The structure of phosphorylated p38gamma is monomeric and reveals a conserved activation-loop conformation
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GSK-3: tricks of the trade for a multi-tasking kinaseActivation of MTK1/MEKK4 by GADD45 through induced N-C dissociation and dimerization-mediated trans autophosphorylation of the MTK1 kinase domainp38 MAPK in cardioprotection - are we there yet?Structural basis for UCN-01 (7-hydroxystaurosporine) specificity and PDK1 (3-phosphoinositide-dependent protein kinase-1) inhibitionThe Structure of the MAP2K MEK6 Reveals an Autoinhibitory DimerMitogen-activated Protein Kinase (MAPK) Phosphatase 3-mediated Cross-talk between MAPKs ERK2 and p38A Conserved Non-canonical Motif in the Pseudoactive Site of the ROP5 Pseudokinase Domain Mediates Its Effect on Toxoplasma VirulenceReciprocal allosteric regulation of p38γ and PTPN3 involves a PDZ domain-modulated complex formationA two-hybrid screen of the yeast proteome for Hsp90 interactors uncovers a novel Hsp90 chaperone requirement in the activity of a stress-activated mitogen-activated protein kinase, Slt2p (Mpk1p).ERK2 shows a restrictive and locally selective mechanism of recognition by its tyrosine phosphatase inactivators not shared by its activator MEK1Identification of the autophosphorylation sites and characterization of their effects in the protein kinase DYRK1AConformational changes in protein loops and helices induced by post-translational phosphorylation.Conservation, variability and the modeling of active protein kinasesCo-conserved MAPK features couple D-domain docking groove to distal allosteric sites via the C-terminal flanking tailComparative chemical array screening for p38γ/δ MAPK inhibitors using a single gatekeeper residue difference between p38α/β and p38γ/δConserved threonine residues within the A-loop of the receptor NIK differentially regulate the kinase function required for antiviral signalingSubstrate and docking interactions in serine/threonine protein kinasesTranslational control in plant antiviral immunityStructural and evolutionary divergence of eukaryotic protein kinases in Apicomplexa.Active mutants of the human p38alpha mitogen-activated protein kinase.Oxidative stress responses in the human fungal pathogen, Candida albicans.Determining the Functions of HIV-1 Tat and a Second Magnesium Ion in the CDK9/Cyclin T1 Complex: A Molecular Dynamics Simulation Study.Structural basis of p38α regulation by hematopoietic tyrosine phosphatase.T cell receptor-mediated activation of p38{alpha} by mono-phosphorylation of the activation loop results in altered substrate specificityHow mitogen-activated protein kinases recognize and phosphorylate their targets: A QM/MM study.Hydrogen-exchange mass spectrometry reveals activation-induced changes in the conformational mobility of p38alpha MAP kinaseHomo-oligomerization and activation of AMP-activated protein kinase are mediated by the kinase domain alphaG-helix.Monomeric and dimeric models of ERK2 in conjunction with studies on cellular localization, nuclear translocation, and in vitro analysis.Structural insight into effector proteins of Gram-negative bacterial pathogens that modulate the phosphoproteome of their host.Changes in the free-energy landscape of p38α MAP kinase through its canonical activation and binding events as studied by enhanced molecular dynamics simulationsThe crystal structure of phosphorylated MAPK13 reveals common structural features and differences in p38 MAPK family activation.New Insights into the p38γ and p38δ MAPK Pathways.Structural Basis for the Subversion of MAP Kinase Signaling by an Intrinsically Disordered Parasite Secreted Agonist.p38γ activity is required for maintenance of slow skeletal muscle sizeTwo adjacent docking sites in the yeast Hog1 mitogen-activated protein (MAP) kinase differentially interact with the Pbs2 MAP kinase kinase and the Ptp2 protein tyrosine phosphatase.Distinct patterns of activation-dependent changes in conformational mobility between ERK1 and ERK2.Phosphorylation of Tyr-176 of the yeast MAPK Hog1/p38 is not vital for Hog1 biological activity.PEA-15 binding to ERK1/2 MAPKs is required for its modulation of integrin activation.Switching on kinases: oncogenic activation of BRAF and the PDGFR family.MAPK p38: alternative and nonstressful in T cells.
P2860
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P2860
The structure of phosphorylated p38gamma is monomeric and reveals a conserved activation-loop conformation
description
1999 nî lūn-bûn
@nan
1999 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած
@hyw
1999 թվականի սեպտեմբերին հրատարակված գիտական հոդված
@hy
1999年の論文
@ja
1999年学术文章
@wuu
1999年学术文章
@zh-cn
1999年学术文章
@zh-hans
1999年学术文章
@zh-my
1999年学术文章
@zh-sg
1999年學術文章
@yue
name
The structure of phosphorylate ...... d activation-loop conformation
@ast
The structure of phosphorylate ...... d activation-loop conformation
@en
The structure of phosphorylate ...... d activation-loop conformation
@en-gb
The structure of phosphorylate ...... d activation-loop conformation
@nl
type
label
The structure of phosphorylate ...... d activation-loop conformation
@ast
The structure of phosphorylate ...... d activation-loop conformation
@en
The structure of phosphorylate ...... d activation-loop conformation
@en-gb
The structure of phosphorylate ...... d activation-loop conformation
@nl
prefLabel
The structure of phosphorylate ...... d activation-loop conformation
@ast
The structure of phosphorylate ...... d activation-loop conformation
@en
The structure of phosphorylate ...... d activation-loop conformation
@en-gb
The structure of phosphorylate ...... d activation-loop conformation
@nl
P2093
P921
P3181
P1433
P1476
The structure of phosphorylate ...... d activation-loop conformation
@en
P2093
P304
P3181
P356
10.1016/S0969-2126(99)80173-7
P407
P577
1999-09-15T00:00:00Z