ArticleJournal of molecular and cellular cardiology2015
Comprehensive assessment of chamber-specific and transmural heterogeneity in myofilament protein phosphorylation by top-down mass spectrometry.
Article in Journal of molecular and cellular cardiology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed, 30 citations in OpenAlex.
- Spatial control of myosin regulatory light chain phosphorylation modulates cardiac thick filament mechanosensing.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Characteristics of Sarcomere Proteins in Myocardial Sleeves of the Superior Vena Cava and Pulmonary Veins of the Porcine Heart.Bulletin of experimental biology and medicine · 2025Article
- Tissue Usage Preference and Intrinsically Disordered Region Remodeling of Alternative Splicing Derived Proteoforms in the Heart.Journal of proteome research · 2024Article
- Proteomics of the heart.Physiological reviews · 2024Review
- Top-down proteomics.Nature reviews. Methods primers · 2024Article
- Top-down proteomics of myosin light chain isoforms define chamber-specific expression in the human heart.Journal of molecular and cellular cardiology · 2023Article
- Fourier-transform ion cyclotron resonance mass spectrometry for characterizing proteoforms.Mass spectrometry reviews · 2022Review
- PERCEPTRON: an open-source GPU-accelerated proteoform identification pipeline for top-down proteomics.Nucleic acids research · 2021Article
- Top-Down Proteomics Reveals Myofilament Proteoform Heterogeneity among Various Rat Skeletal Muscle Tissues.Journal of proteome research · 2020Article
- Large-Scale Contractility Measurements Reveal Large Atrioventricular and Subtle Interventricular Differences in Cultured Unloaded Rat Cardiomyocytes.Frontiers in physiology · 2020Article
- An Unbiased Proteomics Method to Assess the Maturation of Human Pluripotent Stem Cell-Derived Cardiomyocytes.Circulation research · 2019Article
- Deletion of Enigma Homologue from the Z-disc slows tension development kinetics in mouse myocardium.The Journal of general physiology · 2019Article
- Simultaneous Quantification of Protein Expression and Modifications by Top-down Targeted Proteomics: A Case of the Sarcomeric Subproteome.Molecular & cellular proteomics : MCP · 2019Article
- Analysis of cardiac troponin proteoforms by top-down mass spectrometry.Methods in enzymology · 2019Article
- Temperature-sensitive sarcomeric protein post-translational modifications revealed by top-down proteomics.Journal of molecular and cellular cardiology · 2018Article
- Proteomic analysis of cardiac ventricles: baso-apical differences.Molecular and cellular biochemistry · 2018Article
- Top-Down Proteomics: Ready for Prime Time?Analytical chemistry · 2018Review
- The continuing evolution of cardiac troponin I biomarker analysis: from protein to proteoform.Expert review of proteomics · 2017Review
- Distinct sequences and post-translational modifications in cardiac atrial and ventricular myosin light chains revealed by top-down mass spectrometry.Journal of molecular and cellular cardiology · 2017Article
- Top-down Proteomics: Technology Advancements and Applications to Heart Diseases.Expert review of proteomics · 2016Review
Corrections and comments
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Authors and funding
10 authors at 2 institutions in 1 country.
Funding
Abstract
The heart is characterized by a remarkable degree of heterogeneity, the basis of which is a subject of active investigation. Myofilament protein post-translational modifications (PTMs) represent a critical mechanism regulating cardiac contractility, and emerging evidence shows that pathological cardiac conditions induce contractile heterogeneity that correlates with transmural variations in the modification status of myofilament proteins. Nevertheless, whether there exists basal heterogeneity in myofilament protein PTMs in the heart remains unclear. Here we have systematically assessed chamber-specific and transmural variations in myofilament protein PTMs, specifically, the phosphorylation of cardiac troponin I (cTnI), cardiac troponin T (cTnT), tropomyosin (Tpm), and myosin light chain 2 (MLC2). We show that the phosphorylation of cTnI and αTm vary in the different chambers of the heart, whereas the phosphorylation of MLC2 and cTnT does not. In contrast, no significant transmural differences were observed in the phosphorylation of any of the myofilament proteins analyzed. These results highlight the importance of appropriate tissue sampling-particularly for studies aimed at elucidating disease mechanisms and biomarker discovery-in order to minimize potential variations arising from basal heterogeneity in myofilament PTMs in the heart.
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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.