Evidence map›Paper›PMID 27054028›Full record

ReviewSkeletal muscle2016

The beneficial role of proteolysis in skeletal muscle growth and stress adaptation.

Ryan A V Bell, Mohammad Al-Khalaf, Lynn A Megeney

Erratum issuedOpen access · goldAbstract readReview
In one paragraph

Review in Skeletal muscle, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 69 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
69citing papers in PubMed, 1 pooled it
7.7field-weighted citation impact, top 2% 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

69 citing papers in PubMed, 1 synthesis or guideline pooled it, 117 citations in OpenAlex.

  1. Pooled it
  2. Trial
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9 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

3 authors at 2 institutions in 1 country.

Ryan A V BellRegenerative Medicine Program, Sprott Center for Stem Cell Research, Ottawa Hospital Research Institute, The Ottawa Hospital, Ottawa, ON K1H 8L6 Canada ; Department of Cellular and Molecular Medicine, University of Ottawa, Ottawa, ON Canada.
Mohammad Al-KhalafRegenerative Medicine Program, Sprott Center for Stem Cell Research, Ottawa Hospital Research Institute, The Ottawa Hospital, Ottawa, ON K1H 8L6 Canada ; Department of Cellular and Molecular Medicine, University of Ottawa, Ottawa, ON Canada.
Lynn A MegeneyRegenerative Medicine Program, Sprott Center for Stem Cell Research, Ottawa Hospital Research Institute, The Ottawa Hospital, Ottawa, ON K1H 8L6 Canada ; Department of Cellular and Molecular Medicine, University of Ottawa, Ottawa, ON Canada ; Department of Medicine, Division of Cardiology, University of Ottawa, Ottawa, ON Canada.
Ottawa Hospital Research InstituteUniversity of Ottawa · CA

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Muscle atrophy derived from excessive proteolysis is a hallmark of numerous disease conditions. Accordingly, the negative consequences of skeletal muscle protein breakdown often overshadow the critical nature of proteolytic systems in maintaining normal cellular function. Here, we discuss the major cellular proteolysis machinery-the ubiquitin/proteosome system, the autophagy/lysosomal system, and caspase-mediated protein cleavage-and the critical role of these protein machines in establishing and preserving muscle health. We examine how ordered degradation modifies (1) the spatiotemporal expression of myogenic regulatory factors during myoblast differentiation, (2) membrane fusion during myotube formation, (3) sarcomere remodeling and muscle growth following physical stress, and (4) energy homeostasis during nutrient deprivation. Finally, we review the origin and etiology of a number of myopathies and how these devastating conditions arise from inborn errors in proteolysis.

Indexed as

Muscle DevelopmentProteolysisRegenerationStress, PhysiologicalAdaptation, PhysiologicalAnimalsAutophagyCaspasesHumansLysosomesMuscle, SkeletalMuscular AtrophyPeptide HydrolasesProteasome Endopeptidase ComplexSignal TransductionUbiquitinationCaspasesPeptide HydrolasesProteasome Endopeptidase ComplexAutophagyCaspaseMuscle cell differentiationMuscle growthProteasomeProteolysis

Identifiers

PMID27054028
PMCPMC4822268
OpenAlexW2320267036

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.