ArticleProteomics2014
Label-free profiling of skeletal muscle using high-definition mass spectrometry.
Article in Proteomics, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
What it found
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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.
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.
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Who cites it
21 citing papers in PubMed, 54 citations in OpenAlex.
- Article
- Muscle Proteome Dynamics.Advances in experimental medicine and biology · 2025Review
- Proteomic reference map for sarcopenia research: mass spectrometric identification of key muscle proteins located in the sarcomere, cytoskeleton and the extracellular matrix.European journal of translational myology · 2024Article
- Proteomic reference map for sarcopenia research: mass spectrometric identification of key muscle proteins of organelles, cellular signaling, bioenergetic metabolism and molecular chaperoning.European journal of translational myology · 2024Article
- How Can Proteomics Help to Elucidate the Pathophysiological Crosstalk in Muscular Dystrophy and Associated Multi-System Dysfunction?Proteomes · 2024Article
- Mass Spectrometry-Based Proteomic Technology and Its Application to Study Skeletal Muscle Cell Biology.Cells · 2023Review
- High-quality and robust protein quantification in large clinical/pharmaceutical cohorts with IonStar proteomics investigation.Nature protocols · 2023Review
- Fiber-Type Shifting in Sarcopenia of Old Age: Proteomic Profiling of the Contractile Apparatus of Skeletal Muscles.International journal of molecular sciences · 2023Review
- Identification of Subproteomic Markers for Skeletal Muscle Profiling.Methods in molecular biology (Clifton, N.J.) · 2023Article
- Striated muscle-specific serine/threonine-protein kinase beta segregates with high versus low responsiveness to endurance exercise training.Physiological genomics · 2020Article
- Characterization of Contractile Proteins from Skeletal Muscle Using Gel-Based Top-Down Proteomics.Proteomes · 2019Review
- Cost-effective generation of precise label-free quantitative proteomes in high-throughput by microLC and data-independent acquisition.Scientific reports · 2018Article
- Article
- Review
- Age- and Activity-Related Differences in the Abundance of Myosin Essential and Regulatory Light Chains in Human Muscle.Proteomes · 2016Article
- On the Rate of Synthesis of Individual Proteins within and between Different Striated Muscles of the Rat.Proteomes · 2016Article
- Article
- Will Quantitative Proteomics Redefine Some of the Key Concepts in Skeletal Muscle Physiology?Proteomes · 2016Article
- The biochemical and mass spectrometric profiling of the dystrophin complexome from skeletal muscle.Computational and structural biotechnology journal · 2016Review
- Concurrent Label-Free Mass Spectrometric Analysis of Dystrophin Isoform Dp427 and the Myofibrosis Marker Collagen in Crude Extracts fromProteomes · 2015Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
5 authors at 4 institutions in 3 countries.
Funding
Abstract
We report automated and time-efficient (2 h per sample) profiling of muscle using ultra-performance LC coupled directly with high-definition MS (HDMS(E)). Soluble proteins extracted from rat gastrocnemius (n = 10) were digested with trypsin and analyzed in duplicate using a 90 min RPLC gradient. Protein identification and label-free quantitation were performed from HDMS(E) spectra analyzed using Progenesis QI for Proteomics software. In total 1514 proteins were identified. Of these, 811 had at least three unique peptides and were subsequently used to assess the dynamic range and precision of LC-HDMS(E) label-free profiling. Proteins analyzed by LC-HDMS(E) encompass the entire complement of glycolytic, β-oxidation, and tricarboxylic acid enzymes. In addition, numerous components of the electron transport chain and protein kinases involved in skeletal muscle regulation were detected. The dynamic range of protein abundances spanned four orders of magnitude. The correlation between technical replicates of the ten biological samples was R(2) = 0.9961 ± 0.0036 (95% CI = 0.9940 - 0.9992) and the technical CV averaged 7.3 ± 6.7% (95% CI = 6.87 - 7.79%). This represents the most sophisticated label-free profiling of skeletal muscle to date.
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What OpenQuestion holds
Registered trials
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.