PMID
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Article Title
Organization
Synthesis, biological, and biophysical studies of DAG-indololactones designed as selective activators of RasGRP.

National Institute of Industrial Technology
Diacylglycerol lactones targeting the structural features that distinguish the atypical C1 domains of protein kinase C¿ and¿ from typical C1 domains.

National Cancer Institute-Bethesda
Thiazole-4-carboxamide adenine dinucleotide (TAD). Analogues stable to phosphodiesterase hydrolysis.

TBA
Conformationally constrained analogues of diacylglycerol (DAG). 27. Modulation of membrane translocation of protein kinase C (PKC) isozymes alpha and delta by diacylglycerol lactones (DAG-lactones) containing rigid-rod acyl groups.

National Cancer Institute-Frederick
Conformationally constrained analogues of diacylglycerol (DAG). 23. Hydrophobic ligand-protein interactions versus ligand-lipid interactions of DAG-lactones with protein kinase C (PK-C).

National Cancer Institute-Frederick
Synthesis and biological evaluation of 5-substituted derivatives of the potent antiherpes agent (north)-methanocarbathymine.

National Cancer Institute-Frederick
Conformationally constrained analogues of diacylglycerol. 20. The search for an elusive binding site on protein kinase C through relocation of the carbonyl pharmacophore along the sn-1 side chain of 1,2-diacylglycerol lactones.

National Cancer Institute-Frederick
A conformationally locked analogue of the anti-HIV agent stavudine. An important correlation between pseudorotation and maximum amplitude.

National Cancer Institute-Frederick
Conformationally constrained analogues of diacylglycerol. 19. Synthesis and protein kinase C binding affinity of diacylglycerol lactones bearing an N-hydroxylamide side chain.

National Cancer Institute-Frederick
Methanocarba modification of uracil and adenine nucleotides: high potency of Northern ring conformation at P2Y1, P2Y2, P2Y4, and P2Y11 but not P2Y6 receptors.

National Institute of Diabetes
An optimized protein kinase C activating diacylglycerol combining high binding affinity (Ki) with reduced lipophilicity (log P).

National Cancer Institute-Frederick
Synthesis, biological activity, and molecular modeling of ribose-modified deoxyadenosine bisphosphate analogues as P2Y(1) receptor ligands.

National Institute of Diabetes
Methanocarba analogues of purine nucleosides as potent and selective adenosine receptor agonists.

National Institute of Diabetes
Molecular modeling and site-directed mutagenesis studies of a phorbol ester-binding site in protein kinase C.

National Cancer Institute-Bethesda
Dehydrogenase binding by tiazofurin anabolites.

University of Rochester Medical Center
Synthesis of pyrimidin-2-one nucleosides as acid-stable inhibitors of cytidine deaminase.

TBA
Cyclic urea nucleosides. Cytidine deaminase activity as a function of aglycon ring size.

TBA
Synthesis of 1,3-diazepin-2-one nucleosides as transition-state inhibitors of cytidine deaminase.

TBA
Ring-Constrained (N)-methanocarba nucleosides as adenosine receptor agonists: independent 5'-uronamide and 2'-deoxy modifications.

Niddk
3-Acyloxy-2-phenalkylpropyl amides and esters of homovanillic acid as novel vanilloid receptor agonists.

Seoul National University
Thiourea analogues of resiniferatoxin as ligands for the vanilloid receptor

TBA
Conformationally constrained analogues of DAG.7. Interaction of a medium-size ε-lactone with protein kinase C (PK-C)_

TBA
Conformationally constrained analogues of diacylglycerol. 9.
1 the effect of side-chain orientation on the protein kinase C (PK-C) binding affinity of σ-lactones

TBA
Conformationally constrained analogues of dag .8. Changes in PK-C binding affinity produced by isosteric groups of the 3-
O-acyl function in 2-deoxy-L-ribonolactones

TBA
Conformationally constrained analogues of diacylglycerol (DAG). 4. Interaction of α-alkylidene-γ-lactones with protein kinase C (PK-C)

TBA
Conformationally constrained analogues of diacylglycerol. 5. 2,5-Dideoxy-3-O-tetradecanoyl-D-galactono-1,4-lactone: A superior homologue of 3-O-tetradecanoyl-2-deoxy-L-ribonolactone with PK-C binding affinity.

TBA
Arylamides of hydroxylated isoquinolines as protein-tyrosine kinase inhibitors

TBA
Structural influences of styryl-based inhibitors on epidermal growth factor receptor and p56
lck tyrosine-specific protein kinases.

TBA
Conformationally 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 lengths.

National Cancer Institute-Frederick
Conformationally constrained analogues of diacylglycerol. 30. An investigation of diacylglycerol-lactones containing heteroaryl groups reveals compounds with high selectivity for Ras guanyl nucleotide-releasing proteins.

National Cancer Institute-Frederick
Conformationally constrained analogues of diacylglycerol. 29. Cells sort diacylglycerol-lactone chemical zip codes to produce diverse and selective biological activities.

National Cancer Institute-Frederick
Conformationally constrained analogues of diacylglycerol (DAG). 28. DAG-dioxolanones reveal a new additional interaction site in the C1b domain of PKC delta.

National Cancer Institute-Frederick
Conformationally constrained analogues of diacylglycerol. 26. Exploring the chemical space surrounding the C1 domain of protein kinase C with DAG-lactones containing aryl groups at the sn-1 and sn-2 positions.

National Cancer Institute-Frederick
Branched diacylglycerol-lactones as potent protein kinase C ligands and alpha-secretase activators.

Research Institute of Pharmaceutical Sciences
Human P2Y(6) receptor: molecular modeling leads to the rational design of a novel agonist based on a unique conformational preference.

Niddk
Conformationally 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 C.

National Cancer Institute-Frederick
Conformationally constrained analogues of diacylglycerol. 21. A solid-phase method of synthesis of diacylglycerol lactones as a prelude to a combinatorial approach for the synthesis of protein kinase C isozyme-specific ligands.

National Cancer Institute At Frederick
2-Substitution of adenine nucleotide analogues containing a bicyclo[3.1.0]hexane ring system locked in a northern conformation: enhanced potency as P2Y1 receptor antagonists.

Niddk
Differential binding modes of diacylglycerol (DAG) and DAG lactones to protein kinase C (PK-C).

National Cancer Institute-Frederick
Conformationally constrained analogues of diacylglycerol. 18. The incorporation of a hydroxamate moiety into diacylglycerol-lactones reduces lipophilicity and helps discriminate between sn-1 and sn-2 binding modes to protein kinase C (PK-C). Implications for isozyme specificity.

Seoul National University
Synthesis and purine receptor affinity of 6-oxopurine nucleosides and nucleotides containing (N)-methanocarba-pseudoribose rings.

Niddk
Conformationally constrained analogues of diacylglycerol (DAG). 17. Contrast between sn-1 and sn-2 DAG lactones in binding to protein kinase C.

National Cancer Institute-Bethesda
Diacylglycerols with lipophilically equivalent branched acyl chains display high affinity for protein kinase C (PK-C). A direct measure of the effect of constraining the glycerol backbone in DAG lactones.

National Cancer Institute-Bethesda
Conformationally constrained analogues of diacylglycerol (DAG). 16. How much structural complexity is necessary for recognition and high binding affinity to protein kinase C?

National Cancer Institute-Bethesda
Protein kinase C ligands based on tetrahydrofuran templates containing a new set of phorbol ester pharmacophores.

Seoul National University
Conformationally constrained analogues of diacylglycerol (DAG). 15. The indispensable role of the sn-1 and sn-2 carbonyls in the binding of DAG-lactones to protein kinase C (PK-C).

National Institutes of Health
Conformationally constrained analogues of diacylglycerol (DAG). 14. Dissection of the roles of the sn-1 and sn-2 carbonyls in DAG mimetics by isopharmacophore replacement.

National Cancer Institute-Bethesda
Carbocyclic analogues of the potent cytidine deaminase inhibitor 1-(beta-D-ribofuranosyl)-1,2-dihydropyrimidin-2-one (zebularine).

National Cancer Institute-Bethesda
Conformationally constrained analogues of diacylglycerol. 13. Protein kinase C ligands based on templates derived from 2,3-dideoxy-L-erythro(threo)-hexono-1,4-lactone and 2-deoxyapiolactone.

National Cancer Institute-Bethesda
Conformationally constrained analogues of diacylglycerol. 12. Ultrapotent protein kinase C ligands based on a chiral 4,4-disubstituted heptono-1,4-lactone template.

National Cancer Institute-Bethesda
Conformationally constrained analogues of diacylglycerol. 11. Ultrapotent protein kinase C ligands based on a chiral 5-disubstituted tetrahydro-2-furanone template.

National Cancer Institute-Bethesda
Conformationally constrained analogues of diacylglycerol. 10. Ultrapotent protein kinase C ligands based on a racemic 5-disubstituted tetrahydro-2-furanone template.

National Cancer Institute-Bethesda
Bicyclic compounds as ring-constrained inhibitors of protein-tyrosine kinase p56lck.

National Cancer Institute-Bethesda
Protein kinase C. Modeling of the binding site and prediction of binding constants.

National Cancer Institute-Bethesda
The discovery of novel, structurally diverse protein kinase C agonists through computer 3D-database pharmacophore search. Molecular modeling studies.

National Cancer Institute-Bethesda
The nucleoside analogue D-carba T blocks HIV-1 reverse transcription.

Nci-Frederick
Cyclopentenyluridine and cyclopentenylcytidine analogues as inhibitors of uridine-cytidine kinase.

TBA
Furanose-pyranose isomerization of reduced pyrimidine and cyclic urea ribosides.

TBA
Synthesis and biological activity of unsaturated carboacyclic purine nucleoside analogues.

TBA
Phosphonate-containing inhibitors of tyrosine-specific protein kinases.

National Cancer Institute-Bethesda
Development of GlcNAc-inspired iminocyclitiols as potent and selective N-acetyl-beta-hexosaminidase inhibitors.

Academia Sinica