Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Identification of biochemical adaptations in hyper- or hypocontractile hearts from phospholamban mutant mice by expression proteomics.

Proceedings of the National Academy of Sciences of the United States of America - 24 Feb 2004

Pan Yan, Kislinger Thomas, Gramolini Anthony O, Zvaritch Elena, Kranias Evangelia G, MacLennan David H, Emili Andrew

Abstract excerpt

Phospholamban (PLN) is a critical regulator of cardiac contractility through its binding to and regulation of the activity of the sarco(endo)plasmic reticulum Ca2+ ATPase. To uncover biochemical adaptations associated with extremes of cardiac muscle contractility, we used high-throughput gel-free tandem MS to monitor differences in the relative abundance of membrane proteins in standard microsomal fractions...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Atrial Natriuretic Factor
Share to Calcium-Binding Proteins

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Enzymes

Share to Mice, Transgenic

Share to Microsomes

Share to Myocardial Contraction

Share to Myosin Heavy Chains

Share to Proteins

Source

Open in PubMed Open full text

Identifiers

PMID: 14982994
DOI: 10.1073/pnas.0308174101
PMCID: PMC356935

Genes

PLN

Variants

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Identification of biochemical adaptations in hyper- or hypocontractile hearts from phospholamban mutant mice by expression proteomics.PMID 14982994Read ↗

Comparative proteomics profiling of a phospholamban mutant mouse model of dilated cardiomyopathy reveals progressive intracellular stress responses.Semantic proximity Read ↗

Global phosphoproteomic profiling reveals perturbed signaling in a mouse model of dilated cardiomyopathy.Semantic proximity Read ↗

Protein Aggregation Is an Early Manifestation of Phospholamban p.(Arg14del)-Related Cardiomyopathy: Development of PLN-R14del-Related Cardiomyopathy.Semantic proximity Read ↗

The enhanced contractility of the phospholamban-deficient mouse heart persists with aging.Semantic proximity Read ↗

Early consequences of the phospholamban mutation PLN-R14del+/- in a transgenic mouse model.Semantic proximity Read ↗

Phospholamban Cardiomyopathy: Unveiling a Distinct Phenotype Through Heart Failure Stages Progression.Semantic proximity Read ↗

Sarcoplasmic reticulum Ca-ATPase-phospholamban interactions and dilated cardiomyopathy.Semantic proximity Read ↗

A mutation in the human phospholamban gene, deleting arginine 14, results in lethal, hereditary cardiomyopathy.Semantic proximity Read ↗

A novel human R25C-phospholamban mutation is associated with super-inhibition of calcium cycling and ventricular arrhythmia.Semantic proximity Read ↗

Hypertrophy, increased ejection fraction, and reduced Na-K-ATPase activity in phospholemman-deficient mice.Semantic proximity Read ↗

Myotonic dystrophy protein kinase phosphorylates phospholamban and regulates calcium uptake in cardiomyocyte sarcoplasmic reticulum.Semantic proximity Read ↗

Proteomic analysis of physiological versus pathological cardiac remodeling in animal models expressing mutations in myosin essential light chains.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.