Crystal structure of the potent natural product inhibitor balanol in complex with the catalytic subunit of cAMP-dependent protein kinase
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A unified approach to the important protein kinase inhibitor balanol and a proposed analogueHigh resolution crystal structure of the human PDK1 catalytic domain defines the regulatory phosphopeptide docking site.Structure of Human G Protein-Coupled Receptor Kinase 2 in Complex with the Kinase Inhibitor BalanolMolecular Mechanism of Selectivity among G Protein-Coupled Receptor Kinase 2 InhibitorsProtein kinase C: poised to signalDesign and synthesis of inositolphosphoglycan putative insulin mediators.Design, selection, and evaluation of a general kinase-focused library.The protein kinase C inhibitor bisindolyl maleimide 2 binds with reversed orientations to different conformations of protein kinase A.Molecular basis for small molecule inhibition of G protein-coupled receptor kinasesActive site inhibitors protect protein kinase C from dephosphorylation and stabilize its mature form.Crystal Structure of G Protein-coupled Receptor Kinase 5 in Complex with a Rationally Designed InhibitorDocking flexible peptide to flexible protein by molecular dynamics using two implicit-solvent models: an evaluation in protein kinase and phosphatase systems.Natural products as kinase inhibitors.Protein kinase C pharmacology: refining the toolbox.Uncoupling Catalytic and Binding Functions in the Cyclic AMP-Dependent Protein Kinase AA novel inhibitor of active protein kinase G attenuates chronic inflammatory and osteoarthritic pain.Crystal structure of the E230Q mutant of cAMP-dependent protein kinase reveals an unexpected apoenzyme conformation and an extended N-terminal A helix.Exploration of charge states of balanol analogues acting as ATP-competitive inhibitors in kinases.Divergent response of homologous ATP sites to stereospecific ligand fluorination for selectivity enhancement.Efficient inclusion of receptor flexibility in grid-based protein-ligand docking.Water-mediated conformational preselection mechanism in substrate binding cooperativity to protein kinase A.Structural basis for selective inhibition of human PKG Iα by the balanol-like compound N46.Structural basis of conformational variance in phosphorylated and non-phosphorylated states of PKCβII.
P2860
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P2860
Crystal structure of the potent natural product inhibitor balanol in complex with the catalytic subunit of cAMP-dependent protein kinase
description
1999 nî lūn-bûn
@nan
1999 թուականի Փետրուարին հրատարակուած գիտական յօդուած
@hyw
1999 թվականի փետրվարին հրատարակված գիտական հոդված
@hy
1999年の論文
@ja
1999年論文
@yue
1999年論文
@zh-hant
1999年論文
@zh-hk
1999年論文
@zh-mo
1999年論文
@zh-tw
1999年论文
@wuu
name
Crystal structure of the poten ...... cAMP-dependent protein kinase
@ast
Crystal structure of the poten ...... cAMP-dependent protein kinase
@en
Crystal structure of the poten ...... cAMP-dependent protein kinase
@nl
type
label
Crystal structure of the poten ...... cAMP-dependent protein kinase
@ast
Crystal structure of the poten ...... cAMP-dependent protein kinase
@en
Crystal structure of the poten ...... cAMP-dependent protein kinase
@nl
prefLabel
Crystal structure of the poten ...... cAMP-dependent protein kinase
@ast
Crystal structure of the poten ...... cAMP-dependent protein kinase
@en
Crystal structure of the poten ...... cAMP-dependent protein kinase
@nl
P2093
P356
P1433
P1476
Crystal structure of the poten ...... cAMP-dependent protein kinase
@en
P2093
K C Nicolaou
L F Ten Eyck
L L Brunton
M E Bunnage
N Narayana
S S Taylor
T C Diller
P304
P356
10.1021/BI9820659
P407
P577
1999-02-23T00:00:00Z