Evidence map›Paper›PMID 31461340›Full record

ReviewAmerican journal of physiology. Cell physiology2019

Molecular regulation of human skeletal muscle protein synthesis in response to exercise and nutrients: a compass for overcoming age-related anabolic resistance.

Nathan Hodson, Daniel W D West, Andrew Philp, Nicholas A Burd, Daniel R Moore

Open access · bronzeAbstract readReview
PubMed Full text at PMC Publisher
In one paragraph

Review in American journal of physiology. Cell physiology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
35citing papers in PubMed, 1 pooled it
4.9field-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

35 citing papers in PubMed, 1 synthesis or guideline pooled it, 68 citations in OpenAlex.

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  15. Weight gain during the menopause transition: Evidence for a mechanism dependent on protein leverage.BJOG : an international journal of obstetrics and gynaecology · 2023
    Article
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  17. Ubiquitin Ligases in Longevity and Aging Skeletal Muscle.International journal of molecular sciences · 2022
    Review
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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 3 countries.

Nathan HodsonFaculty of Kinesiology and Physical Education, University of Toronto, Toronto, Ontario, Canada.ORCID 0000-0003-1330-4030
Daniel W D WestFaculty of Kinesiology and Physical Education, University of Toronto, Toronto, Ontario, Canada.
Andrew PhilpGarvan Institute of Medical Research, Darlinghurst, Sydney, New South Wales, Australia.
Nicholas A BurdDepartment of Kinesiology and Community Health, University of Illinois, Urbana, Illinois.ORCID 0000-0001-5581-3154
Daniel R MooreFaculty of Kinesiology and Physical Education, University of Toronto, Toronto, Ontario, Canada.
University of Toronto · CAGarvan Institute of Medical Research · AUUniversity of Illinois Urbana-Champaign · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Skeletal muscle mass, a strong predictor of longevity and health in humans, is determined by the balance of two cellular processes, muscle protein synthesis (MPS) and muscle protein breakdown. MPS seems to be particularly sensitive to changes in mechanical load and/or nutritional status; therefore, much research has focused on understanding the molecular mechanisms that underpin this cellular process. Furthermore, older individuals display an attenuated MPS response to anabolic stimuli, termed anabolic resistance, which has a negative impact on muscle mass and function, as well as quality of life. Therefore, an understanding of which, if any, molecular mechanisms contribute to anabolic resistance of MPS is of vital importance in formulation of therapeutic interventions for such populations. This review summarizes the current knowledge of the mechanisms that underpin MPS, which are broadly divided into mechanistic target of rapamycin complex 1 (mTORC1)-dependent, mTORC1-independent, and ribosomal biogenesis-related, and describes the evidence that shows how they are regulated by anabolic stimuli (exercise and/or nutrition) in healthy human skeletal muscle. This review also summarizes evidence regarding which of these mechanisms may be implicated in age-related skeletal muscle anabolic resistance and provides recommendations for future avenues of research that can expand our knowledge of this area.

Indexed as

Protein BiosynthesisDietary ProteinsGene Expression RegulationHumansLongevityMechanistic Target of Rapamycin Complex 1Mitogen-Activated Protein Kinase 1Mitogen-Activated Protein Kinase 3Muscle ProteinsMuscle, SkeletalNutrientsNutritional StatusProteolysisQuality of LifeResistance TrainingRibosomal ProteinsDietary ProteinsMAPK1 protein, humanMAPK3 protein, humanMechanistic Target of Rapamycin Complex 1Mitogen-Activated Protein Kinase 1Mitogen-Activated Protein Kinase 3Muscle ProteinsNutrientsRibosomal Proteinsanabolic resistanceERK1/2mTORC1muscle protein synthesis

Identifiers

PMID31461340
PMCPMC6962519
OpenAlexW2970087283

What OpenQuestion holds

Textmetadata
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.