Controlling the inhibition of the sarcoplasmic Ca2+-ATPase by tuning phospholamban structural dynamics. - Wikidata - wikimedia - TriplyDB

Controlling the inhibition of the sarcoplasmic Ca2+-ATPase by tuning phospholamban structural dynamics.

Controlling the inhibition of the sarcoplasmic Ca2+-ATPase by tuning phospholamban structural dynamics.

http://www.wikidata.org/entity/Q45871651

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Structural topology of phospholamban pentamer in lipid bilayers by a hybrid solution and solid-state NMR method Structures of the Excited States of Phospholamban and Shifts in Their Populations upon Phosphorylation Structural Dynamics and Topology of Phosphorylated Phospholamban Homopentamer Reveal Its Role in the Regulation of Calcium Transport Molecular targets in heart failure gene therapy: current controversies and translational perspectives Probing ground and excited states of phospholamban in model and native lipid membranes by magic angle spinning NMR spectroscopy.Tilt and azimuthal angles of a transmembrane peptide: a comparison between molecular dynamics calculations and solid-state NMR data of sarcolipin in lipid membranes.What can we learn from a small regulatory membrane protein?Structural dynamics and conformational equilibria of SERCA regulatory proteins in membranes by solid-state NMR restrained simulations.Effects of naturally occurring arginine 14 deletion on phospholamban conformational dynamics and membrane interactions Phospholamban phosphorylation, mutation, and structural dynamics: a biophysical approach to understanding and treating cardiomyopathy.Atomic-level mechanisms for phospholamban regulation of the calcium pump.Rheostatic Regulation of the SERCA/Phospholamban Membrane Protein Complex Using Non-Coding RNA and Single-Stranded DNA oligonucleotides.Protein-protein interactions in calcium transport regulation probed by saturation transfer electron paramagnetic resonance.Activating and deactivating roles of lipid bilayers on the Ca(2+)-ATPase/phospholamban complex Tuning the structural coupling between the transmembrane and cytoplasmic domains of phospholamban to control sarcoplasmic reticulum Ca(2+)-ATPase (SERCA) function.Cardiac myosin binding protein-C restricts intrafilament torsional dynamics of actin in a phosphorylation-dependent manner.Heteronuclear Adiabatic Relaxation Dispersion (HARD) for quantitative analysis of conformational dynamics in proteins.Structural and dynamic basis of phospholamban and sarcolipin inhibition of Ca(2+)-ATPase.Allosteric regulation of SERCA by phosphorylation-mediated conformational shift of phospholamban Phospholamban modulates the functional coupling between nucleotide domains in Ca-ATPase oligomeric complexes in cardiac sarcoplasmic reticulum.Structural dynamics of muscle protein phosphorylation.Reversal of Phospholamban Inhibition of the Sarco(endo)plasmic Reticulum Ca2+-ATPase (SERCA) Using Short, Protein-interacting RNAs and Oligonucleotide Analogs.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 Phospholamban mutants compete with wild type for SERCA binding in living cells.Phospholamban oligomerization, quaternary structure, and sarco(endo)plasmic reticulum calcium ATPase binding measured by fluorescence resonance energy transfer in living cells.Probing excited states and activation energy for the integral membrane protein phospholamban by NMR CPMG relaxation dispersion experiments.Accurate quantitation of phospholamban phosphorylation by immunoblot.cAMP-dependent protein kinase A selects the excited state of the membrane substrate phospholamban.Structural and functional dynamics of an integral membrane protein complex modulated by lipid headgroup charge 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.1H-detected MAS solid-state NMR experiments enable the simultaneous mapping of rigid and dynamic domains of membrane proteins.Perturbations of Native Membrane Protein Structure in Alkyl Phosphocholine Detergents: A Critical Assessment of NMR and Biophysical Studies.

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Controlling the inhibition of the sarcoplasmic Ca2+-ATPase by tuning phospholamban structural dynamics.

http://www.wikidata.org/entity/Q45871651

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2007 nî lūn-bûn

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2007年の論文

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2007年学术文章

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Controlling the inhibition of ...... pholamban structural dynamics.

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Controlling the inhibition of ...... pholamban structural dynamics.

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Controlling the inhibition of ...... pholamban structural dynamics.

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Controlling the inhibition of ...... pholamban structural dynamics.

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P1476

Controlling the inhibition of ...... spholamban structural dynamics

@en

P2093

Gianluigi Veglia

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Jamillah Zamoon

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Kim N Ha

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Nathaniel J Traaseth

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Raffaello Verardi

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P2860

A mutation in the human phospholamban gene, deleting arginine 14, results in lethal, hereditary cardiomyopathy.

Modeling of the inhibitory interaction of phospholamban with the Ca2+ ATPase.

NMR solution structure and topological orientation of monomeric phospholamban in dodecylphosphocholine micelles

Backbone dynamics of a free and phosphopeptide-complexed Src homology 2 domain studied by 15N NMR relaxation

Transmembrane helix M6 in sarco(endo)plasmic reticulum Ca(2+)-ATPase forms a functional interaction site with phospholamban. Evidence for physical interactions at other sites

Cardiac excitation-contraction coupling

Relationship between nuclear magnetic resonance chemical shift and protein secondary structure

Heteronuclear three-dimensional NMR spectroscopy of the inflammatory protein C5a

Overexpression, purification, and characterization of recombinant Ca-ATPase regulators for high-resolution solution and solid-state NMR studies.

Sites of regulatory interaction between calcium ATPases and phospholamban.

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37205-37214

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scholarly article

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10.1074/JBC.M704056200

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51

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282

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Alessandro Cembran

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2007-09-30T00:00:00Z

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17908690

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