Identification of novel point mutations in ERK2 that selectively disrupt binding to MEK1
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S-sulfhydration of MEK1 leads to PARP-1 activation and DNA damage repairCharacterization of OSR1, a member of the mammalian Ste20p/germinal center kinase subfamilyTumor suppressor density-enhanced phosphatase-1 (DEP-1) inhibits the RAS pathway by direct dephosphorylation of ERK1/2 kinasesRadial spoke protein 3 is a mammalian protein kinase A-anchoring protein that binds ERK1/2Selectivity of docking sites in MAPK kinasesThe Ste5 scaffold directs mating signaling by catalytically unlocking the Fus3 MAP kinase for activationAmylin inhibits bone resorption while the calcitonin receptor controls bone formation in vivoRecognition of ERK MAP kinase by PEA-15 reveals a common docking site within the death domain and death effector domainStructural and functional analysis of phosphorylation-specific binders of the kinase ERK from designed ankyrin repeat protein librariesConformation-Selective ATP-Competitive Inhibitors Control Regulatory Interactions and Noncatalytic Functions of Mitogen-Activated Protein KinasesPseudorabies virus tegument protein Us2 recruits the mitogen-activated protein kinase extracellular-regulated kinase (ERK) to membranes through interaction with the ERK common docking domain.IQGAP1 binds ERK2 and modulates its activityERK2 shows a restrictive and locally selective mechanism of recognition by its tyrosine phosphatase inactivators not shared by its activator MEK1Differential regulation and properties of MAPKsThe N-terminal domain of ERK1 accounts for the functional differences with ERK2Subdomain VIII is a specificity-determining region in MEKK1Rac-PAK signaling stimulates extracellular signal-regulated kinase (ERK) activation by regulating formation of MEK1-ERK complexesNesca, a novel adapter, translocates to the nuclear envelope and regulates neurotrophin-induced neurite outgrowth.Reverse two-hybrid screening identifies residues of JNK required for interaction with the kinase interaction motif of JNK-interacting protein-1.A mitochondrial kinase complex is essential to mediate an ERK1/2-dependent phosphorylation of a key regulatory protein in steroid biosynthesis.Computational insights for the discovery of non-ATP competitive inhibitors of MAP kinasesCharacterization of ERK docking domain inhibitors that induce apoptosis by targeting Rsk-1 and caspase-9.Phosphorylation of the transcription factor Ets-1 by ERK2: rapid dissociation of ADP and phospho-Ets-1.Insights into regulation of human Schwann cell proliferation by Erk1/2 via a MEK-independent and p56Lck-dependent pathway from leprosy bacilli.Docking sites on mitogen-activated protein kinase (MAPK) kinases, MAPK phosphatases and the Elk-1 transcription factor compete for MAPK binding and are crucial for enzymic activity.Dual-specificity MAP kinase phosphatases (MKPs): shaping the outcome of MAP kinase signalling.Epitope-guided engineering of monobody binders for in vivo inhibition of Erk-2 signaling.Solution NMR insights into docking interactions involving inactive ERK2Signalling specificity of Ser/Thr protein kinases through docking-site-mediated interactions.Small-molecule inhibitors of ERK-mediated immediate early gene expression and proliferation of melanoma cells expressing mutated BRafEvolutionary constraints associated with functional specificity of the CMGC protein kinases MAPK, CDK, GSK, SRPK, DYRK, and CK2alpha.Analysis of crystal structure of Arabidopsis MPK6 and generation of its mutants with higher activity.Exploiting conformational ensembles in modeling protein-protein interactions on the proteome scale.Fast regulation of AP-1 activity through interaction of lamin A/C, ERK1/2, and c-Fos at the nuclear envelopeVariants of the yeast MAPK Mpk1 are fully functional independently of activation loop phosphorylation.Docking of PRAK/MK5 to the atypical MAPKs ERK3 and ERK4 defines a novel MAPK interaction motif.Monomeric and dimeric models of ERK2 in conjunction with studies on cellular localization, nuclear translocation, and in vitro analysis.Phosphorylation or Mutation of the ERK2 Activation Loop Alters Oligonucleotide Binding.Phosphorylation meets nuclear import: a review.Phosphorylation of phosphoprotein enriched in astrocytes (PEA-15) regulates extracellular signal-regulated kinase-dependent transcription and cell proliferation.
P2860
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P2860
Identification of novel point mutations in ERK2 that selectively disrupt binding to MEK1
description
2002 nî lūn-bûn
@nan
2002 թուականի Ապրիլին հրատարակուած գիտական յօդուած
@hyw
2002 թվականի ապրիլին հրատարակված գիտական հոդված
@hy
2002年の論文
@ja
2002年論文
@yue
2002年論文
@zh-hant
2002年論文
@zh-hk
2002年論文
@zh-mo
2002年論文
@zh-tw
2002年论文
@wuu
name
Identification of novel point mutations in ERK2 that selectively disrupt binding to MEK1
@ast
Identification of novel point mutations in ERK2 that selectively disrupt binding to MEK1
@en
Identification of novel point mutations in ERK2 that selectively disrupt binding to MEK1
@nl
type
label
Identification of novel point mutations in ERK2 that selectively disrupt binding to MEK1
@ast
Identification of novel point mutations in ERK2 that selectively disrupt binding to MEK1
@en
Identification of novel point mutations in ERK2 that selectively disrupt binding to MEK1
@nl
prefLabel
Identification of novel point mutations in ERK2 that selectively disrupt binding to MEK1
@ast
Identification of novel point mutations in ERK2 that selectively disrupt binding to MEK1
@en
Identification of novel point mutations in ERK2 that selectively disrupt binding to MEK1
@nl
P2860
P3181
P356
P1476
Identification of novel point mutations in ERK2 that selectively disrupt binding to MEK1
@en
P2093
Angelique W Whitehurst
Fred L Robinson
P2860
P304
14844-14852
P3181
P356
10.1074/JBC.M107776200
P407
P577
2002-01-31T00:00:00Z