Christopher Horst Lillig mainly investigates Glutaredoxin, Biochemistry, Thioredoxin, Cell biology and Glutaredoxin 2. His research on Glutaredoxin frequently connects to adjacent areas such as Thioredoxin fold. His work is connected to Active site, Glutathione and Iron–sulfur cluster, as a part of Biochemistry.
Christopher Horst Lillig studied Thioredoxin and Reactive oxygen species that intersect with Signal transduction and Oxidative phosphorylation. In his study, Phenylarsine oxide is inextricably linked to Cytosol, which falls within the broad field of Cell biology. His Glutaredoxin 2 research is multidisciplinary, incorporating elements of Reductase, Molecular biology, Stereochemistry, Thioredoxin reductase and Sulfite.
His primary scientific interests are in Glutaredoxin, Biochemistry, Cell biology, Thioredoxin and Glutaredoxin 2. His biological study spans a wide range of topics, including Reductase, Cofactor, Thioredoxin fold, Active site and Iron–sulfur cluster. Biochemistry is closely attributed to Redox in his work.
His research in Cell biology focuses on subjects like Cytosol, which are connected to Cellular compartment and Cell. His work is dedicated to discovering how Thioredoxin, Protein disulfide-isomerase are connected with Isomerase and other disciplines. He focuses mostly in the field of Glutaredoxin 2, narrowing it down to topics relating to Molecular biology and, in certain cases, Sulfate assimilation.
His scientific interests lie mostly in Cell biology, Thioredoxin, Redox, Glutaredoxin and Oxidative stress. Christopher Horst Lillig interconnects Cancer cell, Receptor, Translation and Glutaredoxin 2 in the investigation of issues within Cell biology. The Thioredoxin study which covers Computational biology that intersects with Protein tertiary structure and Protein disulfide-isomerase.
As a part of the same scientific family, Christopher Horst Lillig mostly works in the field of Redox, focusing on Metabolism and, on occasion, Reductase. He merges many fields, such as Glutaredoxin and Renal damage, in his writings. His study on Reactive oxygen species is covered under Biochemistry.
His primary areas of investigation include Thioredoxin, Glutaredoxin, Oxidative stress, Biochemistry and Three-domain system. The Thioredoxin study combines topics in areas such as Paracrine signalling, Extracellular, Cell biology and Pancreatic islet function, Pancreatic islets. Christopher Horst Lillig has researched Glutaredoxin in several fields, including Plasma protein binding, Transferase, Oxidoreductase, Biophysics and Active site.
His Oxidative stress research incorporates elements of Reactive oxygen species, Pancreatic islet transplantation and Islet. His is doing research in Glutathione, Glutathione reductase, GPX1, Mitochondrial matrix and Thioredoxin reductase, both of which are found in Biochemistry. His Three-domain system research includes a combination of various areas of study, such as Protein tertiary structure, Similarity, Signal transduction, Protein–protein interaction and Computational biology.
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Thioredoxin and related molecules--from biology to health and disease.
Christopher Horst Lillig;Arne Holmgren.
Antioxidants & Redox Signaling (2007)
Thioredoxins, glutaredoxins, and peroxiredoxins--molecular mechanisms and health significance: from cofactors to antioxidants to redox signaling.
Eva-Maria Hanschmann;José Rodrigo Godoy;Carsten Berndt;Christoph Hudemann.
Antioxidants & Redox Signaling (2013)
Thiol redox control via thioredoxin and glutaredoxin systems.
A. Holmgren;C. Johansson;C. Berndt;M.E. Lönn.
Biochemical Society Transactions (2005)
Thiol-based mechanisms of the thioredoxin and glutaredoxin systems: implications for diseases in the cardiovascular system
Carsten Berndt;Christopher Horst Lillig;Arne Holmgren.
American Journal of Physiology-heart and Circulatory Physiology (2007)
Human Mitochondrial Glutaredoxin Reduces S-Glutathionylated Proteins with High Affinity Accepting Electrons from Either Glutathione or Thioredoxin Reductase
Catrine Johansson;Christopher Horst Lillig;Arne Holmgren.
Journal of Biological Chemistry (2004)
Characterization of human glutaredoxin 2 as iron–sulfur protein: A possible role as redox sensor
Christopher Horst Lillig;Carsten Berndt;Olivia Vergnolle;Maria Elisabet Lönn.
Proceedings of the National Academy of Sciences of the United States of America (2005)
Thioredoxins and glutaredoxins as facilitators of protein folding.
Carsten Berndt;Christopher Horst Lillig;Christopher Horst Lillig;Arne Holmgren.
Biochimica et Biophysica Acta (2008)
Cytosolic monothiol glutaredoxins function in intracellular iron sensing and trafficking via their bound iron-sulfur cluster
Ulrich Mühlenhoff;Sabine Molik;José R. Godoy;Marta A. Uzarska.
Cell Metabolism (2010)
Linkage of inflammation and oxidative stress via release of glutathionylated peroxiredoxin-2, which acts as a danger signal
Sonia Salzano;Paola Checconi;Paola Checconi;Eva-Maria Hanschmann;Christopher Horst Lillig.
Proceedings of the National Academy of Sciences of the United States of America (2014)
Overexpression of glutaredoxin 2 attenuates apoptosis by preventing cytochrome c release.
Mari Enoksson;Aristi Potamitou Fernandes;Stefanie Prast;Christopher Horst Lillig.
Biochemical and Biophysical Research Communications (2005)
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