Evidence map›Paper›PMID 23769967›Full record

ReviewThe international journal of biochemistry & cell biology2013

Regulation of muscle protein synthesis and the effects of catabolic states.

Bradley S Gordon, Andrew R Kelleher, Scot R Kimball

Abstract readReview
In one paragraph

Review in The international journal of biochemistry & cell biology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 124 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
124citing papers in PubMed, 1 pooled it
6.5field-weighted citation impact, top 3% 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

124 citing papers in PubMed, 1 synthesis or guideline pooled it, 211 citations in OpenAlex.

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  18. A review of nutritional recommendations for scuba divers.Journal of the International Society of Sports Nutrition · 2024
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64 more citing papers are in PubMed but not listed here.

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.

Bradley S GordonDepartment of Cellular and Molecular Physiology, The Pennsylvania State University College of Medicine, Hershey, PA 17033, USA.
Andrew R Kelleher
Scot R Kimball
Pennsylvania State University · US

Funding

REGULATION OF SKELETAL MUSCLE METABOLISMR01DK015658 · NIDDK · PENNSYLVANIA STATE UNIV HERSHEY MED CTR · PI KIMBALL, SCOT R · 1986 to 2021
$7.4M
NIDDK NIH HHS R01 DK015658
6 · The paper itself

Abstract

Protein synthesis and degradation are dynamically regulated processes that act in concert to control the accretion or loss of muscle mass. The present article focuses on the mechanisms involved in the impairment of protein synthesis that are associated with skeletal muscle atrophy. The vast majority of mechanisms known to regulate protein synthesis involve modulation of the initiation phase of mRNA translation, which comprises a series of reactions that result in the binding of initiator methionyl-tRNAi and mRNA to the 40S ribosomal subunit. The function of the proteins involved in both events has been shown to be repressed under atrophic conditions such as sepsis, cachexia, chronic kidney disease, sarcopenia, and disuse atrophy. The basis for the inhibition of protein synthesis under such conditions is likely to be multifactorial and includes insulin/insulin-like growth factor 1 resistance, pro-inflammatory cytokine expression, malnutrition, corticosteroids, and/or physical inactivity. The present article provides an overview of the existing literature regarding mechanisms and signaling pathways involved in the regulation of mRNA translation as they apply to skeletal muscle wasting, as well as the efficacy of potential clinical interventions such as nutrition and exercise in the maintenance of skeletal muscle protein synthesis under atrophic conditions. This article is part of a Directed Issue entitled: Molecular basis of muscle wasting.

Indexed as

AnimalsCarrier ProteinsHumansMuscle ProteinsMuscle, SkeletalMuscular AtrophyPhosphorylationRNA, MessengerSignal TransductionCarrier ProteinsMuscle ProteinsRNA, Messenger3-phosphoinositol-dependent kinase 14E-BP15′-untranslated region5′-UTR70kDa ribosomal protein S6 kinase 1AMP-activated protein kinaseAMPKdouble-stranded RNA-dependent protein kinaseeIFeIF4E binding protein 1eukaryotic initiation factorGCN2GEFgeneral-control nonderepressibleglycogen synthase kinase-3GSK-3guanine nucleotide exchange factorheme-regulated inhibitorHRIICUIGF-1Inflammationinitiator methionyl-tRNAinsulin-like growth factor-1Insulin resistanceintensive care unitinternal ribosome entry siteIRESlipopolysaccharideLPSmechanistic target of rapamycin in complex 1Met-tRNA(i)mRNA translationmTORmTORC1Muscle atrophyNF-κBnuclear factor kappa-Bp70S6K1PDCD4PDK1PERKphosphatidylinositol-4,5-bisphosphate 3-kinasePI3KPKRPKR-like endoplasmic reticulum-associated protein kinaseprogrammed cell death 4ras homolog enriched in brainREDDregulated in DNA damage and developmentRhebTNFTSCtuberous sclerosis complextumor necrosis factoruORFupstream open reading frame

Identifiers

PMID23769967
PMCPMC3759561
OpenAlexW2029296519

What OpenQuestion holds

Textmetadata
LicenceTDM
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.