about
A systematic comparative and structural analysis of protein phosphorylation sites based on the mtcPTM databasePhosphorylation at intrinsically disordered regions of PAM2 motif-containing proteins modulates their interactions with PABPC1 and influences mRNA fateAllosteric activation of the protein kinase PDK1 with low molecular weight compoundsInvolvement of SIRT7 in resumption of rDNA transcription at the exit from mitosisA phosphoserine/threonine-binding pocket in AGC kinases and PDK1 mediates activation by hydrophobic motif phosphorylation.A walk-through of the yeast mating pheromone response pathwaySIRT3 deacetylates mitochondrial 3-hydroxy-3-methylglutaryl CoA synthase 2 and regulates ketone body productionAssembly of allosteric macromolecular switches: lessons from PKADrugs for allosteric sites on receptorsRegulation of the xylan-degrading apparatus of Cellvibrio japonicus by a novel two-component systemTuning a Three-Component Reaction For Trapping Kinase Substrate ComplexesIntersubunit capture of regulatory segments is a component of cooperative CaMKII activationRole of Unusual P Loop Ejection and Autophosphorylation in HipA-Mediated Persistence and Multidrug ToleranceTyrosine Phosphorylation as a Conformational Switch: A CASE STUDY OF INTEGRIN 3 CYTOPLASMIC TAILStructures and Interaction Analyses of Integrin M 2 Cytoplasmic TailsDynamics-Driven Allostery in Protein KinasesAssay development for the determination of phosphorylation stoichiometry using multiple reaction monitoring methods with and without phosphatase treatment: application to breast cancer signaling pathwaysConformational changes in protein loops and helices induced by post-translational phosphorylation.PTB domain-directed substrate targeting in a tyrosine kinase from the unicellular choanoflagellate Monosiga brevicollisPhosphorylation of the Arp2 subunit relieves auto-inhibitory interactions for Arp2/3 complex activationMutations in the catalytic loop HRD motif alter the activity and function of Drosophila Src64Phosphorelays provide tunable signal processing capabilities for the cellHow Intrinsic Molecular Dynamics Control Intramolecular Communication in Signal Transducers and Activators of Transcription Factor STAT5Archaeal protein kinases and protein phosphatases: insights from genomics and biochemistryThe importance of intrinsic disorder for protein phosphorylationCell signaling, post-translational protein modifications and NMR spectroscopyThe Tribbles 2 (TRB2) pseudokinase binds to ATP and autophosphorylates in a metal-independent mannerSurface comparison of active and inactive protein kinases identifies a conserved activation mechanismProtein kinases: evolution of dynamic regulatory proteinsAn electrostatic network and long-range regulation of Src kinasesPost-translationally-modified structures in the autophagy machinery: an integrative perspective.Prediction of Functionally Important Phospho-Regulatory Events in Xenopus laevis Oocytes.Controlling peptide folding with repulsive interactions between phosphorylated amino acids and tryptophanThe growing story of (ARABIDOPSIS) CRINKLY 4.Chemical and semisynthesis of posttranslationally modified proteins.Coordinated regulation of transcription factor Bcl11b activity in thymocytes by the mitogen-activated protein kinase (MAPK) pathways and protein sumoylation.Post-translational modifications induce significant yet not extreme changes to protein structure.Structural dynamic analysis of apo and ATP-bound IRAK4 kinaseCharge environments around phosphorylation sites in proteins.A rapid method for generation of selective Sox-based chemosensors of Ser/Thr kinases using combinatorial peptide libraries.
P2860
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P2860
description
2001 nî lūn-bûn
@nan
2001 թուականի Օգոստոսին հրատարակուած գիտական յօդուած
@hyw
2001 թվականի օգոստոսին հրատարակված գիտական հոդված
@hy
2001年の論文
@ja
2001年論文
@yue
2001年論文
@zh-hant
2001年論文
@zh-hk
2001年論文
@zh-mo
2001年論文
@zh-tw
2001年论文
@wuu
name
Structural basis for control by phosphorylation.
@ast
Structural basis for control by phosphorylation.
@en
Structural basis for control by phosphorylation.
@nl
type
label
Structural basis for control by phosphorylation.
@ast
Structural basis for control by phosphorylation.
@en
Structural basis for control by phosphorylation.
@nl
prefLabel
Structural basis for control by phosphorylation.
@ast
Structural basis for control by phosphorylation.
@en
Structural basis for control by phosphorylation.
@nl
P356
P1433
P1476
Structural basis for control by phosphorylation.
@en
P2093
P304
P356
10.1021/CR000225S
P577
2001-08-01T00:00:00Z