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GenomicsFast skeletal myosin binding protein-C expression exacerbates dysfunction in heart failure
Fast skeletal myosin binding protein-C expression exacerbates dysfunction in heart failure
PRJNA1477636 | ENA
GenomicsFast skeletal myosin binding protein-C regulates fast skeletal muscle contraction
Fast skeletal myosin binding protein-C regulates fast skeletal muscle contraction
PRJNA674604 | ENA
GenomicsAmino terminus of cardiac myosin binding protein-C regulates cardiac contractility
Amino terminus of cardiac myosin binding protein-C regulates cardiac contractility
PRJNA716300 | ENA
Proteomicsroad therapeutic benefit of myosin inhibition in hypertrophic cardiomyopathy
Myosin inhibitor mavacamten is the first targeted treatment available for hypertrophic cardiomyopathy (HCM), a disease caused by hundreds of genetic variants that affect mainly sarcomeric myosin and its negative regulator cardiac myosin-binding protein C (cMyBP-C, encoded by MYBPC3). Here, we have ...
ORGANISM(S): Mus musculus (Mouse) 
2026-06-02 | PXD076207 | Pride
Hypertrophic cardiomyopathy Myosin inhibition 
ProteomicsIdentification of phosphorylation and other post-translational modifications in the central C4-C5 domains of murine cardiac myosin binding protein C
Cardiac myosin binding protein C (cMyBPC) is a critical multidomain protein that modulates myosin cross bridge behavior and cardiac contractility. cMyBPC is principally regulated by phosphorylation of the residues within the M-domain of its N-terminus. However, not much is known about the phosphoryl...
ORGANISM(S): Mus musculus (Mouse) 
2022-05-04 | PXD031262 | Pride
Post translational modification Cardiac myosin binding protein c Mass spectrometry 
ProteomicsHuman MyBP-C PKA-treated C0-C2 LC-MSMS
Cardiac myosin-binding protein C (cMyBP-C) is a thick filament–associated protein that influences actin–myosin interactions. cMyBP-C alters myofilament structure and contractile properties in a protein kinase A (PKA) phosphorylation–dependent manner. To determine the effects of cMyBP-C and its phosp...
ORGANISM(S): Homo sapiens (Human) 
2019-09-26 | PXD015391 | Pride
Human Lc-msms Myosin binding protein c Cmybp-c Phosphorylated Pka C0-c2 C0c2 
ProteomicsCharacterization of the Cardiac Myosin Binding Protein-C Phosphoproteome in Healthy and Failing Human Hearts
Introduction: Cardiac myosin binding protein-C (cMyBP-C) becomes dephosphorylated in the failing heart and reduced phosphorylation-dependent regulation of cMyBP-C has been implicated in contractile dysfunction. To date, several phosphorylation sites have been identified for human cMyBP-C; however, ...
ORGANISM(S): Mus musculus (Mouse) Homo sapiens (Human) 
2013-05-01 | PXD000158 | Pride
Phosphoprotein Phosphoproteome Mass spectrometry Cardiac myosin binding protein c Cmybpc Cardiac 
ProteomicsFast skeletal myosin binding protein-C regulates fast skeletal muscle contraction
Myosin-binding protein C (MyBP-C) is a thick filament regulatory protein found exclusively in the C-zone of the A band in the sarcomeres of vertebrate striated muscle. Cardiac, slow skeletal and fast skeletal MyBP-C (fMyBP-C) paralogs perform different functions. However, the functional role of fMyB...
ORGANISM(S): Mus musculus (Mouse) 
2021-04-09 | PXD022316 | Pride
Lc ms/ms Proteomics Skeletal myosin binding protein-c Muscle 
TranscriptomicsFast skeletal myosin binding protein-C expression exacerbates dysfunction in heart failure
RNA sequencing was performed to investigate the role of fast skeletal myosin binding protein-C (fMyBP-C) in cardiac pathology and heart failure. fMyBP-C, a paralog of cardiac myosin binding protein-C (cMyBP-C), is upregulated in diseased mouse hearts. To determine its functional consequences, we gen...
ORGANISM(S): Mus musculus 
2026-09-30 | GSE335235 | GEO
TranscriptomicsFast skeletal myosin binding protein-C regulates fast skeletal muscle contraction
Fast skeletal myosin binding protein-C (fMyBP-C) is one of three MyBP-C paralogs and is predominantly expressed in fast skeletal muscle. Mutations in the gene that encodes fMyBP-C, MYBPC2, is associated with distal arthrogryposis, while fMyBP-C protein is reduced in diseased muscle. However, the fun...
ORGANISM(S): Mus musculus 
2020-11-30 | GSE160827 | GEO
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