Zafar, Saima

[["dc.bibliographiccitation.firstpage","114"],["dc.bibliographiccitation.issue","1"],["dc.bibliographiccitation.journal","EMERGING INFECTIOUS DISEASES"],["dc.bibliographiccitation.lastpage","117"],["dc.bibliographiccitation.volume","20"],["dc.contributor.author","Douet, Jean Yves"],["dc.contributor.author","Zafar, Saima"],["dc.contributor.author","Perret-Liaudet, Armand"],["dc.contributor.author","Lacroux, Caroline"],["dc.contributor.author","Lugan, Severine"],["dc.contributor.author","Aron, Naima"],["dc.contributor.author","Cassard, Herve"],["dc.contributor.author","Ponto, Claudia"],["dc.contributor.author","Corbiere, Fabien"],["dc.contributor.author","Torres, Juan Maria"],["dc.contributor.author","Zerr, Inga"],["dc.contributor.author","Andreoletti, Olivier"],["dc.date.accessioned","2018-11-07T09:46:58Z"],["dc.date.available","2018-11-07T09:46:58Z"],["dc.date.issued","2014"],["dc.description.abstract","We report the presence of infectivity in erythrocytes, leukocytes, and plasma of 1 person with variant Creutzfeldt-Jakob disease and in the plasma of 2 in 4 persons whose tests were positive for sporadic Creutzfeldt-Jakob disease. The measured infectivity levels were comparable to those reported in various animals with transmissible spongiform encephalopathies."],["dc.identifier.doi","10.3201/eid2001.130353"],["dc.identifier.isi","000329272100018"],["dc.identifier.pmid","24377668"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/35003"],["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","Detection of Infectivity in Blood of Persons with Variant and Sporadic Creutzfeldt-Jakob Disease"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","1355"],["dc.bibliographiccitation.issue","4"],["dc.bibliographiccitation.journal","Journal of Alzheimer's Disease"],["dc.bibliographiccitation.lastpage","1361"],["dc.bibliographiccitation.volume","73"],["dc.contributor.author","Gmitterova, Karin"],["dc.contributor.author","Varges, Daniela"],["dc.contributor.author","Schmitz, Matthias"],["dc.contributor.author","Zafar, Saima"],["dc.contributor.author","Maass, Fabian"],["dc.contributor.author","Lingor, Paul"],["dc.contributor.author","Zerr, Inga"],["dc.date.accessioned","2020-12-10T18:44:13Z"],["dc.date.available","2020-12-10T18:44:13Z"],["dc.date.issued","2020"],["dc.identifier.doi","10.3233/JAD-191153"],["dc.identifier.eissn","1875-8908"],["dc.identifier.issn","1387-2877"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/78369"],["dc.notes.intern","DOI Import GROB-354"],["dc.title","Chromogranin A Analysis in the Differential Diagnosis Across Lewy Body Disorders"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","551"],["dc.bibliographiccitation.issue","3"],["dc.bibliographiccitation.journal","Journal of Alzheimer's Disease"],["dc.bibliographiccitation.lastpage","565"],["dc.bibliographiccitation.volume","38"],["dc.contributor.author","Schmitz, M."],["dc.contributor.author","Wulf, K."],["dc.contributor.author","Signore, S. C."],["dc.contributor.author","Schulz-Schaeffer, W. J."],["dc.contributor.author","Kermer, P."],["dc.contributor.author","Baehr, M."],["dc.contributor.author","Wouters, F. S."],["dc.contributor.author","Zafar, S."],["dc.contributor.author","Zerr, I."],["dc.date.accessioned","2017-09-07T11:46:57Z"],["dc.date.available","2017-09-07T11:46:57Z"],["dc.date.issued","2014"],["dc.description.abstract","Previous studies indicate an important role for the cellular prion protein (PrPC) in the development of Alzheimer's disease (AD) pathology. In the present study, we analyzed the involvement of PrPC in different pathological mechanisms underlying AD: the processing of the amyloid-beta protein precursor (A beta PP) and its interaction with A beta PP, tau, and different phosphorylated forms of the tau protein (p-tau). The effect of PrPC on tau expression was investigated in various cellular compartments using a HEK293 cell model expressing a tau mutant (3PO-tau) or wild type (WT)-tau. We could show that PrPC reduces A beta PP cleavage, leading to decreased levels of A beta(40) and sA beta PP without changing the protein expression of A beta PP, beta-secretase, or gamma-secretase. Tau and its phosphorylated forms were identified as interactions partners for PrPC, raising the question as to whether PrPC might also be involved in tau pathology. Overexpression of PrPC in PRNP and 3PO-tau transfected cells resulted in a reduction of 3PO-tau and p-tau as well as a decrease of 3PO-tau-related toxicity. In addition, we used the transgenic PrPC knockout (Prnp0/0) mouse line to study the dynamics of tau phosphorylation, an important pathological hallmark in the pathogenesis of AD in vivo. There, an effect of PrPC on tau expression could be observed under oxidative stress conditions but not during aging. In summary, we provide further evidence for interactions of PrPC with proteins that are known to be the key players in AD pathogenesis. We identified tau and its phosphorylated forms as potential PrP-interactors and report a novel protective function of PrPC in AD-like tau pathology."],["dc.identifier.doi","10.3233/JAD-130566"],["dc.identifier.gro","3142228"],["dc.identifier.isi","000327598500009"],["dc.identifier.pmid","24028865"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/10657"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/5954"],["dc.notes.intern","WoS Import 2017-03-10"],["dc.notes.intern","Merged from goescholar"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","PUB_WoS_Import"],["dc.relation.eissn","1875-8908"],["dc.relation.issn","1387-2877"],["dc.rights","CC BY 3.0"],["dc.rights.uri","https://creativecommons.org/licenses/by/3.0"],["dc.title","Impact of the Cellular Prion Protein on Amyloid-beta and 3PO-Tau Processing"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","265"],["dc.bibliographiccitation.issue","1"],["dc.bibliographiccitation.journal","Journal of Alzheimer's Disease"],["dc.bibliographiccitation.lastpage","275"],["dc.bibliographiccitation.volume","59"],["dc.contributor.author","Zafar, Saima"],["dc.contributor.author","Shafiq, Mohsin"],["dc.contributor.author","Younas, Neelam"],["dc.contributor.author","Schmitz, Matthias"],["dc.contributor.author","Ferrer, Isidre"],["dc.contributor.author","Zerr, Inga"],["dc.date.accessioned","2020-12-10T18:44:11Z"],["dc.date.available","2020-12-10T18:44:11Z"],["dc.date.issued","2017"],["dc.identifier.doi","10.3233/JAD-170237"],["dc.identifier.eissn","1875-8908"],["dc.identifier.issn","1387-2877"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/78355"],["dc.notes.intern","DOI Import GROB-354"],["dc.title","Prion Protein Interactome: Identifying Novel Targets in Slowly and Rapidly Progressive Forms of Alzheimer’s Disease"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","115"],["dc.bibliographiccitation.lastpage","124"],["dc.contributor.author","Zerr, Inga"],["dc.contributor.author","Zafar, Saima"],["dc.contributor.author","Schmitz, Matthias"],["dc.contributor.author","Llorens, Franc"],["dc.date.accessioned","2021-06-02T10:44:30Z"],["dc.date.available","2021-06-02T10:44:30Z"],["dc.date.issued","2018"],["dc.identifier.doi","10.1016/B978-0-12-804279-3.00008-3"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/87066"],["dc.notes.intern","DOI-Import GROB-425"],["dc.publisher","Elsevier"],["dc.relation.isbn","978-0-12-804279-3"],["dc.relation.ispartof","Cerebrospinal Fluid in Neurologic Disorders"],["dc.title","Cerebrospinal fluid in Creutzfeldt–Jakob disease"],["dc.type","book_chapter"],["dc.type.internalPublication","yes"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","396"],["dc.bibliographiccitation.issue","1"],["dc.bibliographiccitation.journal","Molecular Neurobiology"],["dc.bibliographiccitation.lastpage","405"],["dc.bibliographiccitation.volume","51"],["dc.contributor.author","Cramm, Maria"],["dc.contributor.author","Schmitz, Matthias"],["dc.contributor.author","Karch, Andre"],["dc.contributor.author","Zafar, Saima"],["dc.contributor.author","Varges, Daniel. A."],["dc.contributor.author","Mitrova, Eva"],["dc.contributor.author","Schroeder, Bjoern"],["dc.contributor.author","Raeber, Alex"],["dc.contributor.author","Kuhn, Franziska"],["dc.contributor.author","Zerr, Inga"],["dc.date.accessioned","2018-11-07T10:01:38Z"],["dc.date.available","2018-11-07T10:01:38Z"],["dc.date.issued","2015"],["dc.description.abstract","The development of in vitro amplification systems allows detecting femtomolar amounts of prion protein scrapie (PrPSc) in human cerebrospinal fluid (CSF). We performed a CSF study to determine the effects of prion disease type, codon 129 genotype, PrPSc type, and other disease-related factors on the real-time quaking-induced conversion (RT-QuIC) response. We analyzed times to 10,000 relative fluorescence units, areas under the curve and the signal maximum of RT-QuIC response as seeding parameters of interest. Interestingly, type of prion disease (sporadic vs. genetic) and the PRNP mutation (E200K vs. V210I and FFI), codon 129 genotype, and PrPSc type affected RT-QuIC response. In genetic forms, type of mutation showed the strongest effect on the observed outcome variables. In sporadic CJD, MM1 patients displayed a higher RT-QuIC signal maximum compared to MV1 and VV1. Age and gender were not associated with RT-QuIC signal, but patients with a short disease course showed a higher seeding efficiency of the RT-QuIC response. This study demonstrated that PrPSc characteristics in the CSF of human prion disease patients are associated with disease subtypes and rate of decline as defined by disease duration."],["dc.identifier.doi","10.1007/s12035-014-8709-6"],["dc.identifier.isi","000349006200031"],["dc.identifier.pmid","24809690"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/10255"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/38062"],["dc.notes.intern","Merged from goescholar"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Humana Press Inc"],["dc.relation.issn","1559-1182"],["dc.relation.issn","0893-7648"],["dc.rights","Goescholar"],["dc.rights.uri","https://goescholar.uni-goettingen.de/licenses"],["dc.title","Characteristic CSF Prion Seeding Efficiency in Humans with Prion Diseases"],["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"]]

[["dc.bibliographiccitation.firstpage","95"],["dc.bibliographiccitation.issue","1"],["dc.bibliographiccitation.journal","Prion"],["dc.bibliographiccitation.lastpage","108"],["dc.bibliographiccitation.volume","14"],["dc.contributor.author","Arora, Amandeep Singh"],["dc.contributor.author","Zafar, Saima"],["dc.contributor.author","Latif, Umair"],["dc.contributor.author","Llorens, Franc"],["dc.contributor.author","Mihm, Sabine"],["dc.contributor.author","Kumar, Prateek"],["dc.contributor.author","Tahir, Waqas"],["dc.contributor.author","Thüne, Katrin"],["dc.contributor.author","Shafiq, Mohsin"],["dc.contributor.author","Schmitz, Matthias"],["dc.contributor.author","Zerr, Inga"],["dc.date.accessioned","2020-12-10T18:15:28Z"],["dc.date.available","2020-12-10T18:15:28Z"],["dc.date.issued","2020"],["dc.identifier.doi","10.1080/19336896.2020.1729074"],["dc.identifier.eissn","1933-690X"],["dc.identifier.issn","1933-6896"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/17401"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/74854"],["dc.language.iso","en"],["dc.notes.intern","DOI Import GROB-354"],["dc.notes.intern","Merged from goescholar"],["dc.rights","Goescholar"],["dc.rights.uri","https://goescholar.uni-goettingen.de/licenses"],["dc.title","The role of cellular prion protein in lipid metabolism in the liver"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","2233"],["dc.bibliographiccitation.issue","11"],["dc.bibliographiccitation.journal","Nature Protocols"],["dc.bibliographiccitation.lastpage","2242"],["dc.bibliographiccitation.volume","11"],["dc.contributor.author","Schmitz, Matthias"],["dc.contributor.author","Cramm, Maria"],["dc.contributor.author","Llorens, Franc"],["dc.contributor.author","Müller-Cramm, Dominik"],["dc.contributor.author","Collins, Steven"],["dc.contributor.author","Atarashi, Ryuichiro"],["dc.contributor.author","Satoh, Katsuya"],["dc.contributor.author","Orrù, Christina D"],["dc.contributor.author","Groveman, Bradley R"],["dc.contributor.author","Zafar, Saima"],["dc.contributor.author","Schulz-Schaeffer, Walter J"],["dc.contributor.author","Caughey, Byron"],["dc.contributor.author","Zerr, Inga"],["dc.date.accessioned","2020-12-10T18:09:33Z"],["dc.date.available","2020-12-10T18:09:33Z"],["dc.date.issued","2016"],["dc.identifier.doi","10.1038/nprot.2016.120"],["dc.identifier.eissn","1750-2799"],["dc.identifier.issn","1754-2189"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/73688"],["dc.language.iso","en"],["dc.notes.intern","DOI Import GROB-354"],["dc.title","The real-time quaking-induced conversion assay for detection of human prion disease and study of other protein misfolding diseases"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","88"],["dc.bibliographiccitation.issue","1"],["dc.bibliographiccitation.journal","Journal of Molecular Neuroscience"],["dc.bibliographiccitation.lastpage","98"],["dc.bibliographiccitation.volume","62"],["dc.contributor.author","Ahmed, Sara"],["dc.contributor.author","Mahmood, Zahra"],["dc.contributor.author","Javed, Aneela"],["dc.contributor.author","Hashmi, Shoaib Naiyer"],["dc.contributor.author","Zerr, Inga"],["dc.contributor.author","Zafar, Saima"],["dc.contributor.author","Zahid, Saadia"],["dc.date.accessioned","2020-12-10T14:14:23Z"],["dc.date.available","2020-12-10T14:14:23Z"],["dc.date.issued","2017"],["dc.identifier.doi","10.1007/s12031-017-0915-z"],["dc.identifier.eissn","1559-1166"],["dc.identifier.issn","0895-8696"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/71337"],["dc.language.iso","en"],["dc.notes.intern","DOI Import GROB-354"],["dc.title","Effect of Metformin on Adult Hippocampal Neurogenesis: Comparison with Donepezil and Links to Cognition"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","710"],["dc.bibliographiccitation.issue","6"],["dc.bibliographiccitation.journal","Alzheimer's & Dementia: The Journal of the Alzheimer's Association"],["dc.bibliographiccitation.lastpage","719"],["dc.bibliographiccitation.volume","13"],["dc.contributor.author","Llorens, Franc"],["dc.contributor.author","Kruse, Niels"],["dc.contributor.author","Schmitz, Matthias"],["dc.contributor.author","Gotzmann, Nadine"],["dc.contributor.author","Golanska, Ewa"],["dc.contributor.author","Thüne, Katrin"],["dc.contributor.author","Zejneli, Orgeta"],["dc.contributor.author","Kanata, Eirini"],["dc.contributor.author","Knipper, Tobias"],["dc.contributor.author","Cramm, Maria"],["dc.contributor.author","Lange, Peter"],["dc.contributor.author","Zafar, Saima"],["dc.contributor.author","Sikorska, Beata"],["dc.contributor.author","Liberski, Pawel P."],["dc.contributor.author","Mitrova, Eva"],["dc.contributor.author","Varges, Daniela"],["dc.contributor.author","Schmidt, Christian"],["dc.contributor.author","Sklaviadis, Theodoros"],["dc.contributor.author","Mollenhauer, Brit"],["dc.contributor.author","Zerr, Inga"],["dc.date.accessioned","2018-10-08T13:38:00Z"],["dc.date.available","2018-10-08T13:38:00Z"],["dc.date.issued","2017-06"],["dc.description.abstract","Accurate diagnosis of prion diseases and discrimination from alternative dementias gain importance in the clinical routine, but partial overlap in cerebrospinal fluid (CSF) biomarkers impedes absolute discrimination in the differential diagnostic context. We established the clinical parameters for prion disease diagnosis for the quantification of CSF α-synuclein in patients with sporadic (n = 234) and genetic (n = 56) prion diseases, in cases with cognitive impairment/dementia or neurodegenerative disease (n = 278), and in the neurologic control group (n = 111). An optimal cutoff value of 680 pg/mL α-synuclein results in 94% sensitivity and 96% specificity when diagnosing sporadic Creutzfeldt-Jakob disease (CJD). Genetic CJD cases showed increased CSF α-synuclein values. No increased α-synuclein levels were detected in non-CJD cases with rapid progression course. Detection of α-synuclein in the CSF of patients with suspected CJD is a valuable diagnostic test reaching almost full discrimination from non-prion disease cases. These data highlight the utility of CSF α-synuclein quantification in front of classical CSF biomarkers in clinical routine."],["dc.fs.pkfprnr","61006"],["dc.identifier.doi","10.1016/j.jalz.2016.09.013"],["dc.identifier.fs","631450"],["dc.identifier.pmid","27870938"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/15884"],["dc.language.iso","en"],["dc.notes.status","final"],["dc.relation.eissn","1552-5279"],["dc.title","Evaluation of α-synuclein as a novel cerebrospinal fluid biomarker in different forms of prion diseases"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dspace.entity.type","Publication"]]