Evidence map›Paper›PMID 35579367›Full record

ArticlePlant physiology2022

Selenium-binding Protein 1 (SBD1): A stress response regulator in Chlamydomonas reinhardtii.

Aikaterini Koletti, Irene Dervisi, Chrysanthi Kalloniati, Maria-Eleftheria Zografaki, Heinz Rennenberg, Andreas Roussis, Emmanouil Flemetakis

Abstract read
In one paragraph

Article in Plant physiology, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.

0numbers the graph read from it
0cells of the map it votes in
9citing 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

9 citing papers in PubMed.

  1. Plants (Basel, Switzerland) · 2026
    Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Review
  7. Article
  8. Evolutionary Aspects of Selenium Binding Protein (SBP).Journal of molecular evolution · 2023
    Article
  9. Article
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.

Aikaterini KolettiDepartment of Biotechnology, School of Applied Biology and Biotechnology, Agricultural University of Athens, Athens 11855, Greece.ORCID 0000-0003-3873-5304
Irene DervisiDepartment of Botany, Faculty of Biology, National & Kapodistrian University of Athens, Athens 15784, Greece.ORCID 0000-0003-3830-3085
Chrysanthi KalloniatiDepartment of Biotechnology, School of Applied Biology and Biotechnology, Agricultural University of Athens, Athens 11855, Greece.
Maria-Eleftheria ZografakiDepartment of Biotechnology, School of Applied Biology and Biotechnology, Agricultural University of Athens, Athens 11855, Greece.ORCID 0000-0001-7312-4096
Heinz RennenbergCenter of Molecular Ecophysiology (CMEP), College of Resources and Environment, Chongqing 400715, China.ORCID 0000-0001-6224-2927
Andreas RoussisDepartment of Botany, Faculty of Biology, National & Kapodistrian University of Athens, Athens 15784, Greece.ORCID 0000-0003-2346-7132
Emmanouil FlemetakisDepartment of Biotechnology, School of Applied Biology and Biotechnology, Agricultural University of Athens, Athens 11855, Greece.ORCID 0000-0003-2530-9592

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Selenium-binding proteins (SBPs) represent a ubiquitous protein family implicated in various environmental stress responses, although the exact molecular and physiological role of the SBP family remains elusive. In this work, we report the identification and characterization of CrSBD1, an SBP homolog from the model microalgae Chlamydomonas reinhardtii. Growth analysis of the C. reinhardtii sbd1 mutant strain revealed that the absence of a functional CrSBD1 resulted in increased growth under mild oxidative stress conditions, although cell viability rapidly declined at higher hydrogen peroxide (H2O2) concentrations. Furthermore, a combined global transcriptomic and metabolomic analysis indicated that the sbd1 mutant exhibited a dramatic quenching of the molecular and biochemical responses upon H2O2-induced oxidative stress when compared to the wild-type. Our results indicate that CrSBD1 represents a cell regulator, which is involved in the modulation of C. reinhardtii early responses to oxidative stress. We assert that CrSBD1 acts as a member of an extensive and conserved protein-protein interaction network including Fructose-bisphosphate aldolase 3, Cysteine endopeptidase 2, and Glutaredoxin 6 proteins, as indicated by yeast two-hybrid assays.

Indexed as

Chlamydomonas reinhardtiiMicroalgaeHydrogen PeroxideOxidative StressSelenium-Binding ProteinsHydrogen PeroxideSelenium-Binding Proteins

Identifiers

PMID35579367
PMCPMC9342975

What OpenQuestion holds

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Registered trials

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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.