Evidence map›Paper›PMID 32316330›Full record

ReviewInternational journal of molecular sciences2020

The Role of Selective Protein Degradation in the Regulation of Iron and Sulfur Homeostasis in Plants.

Anna Wawrzyńska, Agnieszka Sirko

Open access · goldAbstract readReview
In one paragraph

Review in International journal of molecular sciences, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing papers in PubMed
2.5field-weighted citation impact, top 11% 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

10 citing papers in PubMed, 18 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Exploring the Contribution of Autophagy to the Excess-Sucrose Response inInternational journal of molecular sciences · 2022
    Article
  5. Article
  6. Article
  7. Article
  8. Interaction Between Sulfur and Iron in Plants.Frontiers in plant science · 2021
    Review
  9. Article
  10. 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

2 authors at 1 institution in 1 country.

Anna WawrzyńskaInstitute of Biochemistry and Biophysics Polish Academy of Sciences, 02-106 Warsaw, Poland.ORCID 0000-0002-6985-3904
Agnieszka SirkoInstitute of Biochemistry and Biophysics Polish Academy of Sciences, 02-106 Warsaw, Poland.ORCID 0000-0002-5205-2924
Institute of Biochemistry and Biophysics, Polish Academy of Sciences · PL

Funding

Narodowe Centrum Nauki 2014/15/B/NZ1/01887Narodowe Centrum Nauki 2014/15/B/NZ3/04854
6 · The paper itself

Abstract

Plants are able to synthesize all essential metabolites from minerals, water, and light to complete their life cycle. This plasticity comes at a high energy cost, and therefore, plants need to tightly allocate resources in order to control their economy. Being sessile, plants can only adapt to fluctuating environmental conditions, relying on quality control mechanisms. The remodeling of cellular components plays a crucial role, not only in response to stress, but also in normal plant development. Dynamic protein turnover is ensured through regulated protein synthesis and degradation processes. To effectively target a wide range of proteins for degradation, plants utilize two mechanistically-distinct, but largely complementary systems: the 26S proteasome and the autophagy. As both proteasomal- and autophagy-mediated protein degradation use ubiquitin as an essential signal of substrate recognition, they share ubiquitin conjugation machinery and downstream ubiquitin recognition modules. Recent progress has been made in understanding the cellular homeostasis of iron and sulfur metabolisms individually, and growing evidence indicates that complex crosstalk exists between iron and sulfur networks. In this review, we highlight the latest publications elucidating the role of selective protein degradation in the control of iron and sulfur metabolism during plant development, as well as environmental stresses.

Indexed as

AutophagyIronPlant ProteinsPlantsProteasome Endopeptidase ComplexProteolysisSulfurUbiquitinIronPlant ProteinsProteasome Endopeptidase ComplexSulfurUbiquitinautophagyiron metabolismproteasomeprotein degradationsulfur metabolismubiquitin

Identifiers

PMID32316330
PMCPMC7215296
OpenAlexW3016996323

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.