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Phospholamban: a tiny protein with a prominent role in the regulation of cardiac relaxation and contractility

Mattiazzi, Ramona Alicia; Mundiña, Cecilia Beatriz; Vittone, Leticia Beatriz (SAFIS, 2010-11)

Phospholamban (PLN) is a small sarcoplasmic reticulum (SR) protein that in the dephosphorylated state tonically inhibits the SR Ca2+-ATPase (SERCA2a). Different type of evidence to be described, points to PLN as a crucial ...

Immunodetection of phosphorylation sites gives new insights into the mechanisms underlying phospholamban phosphorylation in the intact heart

Mundiña-Weilenmann, Cecilia; Vittone, Leticia Beatriz; Ortale, Manuel; Chiappe de Cingolani, Gladys Ethel; Mattiazzi, Alicia Ramona (1996)

CaMKII regulation of phospholamban and SR Ca<SUP>2+</SUP> load

Mattiazzi, Alicia Ramona; Kranias, Evangelia G. (2011)

Phospholamban: a tiny protein with a prominent role in the regulation of cardiac relaxation and contractility

Mattiazzi, Alicia Ramona; Mundiña-Weilenmann, Cecilia; Vittone, Leticia (2010)

Role of Ca2+-calmodulin dependent phospholamban phosphorylation on the relaxant effect of β-adrenergic agonists

Vittone, Leticia Beatriz; Mundiña-Weilenmann, Cecilia; Chiappe de Cingolani, Gladys Ethel; Mattiazzi, Alicia Ramona (1993)

Phospholamban phosphorylation sites enhance the recovery of intracellular Ca2+ after perfusion arrest in isolated, perfused mouse heart

Valverde, Carlos Alfredo; Mundiña-Weilenmann, Cecilia; Reyes, Mariano; Kranias, Evangelia G.; Escobar, Ariel L.; Mattiazzi, Alicia Ramona (2006)

CaMKLL regulation of phospholamban and SR Ca2 load

Mattiazzi, Ramona Alicia; Kranias, Evangelia G. (Elsevier Science Inc, 2011-05)

Phospholamban (PLN) is a small phosphoprotein in the cardiac sarcoplasmic reticulum (SR). Dephosphorylated PLN tonically inhibits the SR Ca2 -ATPase (SERCA2a), and phosphorylation of PLN, at either Ser16 by PKA or Thr17 ...

Mechanisms involved in the acidosis enhancement of the isoproterenol-induced phosphorylation of phospholamban in the intact heart

Vittone, Leticia Beatriz; Mundiña-Weilenmann, Cecilia; Said, María Matilde; Mattiazzi, Alicia Ramona (1998)

Tracking nitroxyl-derived posttranslational modifications of phospholamban in cardiac myocytes

Mundiña, Cecilia Beatriz; Mattiazzi, Ramona Alicia (Rockefeller University Press, 2019-04-22)

Cardiovascular disease is the leading cause of morbidity and mortality worldwide. Calcium (Ca2+) mishandling is one of the most striking abnormalities in this wide spectrum of pathologies, among which heart failure (HF) ...

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

Mattiazzi, Alicia Ramona; Mundiña-Weilenmann, Cecilia; Guoxiang, Chu; Vittone, Leticia; Kranias, Evangelia (2005)

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Phospholamban: a tiny protein with a prominent role in the regulation of cardiac relaxation and contractility

Immunodetection of phosphorylation sites gives new insights into the mechanisms underlying phospholamban phosphorylation in the intact heart

CaMKII regulation of phospholamban and SR Ca<SUP>2+</SUP> load

Phospholamban: a tiny protein with a prominent role in the regulation of cardiac relaxation and contractility

Role of Ca2+-calmodulin dependent phospholamban phosphorylation on the relaxant effect of β-adrenergic agonists

Phospholamban phosphorylation sites enhance the recovery of intracellular Ca2+ after perfusion arrest in isolated, perfused mouse heart

CaMKLL regulation of phospholamban and SR Ca2 load

Mechanisms involved in the acidosis enhancement of the isoproterenol-induced phosphorylation of phospholamban in the intact heart

Tracking nitroxyl-derived posttranslational modifications of phospholamban in cardiac myocytes

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