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CHIR 090

Known as: CHIR-090, CHIR090 
 
National Institutes of Health

Related topics

Related topics

3 relations

Broader (2)

Hydroxamic AcidsThreonine
analogs & derivatives

Papers overview

Semantic Scholar uses AI to extract papers important to this topic.
2016
2016
Untargeted Metabolomics To Ascertain Antibiotic Modes of Action
ABSTRACT Deciphering the mode of action (MOA) of new antibiotics discovered through phenotypic screening is of increasing… Expand
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2012
2012
Design and stereoselective synthesis of a C-aryl furanoside as a conformationally constrained CHIR-090 analogue.
The UDP-3-O-[(R)-3-hydroxymyristoyl]-N-acetylglucosamine deacetylase (LpxC) is a promising target for the development of novel… Expand
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2011
2011
Structure of the metal-dependent deacetylase LpxC from Yersinia enterocolitica complexed with the potent inhibitor CHIR-090 .
The first committed step of lipid A biosynthesis is catalyzed by UDP-(3-O-((R)-3-hydroxymyristoyl))-N-acetylglucosamine… Expand
2011
2011
Mechanisms Decreasing In Vitro Susceptibility to the LpxC Inhibitor CHIR-090 in the Gram-Negative Pathogen Pseudomonas aeruginosa
ABSTRACT Testing P. aeruginosa efflux pump mutants showed that the LpxC inhibitor CHIR-090 is a substrate for MexAB-OprM, MexCD… Expand
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2011
2011
Design and synthesis of potent Gram-negative specific LpxC inhibitors.
Antibiotic resistant hospital acquired infections are on the rise, creating an urgent need for novel bactericidal drugs. Enzymes… Expand
2010
2010
Antimicrobial Activity of CHIR-090, an Inhibitor of Lipopolysaccharide Biosynthesis, against the Burkholderia cepacia Complex
A striking characteristic of cystic fibrosis (CF) is susceptibility to life-limiting bacterial infections of the respiratory… Expand
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Review
2008
Review
2008
Mechanism and inhibition of LpxC: an essential zinc-dependent deacetylase of bacterial lipid A synthesis.
  • A. Barb, P. Zhou
  • Current pharmaceutical biotechnology
  • 2008
    • Corpus ID: 6146161
Multi-drug resistant (MDR), pathogenic Gram-negative bacteria pose a serious health threat, and novel antibiotic targets must be… Expand
Highly Cited
2007
Highly Cited
2007
Inhibition of lipid A biosynthesis as the primary mechanism of CHIR-090 antibiotic activity in Escherichia coli.
The deacetylation of UDP-3-O-[(R)-3-hydroxymyristoyl]-N-acetylglucosamine (UDP-3-O-acyl-GlcNAc) by LpxC is the committed reaction… Expand
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Highly Cited
2007
Highly Cited
2007
Structure of the deacetylase LpxC bound to the antibiotic CHIR-090: Time-dependent inhibition and specificity in ligand binding
The UDP-3-O-(R-3-hydroxyacyl)-N-acetylglucosamine deacetylase LpxC is an essential enzyme of lipid A biosynthesis in Gram… Expand
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Highly Cited
2005
Highly Cited
2005
A slow, tight-binding inhibitor of the zinc-dependent deacetylase LpxC of lipid A biosynthesis with antibiotic activity comparable to ciprofloxacin.
The zinc-dependent enzyme LpxC catalyzes the deacetylation of UDP-3-O-acyl-GlcNAc, the first committed step of lipid A… Expand
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