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.
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SERCA1 truncated proteins unable to pump calcium reduce the endoplasmic reticulum calcium concentration and induce apoptosis.Histidine-rich Ca-binding protein interacts with sarcoplasmic reticulum Ca-ATPaseModeling 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 phospholambanTransgenic overexpression of the Ca2+-binding protein S100A1 in the heart leads to increased in vivo myocardial contractile performanceCytoplasmic interactions between phospholamban residues 1-20 and the calcium-activated ATPase of the sarcoplasmic reticulumCardiac-specific overexpression of sarcolipin inhibits sarco(endo)plasmic reticulum Ca2+ ATPase (SERCA2a) activity and impairs cardiac function in miceThe alpha-helical propensity of the cytoplasmic domain of phospholamban: a molecular dynamics simulation of the effect of phosphorylation and mutation.Förster transfer recovery reveals that phospholamban exchanges slowly from pentamers but rapidly from the SERCA regulatory complex.Locating phospholamban in co-crystals with Ca(2+)-ATPase by cryoelectron microscopySarco(endo)plasmic reticulum calcium pumps: recent advances in our understanding of structure/function and biology (review).Calmodulin kinase is a molecular switch for cardiac excitation-contraction couplingPhosphorylation and mutation of phospholamban alter physical interactions with the sarcoplasmic reticulum calcium pumpThe MLP family of cytoskeletal Z disc proteins and dilated cardiomyopathy: a stress pathway model for heart failure progression.Phospholamban binds with differential affinity to calcium pump conformersAtomic-level mechanisms for phospholamban regulation of the calcium pump.Metformin increases degradation of phospholamban via autophagy in cardiomyocytesCharacterizing phospholamban to sarco(endo)plasmic reticulum Ca2+-ATPase 2a (SERCA2a) protein binding interactions in human cardiac sarcoplasmic reticulum vesicles using chemical cross-linking.Sarcolipin protein interaction with sarco(endo)plasmic reticulum Ca2+ ATPase (SERCA) is distinct from phospholamban protein, and only sarcolipin can promote uncoupling of the SERCA pump.Regulation of Ca2+ and Na+ in normal and failing cardiac myocytes.Sarcolipin and phospholamban as regulators of cardiac sarcoplasmic reticulum Ca2+ ATPase.Determinants of frequency-dependent contraction and relaxation of mammalian myocardium.The anti-apoptotic protein HAX-1 interacts with SERCA2 and regulates its protein levels to promote cell survival.Phosphorylated phospholamban stabilizes a compact conformation of the cardiac calcium-ATPase.Allosteric regulation of SERCA by phosphorylation-mediated conformational shift of phospholambanPhospholamban modulates the functional coupling between nucleotide domains in Ca-ATPase oligomeric complexes in cardiac sarcoplasmic reticulum.Structural dynamics of muscle protein phosphorylation.Inhibition and conformational change of SERCA3b induced by Bcl-2.Phospholamban mutants compete with wild type for SERCA binding in living cells.Phosphomimetic mutations increase phospholamban oligomerization and alter the structure of its regulatory complex.Cellular trafficking of phospholamban and formation of functional sarcoplasmic reticulum during myocyte differentiation.Phospholemman phosphorylation alters its fluorescence resonance energy transfer with the Na/K-ATPase pump.Time-resolved FRET reveals the structural mechanism of SERCA-PLB regulation.Spatial and dynamic interactions between phospholamban and the canine cardiac Ca2+ pump revealed with use of heterobifunctional cross-linking agents.Characterization of calumenin-SERCA2 interaction in mouse cardiac sarcoplasmic reticulum.Structural and functional dynamics of an integral membrane protein complex modulated by lipid headgroup chargePhospholamban remains associated with the Ca2+- and Mg2+-dependent ATPase following phosphorylation by cAMP-dependent protein kinase.Coordinate downregulation of CaM kinase II and phospholamban accompanies contractile phenotype transition in the hyperthyroid rabbit soleus.Frequency-dependent acceleration of relaxation in mammalian heart: a property not relying on phospholamban and SERCA2a phosphorylation.
P2860
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P2860
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.
description
2000 nî lūn-bûn
@nan
2000年の論文
@ja
2000年学术文章
@wuu
2000年学术文章
@zh-cn
2000年学术文章
@zh-hans
2000年学术文章
@zh-my
2000年学术文章
@zh-sg
2000年學術文章
@yue
2000年學術文章
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2000年學術文章
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name
Physical interactions between ...... rgin, and are enhanced by ATP.
@en
type
label
Physical interactions between ...... rgin, and are enhanced by ATP.
@en
prefLabel
Physical interactions between ...... rgin, and are enhanced by ATP.
@en
P2093
P2860
P356
P1476
Physical interactions between ...... rgin, and are enhanced by ATP.
@en
P2093
P2860
P304
15034-15038
P356
10.1074/JBC.275.20.15034
P407
P577
2000-05-01T00:00:00Z