{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,4,22]],"date-time":"2026-04-22T15:43:51Z","timestamp":1776872631957,"version":"3.51.2"},"reference-count":39,"publisher":"Elsevier BV","issue":"5","license":[{"start":{"date-parts":[[2001,10,1]],"date-time":"2001-10-01T00:00:00Z","timestamp":1001894400000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2001,10,1]],"date-time":"2001-10-01T00:00:00Z","timestamp":1001894400000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"}],"funder":[{"DOI":"10.13039\/501100000780","name":"European Commission","doi-asserted-by":"publisher","award":["BMH4-CT98-6040"],"award-info":[{"award-number":["BMH4-CT98-6040"]}],"id":[{"id":"10.13039\/501100000780","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100001663","name":"Volkswagen Foundation","doi-asserted-by":"publisher","id":[{"id":"10.13039\/501100001663","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["clinicalkey.com","clinicalkey.com.au","clinicalkey.es","clinicalkey.fr","clinicalkey.jp","elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Neurobiology of Disease"],"published-print":{"date-parts":[[2001,10]]},"DOI":"10.1006\/nbdi.2001.0418","type":"journal-article","created":{"date-parts":[[2002,9,18]],"date-time":"2002-09-18T15:46:43Z","timestamp":1032364003000},"page":"881-889","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":27,"title":["Prominent Stress Response of Purkinje Cells in Creutzfeldt\u2013Jakob Disease"],"prefix":"10.1006","volume":"8","author":[{"given":"G\u00e1bor G.","family":"Kov\u00e1cs","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Istv\u00e1n","family":"Kurucz","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Herbert","family":"Budka","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Csaba","family":"\u00c1dori","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Ferenc","family":"M\u00fcller","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"P\u00e9ter","family":"\u00c1cs","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Stefan","family":"Kl\u00f6ppel","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Hermann M.","family":"Sch\u00e4tzl","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"R.John","family":"Mayer","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Lajos","family":"L\u00e1szl\u00f3","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"78","reference":[{"key":"10.1006\/nbdi.2001.0418_RF1","doi-asserted-by":"crossref","first-page":"469","DOI":"10.1038\/35019501","article-title":"Heat-shock protein 70 inhibits apoptosis by preventing recruitment of procaspase-9 to the Apaf-1 apoptosome","volume":"2","author":"Beere","year":"2000","journal-title":"Nature Cell Biol."},{"key":"10.1006\/nbdi.2001.0418_RF2","doi-asserted-by":"crossref","first-page":"26","DOI":"10.1111\/j.1365-2990.1997.tb01182.x","article-title":"Prion protein immuno-cytochemistry\u2014UK five centre consensus report","volume":"23","author":"Bell","year":"1997","journal-title":"Neuropathol. Appl. Neurobiol."},{"key":"10.1006\/nbdi.2001.0418_RF3","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1042\/bj3440001","article-title":"Normal prion protein has an activity like that of superoxide dismutase","volume":"344","author":"Brown","year":"1999","journal-title":"Biochem. J."},{"key":"10.1006\/nbdi.2001.0418_RF4","doi-asserted-by":"crossref","first-page":"880","DOI":"10.1126\/science.7754373","article-title":"Role of chaperone protein Hsp 104 in propagation of the yeast prion-like factor [psi+]","volume":"268","author":"Chernoff","year":"1995","journal-title":"Science"},{"key":"10.1006\/nbdi.2001.0418_RF5","doi-asserted-by":"crossref","first-page":"8103","DOI":"10.1128\/MCB.19.12.8103","article-title":"Evidence for a protein mutator in yeast: Role for the Hsp70-related chaperone Ssb in formation, stability, and toxicity of the [PSI] prion","volume":"19","author":"Chernoff","year":"1999","journal-title":"Mol. Cell. Biol."},{"key":"10.1006\/nbdi.2001.0418_RF6","doi-asserted-by":"crossref","first-page":"382","DOI":"10.1126\/science.2799391","article-title":"A role for a 70-kilodalton heat shock protein in lysosomal degradation of intracellular proteins","volume":"246","author":"Chiang","year":"1989","journal-title":"Science"},{"key":"10.1006\/nbdi.2001.0418_RF7","doi-asserted-by":"crossref","first-page":"1337","DOI":"10.1016\/S0896-6273(00)80424-9","article-title":"Selective neuronal targeting in prion disease","volume":"19","author":"DeArmond","year":"1997","journal-title":"Neuron"},{"key":"10.1006\/nbdi.2001.0418_RF8","doi-asserted-by":"crossref","first-page":"1000","DOI":"10.1097\/00005072-199909000-00010","article-title":"PrPC glycoform heterogeneity as a function of brain region: Implications for selective targeting of neurons by prion strains","volume":"58","author":"DeArmond","year":"1999","journal-title":"J. Neuropath. Exp. Neurol."},{"key":"10.1006\/nbdi.2001.0418_RF9","doi-asserted-by":"crossref","first-page":"13938","DOI":"10.1073\/pnas.94.25.13938","article-title":"Chaperone-supervised conversion of prion protein to its protease-resistant form","volume":"94","author":"DebBurman","year":"1997","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"10.1006\/nbdi.2001.0418_RF10","doi-asserted-by":"crossref","first-page":"391","DOI":"10.1016\/S0166-2236(98)01310-1","article-title":"Microcircuitry and function of the inferior olive","volume":"21","author":"De-Zeeuw","year":"1998","journal-title":"Trends Neurosci."},{"key":"10.1006\/nbdi.2001.0418_RF11","doi-asserted-by":"crossref","first-page":"273","DOI":"10.1046\/j.1365-2990.2000.00239.x","article-title":"Prion protein immunoreactivity in brain samples from an unselected autopsy population: Findings in 200 consecutive cases","volume":"26","author":"Esiri","year":"2000","journal-title":"Neuropathol. Appl. Neurobiol."},{"key":"10.1006\/nbdi.2001.0418_RF12","doi-asserted-by":"crossref","first-page":"979","DOI":"10.1007\/BF01923452","article-title":"Heat shock proteins: The hsp 70 family","volume":"50","author":"Feige","year":"1994","journal-title":"Experientia"},{"key":"10.1006\/nbdi.2001.0418_RF13","doi-asserted-by":"crossref","first-page":"5","DOI":"10.1007\/s004010050949","article-title":"Nuclear DNA fragmentation in Creutzfeldt\u2013Jakob disease: Does a mere positive in situ nuclear end-labeling indicate apoptosis?","volume":"97","author":"Ferrer","year":"1999","journal-title":"Acta Neuropathol."},{"key":"10.1006\/nbdi.2001.0418_RF14","doi-asserted-by":"crossref","first-page":"321","DOI":"10.1097\/00005072-199904000-00002","article-title":"Neuronal apoptosis in Creutzfeldt\u2013Jakob disease","volume":"58","author":"Gray","year":"1999","journal-title":"J. Neuropathol. Exp. Neurol."},{"key":"10.1006\/nbdi.2001.0418_RF15","doi-asserted-by":"crossref","first-page":"615","DOI":"10.1111\/j.1750-3639.1998.tb00188.x","article-title":"Severe, early and selective loss of a subpopulation of GABAergic inhibitory neurons in experimental transmissible spongiform encephalopathies","volume":"8","author":"Guentchev","year":"1998","journal-title":"Brain Pathol."},{"key":"10.1006\/nbdi.2001.0418_RF16","doi-asserted-by":"crossref","first-page":"66","DOI":"10.1002\/1097-0029(20000701)50:1<66::AID-JEMT10>3.0.CO;2-3","article-title":"Synaptic prion protein immuno-reactivity in the rodent cerebellum","volume":"50","author":"Haeberle","year":"2000","journal-title":"Microsc. Res. Tech."},{"key":"10.1006\/nbdi.2001.0418_RF17","doi-asserted-by":"crossref","first-page":"571","DOI":"10.1038\/381571a0","article-title":"Molecular chaperones in cellular protein folding","volume":"381","author":"Hartl","year":"1996","journal-title":"Nature"},{"key":"10.1006\/nbdi.2001.0418_RF18","doi-asserted-by":"crossref","first-page":"379","DOI":"10.1111\/j.1750-3639.1996.tb00869.x","article-title":"Review: Creutzfeldt\u2013Jakob disease","volume":"6","author":"Ironside","year":"1996","journal-title":"Brain Pathol."},{"key":"10.1006\/nbdi.2001.0418_RF19","doi-asserted-by":"crossref","first-page":"1870","DOI":"10.1046\/j.1471-4159.1994.62051870.x","article-title":"Expression of polyubiquitin and heat-shock protein 70 genes increases in the later stages of disease progression in scrapie infected mouse brain","volume":"62","author":"Kenward","year":"1994","journal-title":"J. Neurochem."},{"key":"10.1006\/nbdi.2001.0418_RF20","doi-asserted-by":"crossref","first-page":"18","DOI":"10.1379\/1466-1268(1996)001<0018:HSPMCA>2.3.CO;2","article-title":"Heat shock proteins, molecular chaperones and the prion encephalopathies","volume":"1","author":"Kenward","year":"1996","journal-title":"Cell Stress Chaperones"},{"key":"10.1006\/nbdi.2001.0418_RF21","doi-asserted-by":"crossref","first-page":"139","DOI":"10.1379\/1466-1268(1999)004<0139:ULOHEW>2.3.CO;2","article-title":"Ultrastructural localization of Hsp-72 examined with a new polyclonal antibody raised against the truncated variable domain of the heat shock protein","volume":"4","author":"Kurucz","year":"1999","journal-title":"Cell Stress & Chaperones"},{"key":"10.1006\/nbdi.2001.0418_RF22","doi-asserted-by":"crossref","first-page":"333","DOI":"10.1002\/path.1711660404","article-title":"Lysosomes as key organelles in the pathogenesis of prion encephalopathies","volume":"166","author":"Laszlo","year":"1992","journal-title":"J. Pathol."},{"key":"10.1006\/nbdi.2001.0418_RF23","doi-asserted-by":"crossref","first-page":"1151","DOI":"10.1146\/annurev.bi.55.070186.005443","article-title":"The heat shock response","volume":"55","author":"Lindquist","year":"1986","journal-title":"Annu. Rev. Biochem."},{"key":"10.1006\/nbdi.2001.0418_RF24","doi-asserted-by":"crossref","first-page":"480","DOI":"10.1002\/jnr.490360414","article-title":"Temporal and spatial distribution of heat shock mRNA and protein (hsp70) in the rabbit cerebellum in response to hyperthermia","volume":"36","author":"Manzerra","year":"1993","journal-title":"J. Neurosci. Res."},{"key":"10.1006\/nbdi.2001.0418_RF25","doi-asserted-by":"crossref","first-page":"1325","DOI":"10.1128\/MCB.19.2.1325","article-title":"Antagonistic interactions between yeast chaperones Hsp104 and Hsp70 in prion curing","volume":"19","author":"Newnam","year":"1999","journal-title":"Mol. Cell. Biol."},{"key":"10.1006\/nbdi.2001.0418_RF26","first-page":"689","article-title":"A mouse prion protein transgene rescues mice deficient for the prion protein gene from Purkinje cell degeneration and demyelination","volume":"79","author":"Nishida","year":"1999","journal-title":"Lab. Invest."},{"key":"10.1006\/nbdi.2001.0418_RF27","doi-asserted-by":"crossref","first-page":"139","DOI":"10.1111\/j.1365-2990.1991.tb00705.x","article-title":"Heat shock in cultured neurons and astrocytes: Correlation of ultrastructure and heat shock protein synthesis","volume":"17","author":"Nishimura","year":"1991","journal-title":"Neuropathol. Appl. Neurobiol."},{"key":"10.1006\/nbdi.2001.0418_RF28","doi-asserted-by":"crossref","first-page":"224","DOI":"10.1002\/1531-8249(199908)46:2<224::AID-ANA12>3.0.CO;2-W","article-title":"Classification of sporadic Creutzfeldt\u2013Jakob disease based on molecular and phenotypic analysis of 300 subjects","volume":"46","author":"Parchi","year":"1999","journal-title":"Ann. Neurol."},{"key":"10.1006\/nbdi.2001.0418_RF29","doi-asserted-by":"crossref","first-page":"245","DOI":"10.1126\/science.278.5336.245","article-title":"Prion diseases and the BSE crisis","volume":"278","author":"Prusiner","year":"1997","journal-title":"Science"},{"key":"10.1006\/nbdi.2001.0418_RF30","doi-asserted-by":"crossref","first-page":"511","DOI":"10.1007\/BF00294178","article-title":"Expression of small heat-shock protein hsp 27 in reactive gliosis in Alzheimer disease and other types of dementia","volume":"87","author":"Renkawek","year":"1994","journal-title":"Acta Neuropathol."},{"key":"10.1006\/nbdi.2001.0418_RF31","doi-asserted-by":"crossref","first-page":"528","DOI":"10.1038\/380528a0","article-title":"Loss of cerebellar Purkinje cells in aged mice homozygous for a disrupted PrP gene","volume":"380","author":"Sakaguchi","year":"1996","journal-title":"Nature"},{"key":"10.1006\/nbdi.2001.0418_RF32","doi-asserted-by":"crossref","first-page":"476","DOI":"10.1038\/35019510","article-title":"Negative regulation of the Apaf-1 apoptosome by Hsp70","volume":"2","author":"Saleh","year":"2000","journal-title":"Nature Cell Biol."},{"key":"10.1006\/nbdi.2001.0418_RF33","doi-asserted-by":"crossref","first-page":"98","DOI":"10.1016\/S0962-8924(99)01711-0","article-title":"Protein only inheritance in yeast: Something to get [PSI+]-ched about","volume":"10","author":"Serio","year":"2000","journal-title":"Trends Cell Biol."},{"key":"10.1006\/nbdi.2001.0418_RF34","doi-asserted-by":"crossref","first-page":"97","DOI":"10.1016\/S0166-2236(98)01392-7","article-title":"Heat-shock protein protection","volume":"22","author":"Sharp","year":"1999","journal-title":"Trends Neurosci."},{"key":"10.1006\/nbdi.2001.0418_RF35","doi-asserted-by":"crossref","first-page":"771","DOI":"10.1097\/00001756-200003200-00023","article-title":"Heat shock modulates prion protein expression in human NT-2 cells","volume":"11","author":"Shyu","year":"2000","journal-title":"NeuroReport"},{"key":"10.1006\/nbdi.2001.0418_RF36","doi-asserted-by":"crossref","first-page":"456","DOI":"10.1097\/00005072-199805000-00009","article-title":"Alzheimer disease: DNA fragmentation indicates increased neuronal vulnerability, but not apoptosis","volume":"57","author":"Stadelmann","year":"1998","journal-title":"J. Neuropathol. Exp. Neurol."},{"key":"10.1006\/nbdi.2001.0418_RF37","doi-asserted-by":"crossref","first-page":"721","DOI":"10.1023\/A:1020646321841","article-title":"Abnormalities in stress proteins in prion diseases","volume":"18","author":"Tatzelt","year":"1998","journal-title":"Cell. Mol. Neurobiol."},{"key":"10.1006\/nbdi.2001.0418_RF38","doi-asserted-by":"crossref","first-page":"79","DOI":"10.1016\/0092-8674(95)90236-8","article-title":"Prion propagation in mice expressing human and chimeric PrP transgenes implicates the interaction of cellular PrP with another protein","volume":"83","author":"Telling","year":"1995","journal-title":"Cell"},{"key":"10.1006\/nbdi.2001.0418_RF39","doi-asserted-by":"crossref","first-page":"1150","DOI":"10.1038\/nm1097-1150","article-title":"Bimoclomol: A nontoxic, hydroxylamine derivative with stress protein-inducing activity and cytoprotective effects","volume":"3","author":"V\u0131\u0301gh","year":"1997","journal-title":"Nature Med."}],"container-title":["Neurobiology of Disease"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0969996101904188?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0969996101904188?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2026,4,22]],"date-time":"2026-04-22T14:50:49Z","timestamp":1776869449000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0969996101904188"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2001,10]]},"references-count":39,"journal-issue":{"issue":"5","published-print":{"date-parts":[[2001,10]]}},"alternative-id":["S0969996101904188"],"URL":"https:\/\/doi.org\/10.1006\/nbdi.2001.0418","relation":{},"ISSN":["0969-9961"],"issn-type":[{"value":"0969-9961","type":"print"}],"subject":[],"published":{"date-parts":[[2001,10]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Prominent Stress Response of Purkinje Cells in Creutzfeldt\u2013Jakob Disease","name":"articletitle","label":"Article Title"},{"value":"Neurobiology of Disease","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1006\/nbdi.2001.0418","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"Copyright \u00a9 2001 Academic Press. Published by Elsevier Inc. All rights are reserved, including those for text and data mining, AI training, and similar technologies.","name":"copyright","label":"Copyright"}]}}