Synchronous opening and closing motions are essential for cAMP-dependent protein kinase A signaling. - Wikidata - wikimedia - TriplyDB

Synchronous opening and closing motions are essential for cAMP-dependent protein kinase A signaling.

Synchronous opening and closing motions are essential for cAMP-dependent protein kinase A signaling.

http://www.wikidata.org/entity/Q43054608

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Dynamics-Driven Allostery in Protein Kinases cAMP-dependent protein kinase (PKA) complexes probed by complementary differential scanning fluorimetry and ion mobility-mass spectrometry Gorge Motions of Acetylcholinesterase Revealed by Microsecond Molecular Dynamics Simulations.Mapping the Hydrogen Bond Networks in the Catalytic Subunit of Protein Kinase A Using H/D Fractionation Factors Mapping the Free Energy Landscape of PKA Inhibition and Activation: A Double-Conformational Selection Model for the Tandem cAMP-Binding Domains of PKA RIα.Phosphoryl Transfer Reaction Snapshots in Crystals: INSIGHTS INTO THE MECHANISM OF PROTEIN KINASE A CATALYTIC SUBUNIT.Dynamic Allostery Mediated by a Conserved Tryptophan in the Tec Family Kinases.Solution NMR Spectroscopy for the Study of Enzyme Allostery.Protein Allostery and Conformational Dynamics.Uncoupling Catalytic and Binding Functions in the Cyclic AMP-Dependent Protein Kinase A A Semiautomated Assignment Protocol for Methyl Group Side Chains in Large Proteins.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).A dynamic hydrophobic core orchestrates allostery in protein kinases.Mutation of a kinase allosteric node uncouples dynamics linked to phosphotransfer.Dynamically Driven Protein Allostery Exhibits Disparate Responses for Fast and Slow Motions.Altering the allosteric pathway in IGPS suppresses millisecond motions and catalytic activity Ensemble-based modeling and rigidity decomposition of allosteric interaction networks and communication pathways in cyclin-dependent kinases: Differentiating kinase clients of the Hsp90-Cdc37 chaperone.Network-based modelling and percolation analysis of conformational dynamics and activation in the CDK2 and CDK4 proteins: dynamic and energetic polarization of the kinase lobes may determine divergence of the regulatory mechanisms.CLEAVAGE ALTERS THE MOLECULAR DETERMINANTS OF PROTEIN KINASE C-δ CATALYTIC ACTIVITY.Conformational Landscape of the PRKACA-DNAJB1 Chimeric Kinase, the Driver for Fibrolamellar Hepatocellular Carcinoma.PKA-RII subunit phosphorylation precedes activation by cAMP and regulates activity termination.Probing Protein-Protein Interactions Using Asymmetric Labeling and Carbonyl-Carbon Selective Heteronuclear NMR Spectroscopy

P2860

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P2860

Synchronous opening and closing motions are essential for cAMP-dependent protein kinase A signaling.

http://www.wikidata.org/entity/Q43054608

description

2014 nî lūn-bûn

@nan

2014年の論文

@ja

2014年学术文章

@wuu

2014年学术文章

@zh

2014年学术文章

@zh-cn

2014年学术文章

@zh-hans

2014年学术文章

@zh-my

2014年学术文章

@zh-sg

2014年學術文章

@yue

2014年學術文章

@zh-hant

name

Synchronous opening and closin ...... nt protein kinase A signaling.

@en

Synchronous opening and closin ...... nt protein kinase A signaling.

@nl

type

label

Synchronous opening and closin ...... nt protein kinase A signaling.

@en

Synchronous opening and closin ...... nt protein kinase A signaling.

@nl

prefLabel

Synchronous opening and closin ...... nt protein kinase A signaling.

@en

Synchronous opening and closin ...... nt protein kinase A signaling.

@nl

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P356

J.STR.2014.09.010

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P1476

Synchronous opening and closin ...... ent protein kinase A signaling

@en

P2093

Atul K Srivastava

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

Christopher L McClendon

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

Gianluigi Veglia

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Jonggul Kim

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

Larry R Masterson

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

Leanna R McDonald

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

Susan S Taylor

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

P2860

The protein kinase complement of the human genome

Many local motions cooperate to produce the adenylate kinase conformational transition

A dynamic knockout reveals that conformational fluctuations influence the chemical step of enzyme catalysis

Assembly of allosteric macromolecular switches: lessons from PKA

Modeling conformational ensembles of slow functional motions in Pin1-WW

Crystal structure of a cAMP-dependent protein kinase mutant at 1.26A: new insights into the catalytic mechanism

Intrinsic motions along an enzymatic reaction trajectory

Conformational sampling, catalysis, and evolution of the bacterial phosphotriesterase

Dynamics connect substrate recognition to catalysis in protein kinase A

Structure and dynamics of a primordial catalytic fold generated by in vitro evolution

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1735-1743

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scholarly article

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10.1016/J.STR.2014.09.010

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12

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22

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Alessandro Cembran

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2014-11-06T00:00:00Z

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25458836

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4255147

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