Evidence map›Paper›PMID 36142478›Full record

ReviewInternational journal of molecular sciences2022

Death of a Protein: The Role of E3 Ubiquitin Ligases in Circadian Rhythms of Mice and Flies.

Osama Hasan Mustafa Hasan Abdalla, Brittany Mascarenhas, Hai-Ying Mary Cheng

Open access · goldAbstract readReview
In one paragraph

Review in International journal of molecular sciences, 2022. 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
1.5field-weighted citation impact, top 19% 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, 16 citations in OpenAlex.

  1. Article
  2. Review
  3. Review
  4. Review
  5. Review
  6. Review
  7. Review
  8. Circadian Effects of Melatonin Receptor-Targeting Molecules In Vitro.International journal of molecular sciences · 2024
    Article
  9. The Change Rate of theBiology · 2024
    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

3 authors at 1 institution in 1 country.

Osama Hasan Mustafa Hasan AbdallaDepartment of Biology, University of Toronto Mississauga, Mississauga, ON L5L 1C6, Canada.
Brittany MascarenhasDepartment of Biology, University of Toronto Mississauga, Mississauga, ON L5L 1C6, Canada.
Hai-Ying Mary ChengDepartment of Biology, University of Toronto Mississauga, Mississauga, ON L5L 1C6, Canada.ORCID 0000-0002-9292-7406
University of Toronto · CA

Funding

CIHR PJT-166046Natural Sciences and Engineering Research Council RGPIN-2016-05563
6 · The paper itself

Abstract

Circadian clocks evolved to enable organisms to anticipate and prepare for periodic environmental changes driven by the day-night cycle. This internal timekeeping mechanism is built on autoregulatory transcription-translation feedback loops that control the rhythmic expression of core clock genes and their protein products. The levels of clock proteins rise and ebb throughout a 24-h period through their rhythmic synthesis and destruction. In the ubiquitin-proteasome system, the process of polyubiquitination, or the covalent attachment of a ubiquitin chain, marks a protein for degradation by the 26S proteasome. The process is regulated by E3 ubiquitin ligases, which recognize specific substrates for ubiquitination. In this review, we summarize the roles that known E3 ubiquitin ligases play in the circadian clocks of two popular model organisms: mice and fruit flies. We also discuss emerging evidence that implicates the N-degron pathway, an alternative proteolytic system, in the regulation of circadian rhythms. We conclude the review with our perspectives on the potential for the proteolytic and non-proteolytic functions of E3 ubiquitin ligases within the circadian clock system.

Indexed as

Circadian ClocksCircadian RhythmAnimalsCLOCK ProteinsDrosophilaProteasome Endopeptidase ComplexUbiquitin-Protein LigasesUbiquitinsCLOCK ProteinsProteasome Endopeptidase ComplexUbiquitin-Protein LigasesUbiquitinscircadian rhythmsclock proteinsDrosophilaE3 ubiquitin ligasesN-degron pathwayprotein degradationsuprachiasmatic nucleusubiquitin proteasome systemUBR4

Identifiers

PMID36142478
PMCPMC9502492
OpenAlexW4295846689

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.