI":"10.1016\/j.jmb.2011.06.008","article-title":"Common structural traits across pathogenic mutants of the human prion protein and their implications for familial prion diseases","volume":"411","author":"Rossetti","year":"2011","journal-title":"J. Mol. Biol."},{"key":"2021042513043057100_b84-0070021","doi-asserted-by":"crossref","first-page":"3842","DOI":"10.1074\/jbc.M111.277061","article-title":"Exosome-associated tau is secreted in tauopathy models and is selectively phosphorylated in cerebrospinal fluid in early Alzheimer disease","volume":"287","author":"Saman","year":"2012","journal-title":"J. Biol. Chem."},{"key":"2021042513043057100_b85-0070021","doi-asserted-by":"crossref","first-page":"159","DOI":"10.1016\/j.bbrc.2011.06.007","article-title":"Mutation directional selection sheds light on prion pathogenesis","volume":"410","author":"Shen","year":"2011","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"2021042513043057100_b86-0070021","doi-asserted-by":"crossref","first-page":"7","DOI":"10.1007\/s00401-009-0619-8","article-title":"Astrocytes: biology and pathology","volume":"119","author":"Sofroniew","year":"2010","journal-title":"Acta Neuropathol."},{"key":"2021042513043057100_b87-0070021","doi-asserted-by":"crossref","first-page":"9","DOI":"10.1113\/jphysiol.2004.078915","article-title":"Defined types of cortical interneurone structure space and spike timing in the hippocampus","volume":"562","author":"Somogyi","year":"2005","journal-title":"J. Physiol."},{"key":"2021042513043057100_b88-0070021","doi-asserted-by":"crossref","first-page":"178","DOI":"10.1016\/j.neuron.2009.07.003","article-title":"Amyloid deposition is associated with impaired default network function in older persons without dementia","volume":"63","author":"Sperling","year":"2009","journal-title":"Neuron"},{"key":"2021042513043057100_b89-0070021","doi-asserted-by":"crossref","first-page":"236","DOI":"10.1016\/j.str.2012.12.002","article-title":"Zinc drives a tertiary fold in the prion protein with familial disease mutation sites at the interface","volume":"21","author":"Spevacek","year":"2013","journal-title":"Structure"},{"key":"2021042513043057100_b90-0070021","doi-asserted-by":"crossref","first-page":"229","DOI":"10.1016\/0092-8674(87)90150-4","article-title":"Scrapie prion protein contains a phosphatidylinositol glycolipid","volume":"51","author":"Stahl","year":"1987","journal-title":"Cell"},{"key":"2021042513043057100_b91-0070021","doi-asserted-by":"crossref","first-page":"3416","DOI":"10.1073\/pnas.0511290103","article-title":"Prion protein (PrPc) positively regulates neural precursor proliferation during developmental and adult mammalian neurogenesis","volume":"103","author":"Steele","year":"2006","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"2021042513043057100_b92-0070021","doi-asserted-by":"crossref","first-page":"41","DOI":"10.1002\/mds.25095","article-title":"Neuronal vulnerability, pathogenesis, and Parkinson\u2019s disease","volume":"28","author":"Sulzer","year":"2013","journal-title":"Mov. Disord."},{"key":"2021042513043057100_b93-0070021","doi-asserted-by":"crossref","first-page":"851","DOI":"10.1091\/mbc.3.8.851","article-title":"Synthesis and trafficking of prion proteins in cultured cells","volume":"3","author":"Taraboulos","year":"1992","journal-title":"Mol. Biol. Cell"},{"key":"2021042513043057100_b94-0070021","doi-asserted-by":"crossref","first-page":"53","DOI":"10.1111\/j.1750-3639.1995.tb00577.x","article-title":"Inherited prion diseases and transmission to rodents","volume":"5","author":"Tateishi","year":"1995","journal-title":"Brain Pathol."},{"key":"2021042513043057100_b95-0070021","doi-asserted-by":"crossref","first-page":"434","DOI":"10.1038\/376434a0","article-title":"First experimental transmission of fatal familial insomnia","volume":"376","author":"Tateishi","year":"1995","journal-title":"Nature"},{"key":"2021042513043057100_b96-0070021","doi-asserted-by":"crossref","first-page":"532","DOI":"10.1212\/WNL.46.2.532","article-title":"Experimental transmission of Creutzfeldt-Jakob disease and related diseases to rodents","volume":"46","author":"Tateishi","year":"1996","journal-title":"Neurology"},{"key":"2021042513043057100_b97-0070021","doi-asserted-by":"crossref","first-page":"e13675","DOI":"10.1371\/journal.pone.0013675","article-title":"Analysis of chaperone mRNA expression in the adult mouse brain by meta analysis of the Allen Brain Atlas","volume":"5","author":"Tebbenkamp","year":"2010","journal-title":"PLoS ONE"},{"key":"2021042513043057100_b98-0070021","doi-asserted-by":"crossref","first-page":"253","DOI":"10.1042\/bj3620253","article-title":"Metal imbalance and compromised antioxidant function are early changes in prion disease","volume":"362","author":"Thackray","year":"2002","journal-title":"Biochem. J."},{"key":"2021042513043057100_b99-0070021","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."},{"key":"2021042513043057100_b100-0070021","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":"2021042513043057100_b101-0070021","doi-asserted-by":"crossref","first-page":"582","DOI":"10.1002\/path.2145","article-title":"Packaging of prions into exosomes is associated with a novel pathway of PrP processing","volume":"211","author":"Vella","year":"2007","journal-title":"J. Pathol."},{"key":"2021042513043057100_b102-0070021","doi-asserted-by":"crossref","first-page":"708","DOI":"10.1016\/j.cell.2012.02.046","article-title":"Inhibitory interneuron deficit links altered network activity and cognitive dysfunction in Alzheimer model","volume":"149","author":"Verret","year":"2012","journal-title":"Cell"},{"key":"2021042513043057100_b103-0070021","doi-asserted-by":"crossref","first-page":"905","DOI":"10.1016\/S0896-6273(02)00733-X","article-title":"A long CAG repeat in the mouse Sca1 locus replicates SCA1 features and reveals the impact of protein solubility on selective neurodegeneration","volume":"34","author":"Watase","year":"2002","journal-title":"Neuron"},{"key":"2021042513043057100_b104-0070021","doi-asserted-by":"crossref","first-page":"1134","DOI":"10.1038\/ncomms2135","article-title":"Prion protein facilitates uptake of zinc into neuronal cells","volume":"3","author":"Watt","year":"2012","journal-title":"Nat Commun"},{"key":"2021042513043057100_b105-0070021","doi-asserted-by":"crossref","first-page":"3498","DOI":"10.1073\/pnas.1121556109","article-title":"Spontaneous generation of rapidly transmissible prions in transgenic mice expressing wild-type bank vole prion protein","volume":"109","author":"Watts","year":"2012","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"2021042513043057100_b106-0070021","doi-asserted-by":"crossref","first-page":"1296","DOI":"10.1161\/01.STR.0000217262.03192.d4","article-title":"Deletion of cellular prion protein results in reduced Akt activation, enhanced postischemic caspase-3 activation, and exacerbation of ischemic brain injury","volume":"37","author":"Weise","year":"2006","journal-title":"Stroke"},{"key":"2021042513043057100_b107-0070021","doi-asserted-by":"crossref","first-page":"117","DOI":"10.1016\/0092-8674(94)90177-5","article-title":"Degeneration of skeletal muscle, peripheral nerves, and the central nervous system in transgenic mice overexpressing wild-type prion proteins","volume":"76","author":"Westaway","year":"1994","journal-title":"Cell"},{"key":"2021042513043057100_b108-0070021","doi-asserted-by":"crossref","first-page":"6021","DOI":"10.1074\/jbc.R800013200","article-title":"Tau mutations in neurodegenerative diseases","volume":"284","author":"Wolfe","year":"2009","journal-title":"J. Biol. Chem."},{"key":"2021042513043057100_b109-0070021","doi-asserted-by":"crossref","first-page":"10072","DOI":"10.1523\/JNEUROSCI.2542-09.2009","article-title":"A New Transgenic Mouse Model of Gerstmann-Straussler-Scheinker Syndrome Caused by the A117V Mutation of PRNP","volume":"29","author":"Yang","year":"2009","journal-title":"J. Neurosci."},{"key":"2021042513043057100_b110-0070021","doi-asserted-by":"crossref","first-page":"1737","DOI":"10.1073\/pnas.1110789109","article-title":"A\u03b2 neurotoxicity depends on interactions between copper ions, prion protein, and N-methyl-D-aspartate receptors","volume":"109","author":"You","year":"2012","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"2021042513043057100_b111-0070021","doi-asserted-by":"crossref","first-page":"523","DOI":"10.1006\/nbdi.2000.0346","article-title":"Spinocerebellar ataxias","volume":"7","author":"Zoghbi","year":"2000","journal-title":"Neurobiol. Dis."},{"key":"2021042513043057100_b112-0070021","first-page":"968","article-title":"Characterization of spontaneously generated prion-like conformers in cultured cells","volume":"3","author":"Zou","year":"2011","journal-title":"Aging (Albany, NY Online)"}],"container-title":["Disease Models &amp; Mechanisms"],"original-title":[],"language":"en","link":[{"URL":"http:\/\/journals.biologists.com\/dmm\/article-pdf\/7\/1\/21\/1865825\/21.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"syndication"},{"URL":"http:\/\/journals.biologists.com\/dmm\/article-pdf\/7\/1\/21\/1865825\/21.pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2021,4,25]],"date-time":"2021-04-25T14:36:01Z","timestamp":1619361361000},"score":1,"resource":{"primary":{"URL":"https:\/\/journals.biologists.com\/dmm\/article\/7\/1\/21\/19967\/Selective-vulnerability-to-neurodegenerative"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2014,1,1]]},"references-count":112,"journal-issue":{"issue":"1","published-print":{"date-parts":[[2014,1,1]]}},"URL":"https:\/\/doi.org\/10.1242\/dmm.012146","relation":{},"ISSN":["1754-8411","1754-8403"],"issn-type":[{"value":"1754-8411","type":"electronic"},{"value":"1754-8403","type":"print"}],"subject":[],"published":{"date-parts":[[2014,1,1]]}}}