Design, synthesis, biological evaluation and molecular docking of amide and sulfamide derivatives as Escherichia coli pyruvate dehydrogenase complex E1 inhibitors-Reference-Cited by-同舟云学术

Design, synthesis, biological evaluation and molecular docking of amide and sulfamide derivatives as Escherichia coli pyruvate dehydrogenase complex E1 inhibitors

Published:2016 Issue:6 Volume:6 Page:4310-4320
ISSN:2046-2069
Container-title:RSC Advances
language:en
Short-container-title:RSC Adv.

Author:

He Haifeng¹²³⁴⁵,Feng Jiangtao¹²³⁴⁵,He Junbo⁶⁷⁸⁹,Xia Qin¹²³⁴⁵,Ren Yanliang¹²³⁴⁵,Wang Fang¹²³⁴⁵,Peng Hao¹²³⁴⁵,He Hongwu¹²³⁴⁵,Feng Lingling¹²³⁴⁵

Affiliation:

1. Key Laboratory of Pesticide and Chemical Biology of Ministry of Education

2. College of Chemistry

3. Central China Normal University

4. Wuhan 430079

5. P. R. China

6. College of Food Science & Engineering

7. Wuhan Polytechnic University

8. Wuhan 430023

9. China

Abstract

Optimal binding mode of novel E. coli PDHc E1 inhibitor 9d.

Funder

National Natural Science Foundation of China

Publisher

Royal Society of Chemistry (RSC)

Subject

General Chemical Engineering,General Chemistry

Link

http://pubs.rsc.org/en/content/articlepdf/2016/RA/C5RA22573F

Reference20 articles.

1. Multiple Resistance of Botrytis cinerea from Vegetable Crops to Carbendazim, Diethofencarb, Procymidone, and Pyrimethanil in China

2. In vitro activity of β-lactam and non–β-lactam antibiotics in extended-spectrum β-lactamase–producing clinical isolates of Escherichia coli

3. Self-assembly and catalytic activity of the pyruvate dehydrogenase multienzyme complex of Escherichia coli

4. Swinging Arms and Swinging Domains in Multifunctional Enzymes: Catalytic Machines for Multistep Reactions

5. Expression and purification of the dihydrolipoamide acetyltransferase and dihydrolipoamide dehydrogenase subunits of the Escherichia coli pyruvate dehydrogenase multienzyme complex: a mass spectrometric assay for reductive acetylation of dihydrolipoamide acetyltransferase

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