Kraus, Inga

[["dc.bibliographiccitation.artnumber","12767"],["dc.bibliographiccitation.issue","1"],["dc.bibliographiccitation.journal","Scientific Reports"],["dc.bibliographiccitation.volume","5"],["dc.contributor.author","Kraus, Inga"],["dc.contributor.author","Besong Agbo, Daniela"],["dc.contributor.author","Otto, Markus"],["dc.contributor.author","Wiltfang, Jens"],["dc.contributor.author","Klafki, Hans"],["dc.date.accessioned","2017-09-07T11:44:28Z"],["dc.date.available","2017-09-07T11:44:28Z"],["dc.date.issued","2015"],["dc.description.abstract","The extracellular signal regulated kinases ERK1/2 play important roles in the regulation of diverse cellular functions and have been implicated in several human diseases. In addition to the fully activated, diphosphorylated ERK1/2 protein, monophosphorylated forms of ERK1/2 have been observed, which may have distinct biological functions. We report here on the highly sensitive detection and differentiation of unphosphorylated, threonine-phosphorylated (pT), tyrosine-phosphorylated (pY) and diphosphorylated ERK1 and ERK2 by capillary isoelectric focusing followed by immunological detection (CIEF-immunoassay). Eight different phosphorylated and unphosphorylated forms of ERK1/2 were resolved according to charge. The unequivocal identification and differentiation of ERK1 and ERK2 forms monophosphorylated at either threonine or tyrosine was achieved by competitive blocking with specific phospho-peptides and different phosphorylation-sensitive antibodies. The suitability of the additional pT-ERK1/2 and pY-ERK1/2 differentiation for the time-resolved in-depth study of phospho-form distribution in response to specific stimuli is demonstrated in human neuroblastoma SH-SY5Y and monocytic THP-1 cell lines, and in human peripheral blood mononuclear cells."],["dc.description.sponsorship","Open-Access Publikationsfonds 2015"],["dc.identifier.doi","10.1038/srep12767"],["dc.identifier.gro","3151679"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/12067"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/8497"],["dc.language.iso","en"],["dc.notes.intern","Merged from goescholar"],["dc.notes.status","final"],["dc.notes.submitter","chake"],["dc.relation.issn","2045-2322"],["dc.rights","CC BY 4.0"],["dc.rights.uri","https://creativecommons.org/licenses/by/4.0"],["dc.title","Detection and Differentiation of Threonine- and Tyrosine-Monophosphorylated Forms of ERK1/2 by Capillary Isoelectric Focusing-Immunoassay"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","no"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","e66"],["dc.bibliographiccitation.issue","S 01"],["dc.bibliographiccitation.journal","Methods of Information in Medicine"],["dc.bibliographiccitation.lastpage","e81"],["dc.bibliographiccitation.volume","57"],["dc.contributor.author","Haarbrandt, Birger"],["dc.contributor.author","Schreiweis, Björn"],["dc.contributor.author","Rey, Sabine"],["dc.contributor.author","Sax, Ulrich"],["dc.contributor.author","Scheithauer, Simone"],["dc.contributor.author","Rienhoff, Otto"],["dc.contributor.author","Knaup-Gregori, Petra"],["dc.contributor.author","Bavendiek, Udo"],["dc.contributor.author","Dieterich, Christoph"],["dc.contributor.author","Brors, Benedikt"],["dc.contributor.author","Kraus, Inga"],["dc.contributor.author","Thoms, Caroline"],["dc.contributor.author","Jäger, Dirk"],["dc.contributor.author","Ellenrieder, Volker"],["dc.contributor.author","Bergh, Björn"],["dc.contributor.author","Yahyapour, Ramin"],["dc.contributor.author","Eils, Roland"],["dc.contributor.author","Consortium, HiGHmed"],["dc.contributor.author","Marschollek, Michael"],["dc.date.accessioned","2020-12-10T18:47:27Z"],["dc.date.available","2020-12-10T18:47:27Z"],["dc.date.issued","2018"],["dc.description.abstract","This article is part of the Focus Theme of Methods of Information in Medicine on the German Medical Informatics Initiative. HiGHmed brings together 24 partners from academia and industry, aiming at improvements in care provision, biomedical research and epidemiology. By establishing a shared information governance framework, data integration centers and an open platform architecture in cooperation with independent healthcare providers, the meaningful reuse of data will be facilitated. Complementary, HiGHmed integrates a total of seven Medical Informatics curricula to develop collaborative structures and processes to train medical informatics professionals, physicians and researchers in new forms of data analytics."],["dc.identifier.doi","10.3414/ME18-02-0002"],["dc.identifier.eissn","2511-705X"],["dc.identifier.issn","0026-1270"],["dc.identifier.pmid","30016813"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/15525"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/78770"],["dc.language.iso","en"],["dc.notes.intern","DOI Import GROB-354"],["dc.notes.intern","Merged from goescholar"],["dc.relation.eissn","2511-705X"],["dc.relation.issn","0026-1270"],["dc.relation.issn","2511-705X"],["dc.rights","CC BY-NC-ND 4.0"],["dc.rights.uri","https://creativecommons.org/licenses/by-nc-nd/4.0"],["dc.title","HiGHmed – An Open Platform Approach to Enhance Care and Research across Institutional Boundaries"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","691"],["dc.bibliographiccitation.issue","2"],["dc.bibliographiccitation.journal","Journal of Alzheimer's Disease"],["dc.bibliographiccitation.lastpage","705"],["dc.bibliographiccitation.volume","54"],["dc.contributor.author","Klafki, Hans-Wolfgang"],["dc.contributor.author","Hafermann, Henning"],["dc.contributor.author","Bauer, Chris"],["dc.contributor.author","Haußmann, Ute"],["dc.contributor.author","Kraus, Inga"],["dc.contributor.author","Schuchhardt, Johannes"],["dc.contributor.author","Muck, Stephan"],["dc.contributor.author","Scherbaum, Norbert"],["dc.contributor.author","Wiltfang, Jens"],["dc.date.accessioned","2017-09-07T11:44:28Z"],["dc.date.available","2017-09-07T11:44:28Z"],["dc.date.issued","2016"],["dc.description.abstract","A comprehensive assay validation campaign of a commercially available chemiluminescence multiplex immunoassay for the simultaneous measurement of the amyloid-β peptides Aβ38, Aβ40, and Aβ42 in human cerebrospinal fluid (CSF) is presented. The assay quality parameters we addressed included impact of sample dilution, parallelism, lower limits of detection, lower limits of quantification, intra- and inter-assay repeatability, analytical spike recoveries, and between laboratory reproducibility of the measurements. The assay performed well in our hands and fulfilled a number of predefined acceptance criteria. The CSF levels of Aβ40 and Aβ42 determined in a clinical cohort (n = 203) were statistically significantly correlated with available ELISA data of Aβ1–40 (n = 158) and Aβ1–42 (n = 179) from a different laboratory. However, Bland-Altman method comparison indicated systematic differences between the assays. The data presented here furthermore indicate that the CSF concentration of Aβ40 can surrogate total CSF Aβ and support the hypothesis that the Aβ42/Aβ40 ratio outperforms CSF Aβ42 alone as a biomarker for Alzheimer’s disease due to a normalization to total Aβ levels."],["dc.identifier.doi","10.3233/jad-160398"],["dc.identifier.gro","3151666"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/8483"],["dc.language.iso","en"],["dc.notes.status","public"],["dc.notes.submitter","chake"],["dc.relation.issn","1387-2877"],["dc.title","Validation of a Commercial Chemiluminescence Immunoassay for the Simultaneous Measurement of Three Different Amyloid-β Peptides in Human Cerebrospinal Fluid and Application to a Clinical Cohort"],["dc.type","journal_article"],["dc.type.internalPublication","unknown"],["dc.type.peerReviewed","no"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.artnumber","80"],["dc.bibliographiccitation.issue","1"],["dc.bibliographiccitation.journal","Alzheimer's Research & Therapy"],["dc.bibliographiccitation.volume","9"],["dc.contributor.author","Wirths, Oliver"],["dc.contributor.author","Walter, Susanne"],["dc.contributor.author","Kraus, Inga"],["dc.contributor.author","Klafki, Hans W."],["dc.contributor.author","Stazi, Martina"],["dc.contributor.author","Oberstein, Timo J."],["dc.contributor.author","Ghiso, Jorge"],["dc.contributor.author","Wiltfang, Jens"],["dc.contributor.author","Bayer, Thomas A."],["dc.contributor.author","Weggen, Sascha"],["dc.date.accessioned","2020-12-10T18:39:07Z"],["dc.date.available","2020-12-10T18:39:07Z"],["dc.date.issued","2017"],["dc.description.abstract","Abstract Background The deposition of neurotoxic amyloid-β (Aβ) peptides in plaques in the brain parenchyma and in cerebral blood vessels is considered to be a key event in Alzheimer’s disease (AD) pathogenesis. Although the presence and impact of full-length Aβ peptides such as Aβ1–40 and Aβ1–42 have been analyzed extensively, the deposition of N-terminally truncated Aβ peptide species has received much less attention, largely because of the lack of specific antibodies. Methods This paper describes the generation and characterization of novel antibodies selective for Aβ4–x peptides and provides immunohistochemical evidence of Aβ4–x in the human brain and its distribution in the APP/PS1KI and 5XFAD transgenic mouse models. Results The Aβ4–x staining pattern was restricted mainly to amyloid plaque cores and cerebral amyloid angiopathy in AD and Down syndrome cases and in both AD mouse models. In contrast, diffuse amyloid deposits were largely negative for Aβ4–x immunoreactivity. No overt intraneuronal staining was observed. Conclusions The findings of this study are consistent with previous reports demonstrating a high aggregation propensity of Aβ4–x peptides and suggest an important role of these N-truncated Aβ species in the process of amyloidogenesis and plaque core formation."],["dc.identifier.doi","10.1186/s13195-017-0309-z"],["dc.identifier.eissn","1758-9193"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/15154"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/77547"],["dc.language.iso","en"],["dc.notes.intern","DOI Import GROB-354"],["dc.notes.intern","Merged from goescholar"],["dc.notes.intern","In goescholar not merged with http://resolver.sub.uni-goettingen.de/purl?gs-1/16990 but duplicate"],["dc.publisher","BioMed Central"],["dc.rights","CC BY 4.0"],["dc.rights.holder","The Author(s)."],["dc.rights.uri","https://creativecommons.org/licenses/by/4.0"],["dc.title","N-truncated Aβ4–x peptides in sporadic Alzheimer’s disease cases and transgenic Alzheimer mouse models"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","691"],["dc.bibliographiccitation.issue","2"],["dc.bibliographiccitation.journal","Journal of Alzheimer s Disease"],["dc.bibliographiccitation.lastpage","705"],["dc.bibliographiccitation.volume","54"],["dc.contributor.author","Klafki, Hans-W."],["dc.contributor.author","Hafermann, Henning"],["dc.contributor.author","Bauer, Christian R."],["dc.contributor.author","Haussmann, Ute"],["dc.contributor.author","Kraus, Inga"],["dc.contributor.author","Schuchhardt, Johannes"],["dc.contributor.author","Muck, Stephan"],["dc.contributor.author","Scherbaum, Norbert"],["dc.contributor.author","Wiltfang, Jens"],["dc.date.accessioned","2018-11-07T10:19:59Z"],["dc.date.available","2018-11-07T10:19:59Z"],["dc.date.issued","2016"],["dc.description.abstract","Acomprehensive assay validation campaign of a commercially available chemiluminescence multiplex immunoassay for the simultaneous measurement of the amyloid-beta peptides A beta(38), A beta(40), and A beta(42) in human cerebrospinal fluid (CSF) is presented. The assay quality parameters we addressed included impact of sample dilution, parallelism, lower limits of detection, lower limits of quantification, intra- and inter-assay repeatability, analytical spike recoveries, and between laboratory reproducibility of the measurements. The assay performed well in our hands and fulfilled a number of predefined acceptance criteria. The CSF levels of A beta(40) and A beta(42) determined in a clinical cohort (n = 203) were statistically significantly correlated with available ELISA data of A beta(1-40) (n = 158) and A beta(1-42) (n = 179) from a different laboratory. However, Bland-Altman method comparison indicated systematic differences between the assays. The data presented here furthermore indicate that the CSF concentration of A beta(40) can surrogate total CSF A beta and support the hypothesis that the A beta(42)/A beta(40) ratio outperforms CSF A beta(42) alone as a biomarker for Alzheimer's disease due to a normalization to total A beta levels."],["dc.identifier.doi","10.3233/JAD-160398"],["dc.identifier.isi","000384087200023"],["dc.identifier.pmid","27567847"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/41786"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Ios Press"],["dc.relation.issn","1875-8908"],["dc.relation.issn","1387-2877"],["dc.title","Validation of a Commercial Chemiluminescence Immunoassay for the Simultaneous Measurement of Three Different Amyloid-beta Peptides in Human Cerebrospinal Fluid and Application to a Clinical Cohort"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","1219"],["dc.bibliographiccitation.issue","10"],["dc.bibliographiccitation.journal","Structure"],["dc.bibliographiccitation.lastpage","1226"],["dc.bibliographiccitation.volume","11"],["dc.contributor.author","Rudolph, M."],["dc.contributor.author","Kraus, I."],["dc.contributor.author","Dickmanns, Achim"],["dc.contributor.author","Eickmann, M."],["dc.contributor.author","Garten, W."],["dc.contributor.author","Ficner, R."],["dc.date.accessioned","2017-09-07T11:44:16Z"],["dc.date.available","2017-09-07T11:44:16Z"],["dc.date.issued","2003"],["dc.description.abstract","Borna disease virus (BDV) causes an infection of the central nervous system in a wide range of vertebrates, which can fatally progress to an immune-mediated disease, called Borna disease. BDV is a member of the Mononegavirales, which also includes the highly infectious measles and Ebola viruses. The viral nucleo-proteins are central to transcription, replication, and packaging of the RNA genome. We present the X-ray structure of the BDV nucleoprotein determined at 1.76 Angstrom resolution. The structure reveals a novel fold, organized into two distinct domains, and an assembly into a planar homotetramer. Surface potential calculations strongly support an RNA binding model with the RNA wrapping around the outside of the tetramer, although a positively charged central channel in the tetramer could fit single-stranded RNA in an alternative binding mode. This first structure of an RNA virus nucleoprotein provides a paradigmatic model for RNA packaging and replication of single-stranded RNA viruses."],["dc.identifier.doi","10.1016/j.str.2003.08.011"],["dc.identifier.gro","3144057"],["dc.identifier.isi","000185758500009"],["dc.identifier.pmid","14527390"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/1639"],["dc.notes.intern","WoS Import 2017-03-10"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.relation.issn","0969-2126"],["dc.title","Crystal structure of the Borna disease virus nucleoprotein"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]