Journal ArticleDOI
DNA gyrase as a drug target
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TLDR
DNA gyrase is a remarkable enzyme, catalysing the seemingly complex reaction of DNA supercoiling, and it is a good target for antibacterial agents.About:
This article is published in Trends in Microbiology.The article was published on 1997-03-01. It has received 361 citations till now. The article focuses on the topics: DNA gyrase & DNA supercoil.read more
Citations
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Cellular roles of DNA topoisomerases: a molecular perspective.
TL;DR: In this review, the cellular roles of these enzymes are examined from a molecular point of view.
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Molecular mechanisms that confer antibacterial drug resistance
TL;DR: The authors live in an era when antibiotic resistance has spread at an alarming rate and dire predictions concerning the lack of effective antibacterial drugs occur with increasing frequency, so it is apposite to ask a few simple questions about these life-saving molecules.
Journal ArticleDOI
Drugging Topoisomerases: Lessons and Challenges
TL;DR: This review discusses how topoisomerase inhibitors kill cells by trapping topoisomersases on DNA rather than by classical enzymatic inhibition, and extends to a novel mechanism of action of PARP inhibitors and could be applied to the targeting of transcription factors.
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TROSY in triple-resonance experiments: New perspectives for sequential NMR assignment of large proteins
TL;DR: The present paper shows that the implementation of transverse relaxation-optimized spectroscopy ([15N,1H]-TROSY) into triple resonance experiments results in several-fold improved sensitivity for 2H/13C/ 15N-labeled proteins and approximately twofold sensitivity gain for 13C/15N- labeled proteins.
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Where will new antibiotics come from
TL;DR: In this paper, the authors investigated the robustness of antibiotic discovery processes and found that a new class of antibiotic is effective at first, but will eventually select for survival of the small fraction of bacterial populations that have an intrinsic or acquired resistance mechanism.
References
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Journal Article
Arrest of Replication Forks by Drug-stabilized Topoisomerase I-DNA Cleavable Complexes as a Mechanism of Cell Killing by Camptothecin
TL;DR: It is proposed that the collision between moving replication forks and camptothecin-stabilized topoisomerase I-DNA cleavable complexes results in fork arrest and possibly fork breakage, which are lethal to proliferating cells.
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Structure and mechanism of DNA topoisomerase II
TL;DR: The crystal structure of a large fragment of yeast type II DNA topoisomerase reveals a heart-shaped dimeric protein with a large central hole that provides a molecular model of the enzyme as an ATP-modulated clamp with two sets of jaws at opposite ends, connected by multiple joints.
Book
Nucleic Acids and Molecular Biology
Fritz Eckstein,David M.J. Lilley +1 more
TL;DR: A wide range of topics are covered, including articles on nucleic acid structure, through their interactions with proteins to the control of gene expressions and the plant kingdom has not been forgotten with articles on development and transposition in plants.
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DNA Topoisomerases: Essential Enzymes and Lethal Targets
Allan Y. Chen,Leroy F. Liu +1 more
TL;DR: The discovery of E. coli topoisomerase I led to the proposal that the enzyme may form a high-energy covalent bond between itself and the transiently broken DNA phosphodiester bond, and these predictions have turned out to be correct.
Journal ArticleDOI
Structure-activity and structure-side-effect relationships for the quinolone antibacterials
TL;DR: The various structural features of the quinolones which govern antibacterial efficacy and influence the side-effect profile are delineated and summarized at the molecular level and those groups which mutually improve efficacy while reducing side-effects are identified.