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References from A Streamlined One-Pot Extraction Method Enables High-Sensitivity Top-Down Proteomic Characterization of Phospholamban from Biopsy-Scale Cardiac Tissue. Local targets link to admitted publications; unresolved targets remain external evidence.
Proteoforms as the next Proteomics Currency
10.1126/science.aat1884 · 2018 · External reference
Proteoform: A Single Term Describing Protein Complexity
10.1038/nmeth.2369 · 2013 · External reference
Progress in Top-Down Proteomics and the Analysis of Proteoforms
10.1146/annurev-anchem-071015-041550 · 2016 · External reference
Deciphering Combinatorial Post-Translational Modifications by Top-down Mass Spectrometry
10.1016/j.cbpa.2022.102180 · 2022 · External reference
Top-down Mass Spectrometry for the Analysis of Combinatorial Post-Translational Modifications
10.1002/mas.21348 · 2013 · External reference
Peer Reviewed: Top-Down Proteomics
10.1021/ac0415657 · 2004 · External reference
Top-Down Proteomics: Ready for Prime Time?
10.1021/acs.analchem.7b04747 · 2018 · External reference
Top-down Proteomics
10.1038/s43586-024-00318-2 · 2024 · External reference
Top Down Proteomics: Facts and Perspectives
10.1016/j.bbrc.2014.02.041 · 2014 · External reference
Computational Analysis of Membrane Proteins: The Largest Class of Drug Targets
10.1016/j.drudis.2009.08.006 · 2009 · External reference
Drugging Membrane Protein Interactions
10.1146/annurev-bioeng-092115-025322 · 2016 · External reference
Integral Membrane Proteins and Bilayer Proteomics
10.1021/ac303064a · 2013 · External reference
Integral Membrane Proteins: Bottom-up, Top-down and Structural Proteomics
10.1080/14789450.2017.1359545 · 2017 · External reference
Tandem Mass Spectrometry of Integral Membrane Proteins for Top-down Proteomics
10.1016/j.trac.2005.04.010 · 2005 · External reference
Novel Strategies to Address the Challenges in Top-Down Proteomics
10.1021/jasms.1c00099 · 2021 · External reference
Exploring the Membrane Proteome─Challenges and Analytical Strategies
10.1016/j.jprot.2010.01.005 · 2010 · External reference
Proteomics of Integral Membrane ProteinsTheory and Application
10.1021/cr068286z · 2007 · External reference
Top-Down Proteomics of Endogenous Membrane Proteins Enabled by Cloud Point Enrichment and Multidimensional Liquid Chromatography–Mass Spectrometry
10.1021/acs.analchem.0c02533 · 2020 · External reference
A Photocleavable Surfactant for Top-down Proteomics
10.1038/s41592-019-0391-1 · 2019 · External reference
High-Throughput Proteomics Enabled by a Photocleavable Surfactant
10.1002/ange.201915374 · 2020 · External reference
Comprehensive Characterization of Endogenous Phospholamban Proteoforms Enabled by Photocleavable Surfactant and Top-down Proteomics
10.1021/acs.analchem.3c01618 · 2023 · External reference
Phospholamban: A Crucial Regulator of Cardiac Contractility
10.1038/nrm1151 · 2003 · External reference
Phospholamban and Cardiac Contractility
10.3109/07853890008998837 · 2000 · External reference
Phosphorylation of a 22,000-Dalton Component of the Cardiac Sarcoplasmic Reticulum by Adenosine 3′:5′-Monophosphate-Dependent Protein Kinase
10.1016/s0021-9258(19)41650-5 · 1975 · External reference
Phosphorylation of Troponin I and Phospholamban during Catecholamine Stimulation of Rabbit Heart
10.1038/298182a0 · 1982 · External reference
The Structural Basis for Phospholamban Inhibition of the Calcium Pump in Sarcoplasmic Reticulum
10.1074/jbc.m113.501585 · 2013 · External reference
Phospholamban: A Prominent Regulator of Myocardial Contractility
10.1161/01.res.79.6.1059 · 1996 · External reference
Modulation of Cardiac Contractility by the Phopholamban/SERCA2a Regulatome
10.1161/circresaha.111.259754 · 2012 · External reference
Sequence Analysis of Phospholamban. Identification of Phosphorylation Sites and Two Major Structural Domains
10.1016/s0021-9258(18)69309-3 · 1986 · External reference
Palmitoyl Acyltransferase Aph2 in Cardiac Function and the Development of Cardiomyopathy
10.1073/pnas.1518368112 · 2015 · External reference
Dilated Cardiomyopathy and Heart Failure Caused by a Mutation in Phospholamban
10.1126/science.1081578 · 2003 · External reference
A Mutation in the Human Phospholamban Gene, Deleting Arginine 14, Results in Lethal, Hereditary Cardiomyopathy
10.1073/pnas.0510519103 · 2006 · External reference
Arrhythmogenic Cardiomyopathy
10.1161/circresaha.117.309345 · 2017 · External reference
HRS Expert Consensus Statement on Evaluation, Risk Stratification, and Management of Arrhythmogenic Cardiomyopathy
10.1016/j.hrthm.2019.05.007 · 2019 · External reference
Sensitive Top-Down Proteomics Analysis of a Low Number of Mammalian Cells Using a Nanodroplet Sample Processing Platform
10.1021/acs.analchem.0c00467 · 2020 · External reference
Digital Microfluidics and Magnetic Bead-Based Intact Proteoform Elution for Quantitative Top-down Nanoproteomics of Single C. Elegans Nematodes
10.1002/anie.202301969 · 2023 · External reference
High Sensitivity Top–down Proteomics Captures Single Muscle Cell Heterogeneity in Large Proteoforms
10.1073/pnas.2222081120 · 2023 · External reference
MASH Native: A Unified Solution for Native Top-down Proteomics Data Processing
10.1093/bioinformatics/btad359 · 2023 · External reference
Aberrant PLN-R14del Protein Interactions Intensify SERCA2a Inhibition, Driving Impaired Ca2+ Handling and Arrhythmogenesis
10.3390/ijms23136947 · 2022 · External reference
Reduced Ca(2+)-Sensitivity of SERCA 2a in Failing Human Myocardium Due to Reduced Serin-16 Phospholamban Phosphorylation
10.1006/jmcc.1998.0897 · 1999 · External reference
Lethal, Hereditary Mutants of Phospholamban Elude Phosphorylation by Protein Kinase A
10.1074/jbc.m112.382713 · 2012 · External reference
Comparison of the Structure and Function of Phospholamban and the Arginine-14 Deficient Mutant Associated with Dilated Cardiomyopathy
10.1371/journal.pone.0106746 · 2014 · External reference
14–3-3 Binding Creates a Memory of Kinase Action by Stabilizing the Modified State of Phospholamban
10.1126/scisignal.aaz1436 · 2020 · External reference
CAMKII REGULATION OF PHOSPHOLAMBAN AND SR Ca2+ LOAD
10.1016/j.hrthm.2010.11.035 · 2011 · External reference
Electron Capture Dissociation of Multiply Charged Protein Cations. A Nonergodic Process
10.1021/ja973478k · 1998 · External reference
Localization of Labile Posttranslational Modifications by Electron Capture Dissociation: The Case of γ-Carboxyglutamic Acid
10.1021/ac990684x · 1999 · External reference
The Impact of Phosphorylation on Electron Capture Dissociation of Proteins: A Top-down Perspective
10.1007/s13361-017-1710-3 · 2017 · External reference
The Role of Electron Transfer Dissociation in Modern Proteomics
10.1021/acs.analchem.7b04810 · 2018 · External reference
Complete Protein Characterization Using Top-Down Mass Spectrometry and Ultraviolet Photodissociation
10.1021/ja4029654 · 2013 · External reference
Ultraviolet Photodissociation Mass Spectrometry for Analysis of Biological Molecules
10.1021/acs.chemrev.9b00440 · 2020 · External reference
Heart Failure Association of the ESC, Heart Failure Society of America and Japanese Heart Failure Society Position Statement on Endomyocardial Biopsy
10.1002/ejhf.2190 · 2021 · External reference
Endomyocardial Biopsy in the Clinical Context: Current Indications and Challenging Scenarios
10.1007/s10741-022-10247-5 · 2023 · External reference
Defining the Sarcomeric Proteoform Landscape in Ischemic Cardiomyopathy by Top-Down Proteomics
10.1021/acs.jproteome.2c00729 · 2023 · External reference
Biomarkers in Transplantation Team; NCE CECR PROOF Centre of Excellence. Molecular Signatures of End-Stage Heart Failure
10.1016/j.cardfail.2011.07.001 · 2011 · External reference
Global Proteoform Alterations Across Multiple Cellular Compartments Underlie Obstructive Hypertrophic Cardiomyopathy
10.1161/circheartfailure.125.012899 · 2025 · External reference
Distinct Hypertrophic Cardiomyopathy Genotypes Result in Convergent Sarcomeric Proteoform Profiles Revealed by Top-down Proteomics
10.1073/pnas.2006764117 · 2020 · External reference
High-Throughput Proteomics Enabled by a Photocleavable Surfactant
10.1002/ange.201915374 · ExternalCitation · doi-reference
Digital Microfluidics and Magnetic Bead-Based Intact Proteoform Elution for Quantitative Top-down Nanoproteomics of Single C. Elegans Nematodes
10.1002/anie.202301969 · ExternalCitation · doi-reference
Heart Failure Association of the ESC, Heart Failure Society of America and Japanese Heart Failure Society Position Statement on Endomyocardial Biopsy
10.1002/ejhf.2190 · ExternalCitation · doi-reference
Top-down Mass Spectrometry for the Analysis of Combinatorial Post-Translational Modifications
10.1002/mas.21348 · ExternalCitation · doi-reference
Reduced Ca(2+)-Sensitivity of SERCA 2a in Failing Human Myocardium Due to Reduced Serin-16 Phospholamban Phosphorylation
10.1006/jmcc.1998.0897 · ExternalCitation · doi-reference
Endomyocardial Biopsy in the Clinical Context: Current Indications and Challenging Scenarios
10.1007/s10741-022-10247-5 · ExternalCitation · doi-reference
The Impact of Phosphorylation on Electron Capture Dissociation of Proteins: A Top-down Perspective
10.1007/s13361-017-1710-3 · ExternalCitation · doi-reference
Top Down Proteomics: Facts and Perspectives
10.1016/j.bbrc.2014.02.041 · ExternalCitation · doi-reference
Biomarkers in Transplantation Team; NCE CECR PROOF Centre of Excellence. Molecular Signatures of End-Stage Heart Failure
10.1016/j.cardfail.2011.07.001 · ExternalCitation · doi-reference
Deciphering Combinatorial Post-Translational Modifications by Top-down Mass Spectrometry
10.1016/j.cbpa.2022.102180 · ExternalCitation · doi-reference
Computational Analysis of Membrane Proteins: The Largest Class of Drug Targets
10.1016/j.drudis.2009.08.006 · ExternalCitation · doi-reference
CAMKII REGULATION OF PHOSPHOLAMBAN AND SR Ca2+ LOAD
10.1016/j.hrthm.2010.11.035 · ExternalCitation · doi-reference
HRS Expert Consensus Statement on Evaluation, Risk Stratification, and Management of Arrhythmogenic Cardiomyopathy
10.1016/j.hrthm.2019.05.007 · ExternalCitation · doi-reference
Exploring the Membrane Proteome─Challenges and Analytical Strategies
10.1016/j.jprot.2010.01.005 · ExternalCitation · doi-reference
Tandem Mass Spectrometry of Integral Membrane Proteins for Top-down Proteomics
10.1016/j.trac.2005.04.010 · ExternalCitation · doi-reference
Sequence Analysis of Phospholamban. Identification of Phosphorylation Sites and Two Major Structural Domains
10.1016/s0021-9258(18)69309-3 · ExternalCitation · doi-reference
Phosphorylation of a 22,000-Dalton Component of the Cardiac Sarcoplasmic Reticulum by Adenosine 3′:5′-Monophosphate-Dependent Protein Kinase
10.1016/s0021-9258(19)41650-5 · ExternalCitation · doi-reference
Peer Reviewed: Top-Down Proteomics
10.1021/ac0415657 · ExternalCitation · doi-reference
Integral Membrane Proteins and Bilayer Proteomics
10.1021/ac303064a · ExternalCitation · doi-reference
Localization of Labile Posttranslational Modifications by Electron Capture Dissociation: The Case of γ-Carboxyglutamic Acid
10.1021/ac990684x · ExternalCitation · doi-reference
Sensitive Top-Down Proteomics Analysis of a Low Number of Mammalian Cells Using a Nanodroplet Sample Processing Platform
10.1021/acs.analchem.0c00467 · ExternalCitation · doi-reference
Top-Down Proteomics of Endogenous Membrane Proteins Enabled by Cloud Point Enrichment and Multidimensional Liquid Chromatography–Mass Spectrometry
10.1021/acs.analchem.0c02533 · ExternalCitation · doi-reference
Comprehensive Characterization of Endogenous Phospholamban Proteoforms Enabled by Photocleavable Surfactant and Top-down Proteomics
10.1021/acs.analchem.3c01618 · ExternalCitation · doi-reference
Top-Down Proteomics: Ready for Prime Time?
10.1021/acs.analchem.7b04747 · ExternalCitation · doi-reference
The Role of Electron Transfer Dissociation in Modern Proteomics
10.1021/acs.analchem.7b04810 · ExternalCitation · doi-reference
Ultraviolet Photodissociation Mass Spectrometry for Analysis of Biological Molecules
10.1021/acs.chemrev.9b00440 · ExternalCitation · doi-reference
Defining the Sarcomeric Proteoform Landscape in Ischemic Cardiomyopathy by Top-Down Proteomics
10.1021/acs.jproteome.2c00729 · ExternalCitation · doi-reference
Proteomics of Integral Membrane ProteinsTheory and Application
10.1021/cr068286z · ExternalCitation · doi-reference
Complete Protein Characterization Using Top-Down Mass Spectrometry and Ultraviolet Photodissociation
10.1021/ja4029654 · ExternalCitation · doi-reference
Electron Capture Dissociation of Multiply Charged Protein Cations. A Nonergodic Process
10.1021/ja973478k · ExternalCitation · doi-reference
Novel Strategies to Address the Challenges in Top-Down Proteomics
10.1021/jasms.1c00099 · ExternalCitation · doi-reference
Phosphorylation of Troponin I and Phospholamban during Catecholamine Stimulation of Rabbit Heart
10.1038/298182a0 · ExternalCitation · doi-reference
Proteoform: A Single Term Describing Protein Complexity
10.1038/nmeth.2369 · ExternalCitation · doi-reference
Phospholamban: A Crucial Regulator of Cardiac Contractility
10.1038/nrm1151 · ExternalCitation · doi-reference
A Photocleavable Surfactant for Top-down Proteomics
10.1038/s41592-019-0391-1 · ExternalCitation · doi-reference
Top-down Proteomics
10.1038/s43586-024-00318-2 · ExternalCitation · doi-reference
A Mutation in the Human Phospholamban Gene, Deleting Arginine 14, Results in Lethal, Hereditary Cardiomyopathy
10.1073/pnas.0510519103 · ExternalCitation · doi-reference
Palmitoyl Acyltransferase Aph2 in Cardiac Function and the Development of Cardiomyopathy
10.1073/pnas.1518368112 · ExternalCitation · doi-reference
Distinct Hypertrophic Cardiomyopathy Genotypes Result in Convergent Sarcomeric Proteoform Profiles Revealed by Top-down Proteomics
10.1073/pnas.2006764117 · ExternalCitation · doi-reference
High Sensitivity Top–down Proteomics Captures Single Muscle Cell Heterogeneity in Large Proteoforms
10.1073/pnas.2222081120 · ExternalCitation · doi-reference
Lethal, Hereditary Mutants of Phospholamban Elude Phosphorylation by Protein Kinase A
10.1074/jbc.m112.382713 · ExternalCitation · doi-reference
The Structural Basis for Phospholamban Inhibition of the Calcium Pump in Sarcoplasmic Reticulum
10.1074/jbc.m113.501585 · ExternalCitation · doi-reference
Integral Membrane Proteins: Bottom-up, Top-down and Structural Proteomics
10.1080/14789450.2017.1359545 · ExternalCitation · doi-reference
MASH Native: A Unified Solution for Native Top-down Proteomics Data Processing
10.1093/bioinformatics/btad359 · ExternalCitation · doi-reference
Dilated Cardiomyopathy and Heart Failure Caused by a Mutation in Phospholamban
10.1126/science.1081578 · ExternalCitation · doi-reference
Proteoforms as the next Proteomics Currency
10.1126/science.aat1884 · ExternalCitation · doi-reference
14–3-3 Binding Creates a Memory of Kinase Action by Stabilizing the Modified State of Phospholamban
10.1126/scisignal.aaz1436 · ExternalCitation · doi-reference
Progress in Top-Down Proteomics and the Analysis of Proteoforms
10.1146/annurev-anchem-071015-041550 · ExternalCitation · doi-reference
Drugging Membrane Protein Interactions
10.1146/annurev-bioeng-092115-025322 · ExternalCitation · doi-reference
Phospholamban: A Prominent Regulator of Myocardial Contractility
10.1161/01.res.79.6.1059 · ExternalCitation · doi-reference
Global Proteoform Alterations Across Multiple Cellular Compartments Underlie Obstructive Hypertrophic Cardiomyopathy
10.1161/circheartfailure.125.012899 · ExternalCitation · doi-reference
Modulation of Cardiac Contractility by the Phopholamban/SERCA2a Regulatome
10.1161/circresaha.111.259754 · ExternalCitation · doi-reference
Arrhythmogenic Cardiomyopathy
10.1161/circresaha.117.309345 · ExternalCitation · doi-reference
Comparison of the Structure and Function of Phospholamban and the Arginine-14 Deficient Mutant Associated with Dilated Cardiomyopathy
10.1371/journal.pone.0106746 · ExternalCitation · doi-reference
Phospholamban and Cardiac Contractility
10.3109/07853890008998837 · ExternalCitation · doi-reference
Aberrant PLN-R14del Protein Interactions Intensify SERCA2a Inhibition, Driving Impaired Ca2+ Handling and Arrhythmogenesis
10.3390/ijms23136947 · ExternalCitation · doi-reference
