Phospholamban domain Ib mutations influence functional interactions with the Ca2+-ATPase isoform of cardiac sarcoplasmic reticulum.
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Modeling of the inhibitory interaction of phospholamban with the Ca2+ ATPase.Phospholamban domain IB forms an interaction site with the loop between transmembrane helices M6 and M7 of sarco(endo)plasmic reticulum Ca2+ ATPasesSarcolipin regulates sarco(endo)plasmic reticulum Ca2+-ATPase (SERCA) by binding to transmembrane helices alone or in association with phospholambanThe Structural Basis for Phospholamban Inhibition of the Calcium Pump in Sarcoplasmic ReticulumStructural Dynamics and Topology of Phosphorylated Phospholamban Homopentamer Reveal Its Role in the Regulation of Calcium TransportTransmembrane helix M6 in sarco(endo)plasmic reticulum Ca(2+)-ATPase forms a functional interaction site with phospholamban. Evidence for physical interactions at other sitesThe anti-apoptotic protein HAX-1 is a regulator of cardiac functionEndoplasmic reticulum protein targeting of phospholamban: a common role for an N-terminal di-arginine motif in ER retention?Mapping the interaction surface of a membrane protein: unveiling the conformational switch of phospholamban in calcium pump regulation.Superinhibitory phospholamban mutants compete with Ca2+ for binding to SERCA2a by stabilizing a unique nucleotide-dependent conformational state.Locating phospholamban in co-crystals with Ca(2+)-ATPase by cryoelectron microscopyMapping the energy surface of transmembrane helix-helix interactionsPhosphorylation and mutation of phospholamban alter physical interactions with the sarcoplasmic reticulum calcium pumpRegulation of the sarcoplasmic reticulum calcium pump by divergent phospholamban isoforms in zebrafish.Characterizing phospholamban to sarco(endo)plasmic reticulum Ca2+-ATPase 2a (SERCA2a) protein binding interactions in human cardiac sarcoplasmic reticulum vesicles using chemical cross-linking.Identification of Small Ankyrin 1 as a Novel Sarco(endo)plasmic Reticulum Ca2+-ATPase 1 (SERCA1) Regulatory Protein in Skeletal Muscle.Activating and deactivating roles of lipid bilayers on the Ca(2+)-ATPase/phospholamban complexTuning the structural coupling between the transmembrane and cytoplasmic domains of phospholamban to control sarcoplasmic reticulum Ca(2+)-ATPase (SERCA) function.Sarco(endo)plasmic reticulum calcium ATPase (SERCA) inhibition by sarcolipin is encoded in its luminal tail.Structural and dynamic basis of phospholamban and sarcolipin inhibition of Ca(2+)-ATPase.Calmodulin in a heartbeat.Phospholamban mutants compete with wild type for SERCA binding in living cells.Spatial and dynamic interactions between phospholamban and the canine cardiac Ca2+ pump revealed with use of heterobifunctional cross-linking agents.Alanine-scanning mutagenesis of the sixth transmembrane segment of gastric H+,K+-ATPase alpha-subunit.Physical interactions between phospholamban and sarco(endo)plasmic reticulum Ca2+-ATPases are dissociated by elevated Ca2+, but not by phospholamban phosphorylation, vanadate, or thapsigargin, and are enhanced by ATP.Cardiac-specific overexpression of a superinhibitory pentameric phospholamban mutant enhances inhibition of cardiac function in vivo.Probing excited states and activation energy for the integral membrane protein phospholamban by NMR CPMG relaxation dispersion experiments.Co-reconstitution of phospholamban mutants with the Ca-ATPase reveals dependence of inhibitory function on phospholamban structure.The transgenic expression of highly inhibitory monomeric forms of phospholamban in mouse heart impairs cardiac contractility.Solid-state (2)H and (15)N NMR studies of side-chain and backbone dynamics of phospholamban in lipid bilayers: investigation of the N27A mutation.Role of leucine 31 of phospholamban in structural and functional interactions with the Ca2+ pump of cardiac sarcoplasmic reticulum.Controlling the inhibition of the sarcoplasmic Ca2+-ATPase by tuning phospholamban structural dynamics.A phospholamban-tethered cardiac Ca2+ pump reveals stoichiometry and dynamic interactions between the two proteins.Phospholamban as a crucial determinant of the inotropic response of human pluripotent stem cell-derived ventricular cardiomyocytes and engineered 3-dimensional tissue constructs.Solid-state NMR reveals structural changes in phospholamban accompanying the functional regulation of Ca2+-ATPase
P2860
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P2860
Phospholamban domain Ib mutations influence functional interactions with the Ca2+-ATPase isoform of cardiac sarcoplasmic reticulum.
description
1998 nî lūn-bûn
@nan
1998年の論文
@ja
1998年論文
@yue
1998年論文
@zh-hant
1998年論文
@zh-hk
1998年論文
@zh-mo
1998年論文
@zh-tw
1998年论文
@wuu
1998年论文
@zh
1998年论文
@zh-cn
name
Phospholamban domain Ib mutati ...... ardiac sarcoplasmic reticulum.
@en
type
label
Phospholamban domain Ib mutati ...... ardiac sarcoplasmic reticulum.
@en
prefLabel
Phospholamban domain Ib mutati ...... ardiac sarcoplasmic reticulum.
@en
P2093
P2860
P356
P1476
Phospholamban domain Ib mutati ...... ardiac sarcoplasmic reticulum.
@en
P2093
P2860
P304
14238-14241
P356
10.1074/JBC.273.23.14238
P407
P577
1998-06-01T00:00:00Z