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phospholamban


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phospholamban

phospholamban

Regional expression of phospholamban in the human heart

Combined phospholamban ablation and SERCA1a overexpression result in a new hyperdynamic cardiac state

Hypertrophy and functional alterations in hyperdynamic phospholamban-knockout mouse hearts under chronic aortic stenosis

Role of phosphorylation of Thr17 residue of phospholamban in mechanical recovery during hypercapnic acidosis

Phospholamban gene ablation improves calcium transients but not cardiac function in a heart failure model

Role of phospholamban phosphorylation on Thr17 in cardiac physiological and pathological conditions

Regulation of sarcoplasmic reticulum Ca2+-ATPase and phospholamban in the failing and nonfailing heart

Delayed phospholamban phosphorylation in post-conditioned heart favours Ca2+ normalization and contributes to protection

Ablation of phospholamban and sarcolipin results in cardiac hypertrophy and decreased cardiac contractility

Targeting of phospholamban by peroxynitrite decreases β-adrenergic stimulation in cardiomyocytes

Inhibition of phospholamban phosphorylation by O-GlcNAcylation: implications for diabetic cardiomyopathy

682 Phospholamban is critically involved in beta-adrenergic receptor induced cardiac hypertrophy and failure

Structural and functional implications of the phospholamban hinge domain: impaired SR Ca2+ uptake as a primary cause of heart failure

Messenger RNA expression and immunological quantification of phospholamban and SR-Ca2+-ATPase in failing and nonfailing human hearts

Thyroid hormones increase the contractility but suppress the effects of β-adrenergic agonist by decreasing phospholamban expression in rat atria

Reduced level of serine16 phosphorylated phospholamban in the failing rat myocardium: a major contributor to reduced SERCA2 activity

Mutational screening of phospholamban gene in hypertrophic and idiopathic dilated cardiomyopathy and functional study of the PLN –42 C>G mutation

 

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An integral membrane protein (a homopentamer with subunits of 52 aa) that is the endogenous regulator of the calcium ATPase of sarcoplasmic reticulum (SERCA). Phosphorylation by protein kinase A blocks the inhibition which can be reversed by protein phosphatase 1 dephosphorylation. Mutations affect control of cardiac muscle and cause dilated cardiomyopathy. See sarcolipin.

Subjects: Medicine and Health — Chemistry.


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