Evidence map›Paper›PMID 33114658›Full record

ReviewInternational journal of molecular sciences2020

The Role of Cullin-RING Ligases in Striated Muscle Development, Function, and Disease.

Jordan Blondelle, Andrea Biju, Stephan Lange

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 16 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed, 1 pooled it
0.9field-weighted citation impact, top 26% 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

16 citing papers in PubMed, 1 synthesis or guideline pooled it, 24 citations in OpenAlex.

  1. Pooled it
  2. Article
  3. Article
  4. Article
  5. New insights into the skeletal muscle circadian clock in ruminants.Journal of animal science and biotechnology · 2026
    Review
  6. Article
  7. Article
  8. Article
  9. Review
  10. Article
  11. Review
  12. Ubiquitin Ligases in Longevity and Aging Skeletal Muscle.International journal of molecular sciences · 2022
    Review
  13. Article
  14. Article
  15. Exploring Obscurin and SPEG Kinase Biology.Journal of clinical medicine · 2021
    Article
  16. 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 2 countries.

Jordan BlondelleDepartment of Medicine, University of California, La Jolla, CA 92093, USA.
Andrea BijuDepartment of Medicine, University of California, La Jolla, CA 92093, USA.
Stephan LangeDepartment of Medicine, University of California, La Jolla, CA 92093, USA.ORCID 0000-0001-9361-6602
University of California San Diego · US

Funding

Training In Cardiovascular Physiology & PharmacologyT32HL007444 · NHLBI · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI Ju Chen, Robert Scott Ross · 1985 to 2026
$11.1M
U of Calif, San Diego Neuroscience Microscopy ImagingP30NS047101 · NINDS · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI GLEESON, JOSEPH G, ZHENG, BINHAI · 2003 to 2022
$9.0M
San Diego Skeletal Muscle Research CenterP30AR061303 · NIAMS · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI CHEN, JU · 2011 to 2015
$3.3M
The role of obscurin and Obsl1 as key determinants for diastolic functionR01HL152251 · NHLBI · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI CHO, YOSHITAKE, LANGE, STEPHAN · 2021 to 2024
$2.3M
Signaling Pathways in Dilated CardiomyopathyR01HL128457 · NHLBI · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI LANGE, STEPHAN · 2015 to 2019
$1.9M
Cullin mediated protein turnover in skeletal and cardiac musclesR00HL107744 · NHLBI · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI LANGE, STEPHAN · 2013 to 2015
$726k
NHLBI NIH HHS HL107744NHLBI NIH HHS HL128457NHLBI NIH HHS R00 HL107744NHLBI NIH HHS R01 HL128457NHLBI NIH HHS R01 HL152251NHLBI NIH HHS T32 HL007444NIAMS NIH HHS P30 AR061303NIH HHS NS047101NINDS NIH HHS P30 NS047101
6 · The paper itself

Abstract

The well-orchestrated turnover of proteins in cross-striated muscles is one of the fundamental processes required for muscle cell function and survival. Dysfunction of the intricate protein degradation machinery is often associated with development of cardiac and skeletal muscle myopathies. Most muscle proteins are degraded by the ubiquitin-proteasome system (UPS). The UPS involves a number of enzymes, including E3-ligases, which tightly control which protein substrates are marked for degradation by the proteasome. Recent data reveal that E3-ligases of the cullin family play more diverse and crucial roles in cross striated muscles than previously anticipated. This review highlights some of the findings on the multifaceted functions of cullin-RING E3-ligases, their substrate adapters, muscle protein substrates, and regulatory proteins, such as the Cop9 signalosome, for the development of cross striated muscles, and their roles in the etiology of myopathies.

Indexed as

COP9 Signalosome ComplexCullin ProteinsGene Expression Regulation, DevelopmentalHumansMuscle ProteinsMuscle, StriatedMuscular DiseasesProteolysisCOP9 Signalosome ComplexCullin ProteinsMuscle Proteinsautophagy-lysosome systemcardiomyopathycullin-RING ligase (CRL)muscular dystrophyNedd8protein degradationstriated muscle developmentstriated muscle functionubiquitin-proteasome system (UPS)

Identifiers

PMID33114658
PMCPMC7672578
OpenAlexW3097502903

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.