30 articles for DL Boger
The following articles (labelled with PubMed ID or TBD) are for your review
PMID
Data
Article Title
Organization
Discovery and Structure-Activity Relationships of the Neoseptins: A New Class of Toll-like Receptor-4 (TLR4) Agonists.
The Scripps Research Institute
Discovery libraries targeting the major enzyme classes: the serine hydrolases.
The Scripps Research Institute
a-Ketoheterocycle inhibitors of fatty acid amide hydrolase: exploration of conformational constraints in the acyl side chain.
The Scripps Research Institute
Design, synthesis, and characterization ofa-ketoheterocycles that additionally target the cytosolic port Cys269 of fatty acid amide hydrolase.
The Scripps Research Institute
Insights into the mechanism of streptonigrin-induced protein arginine deiminase inactivation.
The Scripps Research Institute-Florida
Optimization of the central heterocycle of alpha-ketoheterocycle inhibitors of fatty acid amide hydrolase.
Institute For Chemical Biology
Optimization of alpha-ketooxazole inhibitors of fatty acid amide hydrolase.
The Scripps Research Institute
Potent and selective alpha-ketoheterocycle-based inhibitors of the anandamide and oleamide catabolizing enzyme, fatty acid amide hydrolase.
The Scripps Research Institute
Discovery of a potent, nonpolyglutamatable inhibitor of glycinamide ribonucleotide transformylase.
The Scripps Research Institute
The discovery and development of inhibitors of fatty acid amide hydrolase (FAAH).
The Scripps Research Institute
Reversible competitivea-ketoheterocycle inhibitors of fatty acid amide hydrolase containing additional conformational constraints in the acyl side chain: orally active, long-acting analgesics.
The Scripps Research Institute
X-ray crystallographic analysis of alpha-ketoheterocycle inhibitors bound to a humanized variant of fatty acid amide hydrolase.
The Scripps Research Institute
Correlation of inhibitor effects on enzyme activity and thermal stability for the integral membrane protein fatty acid amide hydrolase.
The Scripps Research Institute
Exploration of a fundamental substituent effect of alpha-ketoheterocycle enzyme inhibitors: Potent and selective inhibitors of fatty acid amide hydrolase.
The Scripps Research Institute
Next-Generation Diprovocims with Potent Human and Murine TLR1/TLR2 Agonist Activity That Activate the Innate and Adaptive Immune Response.
The Scripps Research Institute
Discovery of AICAR Tfase inhibitors that disrupt requisite enzyme dimerization.
The Scripps Research Institute
Discovery of a potent, selective, and efficacious class of reversible alpha-ketoheterocycle inhibitors of fatty acid amide hydrolase effective as analgesics.
The Scripps Research Institute
Discovery of an exceptionally potent and selective class of fatty acid amide hydrolase inhibitors enlisting proteome-wide selectivity screening: concurrent optimization of enzyme inhibitor potency and selectivity.
The Scripps Research Institute
Heterocyclic sulfoxide and sulfone inhibitors of fatty acid amide hydrolase.
The Scripps Research Institute
alpha-Keto heterocycle inhibitors of fatty acid amide hydrolase: carbonyl group modification and alpha-substitution.
The Scripps Research Institute
Design, synthesis, and biological evaluation of fluoronitrophenyl substituted folate analogues as potential inhibitors of GAR transformylase and AICAR transformylase.
The Scripps Research Institute
Trifluoromethyl ketone inhibitors of fatty acid amide hydrolase: a probe of structural and conformational features contributing to inhibition.
Scripps Research Institute
An endogenous sleep-inducing compound is a novel competitive inhibitor of fatty acid amide hydrolase.
Institute For Chemical Biology
N-Acyl pyrazoles: Effective and tunable inhibitors of serine hydrolases.
The Scripps Research Institute
Comprehensive Analysis of Structure-Activity Relationships of α-Ketoheterocycles as sn-1-Diacylglycerol Lipase α Inhibitors.
Leiden University
Antitumor compound targeting IDH2 mutation and method of use thereof
Chia Tai Tianqing Pharmaceutical Group
Substituted bicyclic dihydropyrimidinones and their use as inhibitors of neutrophil elastase activity
Boehringer Ingelheim International