Evidence map›Paper›PMID 32651396›Full record

ArticleNature communications2020

Molecular basis for the distinct functions of redox-active and FeS-transfering glutaredoxins.

Daniel Trnka, Anna D Engelke, Manuela Gellert, Anna Moseler, Md Faruq Hossain, Tobias T Lindenberg, Luca Pedroletti, Benjamin Odermatt, João V de Souza, Agnieszka K Bronowska and 5 more

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.

0numbers the graph read from it
0cells of the map it votes in
34citing papers in PubMed
5.0field-weighted citation impact, top 4% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

34 citing papers in PubMed, 82 citations in OpenAlex.

  1. Disulphide maintenance systems and proteostasis.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2026
    Review
  2. Emerging roles of glutaredoxins in plant metabolism.Journal of experimental botany · 2026
    Review
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

15 authors at 6 institutions in 3 countries.

Daniel Trnka *Institute for Medical Biochemistry and Molecular Biology, University Medicine, University of Greifswald, Greifswald, Germany.ORCID http://orcid.org/0000-0002-6609-6880
Anna D Engelke *Department of Neurology, Medical Faculty, Heinrich-Heine University Düsseldorf, Düsseldorf, Germany.
Manuela Gellert *Institute for Medical Biochemistry and Molecular Biology, University Medicine, University of Greifswald, Greifswald, Germany.ORCID http://orcid.org/0000-0002-2545-7125
Anna MoselerInstitute of Crop Science and Resource Conservation, University of Bonn, Bonn, Germany.ORCID http://orcid.org/0000-0003-4641-8093
Md Faruq HossainInstitute for Medical Biochemistry and Molecular Biology, University Medicine, University of Greifswald, Greifswald, Germany.ORCID http://orcid.org/0000-0002-8346-063X
Tobias T LindenbergInstitute of Neuroanatomy, University Clinics, University of Bonn, Bonn, Germany.
Luca PedrolettiInstitute of Crop Science and Resource Conservation, University of Bonn, Bonn, Germany.
Benjamin OdermattInstitute of Neuroanatomy, University Clinics, University of Bonn, Bonn, Germany.ORCID http://orcid.org/0000-0002-9361-2772
João V de SouzaChemistry, School of Natural and Environmental Sciences, Newcastle University, Newcastle, NE1 7RU, UK.
Agnieszka K BronowskaChemistry, School of Natural and Environmental Sciences, Newcastle University, Newcastle, NE1 7RU, UK.
Tobias P DickDivision of Redox Regulation, DKFZ-ZMBH Alliance, German Cancer Research Center (DKFZ), Heidelberg, Germany.ORCID http://orcid.org/0000-0003-1367-973X
Uli MühlenhoffInstitute for Cytobiology and Cytopathology, Philipps University Marburg, Marburg, Germany.
Andreas J MeyerInstitute of Crop Science and Resource Conservation, University of Bonn, Bonn, Germany.ORCID http://orcid.org/0000-0001-8144-4364
Carsten BerndtDepartment of Neurology, Medical Faculty, Heinrich-Heine University Düsseldorf, Düsseldorf, Germany.ORCID http://orcid.org/0000-0001-8583-7966
Christopher Horst LilligInstitute for Medical Biochemistry and Molecular Biology, University Medicine, University of Greifswald, Greifswald, Germany. horst@lillig.de.ORCID http://orcid.org/0000-0003-2509-5117
University of Bonn · DEUniversitätsmedizin Greifswald · DEHeinrich Heine University Düsseldorf · DENewcastle University · GBGerman Cancer Research Center · DEPhilipps University of Marburg · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Despite their very close structural similarity, CxxC/S-type (class I) glutaredoxins (Grxs) act as oxidoreductases, while CGFS-type (class II) Grxs act as FeS cluster transferases. Here we show that the key determinant of Grx function is a distinct loop structure adjacent to the active site. Engineering of a CxxC/S-type Grx with a CGFS-type loop switched its function from oxidoreductase to FeS transferase. Engineering of a CGFS-type Grx with a CxxC/S-type loop abolished FeS transferase activity and activated the oxidative half reaction of the oxidoreductase. The reductive half-reaction, requiring the interaction with a second GSH molecule, was enabled by switching additional residues in the active site. We explain how subtle structural differences, mostly depending on the structure of one particular loop, act in concert to determine Grx function.

Indexed as

AnimalsCatalytic DomainGlutaredoxinsHumansIron-Sulfur ProteinsOxidation-ReductionProtein BindingProtein Structure, SecondarySignal TransductionSubstrate SpecificityGLRX2 protein, humanGlutaredoxinsIron-Sulfur Proteins

Identifiers

PMID32651396
PMCPMC7351949
OpenAlexW3042045665

What OpenQuestion holds

Textmetadata
LicenceCC BY
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.