Synthetic diacylglycerols (DAG) and DAG-lactones as activators of protein kinase C (PK-C).
about
Combining docking with pharmacophore filtering for improved virtual screeningConformationally constrained analogues of diacylglycerol. 29. Cells sort diacylglycerol-lactone chemical zip codes to produce diverse and selective biological activitiesMembrane anchoring of diacylglycerol lactones substituted with rigid hydrophobic acyl domains correlates with biological activities.Synthesis of protein kinase Cdelta C1b domain by native chemical ligation methodology and characterization of its folding and ligand binding.Binding of curcumin and its long chain derivatives to the activator binding domain of novel protein kinase C.Synthesis, biological, and biophysical studies of DAG-indololactones designed as selective activators of RasGRP.Charge density influences C1 domain ligand affinity and membrane interactionsMolecular systems pharmacology: isoelectric focusing signature of protein kinase Cδ provides an integrated measure of its modulation in response to ligandsFluorescent-responsive synthetic C1b domains of protein kinase Cδ as reporters of specific high-affinity ligand bindingDiacylglycerol lactones targeting the structural features that distinguish the atypical C1 domains of protein kinase C ζ and ι from typical C1 domains.Protein Kinase C: One Pathway towards the Eradication of Latent HIV-1 Reservoirs.Molecular basis for failure of "atypical" C1 domain of Vav1 to bind diacylglycerol/phorbol ester.Wealth of opportunity - the C1 domain as a target for drug development.PKC in Regenerative Therapy: New Insights for Old Targets.Biological profile of the less lipophilic and synthetically more accessible bryostatin 7 closely resembles that of bryostatin 1.N-methyl-substituted fluorescent DAG-indololactone isomers exhibit dramatic differences in membrane interactions and biological activityConformationally constrained analogues of diacylglycerol (DAG). 25. Exploration of the sn-1 and sn-2 carbonyl functionality reveals the essential role of the sn-1 carbonyl at the lipid interface in the binding of DAG-lactones to protein kinase CConformationally constrained analogues of diacylglycerol. 30. An investigation of diacylglycerol-lactones containing heteroaryl groups reveals compounds with high selectivity for Ras guanyl nucleotide-releasing proteinsCharacterization of the differential roles of the twin C1a and C1b domains of protein kinase C-deltaPolar 3-alkylidene-5-pivaloyloxymethyl-5'-hydroxymethyl-gamma-lactones as protein kinase C ligands and antitumor agentsMembrane-surface anchoring of charged diacylglycerol-lactones correlates with biological activitiesConformationally constrained analogues of diacylglycerol (DAG). 31. Modulation of the biological properties of diacylgycerol lactones (DAG-lactones) containing rigid-rod acyl groups separated from the core lactone by spacer units of different lengthSelf-assembly and lipid interactions of diacylglycerol lactone derivatives studied at the air/water interface.Protein kinase C pharmacology: refining the toolbox.Protein kinase C inhibitors: a patent review (2008 - 2009).Peptide-based ligand screening and functional analysis of protein kinase C.Synthesis and biological activities of simplified analogs of the natural PKC ligands, bryostatin-1 and aplysiatoxin.Development of diacyltetrol lipids as activators for the C1 domain of protein kinase C.S-Phase-specific activation of PKC alpha induces senescence in non-small cell lung cancer cells.Effects on ligand interaction and membrane translocation of the positively charged arginine residues situated along the C1 domain binding cleft in the atypical protein kinase C isoforms.A novel diacylglycerol-lactone shows marked selectivity in vitro among C1 domains of protein kinase C (PKC) isoforms alpha and delta as well as selectivity for RasGRP compared with PKCalpha.A single residue in the C1 domain sensitizes novel protein kinase C isoforms to cellular diacylglycerol production.The C1 domain of Vav3, a novel potential therapeutic target.Exploring the influence of indololactone structure on selectivity for binding to the C1 domains of PKCα, PKCε, and RasGRP.Characterization of AJH-836, a DAG-lactone with selectivity for novel PKC isozymes.Synthetic caged DAG-lactones for photochemically controlled activation of protein kinase C.Elucidating the interaction of γ-hydroxymethyl-γ-butyrolactone substituents with model membranes and protein kinase C-C1 domains.
P2860
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P2860
Synthetic diacylglycerols (DAG) and DAG-lactones as activators of protein kinase C (PK-C).
description
2003 nî lūn-bûn
@nan
2003 թուականի Յունիսին հրատարակուած գիտական յօդուած
@hyw
2003 թվականի հունիսին հրատարակված գիտական հոդված
@hy
2003年の論文
@ja
2003年論文
@yue
2003年論文
@zh-hant
2003年論文
@zh-hk
2003年論文
@zh-mo
2003年論文
@zh-tw
2003年论文
@wuu
name
Synthetic diacylglycerols (DAG ...... rs of protein kinase C (PK-C).
@ast
Synthetic diacylglycerols (DAG ...... rs of protein kinase C (PK-C).
@en
type
label
Synthetic diacylglycerols (DAG ...... rs of protein kinase C (PK-C).
@ast
Synthetic diacylglycerols (DAG ...... rs of protein kinase C (PK-C).
@en
prefLabel
Synthetic diacylglycerols (DAG ...... rs of protein kinase C (PK-C).
@ast
Synthetic diacylglycerols (DAG ...... rs of protein kinase C (PK-C).
@en
P356
P1476
Synthetic diacylglycerols (DAG ...... rs of protein kinase C (PK-C).
@en
P2093
Peter M Blumberg
Victor E Marquez
P304
P356
10.1021/AR020124B
P577
2003-06-01T00:00:00Z