A. Holmgren

Publications426
h-index106
Citations37,544
Highly Influential Citations1,306
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From selenium to selenoproteins: synthesis, identity, and their role in human health.
TLDR
The function of most selenoproteins is currently unknown; however, thioredoxin reductases, glutathione peroxidases and thyroid hormone deiodinases are well characterised selenobroteins involved in redox regulation of intracellular signalling, redox homeostasis and thyroid hormones metabolism. Expand
Thioredoxin catalyzes the reduction of insulin disulfides by dithiothreitol and dihydrolipoamide.
  • A. Holmgren
  • Chemistry, Medicine
  • The Journal of biological chemistry
  • 10 October 1979
TLDR
The fast spontaneous reaction between dihydrolipoamide and thioredoxin-S2 provides a mechanism for NADH or pyruvate-dependent disulfides reduction and the implication of the dithiol-disulfide oxidoreductase activity of thiOREDoxin for the regulation of enzyme activities by thiol oxidation-reduction control is discussed. Expand
The thioredoxin antioxidant system.
  • J. Lu, A. Holmgren
  • Biology, Medicine
  • Free radical biology & medicine
  • 8 January 2014
TLDR
The absence of a GSH-Grx system in some pathogenic bacteria such as Helicobacter pylori, Mycobacterium tuberculosis, and Staphylococcus aureus makes the bacterial Trx system essential for survival under oxidative stress, and provides an opportunity to kill these bacteria by targeting the TrxR-Trx system. Expand
Glutaredoxins: glutathione-dependent redox enzymes with functions far beyond a simple thioredoxin backup system.
TLDR
Glutaredoxins uniquely reduce mixed disulfides with glutathione via a monothiol mechanism where only an N-terminal low pKa Cys residue is required, by using their glutathionylation site. Expand
Thioredoxin and thioredoxin reductase.
The Role of the Thioredoxin and Glutaredoxin Pathways in Reducing Protein Disulfide Bonds in the Escherichia coliCytoplasm*
TLDR
E. coli requires either a functional thioredoxin or glutaredoxin system to reduce disulfide bonds which appear after each catalytic cycle in the essential enzyme ribonucleotide reductase and perhaps to reduce non-native disulfides in cytoplasmic proteins. Expand
The thioredoxin system in cancer.
TLDR
Current data suggest that high expression of Trx and TrxR may induce apoptosis and reduce the mitotic index of certain tumors linked to the p53 dependent cell death. Expand
Thioredoxin and related molecules--from biology to health and disease.
TLDR
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. Expand
Redox Potentials of Glutaredoxins and Other Thiol-Disulfide Oxidoreductases of the Thioredoxin Superfamily Determined by Direct Protein-Protein Redox Equilibria*
TLDR
Determining redox potentials through direct protein-protein equilibria is of general interest as it overcomes errors in determining redox possibles calculated from large equilibrium constants with the strongly reducing NADPH or by accumulating mixed disulfides with GSH. Expand
Identification of S-glutathionylated cellular proteins during oxidative stress and constitutive metabolism by affinity purification and proteomic analysis.
TLDR
The ability to chemically tag, select, and identify S-glutathionylated proteins, particularly during constitutive metabolism, will greatly enhance efforts to establish posttranslational redox modification of cellular proteins as an important biochemical control mechanism in coordinating cellular function. Expand
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