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Elias S.J. Arnér

Elias S.J. Arnér

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Biology and Biochemistry
Sweden
2023

D-Index & Metrics

Biology and Biochemistry

D-Index
77
Citations
28056
World Ranking
4700
National Ranking
70

Research.com Recognitions

  • 2023 - Research.com Biology and Biochemistry in Sweden Leader Award

Overview

Elias S.J. Arnér is affiliated with the Karolinska Institute in Sweden and has a research focus primarily within biochemistry, genetics, and molecular biology. Their work spans multiple interconnected subfields including molecular biology, nutrition and dietetics, organic chemistry, materials chemistry, and immunology.

Their research topics frequently cover areas such as redox biology and oxidative stress, selenium in biological systems, glutathione transferases and polymorphisms, sulfur compounds in biology, genomics, phytochemicals, and oxidative stress, organoselenium and organotellurium chemistry, and trace elements in health.

Among their recent scholarly papers are the following:

  • The ferroptosis inducing compounds RSL3 and ML162 are not direct inhibitors of GPX4 but of TXNRD1 (2023, Redox Biology)
  • Control of protein function through oxidation and reduction of persulfidated states (2020, Science Advances)
  • Thioredoxin Reductase Inhibition for Cancer Therapy (2021, The Annual Review of Pharmacology and Toxicology)
  • Comprehensive chemical proteomics for target deconvolution of the redox active drug auranofin (2020, Redox Biology)
  • System-wide identification and prioritization of enzyme substrates by thermal analysis (2021, Nature Communications)

Arnér's collaborative network includes frequent co-authors such as Qing Cheng, Karoline Scholzen, Radosveta Gencheva, Lukas Zeisel, and Oliver Thorn-Seshold, with collaboration counts ranging from 13 to 33 publications each.

The scientist's work has been published extensively in several venues, with the highest number of publications appearing in Free Radical Biology and Medicine, Redox Biology, SSRN Electronic Journal, The Cambridge Structural Database, and bioRxiv (Cold Spring Harbor Laboratory).

Best Publications

  • Reactive oxygen species, antioxidants, and the mammalian thioredoxin system.

    Jonas Nordberg;Elias S.J. Arnér

  • Physiological functions of thioredoxin and thioredoxin reductase.

    Elias S. J. Arnér;Arne Holmgren

  • Selenium Utilization by GPX4 Is Required to Prevent Hydroperoxide-Induced Ferroptosis

    Irina Ingold;Carsten Berndt;Sabine Schmitt;Sebastian Doll

  • Mammalian Deoxyribonucleoside Kinases

    Elias S.J. Arnér;Staffan Eriksson

  • Focus on mammalian thioredoxin reductases — Important selenoproteins with versatile functions

    Elias S.J. Arnér

  • The thioredoxin system in cancer.

    Elias S.J. Arnér;Arne Holmgren

  • Structure and mechanism of mammalian thioredoxin reductase: The active site is a redox-active selenolthiol/selenenylsulfide formed from the conserved cysteine-selenocysteine sequence

    Liangwei Zhong;Elias S. J. Arnér;Arne Holmgren

  • Selenocysteine in proteins : Properties and biotechnological use

    Linda Johansson;Guro Gafvelin;Elias S.J. Arnér

  • Thioredoxin Glutathione Reductase from Schistosoma mansoni: An Essential Parasite Enzyme and a Key Drug Target

    Angela N Kuntz;Elisabeth Davioud-Charvet;Elisabeth Davioud-Charvet;Ahmed A Sayed;Lindsay L Califf

  • Paradoxical Roles of Antioxidant Enzymes: Basic Mechanisms and Health Implications

    Xin Gen Lei;Jian Hong Zhu;Wen Hsing Cheng;Yongping Bao

  • Preparation and assay of mammalian thioredoxin and thioredoxin reductase.

    Elias S.J. Arnér;Liangwei Zhong;Arne Holmgren

  • Rat and Calf Thioredoxin Reductase Are Homologous to Glutathione Reductase with a Carboxyl-terminal Elongation Containing a Conserved Catalytically Active Penultimate Selenocysteine Residue

    Liangwei Zhong;Elias S. J. Arnér;Johanna Ljung;Fredrik Åslund

  • Selenoproteins—What unique properties can arise with selenocysteine in place of cysteine?

    Elias S.J. Arnér

  • High-level expression in Escherichia coli of selenocysteine-containing rat thioredoxin reductase utilizing gene fusions with engineered bacterial-type SECIS elements and co-expression with the selA, selB and selC genes.

    Elias S.J Arnér;Hakan Sarioglu;Friedrich Lottspeich;Arne Holmgren

  • A novel persulfide detection method reveals protein persulfide- and polysulfide-reducing functions of thioredoxin and glutathione systems.

    Éva Dóka;Irina Pader;Adrienn Bíró;Katarina Johansson

  • The mammalian cytosolic selenoenzyme thioredoxin reductase reduces ubiquinone. A novel mechanism for defense against oxidative stress.

    Ling Xia;Tomas Nordman;Jerker M. Olsson;Anastassios Damdimopoulos

  • 1-Chloro-2,4-dinitrobenzene Is an Irreversible Inhibitor of Human Thioredoxin Reductase LOSS OF THIOREDOXIN DISULFIDE REDUCTASE ACTIVITY IS ACCOMPANIED BY A LARGE INCREASE IN NADPH OXIDASE ACTIVITY

    Elias S.J. Arnér;Mikael Björnstedt;Arne Holmgren

  • Selenoprotein Gene Nomenclature

    Vadim N. Gladyshev;Vadim N. Gladyshev;Elias S. Arnér;Marla J. Berry;Regina Brigelius-Flohé

  • Crystal Structure and Catalysis of the Selenoprotein Thioredoxin Reductase 1

    Qing Cheng;Tatyana Sandalova;Ylva Lindqvist;Elias S. J. Arnér

  • Analysis of the inhibition of mammalian thioredoxin, thioredoxin reductase, and glutaredoxin by cis-diamminedichloroplatinum (II) and its major metabolite, the glutathione-platinum complex.

    Elias S.J. Arnér;Hajime Nakamura;Tetsuro Sasada;Junji Yodoi

Frequent Co-Authors

Arne Holmgren
Arne Holmgren Karolinska Institute
Stig Linder
Stig Linder Linköping University
Roman A. Zubarev
Roman A. Zubarev Karolinska Institute
Mark B. Hampton
Mark B. Hampton University of Otago
Antonio Miranda-Vizuete
Antonio Miranda-Vizuete Spanish National Research Council
Galina Selivanova
Galina Selivanova Karolinska Institute
Marcus Conrad
Marcus Conrad Helmholtz Zentrum München
Anton Simeonov
Anton Simeonov National Institutes of Health
Giannis Spyrou
Giannis Spyrou Linköping University
Ajit Jadhav
Ajit Jadhav Pfizer (Germany)

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