Exploiting bacterial DNA gyrase as a drug target: current state and perspectives. - Wikidata - awgldk - TriplyDB

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

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

http://www.wikidata.org/entity/Q34214929

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Structure of an 'open' clamp type II topoisomerase-DNA complex provides a mechanism for DNA capture and transport A New Crystal Structure of the Bifunctional Antibiotic Simocyclinone D8 Bound to DNA Gyrase Gives Fresh Insight into the Mechanism of Inhibition Direct control of type IIA topoisomerase activity by a chromosomally encoded regulatory protein Protein/DNA interactions in complex DNA topologies: expect the unexpected Fragments of the bacterial toxin microcin B17 as gyrase poisons Application of a novel microtitre plate-based assay for the discovery of new inhibitors of DNA gyrase and DNA topoisomerase VI Synthesis, structure and antibacterial activity of potent DNA gyrase inhibitors: N'-benzoyl-3-(4-bromophenyl)-1H-pyrazole-5-carbohydrazide derivatives Tricyclic GyrB/ParE (TriBE) inhibitors: a new class of broad-spectrum dual-targeting antibacterial agents Toward discovering new anti-cancer agents targeting topoisomerase IIα: a facile screening strategy adaptable to high throughput platform Ciprofloxacin Derivatives Affect Parasite Cell Division and Increase the Survival of Mice Infected with Toxoplasma gondii Proteomics of Aggregatibacter actinomycetemcomitans Outer Membrane Vesicles Investigating the Roles of the C-Terminal Domain of Plasmodium falciparum GyrA Identification of novel bacterial DNA gyrase inhibitors: An in silico study Thiophene antibacterials that allosterically stabilize DNA-cleavage complexes with DNA gyrase Gyramides prevent bacterial growth by inhibiting DNA gyrase and altering chromosome topology.High in vitro activity of the novel spiropyrimidinetrione AZD0914, a DNA gyrase inhibitor, against multidrug-resistant Neisseria gonorrhoeae isolates suggests a new effective option for oral treatment of gonorrhea.Investigational antimicrobial agents of 2013.Identification of the likely translational start of Mycobacterium tuberculosis GyrB.Time- and cost-efficient identification of T-DNA insertion sites through targeted genomic sequencing.Unique features of apicoplast DNA gyrases from Toxoplasma gondii and Plasmodium falciparum.Targeting Mycobacterium tuberculosis topoisomerase I by small-molecule inhibitors.Mode of action of closthioamide: the first member of the polythioamide class of bacterial DNA gyrase inhibitors.Discovery of Indazole Derivatives as a Novel Class of Bacterial Gyrase B Inhibitors.Functional Analyses of the Toxoplasma gondii DNA Gyrase Holoenzyme: A Janus Topoisomerase with Supercoiling and Decatenation Abilities.New Structural Templates for Clinically Validated and Novel Targets in Antimicrobial Drug Research and Development.Residues of E. coli topoisomerase I conserved for interaction with a specific cytosine base to facilitate DNA cleavage.Isolation and quantitation of topoisomerase complexes accumulated on Escherichia coli chromosomal DNA.Optimized droplet digital CFU assay (ddCFU) provides precise quantification of bacteria over a dynamic range of 6 logs and beyond.Structure-based design of novel combinatorially generated NBTIs as potential DNA gyrase inhibitors against various Staphylococcus aureus mutant strains.Mycobacterium fluoroquinolone resistance protein B, a novel small GTPase, is involved in the regulation of DNA gyrase and drug resistance.The naphthoquinone diospyrin is an inhibitor of DNA gyrase with a novel mechanism of action.PprA Protein Is Involved in Chromosome Segregation via Its Physical and Functional Interaction with DNA Gyrase in Irradiated Deinococcus radiodurans Bacteria Optimization of a novel potent and selective bacterial DNA helicase inhibitor scaffold from a high throughput screening hit.The Chromosomal parDE2 Toxin-Antitoxin System of Mycobacterium tuberculosis H37Rv: Genetic and Functional Characterization.Real-time detection of DNA topological changes with a fluorescently labeled cruciform.Ciprofloxacin is an inhibitor of the Mcm2-7 replicative helicase.Biological evaluation of benzothiazole ethyl urea inhibitors of bacterial type II topoisomerases.Fluorescently labeled circular DNA molecules for DNA topology and topoisomerases.Protein/DNA interactions in complex DNA topologies: expect the unexpected.A Systematic Review of In vitro and In vivo Activities of Anti-Toxoplasma Drugs and Compounds (2006-2016).

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

http://www.wikidata.org/entity/Q34214929

description

2011 nî lūn-bûn

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2011 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած

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2011 թվականի նոյեմբերին հրատարակված գիտական հոդված

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2011年の論文

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2011年論文

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2011年論文

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2011年論文

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2011年論文

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2011年論文

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2011年论文

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name

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

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

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

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type

label

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

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

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

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

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

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

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Applied Microbiology and Biotechnology

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

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Shantanu Karkare

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DNA T OPOISOMERASES : Structure, Function, and Mechanism

Structure-activity relationships of aminocoumarin-type gyrase and topoisomerase IV inhibitors obtained by combinatorial biosynthesis

Pentapeptide repeat proteins

Glutamate racemase from Mycobacterium tuberculosis inhibits DNA gyrase by affecting its DNA-binding

Structural basis of gate-DNA breakage and resealing by type II topoisomerases

Dimerization of Escherichia coli DNA-gyrase B provides a structural mechanism for activating the ATPase catalytic center

An open conformation of the Thermus thermophilus gyrase B ATP-binding domain

Crystal structure of the Escherichia coli SbmC protein that protects cells from the DNA replication inhibitor microcin B17

DNA gyrase interaction with coumarin-based inhibitors: the role of the hydroxybenzoate isopentenyl moiety and the 5'-methyl group of the noviose

NMR structure of the Escherichia coli protein YacG: a novel sequence motif in the zinc-finger family of proteins

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10.1007/S00253-011-3557-Z

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3

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Anthony Maxwell

Frédéric Collin

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2011-09-09T00:00:00Z

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2011-11-01T00:00:00Z

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21904817

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mechanism of action

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3189412

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