Mitogen-activated Protein Kinase (MAPK) Phosphatase 3-mediated Cross-talk between MAPKs ERK2 and p38
about
Design principles underpinning the regulatory diversity of protein kinasesCrystal structure of the p38α MAP kinase in complex with a docking peptide from TAB1Reciprocal allosteric regulation of p38γ and PTPN3 involves a PDZ domain-modulated complex formationCo-conserved MAPK features couple D-domain docking groove to distal allosteric sites via the C-terminal flanking tail(±)-Japonones A and B, two pairs of new enantiomers with anti-KSHV activities from Hypericum japonicumHydrogen peroxide primes heart regeneration with a derepression mechanism.The p38β mitogen-activated protein kinase possesses an intrinsic autophosphorylation activity, generated by a short region composed of the α-G helix and MAPK insert.Dual-specificity MAP kinase phosphatases (MKPs): shaping the outcome of MAP kinase signalling.Design, Synthesis, and Biological Evaluation of Tetra-Substituted Thiophenes as Inhibitors of p38α MAPK.p38γ Mitogen-activated protein kinase signals through phosphorylating its phosphatase PTPH1 in regulating ras protein oncogenesis and stress response.Tighter αC-helix-αL16-helix interactions seem to make p38α less prone to activation by autophosphorylation than Hog1.p38β Mitogen-Activated Protein Kinase Modulates Its Own Basal Activity by Autophosphorylation of the Activating Residue Thr180 and the Inhibitory Residues Thr241 and Ser261Analysis of crystal structure of Arabidopsis MPK6 and generation of its mutants with higher activity.The differential regulation of p38α by the neuronal kinase interaction motif protein tyrosine phosphatases, a detailed molecular studyMolecular mechanism of ERK dephosphorylation by striatal-enriched protein tyrosine phosphatase.Molecular basis of MAP kinase regulation.Changes in the free-energy landscape of p38α MAP kinase through its canonical activation and binding events as studied by enhanced molecular dynamics simulationsDUSP6 regulates drug sensitivity by modulating DNA damage response.The crystal structure of phosphorylated MAPK13 reveals common structural features and differences in p38 MAPK family activation.DEF pocket in p38α facilitates substrate selectivity and mediates autophosphorylation.Functional analysis of Arabidopsis immune-related MAPKs uncovers a role for MPK3 as negative regulator of inducible defences.p38α MAP kinase phosphorylates RCAN1 and regulates its interaction with calcineurin.Structural Studies of ERK2 Protein Complexes.Dynamic activation and regulation of the mitogen-activated protein kinase p38.Allosteric enhancement of MAP kinase p38α's activity and substrate selectivity by docking interactions.Productive induced metastability in allosteric modulation of kinase function.NMR Spectroscopic Investigations of the Activated p38α Mitogen-Activated Protein Kinase
P2860
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P2860
Mitogen-activated Protein Kinase (MAPK) Phosphatase 3-mediated Cross-talk between MAPKs ERK2 and p38
description
2011 nî lūn-bûn
@nan
2011 թուականի Մայիսին հրատարակուած գիտական յօդուած
@hyw
2011 թվականի մայիսին հրատարակված գիտական հոդված
@hy
2011年の論文
@ja
2011年論文
@yue
2011年論文
@zh-hant
2011年論文
@zh-hk
2011年論文
@zh-mo
2011年論文
@zh-tw
2011年论文
@wuu
name
Mitogen-activated Protein Kina ...... alk between MAPKs ERK2 and p38
@ast
Mitogen-activated Protein Kina ...... alk between MAPKs ERK2 and p38
@en
Mitogen-activated Protein Kina ...... alk between MAPKs ERK2 and p38
@nl
type
label
Mitogen-activated Protein Kina ...... alk between MAPKs ERK2 and p38
@ast
Mitogen-activated Protein Kina ...... alk between MAPKs ERK2 and p38
@en
Mitogen-activated Protein Kina ...... alk between MAPKs ERK2 and p38
@nl
prefLabel
Mitogen-activated Protein Kina ...... alk between MAPKs ERK2 and p38
@ast
Mitogen-activated Protein Kina ...... alk between MAPKs ERK2 and p38
@en
Mitogen-activated Protein Kina ...... alk between MAPKs ERK2 and p38
@nl
P2093
P2860
P3181
P356
P1476
Mitogen-activated Protein Kina ...... alk between MAPKs ERK2 and p38
@en
P2093
Jia-Wei Wu
Yuan-Yuan Zhang
Zhi-Xin Wang
P2860
P304
P3181
P356
10.1074/JBC.M110.203786
P407
P577
2011-05-06T00:00:00Z