Phosphorylation-dependent conformational switch in spin-labeled phospholamban bound to SERCA.
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Hydrophobic imbalance in the cytoplasmic domain of phospholamban is a determinant for lethal dilated cardiomyopathyStructure and topology of monomeric phospholamban in lipid membranes determined by a hybrid solution and solid-state NMR approachStructural topology of phospholamban pentamer in lipid bilayers by a hybrid solution and solid-state NMR methodStructures of the Excited States of Phospholamban and Shifts in Their Populations upon PhosphorylationNa+/Ca2+ exchange and Na+/K+-ATPase in the heartAtomic-level characterization of the activation mechanism of SERCA by calciumProbing ground and excited states of phospholamban in model and native lipid membranes by magic angle spinning NMR spectroscopy.An allosteric mechanism inferred from molecular dynamics simulations on phospholamban pentamer in lipid membranesFörster transfer recovery reveals that phospholamban exchanges slowly from pentamers but rapidly from the SERCA regulatory complex.What can we learn from a small regulatory membrane protein?Changes in reflectin protein phosphorylation are associated with dynamic iridescence in squid.Structural dynamics and conformational equilibria of SERCA regulatory proteins in membranes by solid-state NMR restrained simulations.Phosphorylation-induced structural changes in smooth muscle myosin regulatory light chainLong-term obesity promotes alterations in diastolic function induced by reduction of phospholamban phosphorylation at serine-16 without affecting calcium handling.Phospholamban C-terminal residues are critical determinants of the structure and function of the calcium ATPase regulatory complex.Synthetic phosphopeptides enable quantitation of the content and function of the four phosphorylation states of phospholamban in cardiac muscleHigh-throughput FRET assay yields allosteric SERCA activatorsA spirocyclohexyl nitroxide amino acid spin label for pulsed EPR spectroscopy distance measurements.Phosphorylation and mutation of phospholamban alter physical interactions with the sarcoplasmic reticulum calcium pumpPhospholamban phosphorylation, mutation, and structural dynamics: a biophysical approach to understanding and treating cardiomyopathy.Molecular dynamics simulations reveal a disorder-to-order transition on phosphorylation of smooth muscle myosin.Spectroscopic validation of the pentameric structure of phospholambanRotational dynamics of phospholamban determined by multifrequency electron paramagnetic resonance.Protein-protein interactions in calcium transport regulation probed by saturation transfer electron paramagnetic resonance.CLC anion channel regulatory phosphorylation and conserved signal transduction domainsActivating and deactivating roles of lipid bilayers on the Ca(2+)-ATPase/phospholamban complexA bifunctional spin label reports the structural topology of phospholamban in magnetically-aligned bicelles.Cardiac myosin binding protein-C restricts intrafilament torsional dynamics of actin in a phosphorylation-dependent manner.Sarco(endo)plasmic reticulum calcium ATPase (SERCA) inhibition by sarcolipin is encoded in its luminal tail.Na+ transport in cardiac myocytes; Implications for excitation-contraction coupling.Allosteric regulation of SERCA by phosphorylation-mediated conformational shift of phospholambanThe Ca2+ pumps of the endoplasmic reticulum and Golgi apparatus.Protein structural dynamics revealed by site-directed spin labeling and multifrequency EPR.The spin label amino acid TOAC and its uses in studies of peptides: chemical, physicochemical, spectroscopic, and conformational aspects.Close allies in membrane protein research: cell-free synthesis and nanotechnology.Phospholamban and sarcolipin: Are they functionally redundant or distinct regulators of the Sarco(Endo)Plasmic Reticulum Calcium ATPase?Secondary structure, backbone dynamics, and structural topology of phospholamban and its phosphorylated and Arg9Cys-mutated forms in phospholipid bilayers utilizing 13C and 15N solid-state NMR spectroscopy.Functional and physical competition between phospholamban and its mutants provides insight into the molecular mechanism of gene therapy for heart failure.(15)N Solid-state NMR spectroscopic studies on phospholamban at its phosphorylated form at ser-16 in aligned phospholipid bilayers.Lipid-mediated folding/unfolding of phospholamban as a regulatory mechanism for the sarcoplasmic reticulum Ca2+-ATPase
P2860
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P2860
Phosphorylation-dependent conformational switch in spin-labeled phospholamban bound to SERCA.
description
2006 nî lūn-bûn
@nan
2006年の論文
@ja
2006年論文
@yue
2006年論文
@zh-hant
2006年論文
@zh-hk
2006年論文
@zh-mo
2006年論文
@zh-tw
2006年论文
@wuu
2006年论文
@zh
2006年论文
@zh-cn
name
Phosphorylation-dependent conf ...... phospholamban bound to SERCA.
@en
Phosphorylation-dependent conf ...... phospholamban bound to SERCA.
@nl
type
label
Phosphorylation-dependent conf ...... phospholamban bound to SERCA.
@en
Phosphorylation-dependent conf ...... phospholamban bound to SERCA.
@nl
prefLabel
Phosphorylation-dependent conf ...... phospholamban bound to SERCA.
@en
Phosphorylation-dependent conf ...... phospholamban bound to SERCA.
@nl
P2093
P1476
Phosphorylation-dependent conf ...... d phospholamban bound to SERCA
@en
P2093
Edmund C Howard
Kurt D Torgersen
Zhiwen Zhang
P304
P356
10.1016/J.JMB.2006.02.051
P407
P577
2006-03-09T00:00:00Z