Evidence map›Paper›PMID 35886949›Full record

ReviewInternational journal of molecular sciences2022

Ubiquitin Ligases in Longevity and Aging Skeletal Muscle.

David C Hughes, Leslie M Baehr, David S Waddell, Adam P Sharples, Sue C Bodine

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 29 papers.

0numbers the graph read from it
0cells of the map it votes in
29citing 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

29 citing papers in PubMed, 34 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Review
  10. Review
  11. Review
  12. Article
  13. Article
  14. Reactive oxygen species in the pathogenesis of sarcopenia.Free radical biology & medicine · 2025
    Review
  15. Article
  16. Review
  17. Review
  18. Review
  19. Potential Vitamin E Signaling Mediators in Skeletal Muscle.Antioxidants (Basel, Switzerland) · 2024
    Review
  20. 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

5 authors at 3 institutions in 2 countries.

David C HughesDivision of Endocrinology and Metabolism, Department of Internal Medicine, Carver College of Medicine, University of Iowa, Iowa City, IA 52242, USA.ORCID 0000-0002-5433-8782
Leslie M BaehrDivision of Endocrinology and Metabolism, Department of Internal Medicine, Carver College of Medicine, University of Iowa, Iowa City, IA 52242, USA.ORCID 0000-0002-8778-3567
David S WaddellDepartment of Biology, University of North Florida, Jacksonville, FL 32224, USA.ORCID 0000-0001-6749-4461
Adam P SharplesInstitute for Physical Performance, Norwegian School of Sport Sciences (NiH), 0863 Oslo, Norway.ORCID 0000-0003-1526-9400
Sue C BodineDivision of Endocrinology and Metabolism, Department of Internal Medicine, Carver College of Medicine, University of Iowa, Iowa City, IA 52242, USA.
University of Iowa · USNorwegian School of Sport Sciences · NOUniversity of North Florida · US

Funding

The role of Fbxl22 in the regulation of skeletal muscle massK01AR077684 · NIAMS · UNIVERSITY OF IOWA · PI HUGHES, DAVID C · 2021 to 2025
$602k
NIAMS NIH HHS K01 AR077684NIAMS NIH HHS K01AR077684The Research Council of Norway 314157
6 · The paper itself

Abstract

The development and prevalence of diseases associated with aging presents a global health burden on society. One hallmark of aging is the loss of proteostasis which is caused in part by alterations to the ubiquitin-proteasome system (UPS) and lysosome-autophagy system leading to impaired function and maintenance of mass in tissues such as skeletal muscle. In the instance of skeletal muscle, the impairment of function occurs early in the aging process and is dependent on proteostatic mechanisms. The UPS plays a pivotal role in degradation of misfolded and aggregated proteins. For the purpose of this review, we will discuss the role of the UPS system in the context of age-related loss of muscle mass and function. We highlight the significant role that E3 ubiquitin ligases play in the turnover of key components (e.g., mitochondria and neuromuscular junction) essential to skeletal muscle function and the influence of aging. In addition, we will briefly discuss the contribution of the UPS system to lifespan. By understanding the UPS system as part of the proteostasis network in age-related diseases and disorders such as sarcopenia, new discoveries can be made and new interventions can be developed which will preserve muscle function and maintain quality of life with advancing age.

Indexed as

LongevityUbiquitinMuscle, SkeletalProteasome Endopeptidase ComplexQuality of LifeUbiquitin-Protein LigasesProteasome Endopeptidase ComplexUbiquitinUbiquitin-Protein LigasesE3 ubiquitin ligasehealthspanprotein degradationproteostasissarcopenia

Identifiers

PMID35886949
PMCPMC9315556
OpenAlexW4285010331

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.