Top-down high-resolution mass spectrometry of cardiac myosin binding protein C revealed that truncation alters protein phosphorylation state (Q28249208)

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Language	Label	Description	Also known as
English	Top-down high-resolution mass spectrometry of cardiac myosin binding protein C revealed that truncation alters protein phosphorylation state	scientific article

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scholarly article

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Top-down high-resolution mass spectrometry of cardiac myosin binding protein C revealed that truncation alters protein phosphorylation state (English)

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phosphorylation

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based on heuristic

inferred from title

mass spectrometry

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author name string

Ying Ge

1

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Inna N Rybakova

2

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Qingge Xu

3

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Richard L Moss

4

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language of work or name

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publication date

4 August 2009

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Proceedings of the National Academy of Sciences of the United States of America

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106

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31

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12658-63

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Crystal structure of the C1 domain of cardiac myosin binding protein-C: implications for hypertrophic cardiomyopathy

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20 March 2017

Extending top-down mass spectrometry to proteins with masses greater than 200 kilodaltons

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Chemistry. Mass spectrometry: bottom-up or top-down?

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20 March 2017

Cardiac myosin binding protein C: its role in physiology and disease

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20 March 2017

Myosin binding protein C, a phosphorylation-dependent force regulator in muscle that controls the attachment of myosin heads by its interaction with myosin S2

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Cardiac myosin-binding protein C (MyBP-C): identification of protein kinase A and protein kinase C phosphorylation sites

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A molecular map of the interactions between titin and myosin-binding protein C. Implications for sarcomeric assembly in familial hypertrophic cardiomyopathy

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Phosphorylation switches specific for the cardiac isoform of myosin binding protein-C: a modulator of cardiac contraction?

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Cardiac myosin binding protein C phosphorylation is cardioprotective

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Cardiac myosin-binding protein-C phosphorylation and cardiac function

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Alteration of myosin cross bridges by phosphorylation of myosin-binding protein C in cardiac muscle

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Proteomic analysis of post-translational modifications

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Protein kinase A-mediated phosphorylation of cMyBP-C increases proximity of myosin heads to actin in resting myocardium

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Three-dimensional structure of vertebrate cardiac muscle myosin filaments

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Decoding protein modifications using top-down mass spectrometry

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On studying protein phosphorylation patterns using bottom-up LC-MS/MS: the case of human alpha-casein

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Myosin binding protein-C: enigmatic regulator of cardiac contraction.

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Stepwise deamidation of ribonuclease A at five sites determined by top down mass spectrometry

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29 September 2017

The role of electron capture dissociation in biomolecular analysis.

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29 September 2017

Myosin crossbridge activation of cardiac thin filaments: implications for myocardial function in health and disease

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Unraveling molecular complexity of phosphorylated human cardiac troponin I by top down electron capture dissociation/electron transfer dissociation mass spectrometry

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The management of hypertrophic cardiomyopathy

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Quantitative analysis of modified proteins and their positional isomers by tandem mass spectrometry: human histone H4.

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Electron Capture Dissociation of Multiply Charged Protein Cations. A Nonergodic Process

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https://api.crossref.org/works/10.1073%2FPNAS.0813369106

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Detecting deamidation products in proteins by electron capture dissociation

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https://api.crossref.org/works/10.1073%2FPNAS.0813369106

21 January 2018

Characterization of a new qQq-FTICR mass spectrometer for post-translational modification analysis and top-down tandem mass spectrometry of whole proteins

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Localization of O-glycosylation sites in peptides by electron capture dissociation in a Fourier transform mass spectrometer

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https://pubmed.ncbi.nlm.nih.gov/19541641

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Techview: biochemistry. Biomolecule mass spectrometry

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https://pubmed.ncbi.nlm.nih.gov/19541641

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cAPK-phosphorylation controls the interaction of the regulatory domain of cardiac myosin binding protein C with myosin-S2 in an on-off fashion

1 reference

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Ablation of cardiac myosin-binding protein-C accelerates stretch activation in murine skinned myocardium

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Myosin binding protein C is differentially phosphorylated upon myocardial stunning in canine and rat hearts-- evidence for novel phosphorylation sites

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Identifiers

10.1073/PNAS.0813369106

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2009PNAS..10612658G

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