Escoll 2019 Immunometabolism: Difference between revisions
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{{Publication | {{Publication | ||
|title=Escoll P, Platon L, Buchrieser C ( | |title=Escoll P, Platon L, Buchrieser C (2019) Roles of mitochondrial respiratory Complexes during infection. Immunometabolism 1:e190011. https://doi.org/10.20900/immunometab20190011 | ||
|info=[ | |info=[https://journals.lww.com/immunometabolism/Abstract/2019/10000/Roles_of_Mitochondrial_Respiratory_Complexes.2.aspx Immunometabolism] | ||
|authors=Escoll P, Platon L, Buchrieser C | |authors=Escoll P, Platon L, Buchrieser C | ||
|year=2019 | |year=2019 | ||
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|editor=Gnaiger E | |editor=Gnaiger E | ||
}} | }} | ||
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{{Labeling | {{Labeling | ||
|enzymes=Complex II;succinate dehydrogenase | |enzymes=Complex II;succinate dehydrogenase | ||
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Latest revision as of 06:27, 2 May 2023
Escoll P, Platon L, Buchrieser C (2019) Roles of mitochondrial respiratory Complexes during infection. Immunometabolism 1:e190011. https://doi.org/10.20900/immunometab20190011 |
Escoll P, Platon L, Buchrieser C (2019) Immunometabolism
Abstract: Beyond oxidative phosphorylation (OXPHOS), mitochondria have also immune functions against infection, such as the regulation of cytokine production, the generation of metabolites with antimicrobial proprieties and the regulation of inflammasome-dependent cell death, which seem in turn to be regulated by the metabolic status of the organelle. Although OXPHOS is one of the main metabolic programs altered during infection, the mechanisms by which pathogens impact the mitochondrial electron transport chain (ETC) complexes to alter OXPHOS are not well understood. Similarly, how changes on ETC components affect infection is only starting to be characterized. Herein we summarize and discuss the existing data about the regulation of ETC complexes and super-complexes during infection, in order to shed some light on the mechanisms underlying the regulation of the mitochondrial OXPHOS machinery when intracellular pathogens infect eukaryotic host cells.
β’ Bioblast editor: Gnaiger E
Correction: FADH2 and Complex II
- FADH2 is shown as the substrate feeding electrons into Complex II (CII). This is wrong and requires correction - for details see Gnaiger (2024).
- Gnaiger E (2024) Complex II ambiguities β FADH2 in the electron transfer system. J Biol Chem 300:105470. https://doi.org/10.1016/j.jbc.2023.105470 - Β»Bioblast linkΒ«
Labels:
Enzyme: Complex II;succinate dehydrogenase