Evidence map›Paper›PMID 31890941›Full record

ArticleHeliyon2019

Substrate specificity of thioredoxins and glutaredoxins - towards a functional classification.

Manuela Gellert, Md Faruq Hossain, Felix Jacob Ferdinand Berens, Lukas Willy Bruhn, Claudia Urbainsky, Volkmar Liebscher, Christopher Horst Lillig

Abstract read
In one paragraph

Article in Heliyon, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
–field-weighted citation impact
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

11 citing papers in PubMed.

  1. Review
  2. Review
  3. Article
  4. Article
  5. Article
  6. Can thiol-based redox systems be utilized as parts for synthetic biology applications?Redox report : communications in free radical research · 2021
    Article
  7. Review
  8. Article
  9. Article
  10. Redox and Thiols in Archaea.Antioxidants (Basel, Switzerland) · 2020
    Review
  11. Review
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

7 authors.

Manuela GellertInstitute for Medical Biochemistry and Molecular Biology, University Medicine Greifswald, Germany.
Md Faruq HossainInstitute for Medical Biochemistry and Molecular Biology, University Medicine Greifswald, Germany.
Felix Jacob Ferdinand BerensInstitute for Medical Biochemistry and Molecular Biology, University Medicine Greifswald, Germany.
Lukas Willy BruhnInstitute for Medical Biochemistry and Molecular Biology, University Medicine Greifswald, Germany.
Claudia UrbainskyInstitute for Medical Biochemistry and Molecular Biology, University Medicine Greifswald, Germany.
Volkmar LiebscherInstitute for Mathematics and Informatics, University of Greifswald, Germany.
Christopher Horst LilligInstitute for Medical Biochemistry and Molecular Biology, University Medicine Greifswald, Germany.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The spatio-temporal reduction and oxidation of protein thiols is an essential mechanism in signal transduction in all kingdoms of life. Thioredoxin (Trx) family proteins efficiently catalyze thiol-disulfide exchange reactions and the proteins are widely recognized for their importance in the operation of thiol switches. Trx family proteins have a broad and at the same time very distinct substrate specificity - a prerequisite for redox switching. Despite of multiple efforts, the true nature for this specificity is still under debate. Here, we comprehensively compare the classification/clustering of various redoxins from all domains of life based on their similarity in amino acid sequence, tertiary structure, and their electrostatic properties. We correlate these similarities to the existence of common interaction partners, identified in various previous studies and suggested by proteomic screenings. These analyses confirm that primary and tertiary structure similarity, and thereby all common classification systems, do not correlate to the target specificity of the proteins as thiol-disulfide oxidoreductases. Instead, a number of examples clearly demonstrate the importance of electrostatic similarity for their target specificity, independent of their belonging to the Trx or glutaredoxin subfamilies.

Indexed as

Biocomputational methodBiomoleculesElectrostaticsGlutaredoxinGromov-Wasserstein distanceMathematical biosciencesMolecular dockingProtein-protein interactionRedox signalingThioredoxin

Identifiers

PMID31890941
PMCPMC6928294

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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.