Binding affinity analysis of quinolone and dione inhibitors with <i>Mtb</i>-DNA gyrase emphasising the crystal water molecular transfer energy to the protein–ligand association-Reference-Cited by-同舟云学术

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Binding affinity analysis of quinolone and dione inhibitors with Mtb-DNA gyrase emphasising the crystal water molecular transfer energy to the protein–ligand association

Published:2022-02-23 Issue:7 Volume:48 Page:631-646
ISSN:0892-7022
Container-title:Molecular Simulation
language:en
Short-container-title:Molecular Simulation

Author:

Kumar G. Siva¹^ORCID,Sobhia M. Elizabeth¹^ORCID,Ghosh Ketan¹^ORCID

Affiliation:

1. Department of Pharmacoinformatics, National Institute of Pharmaceutical Education and Research (NIPER), S.A.S. Nagar, Punjab, India

Publisher

Informa UK Limited

Subject

Condensed Matter Physics,General Materials Science,General Chemical Engineering,Modeling and Simulation,Information Systems,General Chemistry

Link

https://www.tandfonline.com/doi/pdf/10.1080/08927022.2022.2042530

Reference32 articles.

1. Mycobacterial tuberculosis Enzyme Targets and their Inhibitors

2. Mycobacterium tuberculosis DNA Gyrase as a Target for Drug Discovery

3. Exploiting bacterial DNA gyrase as a drug target: current state and perspectives

4. Global tuberculosis drug development pipeline: the need and the reality

5. Bypassing Fluoroquinolone Resistance with Quinazolinediones: Studies of Drug–Gyrase–DNA Complexes Having Implications for Drug Design

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