The differential regulation of p38α by the neuronal kinase interaction motif protein tyrosine phosphatases, a detailed molecular study

scientific article published on 08 August 2013

The differential regulation of p38α by the neuronal kinase interaction motif protein tyrosine phosphatases, a detailed molecular study is …
instance of (P31):
scholarly articleQ13442814

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P356DOI10.1016/J.STR.2013.07.003
P932PMC publication ID3769431
P698PubMed publication ID23932588
P5875ResearchGate publication ID255733758

P2093author name stringRebecca Page
Wolfgang Peti
Ganesan Senthil Kumar
Antoni Tortajada
Dorothy Koveal
Dana May Francis
P2860cites workPathological roles of MAPK signaling pathways in human diseasesQ37676393
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15S-Lipoxygenase-2 mediates arachidonic acid-stimulated adhesion of human breast carcinoma cells through the activation of TAK1, MKK6, and p38 MAPK.Q40401291
Two clusters of residues at the docking groove of mitogen-activated protein kinases differentially mediate their functional interaction with the tyrosine phosphatases PTP-SL and STEP.Q40768240
Docking interactions of hematopoietic tyrosine phosphatase with MAP kinases ERK2 and p38α.Q41991021
Characterization of multiple transcripts and isoforms derived from the mouse protein tyrosine phosphatase gene PtprrQ45088264
Structure of the hematopoietic tyrosine phosphatase (HePTP) catalytic domain: structure of a KIM phosphatase with phosphate bound at the active siteQ46754193
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The mouse Ptprr gene encodes two protein tyrosine phosphatases, PTP-SL and PTPBR7, that display distinct patterns of expression during neural development.Q52172816
NMR Spectroscopic Investigations of the Activated p38α Mitogen-Activated Protein KinaseQ58062006
NMR backbone assignment of the mitogen-activated protein (MAP) kinase p38Q80406521
Docking interactions induce exposure of activation loop in the MAP kinase ERK2Q83964224
A novel regulatory mechanism of MAP kinases activation and nuclear translocation mediated by PKA and the PTP-SL tyrosine phosphataseQ22010940
Cloning and expression of an inducible lymphoid-specific, protein tyrosine phosphatase (HePTPase)Q24301219
Crystal structures and inhibitor identification for PTPN5, PTPRR and PTPN7: a family of human MAPK-specific protein tyrosine phosphatasesQ24302258
Independent human MAP-kinase signal transduction pathways defined by MEK and MKK isoformsQ24312029
Determination of domain structure of proteins from X-ray solution scatteringQ24537462
Molecular characterization of a protein-tyrosine-phosphatase enriched in striatumQ24563279
Specificity of linear motifs that bind to a common mitogen-activated protein kinase docking grooveQ24610682
Crystal structure of PTP-SL/PTPBR7 catalytic domain: implications for MAP kinase regulationQ27633953
Crystal structures of MAP kinase p38 complexed to the docking sites on its nuclear substrate MEF2A and activator MKK3bQ27639263
A novel lipid binding site formed by the MAP kinase insert in p38 alphaQ27649025
p38α MAP Kinase C-Terminal Domain Binding Pocket Characterized by Crystallographic and Computational AnalysesQ27655779
The third conformation of p38α MAP kinase observed in phosphorylated p38α and in solutionQ27666193
Mitogen-activated Protein Kinase (MAPK) Phosphatase 3-mediated Cross-talk between MAPKs ERK2 and p38Q27667368
Lipid molecules induce p38α activation via a novel molecular switchQ27682881
The structure of mitogen-activated protein kinase p38 at 2.1-A resolutionQ27736668
Clustal W and Clustal X version 2.0Q27860517
HADDOCK: a protein-protein docking approach based on biochemical or biophysical informationQ27860814
Differential interaction of the tyrosine phosphatases PTP-SL, STEP and HePTP with the mitogen-activated protein kinases ERK1/2 and p38alpha is determined by a kinase specificity sequence and influenced by reducing agentsQ28116921
Crosstalk between cAMP-dependent kinase and MAP kinase through a protein tyrosine phosphataseQ28137870
A protein tyrosine phosphatase expressed within dopaminoceptive neurons of the basal ganglia and related structuresQ28260578
Extrasynaptic NMDA receptors couple preferentially to excitotoxicity via calpain-mediated cleavage of STEPQ28567752
A novel receptor-type protein tyrosine phosphatase with a single catalytic domain is specifically expressed in mouse brainQ28586532
HADDOCK versus HADDOCK: new features and performance of HADDOCK2.0 on the CAPRI targetsQ29615981
Interface analysis of the complex between ERK2 and PTP-SLQ33441372
NR2B‐NMDA receptor mediated modulation of the tyrosine phosphatase STEP regulates glutamate induced neuronal cell deathQ34559448
Resting and active states of the ERK2:HePTP complexQ35534815
Strategies to maximize heterologous protein expression in Escherichia coli with minimal costQ36564221
Structural basis of p38α regulation by hematopoietic tyrosine phosphataseQ36852670
P433issue9
P304page(s)1612-1623
P577publication date2013-08-08
P1433published inStructureQ15709970
P1476titleThe differential regulation of p38α by the neuronal kinase interaction motif protein tyrosine phosphatases, a detailed molecular study
P478volume21

Reverse relations

cites work (P2860)
Q93059776Dynamics of transcriptome changes during subcutaneous preadipocyte differentiation in ducks
Q35122900Interaction of kinase-interaction-motif protein tyrosine phosphatases with the mitogen-activated protein kinase ERK2
Q38151621Molecular basis of MAP kinase regulation
Q37626207Molecular mechanism of ERK dephosphorylation by striatal-enriched protein tyrosine phosphatase
Q51577075NMR Spectroscopy to Study MAP Kinase Binding to MAP Kinase Phosphatases.
Q34295063Protein tyrosine phosphatases as potential therapeutic targets
Q27695708Reciprocal allosteric regulation of p38γ and PTPN3 involves a PDZ domain-modulated complex formation
Q26748710Role of Striatal-Enriched Tyrosine Phosphatase in Neuronal Function
Q37201320Structural basis for the regulation of the mitogen-activated protein (MAP) kinase p38α by the dual specificity phosphatase 16 MAP kinase binding domain in solution
Q46387816The KIM-family protein-tyrosine phosphatases use distinct reversible oxidation intermediates: Intramolecular or intermolecular disulfide bond formation

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