| |  Online-Ressource |
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| Verfasst von: | Morgenstern, Jakob [VerfasserIn]  |
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| | Katz, Sylvia [VerfasserIn] |
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| | Krebs-Haupenthal, Jutta [VerfasserIn] |
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| | Chen, Jessy [VerfasserIn] |
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| | Saadatmand, Ali R. [VerfasserIn] |
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| | Garcia Cortizo, Fabiola [VerfasserIn] |
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| | Zemva, Johanna [VerfasserIn] |
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| | Campos Campos, Marta [VerfasserIn] |
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| | Teleman, Aurelio A. [VerfasserIn] |
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| | Backs, Johannes [VerfasserIn] |
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| | Nawroth, Peter Paul [VerfasserIn] |
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| | Fleming, Thomas [VerfasserIn] |
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| Titel: | Phosphorylation of T107 by CamKII[delta] regulates the detoxification efficiency and proteomic integrity of glyoxalase 1 |
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| Verf.angabe: | Jakob Morgenstern, Sylvia Katz, Jutta Krebs-Haupenthal, Jessy Chen, Alireza Saadatmand, Fabiola Garcia Cortizo, Alexandra Moraru, Johanna Zemva, Marta Campos Campos, Aurelio Teleman, Johannes Backs, Peter Nawroth, and Thomas Fleming |
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| E-Jahr: | 2020 |
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| Jahr: | September 22, 2020 |
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| Umfang: | 14 S. |
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| Fussnoten: | Im Titel wird delta als griechischer Buchstabe dargestellt ; Gesehen am 03.11.2020 |
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| Titel Quelle: | Enthalten in: Cell reports |
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| Ort Quelle: | Maryland Heights, MO : Cell Press, 2012 |
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| Jahr Quelle: | 2020 |
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| Band/Heft Quelle: | 32(2020,12) Artikel-Nummer 108160, 14 Seiten |
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| ISSN Quelle: | 2211-1247 |
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| Abstract: | The glyoxalase system is a highly conserved and ubiquitously expressed enzyme system, which is responsible for the detoxification of methylglyoxal (MG), a spontaneous by-product of energy metabolism. This study is able to show that a phosphorylation of threonine-107 (T107) in the (rate-limiting) Glyoxalase 1 (Glo1) protein, mediated by Ca2+/calmodulin-dependent kinase II delta (CamKIIδ), is associated with elevated catalytic efficiency of Glo1 (lower KM; higher Vmax). Additionally, we observe proteasomal degradation of non-phosphorylated Glo1 via ubiquitination does occur more rapidly as compared with native Glo1. The absence of CamKIIδ is associated with poor detoxification capacity and decreased protein content of Glo1 in a murine CamKIIδ knockout model. Therefore, phosphorylation of T107 in the Glo1 protein by CamKIIδ is a quick and precise mechanism regulating Glo1 activity, which is experimentally linked to an altered Glo1 status in cancer, diabetes, and during aging. |
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| DOI: | doi:10.1016/j.celrep.2020.108160 |
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| URL: | Bitte beachten Sie: Dies ist ein Bibliographieeintrag. Ein Volltextzugriff für Mitglieder der Universität besteht hier nur, falls für die entsprechende Zeitschrift/den entsprechenden Sammelband ein Abonnement besteht oder es sich um einen OpenAccess-Titel handelt.
Volltext ; Verlag: https://doi.org/10.1016/j.celrep.2020.108160 |
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| | Volltext: http://www.sciencedirect.com/science/article/pii/S2211124720311499 |
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| | DOI: https://doi.org/10.1016/j.celrep.2020.108160 |
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| Datenträger: | Online-Ressource |
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| Sprache: | eng |
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| Sach-SW: | aging |
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| | Ca/calmodulin-dependent kinase |
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| | cancer |
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| | cellular biochemistry |
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| | diabetes |
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| | glyoxalase system |
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| | methylglyoxal |
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| | Michaelis-Menten kinetics |
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| | phosphorylation |
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| | post-translational modifications |
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| K10plus-PPN: | 1737628457 |
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| Verknüpfungen: | → Zeitschrift |
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Phosphorylation of T107 by CamKII[delta] regulates the detoxification efficiency and proteomic integrity of glyoxalase 1 / Morgenstern, Jakob [VerfasserIn]; September 22, 2020 (Online-Ressource)
