Schulz-Schaeffer, Walter Joachim

[["dc.bibliographiccitation.firstpage","985"],["dc.bibliographiccitation.issue","6"],["dc.bibliographiccitation.journal","EMERGING INFECTIOUS DISEASES"],["dc.bibliographiccitation.lastpage","988"],["dc.bibliographiccitation.volume","19"],["dc.contributor.author","Krasemann, Susanne"],["dc.contributor.author","Mearini, Giulia"],["dc.contributor.author","Kraemer, Elisabeth"],["dc.contributor.author","Wagenfuehr, Katja"],["dc.contributor.author","Schulz-Schaeffer, Walter J."],["dc.contributor.author","Neumann, Melanie"],["dc.contributor.author","Bodemer, Walter"],["dc.contributor.author","Kaup, Franz-Josef"],["dc.contributor.author","Beekes, Michael"],["dc.contributor.author","Carrier, Lucie"],["dc.contributor.author","Aguzzi, Adriano"],["dc.contributor.author","Glatzel, Markus"],["dc.date.accessioned","2018-11-07T09:23:46Z"],["dc.date.available","2018-11-07T09:23:46Z"],["dc.date.issued","2013"],["dc.description.abstract","Prion amyloidosis occurred in the heart of 1 of 3 macaques intraperitoneally inoculated with bovine spongiform encephalopathy prions. This macaque had a remarkably long duration of disease and signs of cardiac distress. Variant Creutzfeldt-Jakob disease, caused by transmission of bovine spongiform encephalopathy to humans, may manifest with cardiac symptoms from prion-amyloid cardiomyopathy."],["dc.identifier.doi","10.3201/eid1906.120906"],["dc.identifier.isi","000328173500020"],["dc.identifier.pmid","23735198"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/29660"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Centers Disease Control"],["dc.relation.issn","1080-6059"],["dc.relation.issn","1080-6040"],["dc.title","BSE-associated Prion-Amyloid Cardiomyopathy in Primates"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.journal","Prion"],["dc.bibliographiccitation.volume","5"],["dc.contributor.author","Daus, Martin L."],["dc.contributor.author","Breyer, Johanna"],["dc.contributor.author","Wagenfuehr, Katjs"],["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","2018-11-07T08:57:51Z"],["dc.date.available","2018-11-07T08:57:51Z"],["dc.date.issued","2011"],["dc.format.extent","101"],["dc.identifier.isi","000209066300231"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/23501"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Landes Bioscience"],["dc.publisher.place","Austin"],["dc.relation.issn","1933-690X"],["dc.relation.issn","1933-6896"],["dc.title","Pathological Prion Protein (PrPTSE) in Skeletal Muscles of Farmed and Free Ranging White-Tailed Deer Infected with Chronic Wasting Disease"],["dc.type","conference_abstract"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["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.firstpage","712"],["dc.bibliographiccitation.issue","5"],["dc.bibliographiccitation.journal","EMERGING INFECTIOUS DISEASES"],["dc.bibliographiccitation.lastpage","720"],["dc.bibliographiccitation.volume","19"],["dc.contributor.author","Holznagel, Edgar"],["dc.contributor.author","Yutzy, Barbara"],["dc.contributor.author","Schulz-Schaeffer, Walter J."],["dc.contributor.author","Kruip, Carina"],["dc.contributor.author","Hahmann, Uwe"],["dc.contributor.author","Bierke, Paer"],["dc.contributor.author","Torres, Juan-Maria"],["dc.contributor.author","Kim, Yong-Sun"],["dc.contributor.author","Thomzig, Achim"],["dc.contributor.author","Beekes, Michael"],["dc.contributor.author","Hunsmann, Gerhard"],["dc.contributor.author","Loewer, Johannes"],["dc.date.accessioned","2018-11-07T09:24:48Z"],["dc.date.available","2018-11-07T09:24:48Z"],["dc.date.issued","2013"],["dc.description.abstract","Risk for human exposure to bovine spongiform encephalopathy (BSE) inducing agent was estimated in a nonhuman primate model. To determine attack rates, incubation times, and molecular signatures, we orally exposed 18 macaques to 1 high dose of brain material from cattle with BSE. Several macaques were euthanized at regular intervals starting at 1 year postinoculation, and others were observed until clinical signs developed. Among those who received >= 5 g BSE-inducing agent, attack rates were 100% and prions could be detected in peripheral tissues from 1 year postinoculation onward. The overall median incubation time was 4.6 years (3.7-5.3). However, for 3 macaques orally exposed on multiple occasions, incubation periods were at least 7-10 years. Before clinical signs were noted, we detected a non-type 2B signature, indicating the existence of atypical prion protein during the incubation period. This finding could affect diagnosis of variant Creutzfeldt-Jakob disease in humans and might be relevant for retrospective studies of positive tonsillectomy or appendectomy specimens because time of infection is unknown."],["dc.identifier.doi","10.3201/eid1905.120274"],["dc.identifier.isi","000328173400002"],["dc.identifier.pmid","23647575"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/29916"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Centers Disease Control"],["dc.relation.issn","1080-6059"],["dc.relation.issn","1080-6040"],["dc.title","Foodborne Transmission of Bovine Spongiform Encephalopathy to Nonhuman Primates"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","2563"],["dc.bibliographiccitation.journal","Journal of General Virology"],["dc.bibliographiccitation.lastpage","2568"],["dc.bibliographiccitation.volume","90"],["dc.contributor.author","Cardone, Franco"],["dc.contributor.author","Thomzig, Achim"],["dc.contributor.author","Schulz-Schaeffer, Walter J."],["dc.contributor.author","Valanzano, Angelina"],["dc.contributor.author","Sbriccoli, Marco"],["dc.contributor.author","Abdel-Haq, Hanin"],["dc.contributor.author","Graziano, Silvia"],["dc.contributor.author","Pritzkow, Sandra"],["dc.contributor.author","Puopolo, Maria"],["dc.contributor.author","Brown, Paul"],["dc.contributor.author","Beekes, Michael"],["dc.contributor.author","Pocchiari, Maurizio"],["dc.date.accessioned","2018-11-07T11:23:51Z"],["dc.date.available","2018-11-07T11:23:51Z"],["dc.date.issued","2009"],["dc.description.abstract","The involvement of muscles in the pathogenesis of transmissible spongiform encephalopathies (TSEs) is irregular and unpredictable. We show that the TSE-specific protein (PrPTSE) is present in muscles of mice fed with a mouse-adapted strain of bovine spongiform encephalopathy as early as 100 days post-infection, corresponding to about one-third of the incubation period. The proportion of mice with PrPTSE-positive muscles and the number of muscles involved increased as infection progressed, but never attained more than a limited distribution, even at the clinical stage of disease. The appearance of PrPTSE in muscles during the preclinical stage of disease was probably due to the haematogenous/lymphatic spread of infectivity from the gastrointestinal tract to lymphatic tissues associated with muscles, whereas in symptomatic animals, the presence of PrPTSE in the nervous system, in neuromuscular junctions and in muscle fibres suggests a centrifugal spread from the central nervous system, as already observed in other TSE models."],["dc.description.sponsorship","EU; Deutsche Forschungsgemeinschaft (DFG) [TH 1376/2-1]"],["dc.identifier.doi","10.1099/vir.0.010801-0"],["dc.identifier.isi","000270499700030"],["dc.identifier.pmid","19535501"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/56276"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Soc General Microbiology"],["dc.relation.issn","0022-1317"],["dc.title","PrPTSE in muscle-associated lymphatic tissue during the preclinical stage of mice infected orally with bovine spongiform encephalopathy"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["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"]]