Structural Basis of the Promiscuous Inhibitor Susceptibility of Escherichia coli LpxC-Reference-Cited by-同舟云学术

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Structural Basis of the Promiscuous Inhibitor Susceptibility of Escherichia coli LpxC

Published:2013-10-31 Issue:1 Volume:9 Page:237-246
ISSN:1554-8929
Container-title:ACS Chemical Biology
language:en
Short-container-title:ACS Chem. Biol.

Author:

Lee Chul-Jin¹²,Liang Xiaofei³,Gopalaswamy Ramesh³,Najeeb Javaria¹²,Ark Eugene D.⁴,Toone Eric J.¹²³,Zhou Pei¹²³

Affiliation:

1. Department of Biochemistry, Duke University Medical Center, Durham, North Carolina 27710, United States

2. Structural Biology & Biophysics Program, Duke University, Durham, North Carolina 27710, United States

3. Department of Chemistry, Duke University, Durham, North Carolina 27708, United States

4. Trinity College of Arts & Sciences, Duke University, Durham, North Carolina 27708, United States

Funder

National Institute of General Medical Sciences

National Institute of Allergy and Infectious Diseases

Publisher

American Chemical Society (ACS)

Subject

Molecular Medicine,General Medicine,Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/cb400067g

Reference36 articles.

1. Lipopolysaccharide Endotoxins

2. UDP-N-acetylglucosamine acyltransferase of Escherichia coli. The first step of endotoxin biosynthesis is thermodynamically unfavorable.

3. Mechanism and Inhibition of LpxC: An Essential Zinc-Dependent Deacetylase of Bacterial Lipid A Synthesis

4. UDP-3-O-(R-3-hydroxymyristoyl)-N-Acetylglucosamine Deacetylase (LpxC) Inhibitors: A New Class of Antibacterial Agents

5. Potent Inhibitors of LpxC for the Treatment of Gram-Negative Infections

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