Mechanism of activation of ERK2 by dual phosphorylation.
about
Activation segment dimerization: a mechanism for kinase autophosphorylation of non-consensus sitesMolecular mechanism of Aurora A kinase autophosphorylation and its allosteric activation by TPX2Dynamics-Driven Allostery in Protein KinasesIdentification of novel point mutations in ERK2 that selectively disrupt binding to MEK1Different domains of the mitogen-activated protein kinases ERK3 and ERK2 direct subcellular localization and upstream specificity in vivo.Phosphorylation-dependent changes in structure and dynamics in ERK2 detected by SDSL and EPR.Transgenic analysis of the Leishmania MAP kinase MPK10 reveals an auto-inhibitory mechanism crucial for stage-regulated activity and parasite viability.In vivo activation of protein kinase A in Schizosaccharomyces pombe requires threonine phosphorylation at its activation loop and is dependent on PDK1Monophosphothreonyl extracellular signal-regulated kinases 1 and 2 (ERK1/2) are formed endogenously in intact cardiac myocytes and are enzymically active.Mixed-lineage kinase control of JNK and p38 MAPK pathways.The energy landscape of adenylate kinase during catalysis.Assignment of backbone resonances in a eukaryotic protein kinase - ERK2 as a representative example.Mek1 kinase is regulated to suppress double-strand break repair between sister chromatids during budding yeast meiosisDynamics of protein kinases: insights from nuclear magnetic resonance.Slow inhibition and conformation selective properties of extracellular signal-regulated kinase 1 and 2 inhibitorsThe protein kinase promiscuities in the cancer-preventive mechanisms of NSAIDs.Phosphorylation or Mutation of the ERK2 Activation Loop Alters Oligonucleotide Binding.Phosphorylation releases constraints to domain motion in ERK2.Phosphorylation-dependent regulation of plant chromatin and chromatin-associated proteins.Extracellular-regulated kinase 2 is activated by the enhancement of hinge flexibility.Selective aptamer-based control of intraneuronal signalingA bipartite mechanism for ERK2 recognition by its cognate regulators and substrates.The complete pathway for catalytic activation of the mitogen-activated protein kinase, ERK2.The activity of the extracellular signal-regulated kinase 2 is regulated by differential phosphorylation in the activation loop.Structural basis for peptide binding in protein kinase A. Role of glutamic acid 203 and tyrosine 204 in the peptide-positioning loop.Phosphorylation of Numb family proteins. Possible involvement of Ca2+/calmodulin-dependent protein kinases.Structural Studies of ERK2 Protein Complexes.How tyrosine 15 phosphorylation inhibits the activity of cyclin-dependent kinase 2-cyclin A.
P2860
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P2860
Mechanism of activation of ERK2 by dual phosphorylation.
description
2001 nî lūn-bûn
@nan
2001 թուականի Յունուարին հրատարակուած գիտական յօդուած
@hyw
2001 թվականի հունվարին հրատարակված գիտական հոդված
@hy
2001年の論文
@ja
2001年論文
@yue
2001年論文
@zh-hant
2001年論文
@zh-hk
2001年論文
@zh-mo
2001年論文
@zh-tw
2001年论文
@wuu
name
Mechanism of activation of ERK2 by dual phosphorylation.
@ast
Mechanism of activation of ERK2 by dual phosphorylation.
@en
type
label
Mechanism of activation of ERK2 by dual phosphorylation.
@ast
Mechanism of activation of ERK2 by dual phosphorylation.
@en
prefLabel
Mechanism of activation of ERK2 by dual phosphorylation.
@ast
Mechanism of activation of ERK2 by dual phosphorylation.
@en
P2860
P356
P1476
Mechanism of activation of ERK2 by dual phosphorylation.
@en
P2860
P304
P356
10.1074/JBC.M008137200
P407
P577
2001-01-01T00:00:00Z