C
Christopher Horst Lillig
Researcher at University of Greifswald
Publications - 91
Citations - 6979
Christopher Horst Lillig is an academic researcher from University of Greifswald. The author has contributed to research in topics: Glutaredoxin & Thioredoxin. The author has an hindex of 40, co-authored 89 publications receiving 6329 citations. Previous affiliations of Christopher Horst Lillig include Harvard University & Greifswald University Hospital.
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Thioredoxin and related molecules--from biology to health and disease.
TL;DR: Thioredoxin and binding proteins appear to control apoptosis or metabolic states such as carbohydrate and lipid metabolism related to diseases such as diabetes and atherosclerosis and the fundamental differences between bacterial and mammalian thiOREDoxin reductases offer new principles for treatment of infections.
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Thioredoxins, glutaredoxins, and peroxiredoxins--molecular mechanisms and health significance: from cofactors to antioxidants to redox signaling.
Eva-Maria Hanschmann,José R. Godoy,Carsten Berndt,Christoph Hudemann,Christopher Horst Lillig +4 more
TL;DR: This review summarizes the almost 50 years of research on these proteins, focusing primarily on data from vertebrates and mammals, that is, their potential impact and functions in different cell types, tissues, and various pathological conditions.
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Thiol redox control via thioredoxin and glutaredoxin systems.
Arne Holmgren,Catrine Johansson,Carsten Berndt,Maria Lönn,Christoph Hudemann,Christopher Horst Lillig +5 more
TL;DR: The main part of this work focuses on the current knowledge about mitochondrial Grx2, which facilitates mitochondrial redox homoeostasis during oxidative stress-induced apoptosis.
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Thiol-based mechanisms of the thioredoxin and glutaredoxin systems: implications for diseases in the cardiovascular system
TL;DR: Cardioprotective effects of endogenous thioredoxin and glutaredoxin systems as well as the high potential in clinical applications of exogenously applied thiOREDoxin or glutaredoxins or the induction of endogenousThioredoxins and glutaringoxin systems are summarized.
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Human Mitochondrial Glutaredoxin Reduces S-Glutathionylated Proteins with High Affinity Accepting Electrons from Either Glutathione or Thioredoxin Reductase
TL;DR: Grx2 was a substrate for NADPH and thioredoxin reductase, which efficiently reduced both the active site disulfide and the GSH-glutaredoxin intermediate formed in the reduction of glutathionylated substrates, suggesting an important role for Grx2 in protection and recovery from oxidative stress.