A model for agonism and antagonism in an ancient and ubiquitous cAMP-binding domain.
about
Cyclic AMP Analog Blocks Kinase Activation by Stabilizing Inactive Conformation: Conformational Selection Highlights a New Concept in Allosteric Inhibitor DesignThe auto-inhibitory role of the EPAC hinge helix as mapped by NMRSignaling through dynamic linkers as revealed by PKAA generalized allosteric mechanism for cis-regulated cyclic nucleotide binding domains.Allosteric communication between cAMP binding sites in the RI subunit of protein kinase A revealed by NMRNMR mapping of protein conformational landscapes using coordinated behavior of chemical shifts upon ligand binding.Active site coupling in PDE:PKA complexes promotes resetting of mammalian cAMP signaling.Cyclic AMP- and (Rp)-cAMPS-induced conformational changes in a complex of the catalytic and regulatory (RI{alpha}) subunits of cyclic AMP-dependent protein kinase.Dynamically driven ligand selectivity in cyclic nucleotide binding domains.The projection analysis of NMR chemical shifts reveals extended EPAC autoinhibition determinants.Mapping the Free Energy Landscape of PKA Inhibition and Activation: A Double-Conformational Selection Model for the Tandem cAMP-Binding Domains of PKA RIα.Allostery through the computational microscope: cAMP activation of a canonical signalling domainCyclic AMP-induced conformational changes in mycobacterial protein acetyltransferases.Parallel Allostery by cAMP and PDE Coordinates Activation and Termination Phases in cAMP Signaling.Signaling through cAMP and cAMP-dependent protein kinase: diverse strategies for drug design.Role of conformational entropy in the activity and regulation of the catalytic subunit of protein kinase A.Communication between tandem cAMP binding domains in the regulatory subunit of protein kinase A-Ialpha as revealed by domain-silencing mutations.Role of Dynamics in the Autoinhibition and Activation of the Hyperpolarization-activated Cyclic Nucleotide-modulated (HCN) Ion Channels.Mechanism of cAMP Partial Agonism in Protein Kinase G (PKG).Free energy landscape remodeling of the cardiac pacemaker channel explains the molecular basis of familial sinus bradycardiaCrystal structure of cGMP-dependent protein kinase Iβ cyclic nucleotide-binding-B domain : Rp-cGMPS complex reveals an apo-like, inactive conformation.Chemical tools selectively target components of the PKA system.Characterization of a cyclic nucleotide-activated K(+) channel and its lipid environment by using solid-state NMR spectroscopy.Regulation of HCN Ion Channels by Non-canonical Cyclic Nucleotides.Structural dynamics in the activation of Epac.
P2860
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P2860
A model for agonism and antagonism in an ancient and ubiquitous cAMP-binding domain.
description
2006 nî lūn-bûn
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2006年の論文
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name
A model for agonism and antagonism in an ancient and ubiquitous cAMP-binding domain.
@en
A model for agonism and antagonism in an ancient and ubiquitous cAMP-binding domain.
@nl
type
label
A model for agonism and antagonism in an ancient and ubiquitous cAMP-binding domain.
@en
A model for agonism and antagonism in an ancient and ubiquitous cAMP-binding domain.
@nl
prefLabel
A model for agonism and antagonism in an ancient and ubiquitous cAMP-binding domain.
@en
A model for agonism and antagonism in an ancient and ubiquitous cAMP-binding domain.
@nl
P2860
P356
P1476
A model for agonism and antagonism in an ancient and ubiquitous cAMP-binding domain
@en
P2093
Giuseppe Melacini
P2860
P304
P356
10.1074/JBC.M607706200
P407
P50
P577
2006-10-30T00:00:00Z