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Kraus, Inga
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Kraus, Inga
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Kraus, Inga
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Kraus, I.
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2015Journal Article [["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"]]Details DOI2018Journal Article [["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"]]Details DOI PMID PMC2017Journal Article [["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"]]Details DOI