Structural and dynamic basis of phospholamban and sarcolipin inhibition of Ca(2+)-ATPase. - Wikidata - wikimedia - TriplyDB

Structural and dynamic basis of phospholamban and sarcolipin inhibition of Ca(2+)-ATPase.

Structural and dynamic basis of phospholamban and sarcolipin inhibition of Ca(2+)-ATPase.

http://www.wikidata.org/entity/Q37032523

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Molecular aspects of thyroid hormone actions The magic of bicelles lights up membrane protein structure Structure and topology of monomeric phospholamban in lipid membranes determined by a hybrid solution and solid-state NMR approach Dynamics connect substrate recognition to catalysis in protein kinase A NMR analysis of the IIb 3 cytoplasmic interaction suggests a mechanism for integrin regulation Structural topology of phospholamban pentamer in lipid bilayers by a hybrid solution and solid-state NMR method Structural Dynamics and Topology of Phosphorylated Phospholamban Homopentamer Reveal Its Role in the Regulation of Calcium Transport A refinement protocol to determine structure, topology, and depth of insertion of membrane proteins using hybrid solution and solid-state NMR restraints.On the performance of spin diffusion NMR techniques in oriented solids: prospects for resonance assignments and distance measurements from separated local field experiments.Probing ground and excited states of phospholamban in model and native lipid membranes by magic angle spinning NMR spectroscopy.Thrombospondin-1 and angiotensin II inhibit soluble guanylyl cyclase through an increase in intracellular calcium concentration.Solid state NMR and protein-protein interactions in membranes An allosteric mechanism inferred from molecular dynamics simulations on phospholamban pentamer in lipid membranes Tilt and azimuthal angles of a transmembrane peptide: a comparison between molecular dynamics calculations and solid-state NMR data of sarcolipin in lipid membranes.Proton-evolved local-field solid-state NMR studies of cytochrome b5 embedded in bicelles, revealing both structural and dynamical information.What can we learn from a small regulatory membrane protein?Effect of membrane thickness on conformational sampling of phospholamban from computer simulations.Structural dynamics and conformational equilibria of SERCA regulatory proteins in membranes by solid-state NMR restrained simulations.Sensitivity enhancement of separated local field experiments: application to membrane proteins Systems analysis of biological networks in skeletal muscle function.Superior calcium homeostasis of extraocular muscles.Synthetic phosphopeptides enable quantitation of the content and function of the four phosphorylation states of phospholamban in cardiac muscle Expression of calcium-buffering proteins in rat intrinsic laryngeal muscles Lethal Arg9Cys phospholamban mutation hinders Ca2+-ATPase regulation and phosphorylation by protein kinase A.Progesterone modulates SERCA2a expression and function in rabbit cardiomyocytes.One-sample approach to determine the relative orientations of proteins in ternary and binary complexes from residual dipolar coupling measurements.Dynamically committed, uncommitted, and quenched states encoded in protein kinase A revealed by NMR spectroscopy.Proton evolved local field solid-state nuclear magnetic resonance using Hadamard encoding: theory and application to membrane proteins.Multiple acquisition of magic angle spinning solid-state NMR experiments using one receiver: application to microcrystalline and membrane protein preparations The N Terminus of Sarcolipin Plays an Important Role in Uncoupling Sarco-endoplasmic Reticulum Ca2+-ATPase (SERCA) ATP Hydrolysis from Ca2+ Transport Paramagnetic-based NMR restraints lift residual dipolar coupling degeneracy in multidomain detergent-solubilized membrane proteins.Frequency-selective heteronuclear dephasing and selective carbonyl labeling to deconvolute crowded spectra of membrane proteins by magic angle spinning NMR.Identification of Small Ankyrin 1 as a Novel Sarco(endo)plasmic Reticulum Ca2+-ATPase 1 (SERCA1) Regulatory Protein in Skeletal Muscle.Sensitivity enhancement in static solid-state NMR experiments via single- and multiple-quantum dipolar coherences Activating and deactivating roles of lipid bilayers on the Ca(2+)-ATPase/phospholamban complex Dual acquisition magic-angle spinning solid-state NMR-spectroscopy: simultaneous acquisition of multidimensional spectra of biomacromolecules.Tuning the structural coupling between the transmembrane and cytoplasmic domains of phospholamban to control sarcoplasmic reticulum Ca(2+)-ATPase (SERCA) function.Isotope labeling for solution and solid-state NMR spectroscopy of membrane proteins 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.When detergent meets bilayer: birth and coming of age of lipid bicelles.

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Structural and dynamic basis of phospholamban and sarcolipin inhibition of Ca(2+)-ATPase.

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article científic

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article scientifique

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articolo scientifico

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artigo científico

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bilimsel makale

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scientific article published on 15 December 2007

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vedecký článok

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vetenskaplig artikel

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videnskabelig artikel

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vědecký článek

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name

Structural and dynamic basis of phospholamban and sarcolipin inhibition of Ca

@nl

Structural and dynamic basis of phospholamban and sarcolipin inhibition of Ca(2+)-ATPase.

@en

type

label

Structural and dynamic basis of phospholamban and sarcolipin inhibition of Ca

@nl

Structural and dynamic basis of phospholamban and sarcolipin inhibition of Ca(2+)-ATPase.

@en

prefLabel

Structural and dynamic basis of phospholamban and sarcolipin inhibition of Ca

@nl

Structural and dynamic basis of phospholamban and sarcolipin inhibition of Ca(2+)-ATPase.

@en

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Structural and dynamic basis of phospholamban and sarcolipin inhibition of Ca(2+)-ATPase.

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P2093

Gianluigi Veglia

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Jarrod J Buffy

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Kim N Ha

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Larry R Masterson

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Lei Shi

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Nathaniel J Traaseth

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Raffaello Verardi

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P2860

Structure and orientation of sarcolipin in lipid environments

Sarcolipin regulates the activity of SERCA1, the fast-twitch skeletal muscle sarcoplasmic reticulum Ca2+-ATPase

Characterization of the gene encoding human sarcolipin (SLN), a proteolipid associated with SERCA1: absence of structural mutations in five patients with Brody disease

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

Sarcolipin regulates sarco(endo)plasmic reticulum Ca2+-ATPase (SERCA) by binding to transmembrane helices alone or in association with phospholamban

Crystal structure of the calcium pump of sarcoplasmic reticulum at 2.6 A resolution

Structural changes in the calcium pump accompanying the dissociation of calcium

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

Determination of membrane protein structure and dynamics by magic-angle-spinning solid-state NMR spectroscopy.

Secondary structure and orientation of phospholamban reconstituted in supported bilayers from polarized attenuated total reflection FTIR spectroscopy.

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3-13

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10.1021/BI701668V

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1

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2007-12-15T00:00:00Z

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18081313

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