A distinct interaction mode revealed by the crystal structure of the kinase p38α with the MAPK binding domain of the phosphatase MKP5
about
JNK Signaling: Regulation and Functions Based on Complex Protein-Protein PartnershipsThe family-wide structure and function of human dual-specificity protein phosphatasesProfiling Subcellular Protein Phosphatase Responses to Coxsackievirus B3 Infection of Cardiomyocytes.A high-throughput assay for phosphoprotein-specific phosphatase activity in cellular extracts.Three-dimensional docking in the MAPK p38α.Dual-specificity MAP kinase phosphatases (MKPs): shaping the outcome of MAP kinase signalling.MAP kinase modules: the excursion model and the steps that count.Interaction of kinase-interaction-motif protein tyrosine phosphatases with the mitogen-activated protein kinase ERK2Structure of human dual-specificity phosphatase 7, a potential cancer drug target.Diversity and specificity of the mitogen-activated protein kinase phosphatase-1 functions.A conserved motif in JNK/p38-specific MAPK phosphatases as a determinant for JNK1 recognition and inactivation.Label transfer reagents to probe p38 MAPK binding partnersA Toxoplasma dense granule protein, GRA24, modulates the early immune response to infection by promoting a direct and sustained host p38 MAPK activation.Structural basis for the regulation of the mitogen-activated protein (MAP) kinase p38α by the dual specificity phosphatase 16 MAP kinase binding domain in solutionMolecular basis of MAP kinase regulation.Revisiting protein kinase-substrate interactions: Toward therapeutic development.Changes in the free-energy landscape of p38α MAP kinase through its canonical activation and binding events as studied by enhanced molecular dynamics simulationsDocking interactions of hematopoietic tyrosine phosphatase with MAP kinases ERK2 and p38α.Systematic discovery of linear binding motifs targeting an ancient protein interaction surface on MAP kinases.Dual-Specificity Phosphatase 12 Targets p38 MAP Kinase to Regulate Macrophage Response to Intracellular Bacterial Infection.Expanding the horizons of microRNA bioinformatics
P2860
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P2860
A distinct interaction mode revealed by the crystal structure of the kinase p38α with the MAPK binding domain of the phosphatase MKP5
description
2011 nî lūn-bûn
@nan
2011 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած
@hyw
2011 թվականի դեկտեմբերին 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
A distinct interaction mode re ...... domain of the phosphatase MKP5
@ast
A distinct interaction mode re ...... domain of the phosphatase MKP5
@en
A distinct interaction mode re ...... domain of the phosphatase MKP5
@en-gb
A distinct interaction mode re ...... domain of the phosphatase MKP5
@nl
type
label
A distinct interaction mode re ...... domain of the phosphatase MKP5
@ast
A distinct interaction mode re ...... domain of the phosphatase MKP5
@en
A distinct interaction mode re ...... domain of the phosphatase MKP5
@en-gb
A distinct interaction mode re ...... domain of the phosphatase MKP5
@nl
prefLabel
A distinct interaction mode re ...... domain of the phosphatase MKP5
@ast
A distinct interaction mode re ...... domain of the phosphatase MKP5
@en
A distinct interaction mode re ...... domain of the phosphatase MKP5
@en-gb
A distinct interaction mode re ...... domain of the phosphatase MKP5
@nl
P2093
P2860
P921
P1433
P1476
A distinct interaction mode re ...... domain of the phosphatase MKP5
@en
P2093
Jia-Wei Wu
Yuan-Yuan Zhang
Zhi-Xin Wang
P2860
P356
10.1126/SCISIGNAL.2002241
P407
P577
2011-12-20T00:00:00Z