Phosphorylation releases constraints to domain motion in ERK2.
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ERK1 and ERK2 Map Kinases: Specific Roles or Functional Redundancy?Dynamics-Driven Allostery in Protein KinasesStructure-Based Assignment of Ile, Leu, and Val Methyl Groups in the Active and Inactive Forms of the Mitogen-Activated Protein Kinase Extracellular Signal-Regulated Kinase 2Structural basis of mitochondrial dysfunction in response to cytochrome c phosphorylation at tyrosine 48Active ERK2 is sufficient to mediate growth arrest and differentiation signalingStructural and Dynamic Features of F-recruitment Site Driven Substrate Phosphorylation by ERK2.Dynamics of protein kinases: insights from nuclear magnetic resonance.Slow inhibition and conformation selective properties of extracellular signal-regulated kinase 1 and 2 inhibitorsAnalysis of Multidomain Protein Dynamics.Networks of Dynamic Allostery Regulate Enzyme FunctionNMR identification of the binding surfaces involved in the Salmonella and Shigella Type III secretion tip-translocon protein-protein interactions.Extracellular-regulated kinase 2 is activated by the enhancement of hinge flexibility.Characterization of Small-Molecule Scaffolds That Bind to the Shigella Type III Secretion System Protein IpaD.A dynamic hydrophobic core orchestrates allostery in protein kinases.Dynamic Equilibrium of the Aurora A Kinase Activation Loop Revealed by Single-Molecule Spectroscopy.Synchronous opening and closing motions are essential for cAMP-dependent protein kinase A signaling.Mass spectrometric analysis of the cell surface N-glycoproteome by combining metabolic labeling and click chemistry.Survey of solution dynamics in Src kinase reveals allosteric cross talk between the ligand binding and regulatory sites.Millisecond dynamics of BTK reveal kinome-wide conformational plasticity within the apo kinase domain.Dynamic activation and regulation of the mitogen-activated protein kinase p38.Endogenous, regulatory cysteine sulfenylation of ERK kinases in response to proliferative signals.
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P2860
Phosphorylation releases constraints to domain motion in ERK2.
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article científic
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article scientifique
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articolo scientifico
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artigo científico
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bilimsel makale
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scientific article published on 03 February 2014
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vedecký článok
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vetenskaplig artikel
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videnskabelig artikel
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vědecký článek
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name
Phosphorylation releases constraints to domain motion in ERK2.
@en
Phosphorylation releases constraints to domain motion in ERK2.
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type
label
Phosphorylation releases constraints to domain motion in ERK2.
@en
Phosphorylation releases constraints to domain motion in ERK2.
@nl
prefLabel
Phosphorylation releases constraints to domain motion in ERK2.
@en
Phosphorylation releases constraints to domain motion in ERK2.
@nl
P2093
P2860
P356
P1476
Phosphorylation releases constraints to domain motion in ERK2.
@en
P2093
Akiko Tanimoto
Arthur Pardi
Natalie G Ahn
Thomas Lee
P2860
P304
P356
10.1073/PNAS.1318899111
P407
P577
2014-02-03T00:00:00Z