K
Karin Sörgjerd
Researcher at Linköping University
Publications - 14
Citations - 885
Karin Sörgjerd is an academic researcher from Linköping University. The author has contributed to research in topics: Amyloid & Amyloid beta. The author has an hindex of 11, co-authored 14 publications receiving 787 citations. Previous affiliations of Karin Sörgjerd include RIKEN Brain Science Institute.
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Journal ArticleDOI
Detection and Characterization of Aggregates, Prefibrillar Amyloidogenic Oligomers, and Protofibrils Using Fluorescence Spectroscopy
TL;DR: A novel pathway for generation of prefibrillar aggregates of TTR is explored, which provides important insight into TTR misfolding and suggests that unbound ThT dramatically increases its fluorescence quantum yield when bound to amyloid fibrils; however, the mechanism behind this property is unknown.
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Lysozyme Amyloidogenesis Is Accelerated by Specific Nicking and Fragmentation but Decelerated by Intact Protein Binding and Conversion
TL;DR: A comprehensive kinetic mechanism is presented where all steps involving protein hydrolysis, fragmentation, assembly and conversion into amyloid fibrils are accounted for and it is shown that intact full-length lysozyme at the end of the lag phase slows the rate of amyloidsogenesis.
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Autophagy-related protein 7 deficiency in amyloid β (Aβ) precursor protein transgenic mice decreases Aβ in the multivesicular bodies and induces Aβ accumulation in the golgi
Per Nilsson,Per Nilsson,Misaki Sekiguchi,Takumi Akagi,Shin-ichi Izumi,Toshihisa Komori,Kelvin Hui,Karin Sörgjerd,Motomasa Tanaka,Takashi Saito,Nobuhisa Iwata,Takaomi C. Saido +11 more
TL;DR: Fluorescence and immunoelectron microscopy are used to elucidate the subcellular localization of the intracellular Aβ accumulation which accumulates in Aβ precursor protein mice lacking Atg7, which indicates that Atg 7 influences the transport of Aβ possibly derived from Golgi to multivesicular bodies.
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Prefibrillar transthyretin oligomers and cold stored native tetrameric transthyretin are cytotoxic in cell culture.
TL;DR: It is found that native tetrameric TTR, when purified and stored under cold conditions (4 degrees C) was highly cytotoxic, and the effect could be partially restored by increasing the temperature of the protein.
Journal ArticleDOI
Prefoldin Protects Neuronal Cells from Polyglutamine Toxicity by Preventing Aggregation Formation
Erika Tashiro,Tamotsu Zako,Hideki Muto,Yoshinori Itoo,Karin Sörgjerd,Naofumi Terada,Akira Abe,Makoto Miyazawa,Akira Kitamura,Hirotake Kitaura,Hiroshi Kubota,Mizuo Maeda,Takashi Momoi,Sanae M.M. Iguchi-Ariga,Masataka Kinjo,Hiroyoshi Ariga +15 more
TL;DR: In vitro single molecule observation demonstrated that prefoldin suppressed HTT aggregation at the small oligomer (dimer to tetramer) stage, and suggest that soluble oligomers of polyQ-expanded HTT are more toxic than are inclusion to cells.