Signaling through dynamic linkers as revealed by PKA - sprookjes - yvandenbroek - TriplyDB

Signaling through dynamic linkers as revealed by PKA

Signaling through dynamic linkers as revealed by PKA

http://www.wikidata.org/entity/Q30352864

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NMR Methods to Study Dynamic Allostery Dopamine Receptors and Neurodegeneration PKA RIα Homodimer Structure Reveals an Intermolecular Interface with Implications for Cooperative cAMP Binding and Carney Complex Disease A Mechanism for the Auto-inhibition of Hyperpolarization-activated Cyclic Nucleotide-gated (HCN) Channel Opening and Its Relief by cAMP Disrupting the allosteric interaction between the Plasmodium falciparum cAMP-dependent kinase and its regulatory subunit NMR Characterization of Information Flow and Allosteric Communities in the MAP Kinase p38γ NMR reveals the allosteric opening and closing of Abelson tyrosine kinase by ATP-site and myristoyl pocket inhibitors.The roles of the RIIβ linker and N-terminal cyclic nucleotide-binding domain in determining the unique structures of the type IIβ protein kinase A: a small angle x-ray and neutron scattering study.Severing of a hydrogen bond disrupts amino acid networks in the catalytically active state of the alpha subunit of tryptophan synthase.NMR 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.Using Markov state models to develop a mechanistic understanding of protein kinase A regulatory subunit RIα activation in response to cAMP binding Dysfunctional conformational dynamics of protein kinase A induced by a lethal mutant of phospholamban hinder phosphorylation.Lipid binding protein response to a bile acid library: a combined NMR and statistical approach.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 domain Parallel Allostery by cAMP and PDE Coordinates Activation and Termination Phases in cAMP Signaling.High-Affinity Interaction of the K-Ras4B Hypervariable Region with the Ras Active Site.Functionalized N,N-Diphenylamines as Potent and Selective EPAC2 Inhibitors.Unidirectional allostery in the regulatory subunit RIα facilitates efficient deactivation of protein kinase A.Allosteric linkers in cAMP signalling.Tapping the translation potential of cAMP signalling: molecular basis for selectivity in cAMP agonism and antagonism as revealed by NMR.cAMP signaling in subcellular compartments.Conformational Rigidity and Protein Dynamics at Distinct Timescales Regulate PTP1B Activity and Allostery.Digested disorder: Quarterly intrinsic disorder digest (July-August-September, 2013)Conformational recognition of an intrinsically disordered protein.Network representation of protein interactions: Theory of graph description and analysis.Role of Dynamics in the Autoinhibition and Activation of the Hyperpolarization-activated Cyclic Nucleotide-modulated (HCN) Ion Channels.Disordered Regions Flanking Ordered Domains Modulate Signaling Transduction A tool set to map allosteric networks through the NMR chemical shift covariance analysis.Discovery of Allostery in PKA Signaling.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 bradycardia Crystal structure of cGMP-dependent protein kinase Iβ cyclic nucleotide-binding-B domain : Rp-cGMPS complex reveals an apo-like, inactive conformation.Signaling at crossroads: the dialogue between PDEs and PKA is spoken in multiple languages.Control of transcriptional activity by design of charge patterning in the intrinsically disordered RAM region of the Notch receptor.Atomic view of the energy landscape in the allosteric regulation of Abl kinase.A dynamic allosteric pathway underlies Rad50 ABC ATPase function in DNA repair.Implementation of the NMR CHEmical Shift Covariance Analysis (CHESCA): A Chemical Biologist's Approach to Allostery.Regulation of HCN Ion Channels by Non-canonical Cyclic Nucleotides.

P2860

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P2860

Signaling through dynamic linkers as revealed by PKA

http://www.wikidata.org/entity/Q30352864

description

2013 nî lūn-bûn

@nan

2013 թուականի Օգոստոսին հրատարակուած գիտական յօդուած

@hyw

2013 թվականի օգոստոսին հրատարակված գիտական հոդված

@hy

2013年の論文

@ja

2013年論文

@yue

2013年論文

@zh-hant

2013年論文

@zh-hk

2013年論文

@zh-mo

2013年論文

@zh-tw

2013年论文

@wuu

name

Signaling through dynamic linkers as revealed by PKA

@ast

Signaling through dynamic linkers as revealed by PKA

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type

label

Signaling through dynamic linkers as revealed by PKA

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Signaling through dynamic linkers as revealed by PKA

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prefLabel

Signaling through dynamic linkers as revealed by PKA

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Signaling through dynamic linkers as revealed by PKA

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P1433

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P1476

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P356

PNAS.1312644110

P1433

Proceedings of the National Academy of Sciences of the United States of America

P1476

Signaling through dynamic linkers as revealed by PKA

@en

P2093

E Tyler McNicholl

http://www.w3.org/2001/XMLSchema#string

Geeta Verma

http://www.w3.org/2001/XMLSchema#string

Giuseppe Melacini

http://www.w3.org/2001/XMLSchema#string

Madoka Akimoto

http://www.w3.org/2001/XMLSchema#string

Susan S Taylor

http://www.w3.org/2001/XMLSchema#string

P2860

Dynamic and static interactions between p120 catenin and E-cadherin regulate the stability of cell-cell adhesion

Molecular characterization of a thyroid tumor-specific transforming sequence formed by the fusion of ret tyrosine kinase and the regulatory subunit RI alpha of cyclic AMP-dependent protein kinase A

NMR insights into protein allostery

Structural basis for relief of autoinhibition of the Dbl homology domain of proto-oncogene Vav by tyrosine phosphorylation

Dynamic regulation of archaeal proteasome gate opening as studied by TROSY NMR

Dynamics connect substrate recognition to catalysis in protein kinase A

Cyclic AMP Analog Blocks Kinase Activation by Stabilizing Inactive Conformation: Conformational Selection Highlights a New Concept in Allosteric Inhibitor Design

Structural basis for regulation of the Crk signaling protein by a proline switch.

Regulatory subunit of protein kinase A: structure of deletion mutant with cAMP binding domains

NMRPipe: a multidimensional spectral processing system based on UNIX pipes

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14231-14236

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scholarly article

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10.1073/PNAS.1312644110

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P433

35

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P478

110

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Rajeevan Selvaratnam

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2013-08-14T00:00:00Z

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23946424

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3761587

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