Schulz-Schaeffer, Walter Joachim

[["dc.bibliographiccitation.firstpage","463"],["dc.bibliographiccitation.issue","4"],["dc.bibliographiccitation.journal","Acta Neuropathologica"],["dc.bibliographiccitation.lastpage","476"],["dc.bibliographiccitation.volume","128"],["dc.contributor.author","Beekes, Michael"],["dc.contributor.author","Thomzig, Achim"],["dc.contributor.author","Schulz-Schaeffer, Walter J."],["dc.contributor.author","Burger, Reinhard"],["dc.date.accessioned","2018-11-07T09:34:50Z"],["dc.date.available","2018-11-07T09:34:50Z"],["dc.date.issued","2014"],["dc.description.abstract","The misfolding and aggregation of endogenous proteins in the central nervous system is a neuropathological hallmark of Alzheimer's disease (AD), Parkinson's disease (PD), as well as prion diseases. A molecular mechanism referred to as \"nucleation-dependent aggregation\" is thought to underlie this neuropathological phenomenon. According to this concept, disease-associated protein particles act as nuclei, or seeds, that recruit cellular proteins and incorporate them, in a misfolded form, into their growing aggregate structure. Experimental studies have shown that the aggregation of the AD-associated proteins amyloid-beta (A beta) and tau, and of the PD-associated protein alpha-synuclein, can be stimulated in laboratory animal models by intracerebral (i.c.) injection of inocula containing aggregated species of the respective proteins. This has raised the question of whether AD or PD can be transmitted, like certain human prion diseases, between individuals by self-propagating protein particles potentially present on medical instruments or in blood or blood products. While the i.c. injection of inocula containing AD- or PD-associated protein aggregates was found to cause neuronal damage and clinical abnormalities (e.g., motor impairments) in some animal models, none of the studies published so far provided evidence for a transmission of severe or even fatal disease. In addition, available epidemiological data do not indicate a transmissibility of AD or PD between humans. The findings published so far on the effects of experimentally transmitted AD- or PD-associated protein seeds do not suggest specific precautionary measures in the context of hemotherapy, but call for vigilance in transfusion medicine and other medical areas."],["dc.description.sponsorship","German Federal Ministry of Health [IIA5-2512NIK004//321-4471-02]"],["dc.identifier.doi","10.1007/s00401-014-1324-9"],["dc.identifier.isi","000341906600001"],["dc.identifier.pmid","25073522"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/10855"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/32262"],["dc.notes.intern","Merged from goescholar"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Springer"],["dc.relation.issn","1432-0533"],["dc.relation.issn","0001-6322"],["dc.rights","CC BY 4.0"],["dc.rights.uri","https://creativecommons.org/licenses/by/4.0"],["dc.title","Is there a risk of prion-like disease transmission by Alzheimer- or Parkinson-associated protein particles?"],["dc.type","review"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.artnumber","151"],["dc.bibliographiccitation.journal","Acta neuropathologica communications"],["dc.bibliographiccitation.volume","2"],["dc.contributor.author","Thomzig, Achim"],["dc.contributor.author","Wagenführ, Katja"],["dc.contributor.author","Daus, Martin L."],["dc.contributor.author","Joncic, Marion"],["dc.contributor.author","Schulz-Schaeffer, Walter J."],["dc.contributor.author","Thanheiser, Marc"],["dc.contributor.author","Mielke, Martin"],["dc.contributor.author","Beekes, Michael"],["dc.date.accessioned","2019-07-09T11:41:35Z"],["dc.date.available","2019-07-09T11:41:35Z"],["dc.date.issued","2014"],["dc.description.abstract","not available"],["dc.identifier.doi","10.1186/s40478-014-0151-5"],["dc.identifier.fs","611476"],["dc.identifier.pmid","25344093"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/12176"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/58453"],["dc.language.iso","en"],["dc.notes.intern","Merged from goescholar"],["dc.relation.issn","2051-5960"],["dc.rights","CC BY 4.0"],["dc.rights.uri","https://creativecommons.org/licenses/by/4.0"],["dc.subject.mesh","Amyloid beta-Peptides"],["dc.subject.mesh","Animals"],["dc.subject.mesh","Brain"],["dc.subject.mesh","Decontamination"],["dc.subject.mesh","Equipment and Supplies"],["dc.subject.mesh","Humans"],["dc.subject.mesh","Mice"],["dc.subject.mesh","Patient Safety"],["dc.subject.mesh","Protein Aggregates"],["dc.subject.mesh","alpha-Synuclein"],["dc.subject.mesh","tau Proteins"],["dc.title","Decontamination of medical devices from pathological amyloid-β-, tau- and α-synuclein aggregates."],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.artnumber","e18345"],["dc.bibliographiccitation.issue","4"],["dc.bibliographiccitation.journal","PLoS ONE"],["dc.bibliographiccitation.volume","6"],["dc.contributor.author","Daus, Martin L."],["dc.contributor.author","Breyer, Johanna"],["dc.contributor.author","Wagenfuehr, Katja"],["dc.contributor.author","Wemheuer, Wiebke M."],["dc.contributor.author","Thomzig, Achim"],["dc.contributor.author","Schulz-Schaeffer, Walter J."],["dc.contributor.author","Beekes, Michael"],["dc.date.accessioned","2018-11-07T08:57:33Z"],["dc.date.available","2018-11-07T08:57:33Z"],["dc.date.issued","2011"],["dc.description.abstract","Chronic wasting disease (CWD) is a contagious, rapidly spreading transmissible spongiform encephalopathy (TSE), or prion disease, occurring in cervids such as white tailed-deer (WTD), mule deer or elk in North America. Despite efficient horizontal transmission of CWD among cervids natural transmission of the disease to other species has not yet been observed. Here, we report for the first time a direct biochemical demonstration of pathological prion protein PrPTSE and of PrPTSE-associated seeding activity, the static and dynamic biochemical markers for biological prion infectivity, respectively, in skeletal muscles of CWD-infected cervids, i.e. WTD for which no clinical signs of CWD had been recognized. The presence of PrPTSE was detected by Western-and postfixed frozen tissue blotting, while the seeding activity of PrPTSE was revealed by protein misfolding cyclic amplification (PMCA). Semi-quantitative Western blotting indicated that the concentration of PrPTSE in skeletal muscles of CWD-infected WTD was approximately 2000-10000 - fold lower than in brain tissue. Tissue-blot-analyses revealed that PrPTSE was located in muscle-associated nerve fascicles but not, in detectable amounts, in myocytes. The presence and seeding activity of PrPTSE in skeletal muscle from CWD-infected cervids suggests prevention of such tissue in the human diet as a precautionary measure for food safety, pending on further clarification of whether CWD may be transmissible to humans."],["dc.description.sponsorship","Alberta Prion Research Institute (APRI)"],["dc.identifier.doi","10.1371/journal.pone.0018345"],["dc.identifier.isi","000289058300012"],["dc.identifier.pmid","21483771"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/8197"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/23427"],["dc.notes.intern","Merged from goescholar"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Public Library Science"],["dc.relation.issn","1932-6203"],["dc.rights","CC BY 2.5"],["dc.rights.uri","https://creativecommons.org/licenses/by/2.5"],["dc.title","Presence and Seeding Activity of Pathological Prion Protein (PrPTSE) in Skeletal Muscles of White-Tailed Deer Infected with Chronic Wasting Disease"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]