cAMP-dependent protein kinase A selects the excited state of the membrane substrate phospholamban.
about
Structures of the Excited States of Phospholamban and Shifts in Their Populations upon PhosphorylationA mechanism of global shape-dependent recognition and phosphorylation of filamin by protein kinase ADifferential dynamic engagement within 24 SH3 domain: peptide complexes revealed by co-linear chemical shift perturbation analysisProbing ground and excited states of phospholamban in model and native lipid membranes by magic angle spinning NMR spectroscopy.Solid state NMR and protein-protein interactions in membranesFLAMEnGO 2.0: an enhanced fuzzy logic algorithm for structure-based assignment of methyl group resonances.Comparison of the structure and function of phospholamban and the arginine-14 deficient mutant associated with dilated cardiomyopathy.Effects of naturally occurring arginine 14 deletion on phospholamban conformational dynamics and membrane interactionsConstitutive PKA activity is essential for maintaining the excitability and contractility in guinea pig urinary bladder smooth muscle: role of the BK channel.Unique structure and dynamics of the EphA5 ligand binding domain mediate its binding specificity as revealed by X-ray crystallography, NMR and MD simulationsPhospholamban phosphorylation, mutation, and structural dynamics: a biophysical approach to understanding and treating cardiomyopathy.Dysfunctional conformational dynamics of protein kinase A induced by a lethal mutant of phospholamban hinder phosphorylation.Rats undernourished in utero have altered Ca2+ signaling and reduced fertility in adulthood.Activating and deactivating roles of lipid bilayers on the Ca(2+)-ATPase/phospholamban complexTuning the structural coupling between the transmembrane and cytoplasmic domains of phospholamban to control sarcoplasmic reticulum Ca(2+)-ATPase (SERCA) function.Proteasome allostery as a population shift between interchanging conformersRole of conformational entropy in the activity and regulation of the catalytic subunit of protein kinase A.Allostery and binding cooperativity of the catalytic subunit of protein kinase A by NMR spectroscopy and molecular dynamics simulations.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.Uncoupling Catalytic and Binding Functions in the Cyclic AMP-Dependent Protein Kinase AProtein dynamics and function from solution state NMR spectroscopy.Capturing Invisible Motions in the Transition from Ground to Rare Excited States of T4 Lysozyme L99A.Structural basis for catalytically restrictive dynamics of a high-energy enzyme state.Mechanism of cAMP Partial Agonism in Protein Kinase G (PKG).Probing the interaction of Arg9Cys mutated phospholamban with phospholipid bilayers by solid-state NMR spectroscopy.Protein dynamics: Catch them if you can.Perturbations of Native Membrane Protein Structure in Alkyl Phosphocholine Detergents: A Critical Assessment of NMR and Biophysical Studies.Dynamic binding
P2860
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P2860
cAMP-dependent protein kinase A selects the excited state of the membrane substrate phospholamban.
description
2011 nî lūn-bûn
@nan
2011年の論文
@ja
2011年論文
@yue
2011年論文
@zh-hant
2011年論文
@zh-hk
2011年論文
@zh-mo
2011年論文
@zh-tw
2011年论文
@wuu
2011年论文
@zh
2011年论文
@zh-cn
name
cAMP-dependent protein kinase ...... brane substrate phospholamban.
@en
cAMP-dependent protein kinase ...... brane substrate phospholamban.
@nl
type
label
cAMP-dependent protein kinase ...... brane substrate phospholamban.
@en
cAMP-dependent protein kinase ...... brane substrate phospholamban.
@nl
prefLabel
cAMP-dependent protein kinase ...... brane substrate phospholamban.
@en
cAMP-dependent protein kinase ...... brane substrate phospholamban.
@nl
P2093
P2860
P1476
cAMP-dependent protein kinase ...... mbrane substrate phospholamban
@en
P2093
Gianluigi Veglia
Larry R Masterson
Michael M Mueller
P2860
P304
P356
10.1016/J.JMB.2011.06.041
P407
P577
2011-07-02T00:00:00Z