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Elias S.J. Arnér

Researcher Next ID · RN-028647

Researcher · Biochemistry, Genetics and Molecular Biology

Karolinska Institutet

Stockholm, Hungary

Not currently recruitingFunding unknown
Works count
299
Citation count
24,054
H-index
73
i10-index
180

Research interests

Biochemistry, Genetics and Molecular Biology
Nursing
Redox biology and oxidative stress
Selenium in Biological Systems
Glutathione Transferases and Polymorphisms
Sulfur Compounds in Biology
Trace Elements in Health

Publications

  • The ferroptosis inducing compounds RSL3 and ML162 are not direct inhibitors of GPX4 but of TXNRD1

    Redox Biology · 2023 · 10.1016/j.redox.2023.102703

  • Control of protein function through oxidation and reduction of persulfidated states

    Science Advances · 2020 · 10.1126/sciadv.aax8358

  • Irreversible inhibition of cytosolic thioredoxin reductase 1 as a mechanistic basis for anticancer therapy

    Science Translational Medicine · 2018 · 10.1126/scitranslmed.aaf7444

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

    Cell · 2017 · https://doi.org/10.1016/j.cell.2017.11.048

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

    Science Advances · 2016 · 10.1126/sciadv.1500968

  • Selenoprotein Gene Nomenclature

    Journal of Biological Chemistry · 2016 · 10.1074/jbc.m116.756155

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

    Physiological Reviews · 2015 · 10.1152/physrev.00010.2014

  • TrxR1 as a Potent Regulator of the Nrf2-Keap1 Response System

    Antioxidants and Redox Signaling · 2015 · 10.1089/ars.2015.6378

  • ROS-dependent activation of JNK converts p53 into an efficient inhibitor of oncogenes leading to robust apoptosis

    Cell Death and Differentiation · 2014 · 10.1038/cdd.2013.186

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

    Experimental Cell Research · 2010 · 10.1016/j.yexcr.2010.02.032

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

    Biochimica et Biophysica Acta (BBA) - General Subjects · 2009 · https://doi.org/10.1016/j.bbagen.2009.01.014

  • Crystal Structure and Catalysis of the Selenoprotein Thioredoxin Reductase 1

    Journal of Biological Chemistry · 2008 · 10.1074/jbc.m807068200

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

    PLoS Medicine · 2007 · 10.1371/journal.pmed.0040206

  • The thioredoxin system in cancer

    Seminars in Cancer Biology · 2006 · https://doi.org/10.1016/j.semcancer.2006.10.009

  • Selenocysteine in proteins—properties and biotechnological use

    Biochimica et Biophysica Acta (BBA) - General Subjects · 2005 · 10.1016/j.bbagen.2005.05.010

  • Inhibition of thioredoxin reductase but not of glutathione reductase by the major classes of alkylating and platinum-containing anticancer compounds

    Free Radical Biology and Medicine · 2005 · 10.1016/j.freeradbiomed.2005.04.025

  • Active sites of thioredoxin reductases: Why selenoproteins?

    Proceedings of the National Academy of Sciences · 2003 · 10.1073/pnas.2134510100

  • The Mammalian Cytosolic Selenoenzyme Thioredoxin Reductase Reduces Ubiquinone

    Journal of Biological Chemistry · 2003 · 10.1074/jbc.m210456200

  • Reactive oxygen species, antioxidants, and the mammalian thioredoxin system1 1This review is based on the licentiate thesis “Thioredoxin reductase—interactions with the redox active compounds 1-chloro-2,4-dinitrobenzene and lipoic acid” by Jonas Nordberg, 2001, Karolinska Institute, Stockholm, ISBN 91-631-1064-4.

    Free Radical Biology and Medicine · 2001 · https://doi.org/10.1016/s0891-5849(01)00724-9

  • Physiological functions of thioredoxin and thioredoxin reductase

    European Journal of Biochemistry · 2000 · https://doi.org/10.1046/j.1432-1327.2000.01701.x

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

    Proceedings of the National Academy of Sciences · 2000 · 10.1073/pnas.100114897

  • 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 1 1Edited by M. Gottesman

    Journal of Molecular Biology · 1999 · 10.1006/jmbi.1999.3085

  • Preparation and assay of mammalian thioredoxin and thioredoxin reductase

    Methods in enzymology on CD-ROM/Methods in enzymology · 1999 · 10.1016/s0076-6879(99)00129-9

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

    Journal of Biological Chemistry · 1998 · 10.1074/jbc.273.15.8581

  • Mammalian deoxyribonucleoside kinases

    Pharmacology & Therapeutics · 1995 · 10.1016/0163-7258(95)00015-9

Current projects

    No projects listed.