Pages that link to "Q73135524"
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The following pages link to Mutation and phosphorylation change the oligomeric structure of phospholamban in lipid bilayers (Q73135524):
Displaying 50 items.
- Sarcolipin regulates the activity of SERCA1, the fast-twitch skeletal muscle sarcoplasmic reticulum Ca2+-ATPase (Q24313260) (← links)
- Stoichiometry of lipid interactions with transmembrane proteins--Deduced from the 3D structures (Q24647836) (← links)
- Pit2 assemblies at the cell surface are modulated by extracellular inorganic phosphate concentration (Q24673772) (← links)
- Molecular dynamics simulations of biological membranes and membrane proteins using enhanced conformational sampling algorithms (Q26772040) (← links)
- Fluorophores, environments, and quantification techniques in the analysis of transmembrane helix interaction using FRET (Q26851539) (← links)
- Structural topology of phospholamban pentamer in lipid bilayers by a hybrid solution and solid-state NMR method (Q27667869) (← links)
- Structures of the Excited States of Phospholamban and Shifts in Their Populations upon Phosphorylation (Q27679786) (← links)
- The Structural Basis for Phospholamban Inhibition of the Calcium Pump in Sarcoplasmic Reticulum (Q27679847) (← links)
- Structural Dynamics and Topology of Phosphorylated Phospholamban Homopentamer Reveal Its Role in the Regulation of Calcium Transport (Q27680562) (← links)
- Cooperativity and specificity of association of a designed transmembrane peptide (Q30717244) (← links)
- Role of cysteine residues in structural stability and function of a transmembrane helix bundle. (Q30998001) (← links)
- Förster transfer recovery reveals that phospholamban exchanges slowly from pentamers but rapidly from the SERCA regulatory complex (Q33304620) (← links)
- The effect of epigenetic modifications on the secondary structures and possible binding positions of the N-terminal tail of histone H3 in the nucleosome: a computational study (Q33563883) (← links)
- Endoplasmic reticulum protein targeting of phospholamban: a common role for an N-terminal di-arginine motif in ER retention? (Q33633909) (← links)
- Mapping the interaction surface of a membrane protein: unveiling the conformational switch of phospholamban in calcium pump regulation. (Q33935080) (← links)
- Superinhibitory phospholamban mutants compete with Ca2+ for binding to SERCA2a by stabilizing a unique nucleotide-dependent conformational state (Q34121188) (← links)
- A fluorescence energy transfer method for analyzing protein oligomeric structure: application to phospholamban (Q34170439) (← links)
- Locating phospholamban in co-crystals with Ca(2+)-ATPase by cryoelectron microscopy (Q34176103) (← links)
- (1)H/(15)N heteronuclear NMR spectroscopy shows four dynamic domains for phospholamban reconstituted in dodecylphosphocholine micelles. (Q34186620) (← links)
- Structure-function relation of phospholamban: modulation of channel activity as a potential regulator of SERCA activity (Q34544548) (← links)
- Interactions between Ca2+-ATPase and the pentameric form of phospholamban in two-dimensional co-crystals (Q34600845) (← links)
- Phosphomimetic mutations enhance oligomerization of phospholemman and modulate its interaction with the Na/K-ATPase. (Q34685103) (← links)
- Molecular physiology of the SERCA and SPCA pumps (Q35051259) (← links)
- Phosphorylation and Mutation of Phospholamban Alter Physical Interactions With the Sarcoplasmic Reticulum Calcium Pump (Q35063543) (← links)
- How do helix-helix interactions help determine the folds of membrane proteins? Perspectives from the study of homo-oligomeric helical bundles (Q35089609) (← links)
- Phospholamban: a crucial regulator of cardiac contractility (Q35167969) (← links)
- Phospholamban phosphorylation, mutation, and structural dynamics: a biophysical approach to understanding and treating cardiomyopathy. (Q35169578) (← links)
- Modeling a spin-labeled fusion peptide in a membrane: implications for the interpretation of EPR experiments (Q35220136) (← links)
- Phospholamban binds with differential affinity to calcium pump conformers (Q35266450) (← links)
- Molecular regulation of phospholamban function and expression (Q35677260) (← links)
- Rotational dynamics of phospholamban determined by multifrequency electron paramagnetic resonance. (Q36008628) (← links)
- Protein-protein interactions in calcium transport regulation probed by saturation transfer electron paramagnetic resonance. (Q36246508) (← links)
- Activating and deactivating roles of lipid bilayers on the Ca(2+)-ATPase/phospholamban complex (Q36366452) (← links)
- Sarco(endo)plasmic reticulum calcium ATPase (SERCA) inhibition by sarcolipin is encoded in its luminal tail (Q36708601) (← links)
- SERCA2a gene therapy in heart failure: an anti-arrhythmic positive inotrope. (Q37418216) (← links)
- Isoform specificity of the Na/K-ATPase association and regulation by phospholemman (Q37446797) (← links)
- Phospholamban structural dynamics in lipid bilayers probed by a spin label rigidly coupled to the peptide backbone (Q37569037) (← links)
- Quantification of protein-lipid selectivity using FRET. (Q37711279) (← links)
- Reversal of Phospholamban Inhibition of the Sarco(endo)plasmic Reticulum Ca2+-ATPase (SERCA) Using Short, Protein-interacting RNAs and Oligonucleotide Analogs (Q38291247) (← links)
- 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 (Q38705315) (← links)
- (15)N Solid-state NMR spectroscopic studies on phospholamban at its phosphorylated form at ser-16 in aligned phospholipid bilayers (Q39239987) (← links)
- Lipid-mediated folding/unfolding of phospholamban as a regulatory mechanism for the sarcoplasmic reticulum Ca2+-ATPase (Q39269002) (← links)
- Cardiac Calcium ATPase Dimerization Measured by Cross-Linking and Fluorescence Energy Transfer (Q39366514) (← links)
- Phosphomimetic mutations increase phospholamban oligomerization and alter the structure of its regulatory complex (Q39949846) (← links)
- Structure of the 1-36 amino-terminal fragment of human phospholamban by nuclear magnetic resonance and modeling of the phospholamban pentamer (Q40140151) (← links)
- Structure of the 1-36 N-terminal fragment of human phospholamban phosphorylated at Ser-16 and Thr-17. (Q40210581) (← links)
- Time-resolved FRET reveals the structural mechanism of SERCA-PLB regulation (Q40619242) (← links)
- Spatial and dynamic interactions between phospholamban and the canine cardiac Ca2+ pump revealed with use of heterobifunctional cross-linking agents (Q40634835) (← links)
- Phospholamban domain Ib mutations influence functional interactions with the Ca2+-ATPase isoform of cardiac sarcoplasmic reticulum (Q41035597) (← links)
- Keeping calcium in its place: Ca2+-ATPase and phospholamban (Q41573472) (← links)