Realizing the Allosteric Potential of the Tetrameric Protein Kinase A RIα Holoenzyme
about
Assembly of allosteric macromolecular switches: lessons from PKALocalization and quaternary structure of the PKA RI holoenzymeCrystal Structure of cGMP-Dependent Protein Kinase Reveals Novel Site of Interchain CommunicationStructure and Allostery of the PKA RII Tetrameric HoloenzymeElectrostatic Switch Function in the Mechanism of Protein Kinase A Iα Activation: Results of the Molecular Dynamics Simulation.Statistical Mechanics of Allosteric Enzymes.Using Markov state models to develop a mechanistic understanding of protein kinase A regulatory subunit RIα activation in response to cAMP bindingStructural insights into mis-regulation of protein kinase A in human tumors.Membrane potential and Ca2+ concentration dependence on pressure and vasoactive agents in arterial smooth muscle: A model.An Isoform-Specific Myristylation Switch Targets Type II PKA Holoenzymes to MembranesEvolution of the eukaryotic protein kinases as dynamic molecular switches.Crystal Structure of PKG I:cGMP Complex Reveals a cGMP-Mediated Dimeric Interface that Facilitates cGMP-Induced Activation.Unidirectional allostery in the regulatory subunit RIα facilitates efficient deactivation of protein kinase A.Human heart failure is accompanied by altered protein kinase A subunit expression and post-translational state.Exploring the Plasmodium falciparum cyclic-adenosine monophosphate (cAMP)-dependent protein kinase (PfPKA) as a therapeutic targetTargeted mutagenesis results in an activation of DNA methyltransferase 1 and confirms an autoinhibitory role of its RFTS domain.A tool set to map allosteric networks through the NMR chemical shift covariance analysis.Structural Basis of Analog Specificity in PKG I and II.Molecular Simulations Reveal an Unresolved Conformation of the Type IA Protein Kinase A Regulatory Subunit and Suggest Its Role in the cAMP Regulatory Mechanism.Electrostatic Interactions as Mediators in the Allosteric Activation of Protein Kinase A RIα.A Gaussian network model study suggests that structural fluctuations are higher for inactive states than active states of protein kinases.Conservation of structural fluctuations in homologous protein kinases and its implications on functional sites.Role of arginine 209 in the conformational transition of the protein kinase A regulatory subunit RIα A-domain.Switching of the folding-energy landscape governs the allosteric activation of protein kinase AA FlAsH-Based Cross-Linker to Study Protein Interactions in Living Cells
P2860
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P2860
Realizing the Allosteric Potential of the Tetrameric Protein Kinase A RIα Holoenzyme
description
2011 nî lūn-bûn
@nan
2011 թուականի Փետրուարին հրատարակուած գիտական յօդուած
@hyw
2011 թվականի փետրվարին հրատարակված գիտական հոդված
@hy
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
name
Realizing the Allosteric Potential of the Tetrameric Protein Kinase A RIα Holoenzyme
@ast
Realizing the Allosteric Potential of the Tetrameric Protein Kinase A RIα Holoenzyme
@en
Realizing the Allosteric Potential of the Tetrameric Protein Kinase A RIα Holoenzyme
@nl
type
label
Realizing the Allosteric Potential of the Tetrameric Protein Kinase A RIα Holoenzyme
@ast
Realizing the Allosteric Potential of the Tetrameric Protein Kinase A RIα Holoenzyme
@en
Realizing the Allosteric Potential of the Tetrameric Protein Kinase A RIα Holoenzyme
@nl
prefLabel
Realizing the Allosteric Potential of the Tetrameric Protein Kinase A RIα Holoenzyme
@ast
Realizing the Allosteric Potential of the Tetrameric Protein Kinase A RIα Holoenzyme
@en
Realizing the Allosteric Potential of the Tetrameric Protein Kinase A RIα Holoenzyme
@nl
P2093
P2860
P1433
P1476
Realizing the allosteric potential of the tetrameric protein kinase A RIα holoenzyme
@en
P2093
Angela J Boettcher
Jessica Bruystens
Juniper K Pennypacker
Nikki Cheung
Susan S Taylor
P2860
P304
P356
10.1016/J.STR.2010.12.005
P577
2011-02-01T00:00:00Z