Evidence map›Paper›PMID 27897395›Full record

ReviewJournal of cachexia, sarcopenia and muscle2017

The Human Skeletal Muscle Proteome Project: a reappraisal of the current literature.

Marta Gonzalez-Freire, Richard D Semba, Ceereena Ubaida-Mohien, Elisa Fabbri, Paul Scalzo, Kurt Højlund, Craig Dufresne, Alexey Lyashkov, Luigi Ferrucci

Open access · goldAbstract readReview
In one paragraph

Review in Journal of cachexia, sarcopenia and muscle, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 57 papers.

0numbers the graph read from it
0cells of the map it votes in
57citing papers in PubMed
4.5field-weighted citation impact, top 5% 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

57 citing papers in PubMed, 98 citations in OpenAlex.

  1. Review
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  11. Review
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  14. Review
  15. A Complete Workflow for High Throughput Human Single Skeletal Muscle Fiber Proteomics.Journal of the American Society for Mass Spectrometry · 2023
    Article
  16. Review
  17. Review
  18. Article
  19. Review
  20. Identification of Subproteomic Markers for Skeletal Muscle Profiling.Methods in molecular biology (Clifton, N.J.) · 2023
    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

9 authors at 5 institutions in 2 countries.

Marta Gonzalez-FreireNational Institute on Aging, National Institutes of Health, Baltimore, MD, USA.
Richard D SembaWilmer Eye Institute, Johns Hopkins University School of Medicine, Baltimore, MD, USA.
Ceereena Ubaida-MohienNational Institute on Aging, National Institutes of Health, Baltimore, MD, USA.
Elisa FabbriNational Institute on Aging, National Institutes of Health, Baltimore, MD, USA.
Paul ScalzoNational Institute on Aging, National Institutes of Health, Baltimore, MD, USA.
Kurt HøjlundDepartment of Endocrinology, Odense University Hospital, Odense, Denmark.
Craig DufresneThermo Fisher Scientific, West Palm Beach, FL, USA.
Alexey LyashkovNational Institute on Aging, National Institutes of Health, Baltimore, MD, USA.
Luigi FerrucciNational Institute on Aging, National Institutes of Health, Baltimore, MD, USA.
National Institutes of Health · USJohns Hopkins Medicine · USNational Institute on Aging · USThermo Fisher Scientific (United States) · USUniversity of Southern Denmark · DK

Funding

GESTALT-Genetic and Epigenetic Signatures of Translational Aging Laboratory TestingZIAAG000996 · NIA · NATIONAL INSTITUTE ON AGING · PI FERRUCCI, LUIGI · 2015 to 2025
$7.6M
Oxidative stress and the pathogenesis of sarcopenia and disability in older womenR01AG027012 · NIA · JOHNS HOPKINS UNIVERSITY · PI SEMBA, RICHARD D · 2005 to 2018
$3.6M
Changes in muscle biomechanical quality with aging: causes and consequencesZIAAG000995 · NIA · NATIONAL INSTITUTE ON AGING · PI FERRUCCI, LUIGI · 2015 to 2025
$875k
NIA NIH HHS R01 AG027012
6 · The paper itself

Abstract

Skeletal muscle is a large organ that accounts for up to half the total mass of the human body. A progressive decline in muscle mass and strength occurs with ageing and in some individuals configures the syndrome of 'sarcopenia', a condition that impairs mobility, challenges autonomy, and is a risk factor for mortality. The mechanisms leading to sarcopenia as well as myopathies are still little understood. The Human Skeletal Muscle Proteome Project was initiated with the aim to characterize muscle proteins and how they change with ageing and disease. We conducted an extensive review of the literature and analysed publically available protein databases. A systematic search of peer-reviewed studies was performed using PubMed. Search terms included 'human', 'skeletal muscle', 'proteome', 'proteomic(s)', and 'mass spectrometry', 'liquid chromatography-mass spectrometry (LC-MS/MS)'. A catalogue of 5431 non-redundant muscle proteins identified by mass spectrometry-based proteomics from 38 peer-reviewed scientific publications from 2002 to November 2015 was created. We also developed a nosology system for the classification of muscle proteins based on localization and function. Such inventory of proteins should serve as a useful background reference for future research on changes in muscle proteome assessed by quantitative mass spectrometry-based proteomic approaches that occur with ageing and diseases. This classification and compilation of the human skeletal muscle proteome can be used for the identification and quantification of proteins in skeletal muscle to discover new mechanisms for sarcopenia and specific muscle diseases that can be targeted for the prevention and treatment.

Indexed as

ProteomeHumansMuscle ProteinsMuscle, SkeletalMuscle ProteinsProteomeAgeingMass spectrometryPost-translational modificationsProteomicsSkeletal muscle

Identifiers

PMID27897395
PMCPMC5326819
OpenAlexW2514031291

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.