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Structure-Based Drug Design and Characterization of Sulfonyl-Piperazine Benzothiazinone Inhibitors of DprE1 from Mycobacterium tuberculosis
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What this work says
Outgoing claims: the papers this work cites, builds on, or argues with.
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Structural studies of Mycobacterium tuberculosis DprE1 interacting with its inhibitors
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Development of selective DprE1 inhibitors: Design, synthesis, crystal structure and antitubercular activity of benzothiazolylpyrimidine-5-carboxamides
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Leads for antitubercular compounds from kinase inhibitor library screens
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DprE1 Is a Vulnerable Tuberculosis Drug Target Due to Its Cell Wall Localization
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Identification of Novel Inhibitors of M. tuberculosis Growth Using Whole Cell Based High-Throughput Screening
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2-Carboxyquinoxalines Kill Mycobacterium tuberculosis through Noncovalent Inhibition of DprE1
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Benzothiazinones: Prodrugs That Covalently Modify the Decaprenylphosphoryl-β- d -ribose 2′-epimerase DprE1 of Mycobacterium tuberculosis
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Azaindoles: Noncovalent DprE1 Inhibitors from Scaffold Morphing Efforts, Kill Mycobacterium tuberculosis and Are Efficacious in Vivo
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Discovery of Pyrazolopyridones as a Novel Class of Noncovalent DprE1 Inhibitor with Potent Anti-Mycobacterial Activity
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4-Aminoquinolone Piperidine Amides: Noncovalent Inhibitors of DprE1 with Long Residence Time and Potent Antimycobacterial Activity
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Structural basis of inhibition of Mycobacterium tuberculosis DprE1 by benzothiazinone inhibitors
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Benzothiazinones Kill Mycobacterium tuberculosis by Blocking Arabinan Synthesis
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The 8-Pyrrole-Benzothiazinones Are Noncovalent Inhibitors of DprE1 from Mycobacterium tuberculosis
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Characterization of DprE1-Mediated Benzothiazinone Resistance in Mycobacterium tuberculosis
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1,4-Azaindole, a Potential Drug Candidate for Treatment of Tuberculosis
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Decaprenylphosphoryl Arabinofuranose, the Donor of the d -Arabinofuranosyl Residues of Mycobacterial Arabinan, Is Formed via a Two-Step Epimerization of Decaprenylphosphoryl Ribose
inferredcites →https://doi.org/10.1371/journal.ppat.1000645openalex-snapshot
High Content Screening Identifies Decaprenyl-Phosphoribose 2′ Epimerase as a Target for Intracellular Antimycobacterial Inhibitors
What points at this work
Incoming claims: where this work appears in other papers’ reference lists and arguments.
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