Phosphoryl Transfer by Protein Kinase A Is Captured in a Crystal Lattice - Wikidata - wikimedia - TriplyDB

Phosphoryl Transfer by Protein Kinase A Is Captured in a Crystal Lattice

Phosphoryl Transfer by Protein Kinase A Is Captured in a Crystal Lattice

http://www.wikidata.org/entity/Q27676687

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Molecular Features of Product Release for the PKA Catalytic Cycle Single Turnover Autophosphorylation Cycle of the PKA RIIβ Holoenzyme Decoding the Interactions Regulating the Active State Mechanics of Eukaryotic Protein Kinases Retroviral DNA Integration cAMP-dependent protein kinase (PKA) complexes probed by complementary differential scanning fluorimetry and ion mobility-mass spectrometry Phosphoribosyl Diphosphate (PRPP): Biosynthesis, Enzymology, Utilization, and Metabolic Significance.Dynamic architecture of a protein kinase.Molecular basis for small molecule inhibition of G protein-coupled receptor kinases Inhibition of the ANT(2")-Ia resistance enzyme and rescue of aminoglycoside antibiotic activity by synthetic α-hydroxytropolones.Mapping the Hydrogen Bond Networks in the Catalytic Subunit of Protein Kinase A Using H/D Fractionation Factors Phosphoryl Transfer Reaction Snapshots in Crystals: INSIGHTS INTO THE MECHANISM OF PROTEIN KINASE A CATALYTIC SUBUNIT.Functional Role of Histidine in the Conserved His-x-Asp Motif in the Catalytic Core of Protein Kinases.Divalent Metal Ions Mg²⁺ and Ca²⁺ Have Distinct Effects on Protein Kinase A Activity and Regulation Structural Basis for Noncanonical Substrate Recognition of Cofilin/ADF Proteins by LIM Kinases A new autoinhibited kinase conformation reveals a salt-bridge switch in kinase activation.An investigation into the role of ATP in the mammalian pre-mRNA 3' cleavage reaction The Carboxy-terminus of BAK1 regulates kinase activity and is required for normal growth of Arabidopsis.Uncoupling Catalytic and Binding Functions in the Cyclic AMP-Dependent Protein Kinase A Understanding how cAMP-dependent protein kinase can catalyze phosphoryl transfer in the presence of Ca2+ and Sr2+: a QM/MM study.A QM/MM study of Kemptide phosphorylation catalyzed by protein kinase A. The role of Asp166 as a general acid/base catalyst.A dynamic hydrophobic core orchestrates allostery in protein kinases.Synchronous opening and closing motions are essential for cAMP-dependent protein kinase A signaling.Distinct structural mechanisms determine substrate affinity and kinase activity of protein kinase Cα.Divalent metal ions control activity and inhibition of protein kinases.A QM/MM study of the associative mechanism for the phosphorylation reaction catalyzed by protein kinase A and its D166A mutant.ATP Analogs in Protein Kinase Research

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P2860

Phosphoryl Transfer by Protein Kinase A Is Captured in a Crystal Lattice

http://www.wikidata.org/entity/Q27676687

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2013 nî lūn-bûn

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2013 թուականի Մարտին հրատարակուած գիտական յօդուած

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2013 թվականի մարտին հրատարակված գիտական հոդված

@hy

2013年の論文

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2013年論文

@yue

2013年論文

@zh-hant

2013年論文

@zh-hk

2013年論文

@zh-mo

2013年論文

@zh-tw

2013年论文

@wuu

name

Phosphoryl Transfer by Protein Kinase A Is Captured in a Crystal Lattice

@ast

Phosphoryl Transfer by Protein Kinase A Is Captured in a Crystal Lattice

@en

Phosphoryl Transfer by Protein Kinase A Is Captured in a Crystal Lattice

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type

label

Phosphoryl Transfer by Protein Kinase A Is Captured in a Crystal Lattice

@ast

Phosphoryl Transfer by Protein Kinase A Is Captured in a Crystal Lattice

@en

Phosphoryl Transfer by Protein Kinase A Is Captured in a Crystal Lattice

@nl

prefLabel

Phosphoryl Transfer by Protein Kinase A Is Captured in a Crystal Lattice

@ast

Phosphoryl Transfer by Protein Kinase A Is Captured in a Crystal Lattice

@en

Phosphoryl Transfer by Protein Kinase A Is Captured in a Crystal Lattice

@nl

P1433

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Journal of the American Chemical Society

P1476

Phosphoryl Transfer by Protein Kinase A Is Captured in a Crystal Lattice

@en

P2093

Adam C Bastidas

http://www.w3.org/2001/XMLSchema#string

Jian Wu

http://www.w3.org/2001/XMLSchema#string

Jon M Steichen

http://www.w3.org/2001/XMLSchema#string

Michael S Deal

http://www.w3.org/2001/XMLSchema#string

Susan S Taylor

http://www.w3.org/2001/XMLSchema#string

Yurong Guo

http://www.w3.org/2001/XMLSchema#string

P2860

Crystal structure of an activated Akt/protein kinase B ternary complex with GSK3-peptide and AMP-PNP

CASK Functions as a Mg2+-independent neurexin kinase

The protein kinase complement of the human genome

Crystal structures of the catalytic domain of human protein kinase associated with apoptosis and tumor suppression

Crystal structure of a transition state mimic of the catalytic subunit of cAMP-dependent protein kinase

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

PKA-I holoenzyme structure reveals a mechanism for cAMP-dependent activation

Structural and biochemical characterization of the KRLB region in insulin receptor substrate-2

Crystal structure of the catalytic subunit of cyclic adenosine monophosphate-dependent protein kinase

Comparative surface geometry of the protein kinase family

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4788-98

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scholarly article

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613506

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10.1021/JA312237Q

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12

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135

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2013-03-27T00:00:00Z

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23458248

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3663052

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