Structural Basis for the Regulation of Protein Kinase A by Activation Loop Phosphorylation - Test2 - elhamkhani - TriplyDB

Structural Basis for the Regulation of Protein Kinase A by Activation Loop Phosphorylation

Structural Basis for the Regulation of Protein Kinase A by Activation Loop Phosphorylation

http://www.wikidata.org/entity/Q27677271

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PKA: lessons learned after twenty years Assembly of allosteric macromolecular switches: lessons from PKA Insights into the inhibition of the p90 ribosomal S6 kinase (RSK) by the flavonol glycoside SL0101 from the 1.5 Å crystal structure of the N-terminal domain of RSK2 with bound inhibitor.Role of N-Terminal Myristylation in the Structure and Regulation of cAMP-Dependent Protein Kinase A conserved water-mediated hydrogen bond network defines bosutinib's kinase selectivity A mechanism of global shape-dependent recognition and phosphorylation of filamin by protein kinase A Deciphering the structural basis of eukaryotic protein kinase regulation Decoding the Interactions Regulating the Active State Mechanics of Eukaryotic Protein Kinases Isoform-specific interactions between meprin metalloproteases and the catalytic subunit of protein kinase A: significance in acute and chronic kidney injury.Performance of protein disorder prediction programs on amino acid substitutions.Identification of new members of the MAPK gene family in plants shows diverse conserved domains and novel activation loop variants.Characterization, expression patterns and functional analysis of the MAPK and MAPKK genes in watermelon (Citrullus lanatus)Cotranslational cis-phosphorylation of the COOH-terminal tail is a key priming step in the maturation of cAMP-dependent protein kinase The structure of Legionella pneumophila LegK4 type four secretion system (T4SS) effector reveals a novel dimeric eukaryotic-like kinase.Evolution of the eukaryotic protein kinases as dynamic molecular switches.Identification of a hidden strain switch provides clues to an ancient structural mechanism in protein kinases O-GlcNAcylation of protein kinase A catalytic subunits enhances its activity: a mechanism linked to learning and memory deficits in Alzheimer's disease.Reciprocal regulation of PKA and Rac signaling.Influence of N-myristylation and ligand binding on the flexibility of the catalytic subunit of protein kinase A.Exploring the Plasmodium falciparum cyclic-adenosine monophosphate (cAMP)-dependent protein kinase (PfPKA) as a therapeutic target Conformational sampling in template-free protein loop structure modeling: an overview.OGlcNAcylation and phosphorylation have opposing structural effects in tau: phosphothreonine induces particular conformational order.OGlcNAcylation and phosphorylation have similar structural effects in α-helices: post-translational modifications as inducible start and stop signals in α-helices, with greater structural effects on threonine modification.Obesity-induced cardiac lipid accumulation in adult mice is modulated by G protein-coupled receptor kinase 2 levels.Characterization of a eukaryotic-like protein kinase, DspB, with an atypical catalytic loop motif from Myxococcus xanthus.Mutation of a kinase allosteric node uncouples dynamics linked to phosphotransfer.Kinase regulation by hydrophobic spine assembly in cancer.In silico evaluation of the resistance of the T790M variant of epidermal growth factor receptor kinase to cancer drug Erlotinib.Design and Profiling of a Subcellular Targeted Optogenetic cAMP-Dependent Protein Kinase.Quantitative Structure-Activity Relationship Modeling of Kinase Selectivity Profiles.Achieving a Graded Immune Response: BTK Adopts a Range of Active/Inactive Conformations Dictated by Multiple Interdomain Contacts.A dynamic mechanism for allosteric activation of Aurora kinase A by activation loop phosphorylation.An N-terminally truncated form of cyclic GMP-dependent protein kinase Iα (PKG Iα) is monomeric, autoinhibited, and provides a model for activation.Genetic code expansion and live cell imaging reveal that Thr308 phosphorylation is irreplaceable and sufficient for Akt1 activity.Mitotic phosphorylation regulates Hsp72 spindle localization by uncoupling ATP binding from substrate release

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Structural Basis for the Regulation of Protein Kinase A by Activation Loop Phosphorylation

http://www.wikidata.org/entity/Q27677271

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2012 nî lūn-bûn

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2012 թուականի Ապրիլին հրատարակուած գիտական յօդուած

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2012 թվականի ապրիլին հրատարակված գիտական հոդված

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2012年の論文

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2012年論文

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2012年論文

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2012年論文

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2012年論文

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2012年論文

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2012年论文

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Structural Basis for the Regul ...... ctivation Loop Phosphorylation

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Structural Basis for the Regul ...... ctivation Loop Phosphorylation

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Structural Basis for the Regul ...... ctivation Loop Phosphorylation

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Structural Basis for the Regul ...... ctivation Loop Phosphorylation

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Structural Basis for the Regul ...... ctivation Loop Phosphorylation

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Journal of Biological Chemistry

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Structural Basis for the Regul ...... ctivation Loop Phosphorylation

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Jie Yang

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Jon M Steichen

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Joseph A Adams

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Malik M Keshwani

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Michael Kuchinskas

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Susan S Taylor

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Trans-activation of the DNA-damage signalling protein kinase Chk2 by T-loop exchange

Activation segment dimerization: a mechanism for kinase autophosphorylation of non-consensus sites

MolProbity: all-atom contacts and structure validation for proteins and nucleic acids

Inhibition of p38 MAP kinase by utilizing a novel allosteric binding site

Crystal structure of an inactive Akt2 kinase domain

Dynamic features of cAMP-dependent protein kinase revealed by apoenzyme crystal structure

Crystal structure of a cAMP-dependent protein kinase mutant at 1.26A: new insights into the catalytic mechanism

Crystal structure of domain-swapped STE20 OSR1 kinase domain

Structural Basis of Human p70 Ribosomal S6 Kinase-1 Regulation by Activation Loop Phosphorylation

A Conserved Glu–Arg Salt Bridge Connects Coevolved Motifs That Define the Eukaryotic Protein Kinase Fold

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phosphorylation

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3340281

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