Structural and dynamic basis of phospholamban and sarcolipin inhibition of Ca(2+)-ATPase.
about
Molecular aspects of thyroid hormone actionsThe magic of bicelles lights up membrane protein structureStructure and topology of monomeric phospholamban in lipid membranes determined by a hybrid solution and solid-state NMR approachDynamics connect substrate recognition to catalysis in protein kinase ANMR analysis of the IIb 3 cytoplasmic interaction suggests a mechanism for integrin regulationStructural topology of phospholamban pentamer in lipid bilayers by a hybrid solution and solid-state NMR methodStructural Dynamics and Topology of Phosphorylated Phospholamban Homopentamer Reveal Its Role in the Regulation of Calcium TransportA 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 membranesAn allosteric mechanism inferred from molecular dynamics simulations on phospholamban pentamer in lipid membranesTilt 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 proteinsSystems 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 muscleExpression of calcium-buffering proteins in rat intrinsic laryngeal musclesLethal 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 preparationsThe N Terminus of Sarcolipin Plays an Important Role in Uncoupling Sarco-endoplasmic Reticulum Ca2+-ATPase (SERCA) ATP Hydrolysis from Ca2+ TransportParamagnetic-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 coherencesActivating and deactivating roles of lipid bilayers on the Ca(2+)-ATPase/phospholamban complexDual 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 proteinsSarcolipin 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.
P2860
Q22306217-973B0363-F96F-46A4-8FEC-8B7575D84C29Q26991483-53F05482-23D3-4DD1-BF2A-2B52711781D6Q27655848-640EF878-DBD0-444C-AF1E-0832694167C9Q27664877-6B5C254F-F9E1-4C13-A699-110D5B1DF99AQ27666309-33F3E77A-1FA0-4191-99DE-8AE98BD3E048Q27667869-5DB172D3-AC20-4437-BBED-62990550E510Q27680562-F959B1C4-7CEC-4604-89FC-200FFE8F18CBQ30378910-925F74A2-1F2C-4A32-9ECF-B9CD05CAC38DQ30394749-B0220CF1-BC03-421A-9907-116441CC8298Q30405936-72BE5342-7F02-425B-BC84-BAF45725E16BQ30503997-489146D4-9E49-4448-8814-436AB52CB12BQ30666800-87089FB1-29F8-42FB-990F-EDAC1216F03DQ31007659-D2082BB7-7BB2-4CD0-B996-06F7EF9CD6A3Q33438716-535B95FE-739F-48DC-9DBC-796BEF9AE353Q33545365-233784BA-B5AB-4C6D-9EF8-173DF9595FA9Q33643066-EA99D755-21B8-4F25-A715-0ADAE6AC7F97Q33696035-BFDC808E-4DC5-41BF-9365-A3C6AAFC0F08Q33803663-04B262CA-F4F2-4F34-86C6-BBFE1CFC43B2Q33817922-54044877-C5EE-4567-AFCD-48E5C854081DQ33828179-2EEB25A3-3483-414F-8BB7-EBF38CD40939Q33861759-A6CE99F6-A43B-4D4E-8139-9DD6F6342645Q34355857-EED1436E-B95E-4DBB-9FBA-57EEFF6D013EQ34482238-6BCC29AD-0EE4-4BF8-A349-CD6BE54C0A84Q34582867-99BDFB3A-A4D1-4233-A1CA-53B48DA376F0Q34627450-EB14F0A2-3F86-4B1C-96BA-84419733C13CQ34702440-D31F5454-04D4-4BC5-B7D8-CDD277DC3EB1Q34881379-F23F72FB-BA06-4C3E-A952-BB29E63CF1BFQ35210442-3CF7665E-A696-4133-9BBE-AAB8B7B7D6F4Q35441442-88D4476A-F451-4656-AD26-A9B285235797Q35662355-F2B4596C-D008-443C-8F59-F9CBF49684A3Q35894280-CD10E60D-0796-4A83-BB2E-6F64B37C837DQ35894301-A4DC72C0-07A1-402D-958C-6D29CDDE3461Q36285059-08F2116B-D02E-4541-9FEF-4B82B75ABFAAQ36348438-ED724503-C000-4507-96BE-1D56B6D06D40Q36366452-EE8691A1-821F-4C97-AD94-FFEDFED6326BQ36441654-BE0E68FD-3D76-40E1-AF3E-D84FC5369A9CQ36467913-3272E26A-E9F7-433B-A03F-1F507BDBADCBQ36564069-8974EBD1-12CD-4799-840D-A4E4F97373BFQ36666112-91AD272A-D313-424E-900C-A92672CF96D1Q37090616-7E79793C-CE5C-4CAA-A9D7-E5C9E4F06068
P2860
Structural and dynamic basis of phospholamban and sarcolipin inhibition of Ca(2+)-ATPase.
description
article científic
@ca
article scientifique
@fr
articolo scientifico
@it
artigo científico
@pt
bilimsel makale
@tr
scientific article published on 15 December 2007
@en
vedecký článok
@sk
vetenskaplig artikel
@sv
videnskabelig artikel
@da
vědecký článek
@cs
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
P2093
P2860
P356
P1433
P1476
Structural and dynamic basis of phospholamban and sarcolipin inhibition of Ca(2+)-ATPase.
@en
P2093
Gianluigi Veglia
Jarrod J Buffy
Larry R Masterson
Nathaniel J Traaseth
Raffaello Verardi
P2860
P356
10.1021/BI701668V
P407
P577
2007-12-15T00:00:00Z