Evidence map›Paper›PMID 40993048›Full record

ReviewExercise and sport sciences reviews2025

UBR5: A New Player in Protein Quality Control for Skeletal Muscle Growth and Remodeling.

David C Hughes, Sue C Bodine

Abstract readReview
In one paragraph

Review in Exercise and sport sciences reviews, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing 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

2 citing papers in PubMed.

  1. Article
  2. 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

2 authors.

David C HughesAging and Metabolism Research Program, Oklahoma Medical Research Foundation, Oklahoma City, OK.
Sue C Bodine

Funding

The role of Fbxl22 in the regulation of skeletal muscle massK01AR077684 · NIAMS · UNIVERSITY OF IOWA · PI HUGHES, DAVID C · 2021 to 2025
$602k
The role of UBR5 in skeletal muscle atrophy and regrowthR03AR083980 · NIAMS · OKLAHOMA MEDICAL RESEARCH FOUNDATION · PI HUGHES, DAVID C · 2024 to 2024
$171k
NIAMS NIH HHS K01 AR077684NIAMS NIH HHS R03 AR083980
6 · The paper itself

Abstract

A balance between protein synthesis and degradation regulates skeletal muscle size. Proteolytic mechanisms, like the ubiquitin-proteasome system, are critical processes in protein quality control. Counterintuitively, the E3 ubiquitin ligase, UBR5, appears to be involved in skeletal muscle hypertrophy and regrowth and interacts with protein synthesis. We present the novel hypothesis for protein quality control being critical for skeletal muscle growth and remodeling.

Indexed as

Muscle DevelopmentMuscle ProteinsMuscle, SkeletalUbiquitin-Protein LigasesAnimalsHumansHypertrophyProtein BiosynthesisProteolysisMuscle ProteinsUbiquitin-Protein LigasesexerciseN-degron pathwayproteasome systemprotein turnoverskeletal muscle

Identifiers

PMID40993048
PMCPMC12459145

What Socratic holds

Textmetadata
LicenceCC BY-NC-ND
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 Socratic graph.