Pre-steady-state kinetic analysis of cAMP-dependent protein kinase using rapid quench flow techniques.
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The crystal structure of a phosphorylase kinase peptide substrate complex: kinase substrate recognition.Structural Basis for the Regulation of Protein Kinase A by Activation Loop PhosphorylationInsights into the Phosphoryl Transfer Catalyzed by cAMP-Dependent Protein Kinase: An X-ray Crystallographic Study of Complexes with Various Metals and Peptide Substrate SP20Metal-Free cAMP-Dependent Protein Kinase Can Catalyze Phosphoryl TransferPhosphatidylinositol 4,5-bisphosphate triggers activation of focal adhesion kinase by inducing clustering and conformational changesSingle Turnover Autophosphorylation Cycle of the PKA RIIβ HoloenzymeApplying the brakes to multisite SR protein phosphorylation: substrate-induced effects on the splicing kinase SRPK1Flow-based systems for rapid and high-precision enzyme kinetics studiesLigand-induced global transitions in the catalytic domain of protein kinase A.A transition path ensemble study reveals a linchpin role for Mg(2+) during rate-limiting ADP release from protein kinase A.Development of a microplate-based, electrophoretic fluorescent protein kinase a assay: comparison with filter-binding and fluorescence polarization assay formats.Using Markov state models to develop a mechanistic understanding of protein kinase A regulatory subunit RIα activation in response to cAMP bindingBacillus anthracis o-succinylbenzoyl-CoA synthetase: reaction kinetics and a novel inhibitor mimicking its reaction intermediatePhosphatase specificity and pathway insulation in signaling networks.Catalytic control in the EGF receptor and its connection to general kinase regulatory mechanisms.Intra-domain Cross-talk Regulates Serine-arginine Protein Kinase 1-dependent Phosphorylation and Splicing Function of Transformer 2β1Conserved water molecules contribute to the extensive network of interactions at the active site of protein kinase APhosphoryl Transfer Reaction Snapshots in Crystals: INSIGHTS INTO THE MECHANISM OF PROTEIN KINASE A CATALYTIC SUBUNIT.Evolution of the eukaryotic protein kinases as dynamic molecular switches.How does activation loop phosphorylation modulate catalytic activity in the cAMP-dependent protein kinase: a theoretical study.Divalent Metal Ions Mg²⁺ and Ca²⁺ Have Distinct Effects on Protein Kinase A Activity and RegulationRelease of ADP from the catalytic subunit of protein kinase A: a molecular dynamics simulation study.The precise sequence of FGF receptor autophosphorylation is kinetically driven and is disrupted by oncogenic mutations.Partitioning RS domain phosphorylation in an SR protein through the CLK and SRPK protein kinases.Molecular mechanisms of drug resistance in tyrosine kinases cAbl and cKit.A stress-induced calcium-dependent protein kinase from Mesembryanthemum crystallinum phosphorylates a two-component pseudo-response regulator.Mutations in conserved regions 1, 2, and 3 of Raf-1 that activate transforming activity.A QM/MM study of Kemptide phosphorylation catalyzed by protein kinase A. The role of Asp166 as a general acid/base catalyst.Electronic measurements of single-molecule catalysis by cAMP-dependent protein kinase A.Insights into nucleotide binding in protein kinase A using fluorescent adenosine derivatives.Mutation of a kinase allosteric node uncouples dynamics linked to phosphotransfer.Splicing kinase SRPK1 conforms to the landscape of its SR protein substrate.Examination of an active-site electrostatic node in the cAMP-dependent protein kinase catalytic subunitCatalytic activity of the anaerobic tyrosine lyase required for thiamine biosynthesis in Escherichia coli.Probing the catalytic mechanism of the insulin receptor kinase with a tetrafluorotyrosine-containing peptide substrate.SRC tail phosphorylation is limited by structural changes in the regulatory tyrosine kinase Csk.Chemical clamping allows for efficient phosphorylation of the RNA carrier protein Npl3.Phosphoryl transfer step in the C-terminal Src kinase controls Src recognition.The Eleventh Datta Lecture. The structural basis for substrate recognition and control by protein kinases.The mechanism of p21-activated kinase 2 autoactivation.
P2860
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P2860
Pre-steady-state kinetic analysis of cAMP-dependent protein kinase using rapid quench flow techniques.
description
1996 nî lūn-bûn
@nan
1996年の論文
@ja
1996年学术文章
@wuu
1996年学术文章
@zh
1996年学术文章
@zh-cn
1996年学术文章
@zh-hans
1996年学术文章
@zh-my
1996年学术文章
@zh-sg
1996年學術文章
@yue
1996年學術文章
@zh-hant
name
Pre-steady-state kinetic analy ...... rapid quench flow techniques.
@en
Pre-steady-state kinetic analy ...... rapid quench flow techniques.
@nl
type
label
Pre-steady-state kinetic analy ...... rapid quench flow techniques.
@en
Pre-steady-state kinetic analy ...... rapid quench flow techniques.
@nl
prefLabel
Pre-steady-state kinetic analy ...... rapid quench flow techniques.
@en
Pre-steady-state kinetic analy ...... rapid quench flow techniques.
@nl
P356
P1433
P1476
Pre-steady-state kinetic analy ...... rapid quench flow techniques.
@en
P2093
P304
P356
10.1021/BI952144+
P407
P577
1996-02-01T00:00:00Z