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anti-Human Phospholamban Antikörper:
anti-Mouse (Murine) Phospholamban Antikörper:
anti-Rat (Rattus) Phospholamban Antikörper:
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Chicken Monoclonal Phospholamban Primary Antibody für ICC, IF - ABIN152737
Liu, Hu, Wang, Xu, Wang, Gong, Mansoor, Lee, Hou, Zeng, Zhang, Jerosch-Herold, Guo, Bache, Zhang: Autologous stem cell transplantation for myocardial repair. in American journal of physiology. Heart and circulatory physiology 2004
Show all 5 Pubmed References
Human Polyclonal Phospholamban Primary Antibody für WB - ABIN1882182
Fujii, Zarain-Herzberg, Willard, Tada, MacLennan: Structure of the rabbit phospholamban gene, cloning of the human cDNA, and assignment of the gene to human chromosome 6. in The Journal of biological chemistry 1991
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Human Polyclonal Phospholamban Primary Antibody für ELISA, WB - ABIN4345330
Møller, Pham, Gustafsson, Hedley, Ersbøll, Bundgaard, Andersen, Torp-Pedersen, Køber, Christiansen: The role of Lamin A/C mutations in Danish patients with idiopathic dilated cardiomyopathy. in European journal of heart failure 2009
Hearts from patients with a p. Arg14del PLN mutation have a pattern of Right Ventricle Fibrofatty Replacement and Left Ventricular Fibrosis with fatty changes mostly in the posterolateral wall, independently of clinical presentation.
LMOD1 (zeige LMOD1 Antikörper), SYNPO2 (zeige SYNPO2 Antikörper), PDLIM7 (zeige PDLIM7 Antikörper), PLN, and SYNM (zeige SYNM Antikörper) down-regulation reflect the altered phenotype of smooth muscle cells in vascular disease and could be early sensitive markers of SMC (zeige DYM Antikörper) dedifferentiation.
microRNAs (miRNAs) 1 and 21 bind PLN strongly and relieve PLN inhibition of SERCA (zeige ATP2A3 Antikörper) to a greater extent than a similar length random sequence RNA mixture.
Data suggest phospholamban (PLN) gene is a rare cause of cardiomyopathy in African patients.
Phospholamban and sarcolipin (zeige SLN Antikörper) are membrane proteins that differentially regulate SERCA (zeige ATP2A3 Antikörper) function. (Review)
PLN may be a key molecular player in rigid substrate-induced cellular hypertrophy in eosinophilic esophagitis.
These data suggest that PLN is, at least partially, oligo-ubiquitinated at Lys (zeige LYZ Antikörper)(3) and degraded through Ser (zeige SIGLEC1 Antikörper)(16)-phosphorylation-mediated poly-ubiquitination during heart failure.
hereditary mutants of phospholamban are associated with heart failure [review]
PLN pentamers reduce phosphorylation of monomers at baseline and delay monomer phosphorylation upon PKA stimulation leading to increased interaction of PLN monomers with SERCA2a (zeige ATP2A2 Antikörper).
Phospholamban R14del mutation carriers are at high risk for malignant ventricular arrhythmias and end-stage heart failure, with left ventricular ejection fraction <45% and sustained or nonsustained ventricular tachycardia as independent risk factors.
Phosphorylation of PLB induces spatial rearrangements between the N- and P-domain elements of proximal Ca-ATPase (zeige CA-P60A Antikörper).
Molecular dynamics simulations of phospholamban in solution and in membrane bilayer show two main features: the presence of two well-defined helical domains at the N- and C-termini, and large-amplitude rigid-body motions of these domains.
The expression of SLN (zeige SLN Antikörper) and PLB mRNA and protein relative to SERCA1 (zeige ATP2A1 Antikörper) or SERCA2 (zeige ATP2A2 Antikörper) was assessed in ventricle, atrium, and skeltal msucle of mouse, rat, rabbit and pig.
A single-dose injection of PLN-targeting locked nucleic acid antisense oligonucleotide improved contractility in pressure overload-induced cardiac dysfunction.
PLN overexpression is associated with severe muscle atrophy and weakness.
the commercially available overexpressing phospholamban mouse phenotypically resembles human Centronuclear myopathy and could be used as a model to test potential mechanisms and therapeutic strategies.
Cardioprotective effects of H2S are mediated through acGMP/PKG (zeige PRKG1 Antikörper)/phospholamban pathway.
combined deletion of Phd2 (zeige EGLN1 Antikörper) and Phd3 (zeige EGLN3 Antikörper) dramatically decreased expression of phospholamban (PLN), resulted in sustained activation of calcium/calmodulin-activated kinase II (CaMKII (zeige CAMK2G Antikörper)), and sensitized mice to chronic beta-adrenergic stress-induced myocardial injury
the N termini of SLN (zeige SLN Antikörper) and PLB influence their respective unique functions
CaMKII (zeige CAMK2G Antikörper)-dependent increase in PLN phosphorylation during reperfusion opposes rather than contributes to ischemia/reperfusion damage.
TNAP (zeige ALPL Antikörper) plays a role in governing the phosphorylation status of phospholamban in the sarcoplasmic reticulum.
Acute expression of R9C mutation of phospholamban in cardiomyocytes was positively inotropic/lusitropic.
Ca(2 (zeige CA2 Antikörper)+) and PLB phosphorylation relieve SERCA (zeige ATP2A3 Antikörper)-PLB inhibition by distinct mechanisms, but both are achieved primarily by structural changes within the SERCA (zeige ATP2A3 Antikörper)-PLB complex, not by dissociation of that complex.
Phosphorylated phospholamban stabilizes a unique conformation of SERCA (zeige ATP2A3 Antikörper) that is characterized by a compact architecture.
Data suggest that phospholamban PLN's conformational equilibrium is central to maintain sarcoplasmic reticulum Ca(2+)-ATPase (zeige CA-P60A Antikörper) SERCA's apparent Ca(2 (zeige CA2 Antikörper)+) affinity within a physiological window.
demonstrate that the role of Arg(9) in phospholamban function is multifaceted: it is important for inhibition of SERCA (zeige ATP2A3 Antikörper), it increases the efficiency of phosphorylation, and it is critical for protein kinase A recognition
The interaction energies between the N-terminal helix of phospholamban and different POPC lipid/cholesterol bilayers quantitatively confirm its stronger interaction with a higher cholesterol-containing membrane.
The lipid bilayer composition influences the regulation of SERCA (zeige ATP2A3 Antikörper) by PLN.
Phospholamban overexpression in rabbit ventricular myocytes does not alter sarcoplasmic reticulum Ca transport.
The protein encoded by this gene is found as a pentamer and is a major substrate for the cAMP-dependent protein kinase in cardiac muscle. The encoded protein is an inhibitor of cardiac muscle sarcoplasmic reticulum Ca(2+)-ATPase in the unphosphorylated state, but inhibition is relieved upon phosphorylation of the protein. The subsequent activation of the Ca(2+) pump leads to enhanced muscle relaxation rates, thereby contributing to the inotropic response elicited in heart by beta-agonists. The encoded protein is a key regulator of cardiac diastolic function. Mutations in this gene are a cause of inherited human dilated cardiomyopathy with refractory congestive heart failure.
, cardiac phospholamban