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Kruss, Sebastian
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Kruss, Sebastian
Official Name
Kruss, Sebastian
Alternative Name
Kruss, S.
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2021Journal Article [["dc.bibliographiccitation.journal","Molecular Neurobiology"],["dc.contributor.author","Noor, Aneeqa"],["dc.contributor.author","Zafar, Saima"],["dc.contributor.author","Shafiq, Mohsin"],["dc.contributor.author","Younas, Neelam"],["dc.contributor.author","Siegert, Anna"],["dc.contributor.author","Mann, Florian A."],["dc.contributor.author","Kruss, Sebastian"],["dc.contributor.author","Schmitz, Matthias"],["dc.contributor.author","Dihazi, Hassan"],["dc.contributor.author","Ferrer, Isidre"],["dc.contributor.author","Zerr, Inga"],["dc.date.accessioned","2021-12-01T09:23:29Z"],["dc.date.available","2021-12-01T09:23:29Z"],["dc.date.issued","2021"],["dc.description.abstract","Abstract The molecular determinants of atypical clinical variants of Alzheimer’s disease, including the recently discovered rapidly progressive Alzheimer’s disease (rpAD), are unknown to date. Fibrilization of the amyloid-β (Aβ) peptide is the most frequently studied candidate in this context. The Aβ peptide can exist as multiple proteoforms that vary in their post-translational processing, amyloidogenesis, and toxicity. The current study was designed to identify these variations in Alzheimer’s disease patients exhibiting classical (sAD) and rapid progression, with the primary aim of establishing if these variants may constitute strains that underlie the phenotypic variability of Alzheimer’s disease. We employed two-dimensional polyacrylamide gel electrophoresis and MALDI-ToF mass spectrometry to validate and identify the Aβ proteoforms extracted from targeted brain tissues. The biophysical analysis was conducted using RT-QuIC assay, confocal microscopy, and atomic force microscopy. Interactome analysis was performed by co-immunoprecipitation. We present a signature of 33 distinct pathophysiological proteoforms, including the commonly targeted Aβ 40 , Aβ 42 , Aβ 4-42 , Aβ 11-42 , and provide insight into their synthesis and quantities. Furthermore, we have validated the presence of highly hydrophobic Aβ seeds in rpAD brains that seeded reactions at a slower pace in comparison to typical Alzheimer’s disease. In vitro and in vivo analyses also verified variations in the molecular pathways modulated by brain-derived Aβ. These variations in the presence, synthesis, folding, and interactions of Aβ among sAD and rpAD brains constitute important points of intervention. Further validation of reported targets and mechanisms will aid in the diagnosis of and therapy for Alzheimer’s disease."],["dc.description.abstract","Abstract The molecular determinants of atypical clinical variants of Alzheimer’s disease, including the recently discovered rapidly progressive Alzheimer’s disease (rpAD), are unknown to date. Fibrilization of the amyloid-β (Aβ) peptide is the most frequently studied candidate in this context. The Aβ peptide can exist as multiple proteoforms that vary in their post-translational processing, amyloidogenesis, and toxicity. The current study was designed to identify these variations in Alzheimer’s disease patients exhibiting classical (sAD) and rapid progression, with the primary aim of establishing if these variants may constitute strains that underlie the phenotypic variability of Alzheimer’s disease. We employed two-dimensional polyacrylamide gel electrophoresis and MALDI-ToF mass spectrometry to validate and identify the Aβ proteoforms extracted from targeted brain tissues. The biophysical analysis was conducted using RT-QuIC assay, confocal microscopy, and atomic force microscopy. Interactome analysis was performed by co-immunoprecipitation. We present a signature of 33 distinct pathophysiological proteoforms, including the commonly targeted Aβ 40 , Aβ 42 , Aβ 4-42 , Aβ 11-42 , and provide insight into their synthesis and quantities. Furthermore, we have validated the presence of highly hydrophobic Aβ seeds in rpAD brains that seeded reactions at a slower pace in comparison to typical Alzheimer’s disease. In vitro and in vivo analyses also verified variations in the molecular pathways modulated by brain-derived Aβ. These variations in the presence, synthesis, folding, and interactions of Aβ among sAD and rpAD brains constitute important points of intervention. Further validation of reported targets and mechanisms will aid in the diagnosis of and therapy for Alzheimer’s disease."],["dc.identifier.doi","10.1007/s12035-021-02566-9"],["dc.identifier.pii","2566"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/94665"],["dc.language.iso","en"],["dc.notes.intern","DOI-Import GROB-478"],["dc.relation.eissn","1559-1182"],["dc.relation.issn","0893-7648"],["dc.title","Molecular Profiles of Amyloid-β Proteoforms in Typical and Rapidly Progressive Alzheimer’s Disease"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dspace.entity.type","Publication"]]Details DOI2021Journal Article [["dc.bibliographiccitation.firstpage","18341"],["dc.bibliographiccitation.issue","33"],["dc.bibliographiccitation.journal","The Journal of Physical Chemistry C"],["dc.bibliographiccitation.lastpage","18351"],["dc.bibliographiccitation.volume","125"],["dc.contributor.author","Spreinat, Alexander"],["dc.contributor.author","Dohmen, Maria M."],["dc.contributor.author","Lüttgens, Jan"],["dc.contributor.author","Herrmann, Niklas"],["dc.contributor.author","Klepzig, Lars F."],["dc.contributor.author","Nißler, Robert"],["dc.contributor.author","Weber, Sabrina"],["dc.contributor.author","Mann, Florian A."],["dc.contributor.author","Lauth, Jannika"],["dc.contributor.author","Kruss, Sebastian"],["dc.date.accessioned","2021-10-01T09:57:41Z"],["dc.date.available","2021-10-01T09:57:41Z"],["dc.date.issued","2021"],["dc.identifier.doi","10.1021/acs.jpcc.1c05432"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/89894"],["dc.language.iso","en"],["dc.notes.intern","DOI Import GROB-469"],["dc.relation.eissn","1932-7455"],["dc.relation.issn","1932-7447"],["dc.title","Quantum Defects in Fluorescent Carbon Nanotubes for Sensing and Mechanistic Studies"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dspace.entity.type","Publication"]]Details DOI2019Preprint [["dc.contributor.author","Selvaggio, Gabriele"],["dc.contributor.author","Preiß, Helen"],["dc.contributor.author","Chizhik, Alexey"],["dc.contributor.author","Nißler, Robert"],["dc.contributor.author","Mann, Florian A."],["dc.contributor.author","Lv, Zhiyi"],["dc.contributor.author","Oswald, Tabea A."],["dc.contributor.author","Spreinat, Alexander"],["dc.contributor.author","Erpenbeck, Luise"],["dc.contributor.author","Großhans, Jörg"],["dc.contributor.author","Giraldo, Juan Pablo"],["dc.contributor.author","Kruss, Sebastian"],["dc.date.accessioned","2020-11-05T15:08:07Z"],["dc.date.available","2020-11-05T15:08:07Z"],["dc.date.issued","2019"],["dc.identifier.doi","10.1101/710384"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/68469"],["dc.notes.intern","DOI Import GROB-352.7"],["dc.title","Exfoliated near infrared fluorescent CaCuSi 4 O 10 nanosheets with ultra-high photostability and brightness for biological imaging"],["dc.type","preprint"],["dc.type.internalPublication","unknown"],["dspace.entity.type","Publication"]]Details DOI2022Journal Article [["dc.bibliographiccitation.firstpage","727"],["dc.bibliographiccitation.issue","3"],["dc.bibliographiccitation.journal","Nature Protocols"],["dc.bibliographiccitation.lastpage","747"],["dc.bibliographiccitation.volume","17"],["dc.contributor.author","Mann, Florian A."],["dc.contributor.author","Galonska, Phillip"],["dc.contributor.author","Herrmann, Niklas"],["dc.contributor.author","Kruss, Sebastian"],["dc.date.accessioned","2022-04-01T10:02:39Z"],["dc.date.available","2022-04-01T10:02:39Z"],["dc.date.issued","2022"],["dc.identifier.doi","10.1038/s41596-021-00663-6"],["dc.identifier.pii","663"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/105973"],["dc.language.iso","en"],["dc.notes.intern","DOI-Import GROB-530"],["dc.relation.eissn","1750-2799"],["dc.relation.issn","1754-2189"],["dc.rights.uri","https://www.springer.com/tdm"],["dc.title","Quantum defects as versatile anchors for carbon nanotube functionalization"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dspace.entity.type","Publication"]]Details DOI2019Journal Article [["dc.bibliographiccitation.firstpage","11469"],["dc.bibliographiccitation.issue","33"],["dc.bibliographiccitation.journal","Angewandte Chemie International Edition"],["dc.bibliographiccitation.lastpage","11473"],["dc.bibliographiccitation.volume","58"],["dc.contributor.author","Mann, Florian A."],["dc.contributor.author","Lv, Zhiyi"],["dc.contributor.author","Großhans, Jörg"],["dc.contributor.author","Opazo, Felipe"],["dc.contributor.author","Kruss, Sebastian"],["dc.date.accessioned","2020-12-10T14:05:38Z"],["dc.date.available","2020-12-10T14:05:38Z"],["dc.date.issued","2019"],["dc.identifier.doi","10.1002/anie.v58.33"],["dc.identifier.eissn","1521-3773"],["dc.identifier.issn","1433-7851"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/69599"],["dc.language.iso","en"],["dc.notes.intern","DOI Import GROB-354"],["dc.title","Nanobody‐Conjugated Nanotubes for Targeted Near‐Infrared In Vivo Imaging and Sensing"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dspace.entity.type","Publication"]]Details DOI