27 articles for thisTarget
The following articles (labelled with PubMed ID or TBD) are for your review
PMID
Data
Article Title
Organization
Drug discovery strategies to outer membrane targets in Gram-negative pathogens.
Astrazeneca
Inhibition of the antibacterial target UDP-(3-O-acyl)-N-acetylglucosamine deacetylase (LpxC): isoxazoline zinc amidase inhibitors bearing diverse metal binding groups.
Duke University
N-Hydroxyformamide LpxC inhibitors, their in vivo efficacy in a mouse Escherichia coli infection model, and their safety in a rat hemodynamic assay.
Entasis Therapeutics
Potent, novel in vitro inhibitors of the Pseudomonas aeruginosa deacetylase LpxC.
Chiron
Fragment-Based Discovery of Novel Non-Hydroxamate LpxC Inhibitors with Antibacterial Activity.
Taisho Pharmaceutical
Application of Virtual Screening to the Identification of New LpxC Inhibitor Chemotypes, Oxazolidinone and Isoxazoline.
Novartis Institutes For Biomedical Research
Carbohydroxamido-oxazolidines: antibacterial agents that target lipid A biosynthesis.
Merck Research Laboratories
Sulfonamide-based non-alkyne LpxC inhibitors as Gram-negative antibacterial agents.
Kyorin Pharmaceutical
LpxC Inhibitors: Design, Synthesis, and Biological Evaluation of Oxazolidinones as Gram-negative Antibacterial Agents.
Kyorin Pharmaceutical
Synthesis, biological evaluation and molecular docking studies of benzyloxyacetohydroxamic acids as LpxC inhibitors.
Institut F£R Pharmazeutische Und Medizinische Chemie Der Westf£Lischen Wilhelms-Universit£T M£Nster
Synthesis, structure, and antibiotic activity of aryl-substituted LpxC inhibitors.
Duke University
Pyridone methylsulfone hydroxamate LpxC inhibitors for the treatment of serious gram-negative infections.
Pfizer
Structure based design of an in vivo active hydroxamic acid inhibitor of P. aeruginosa LpxC.
Pfizer
Design and synthesis of potent Gram-negative specific LpxC inhibitors.
Merck Research Laboratories
Syntheses, structures and antibiotic activities of LpxC inhibitors based on the diacetylene scaffold.
Jilin University
Structure of the deacetylase LpxC bound to the antibiotic CHIR-090: Time-dependent inhibition and specificity in ligand binding.
Duke University Medical Center
Design, Synthesis, and Properties of a Potent Inhibitor of Pseudomonas aeruginosa Deacetylase LpxC.
Novartis Institutes For Biomedical Research
Uridine-based inhibitors as new leads for antibiotics targeting Escherichia coli LpxC.
Duke University