E
Elias S.J. Arnér
Researcher at Karolinska Institutet
Publications - 208
Citations - 18978
Elias S.J. Arnér is an academic researcher from Karolinska Institutet. The author has contributed to research in topics: Thioredoxin reductase & Thioredoxin. The author has an hindex of 58, co-authored 192 publications receiving 16579 citations. Previous affiliations of Elias S.J. Arnér include City University of New York.
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Journal ArticleDOI
Inhibition of thioredoxin reductase but not of glutathione reductase by the major classes of alkylating and platinum-containing anticancer compounds.
TL;DR: Representative compounds of the major classes of clinically used anticancer alkylating agents and most platinum compounds may easily target TrxR, but not GR, which should be considered as a factor that may contribute to the cytotoxicity seen upon clinical use of these drugs.
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Mammalian Thioredoxin Reductase Is Irreversibly Inhibited by Dinitrohalobenzenes by Alkylation of Both the Redox Active Selenocysteine and Its Neighboring Cysteine Residue
TL;DR: A model for the interaction between TrxR and dinitrohalobenzenes is proposed, involving a functional FAD in the alkylated TrXR generating an anion nitroradical in a dinitrophenyl group, which in turn reacts with oxygen to generate superoxide.
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Active sites of thioredoxin reductases: Why selenoproteins?
Stephan Gromer,Linda Johansson,Holger Bauer,L. David Arscott,Susanne Rauch,David P. Ballou,Charles H. Williams,R. Heiner Schirmer,Elias S.J. Arnér +8 more
TL;DR: It is shown that the serine residues flanking the C-terminal Cys residues of Drosophila TrxRs are responsible for activating the cysteines to match the catalytic efficiency of a selenocysteine-cysteine pair as in mammalian TrxR, obviating the need for selenium.
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Efficient Reduction of Lipoamide and Lipoic Acid by Mammalian Thioredoxin Reductase
TL;DR: It is found that thioredoxin reductase from calf thymus, calf liver, human placenta, and rat liver efficiently reduced both lipoic acid and lipoamide with Michaelis-Menten type kinetics in NADPH-dependent reactions.
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ROS-dependent activation of JNK converts p53 into an efficient inhibitor of oncogenes leading to robust apoptosis
Yao Shi,Fedor Nikulenkov,Joanna Zawacka-Pankau,H Li,Razif Gabdoulline,Jianqiang Xu,Sofi E. Eriksson,Elisabeth Hedström,Natalia Issaeva,Alexander E. Kel,Elias S.J. Arnér,Galina Selivanova +11 more
TL;DR: This study reports that concurrent pharmacological activation of p53 and inhibition of thioredoxin reductase followed by generation of reactive oxygen species (ROS), result in the synthetic lethality in cancer cells and provides novel insights for manipulating p53 response in a controlled way.